data_1V0Z
# 
_entry.id   1V0Z 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.282 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   1V0Z         
PDBE  EBI-20011    
WWPDB D_1290020011 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
_pdbx_database_related.details 
PDB 1A14 unspecified 
;COMPLEX BETWEEN NC10 ANTI-INFLUENZA VIRUS NEURAMINIDASE SINGLE CHAIN ANTIBODY WITH A 5 RESIDUE LINKER AND INFLUENZA VIRUS NEURAMINIDASE
;
PDB 1A4G unspecified 'INFLUENZA VIRUS B/BEIJING/1/87 NEURAMINIDASE COMPLEXED WITH ZANAMIVIR' 
PDB 1A4Q unspecified 'INFLUENZA VIRUS B/BEIJING/1/87 NEURAMINIDASE COMPLEXED WITH DIHYDROPYRAN-PHENETHYL-PROPYL- CARBOXAMIDE' 
PDB 1B9S unspecified 
;NOVEL AROMATIC INHIBITORS OF INFLUENZA VIRUS NEURAMINIDASE MAKE SELECTIVE INTERACTIONS WITH CONSERVED RESIDUES AND WATER MOLECULES IN THE ACTIVE SITE
;
PDB 1B9T unspecified 
;NOVEL AROMATIC INHIBITORS OF INFLUENZA VIRUS NEURAMINIDASE MAKE SELECTIVE INTERACTIONS WITH CONSERVED RESIDUES AND WATER MOLECULES IN THE ACTIVE SITE
;
PDB 1B9V unspecified 
;NOVEL AROMATIC INHIBITORS OF INFLUENZA VIRUS NEURAMINIDASE MAKE SELECTIVE INTERACTIONS WITH CONSERVED RESIDUES AND WATER MOLECULES IN TEH ACTIVE SITE
;
PDB 1BJI unspecified 
;THE X-RAY STRUCTURE OF A COMPLEX OF TERN N9 INFLUENZA VIRUS NEURAMINIDASE COMPLEXED WITH THE GLAXO 6-CARBOXAMIDE SIALIC ACID ANALOGUE GR217029
;
PDB 1E8T unspecified 'STRUCTURE OF THE MULTIFUNCTIONAL PARAMYXOVIRUS HEMAGGLUTININ-NEURAMINIDASE' 
PDB 1E8U unspecified 'STRUCTURE OF THE MULTIFUNCTIONAL PARAMYXOVIRUS HEMAGGLUTININ-NEURAMINIDASE' 
PDB 1E8V unspecified 'STRUCTURE OF THE MULTIFUNCTIONAL PARAMYXOVIRUS HEMAGGLUTININ-NEURAMINIDASE' 
PDB 1EUU unspecified 'SIALIDASE OR NEURAMINIDASE, LARGE 68KD FORM' 
PDB 1F8B unspecified 'NATIVE INFLUENZA VIRUS NEURAMINIDASE IN COMPLEX WITHNEU5AC2EN' 
PDB 1F8C unspecified 'NATIVE INFLUENZA NEURAMINIDASE IN COMPLEX WITH 4-AMINO-2-DEOXY-2,3-DEHYDRO-N- NEURAMINIC ACID' 
PDB 1F8D unspecified 'NATIVE INFLUENZA NEURAMINIDASE IN COMPLEX WITH 9-AMINO-2-DEOXY-2,3-DEHYDRO-N- NEURAMINIC ACID' 
PDB 1F8E unspecified 'NATIVE INFLUENZA NEURAMINIDASE IN COMPLEX WITH 4,9-DIAMINO-2-DEOXY-2,3-DEHYDRO-N- ACETYL-NEURAMINIC ACID' 
PDB 1INF unspecified 'INFLUENZA VIRUS B/LEE/40 NEURAMINIDASE COMPLEXED WITH BANA113 INHIBITOR' 
PDB 1ING unspecified 'INFLUENZA A SUBTYPE N2 NEURAMINIDASE COMPLEXED WITH AROMATIC BANA109 INHIBITOR' 
PDB 1INH unspecified 'INFLUENZA A SUBTYPE N2 NEURAMINIDASE COMPLEXED WITH AROMATIC BANA111 INHIBITOR' 
PDB 1INV unspecified 
;INFLUENZA B/LEE/40 NEURAMINIDASE (SIALIDASE) COMPLEXED WITH EPANA INHIBITOR (4-ACETAMIDO- 2,4-DIDEOXY-D-GLYCERO-ALPHA-D-GALACTO-1 -OCTOPYRANOSYL) PHOSPHONIC ACID
;
PDB 1INW unspecified 
;INFLUENZA A SUBTYPE N2 NEURAMINIDASE ( SIALIDASE) COMPLEXED WITH APANA INHIBITOR (4- ACETAMIDO- 2,4-DIDEOXY-D-GLYCERO-BETA-D- GALACTO-1-OCTOPYRANOSYL) PHOSPHONIC ACID
;
PDB 1INX unspecified 
;INFLUENZA A SUBTYPE N2 NEURAMINIDASE ( SIALIDASE) COMPLEXED WITH EPANA INHIBITOR (4- ACETAMIDO- 2,4-DIDEOXY-D-GLYCERO-ALPHA-D- GALACTO-1-OCTOPYRANOSYL) PHOSPHONIC ACID
;
PDB 1INY unspecified 
;INFLUENZA A SUBTYPE N9 NEURAMINIDASE ( SIALIDASE) COMPLEXED WITH EPANA INHIBITOR (4- ACETAMIDO- 2,4-DIDEOXY-D-GLYCERO-ALPHA-D- GALACTO-1-OCTOPYRANOSYL) PHOSPHONIC ACID
;
PDB 1IVB unspecified 
;INFLUENZA VIRUS B/LEE/40 NEURAMINIDASE ( SIALIDASE) COMPLEXED WITH BANA105 INHIBITOR (4 -(ACETYLAMINO)-3-HYDROXY-5-NITROBENZOIC ACID )
;
PDB 1IVC unspecified 
;INFLUENZA A SUBTYPE N2 NEURAMINIDASE ( SIALIDASE) COMPLEXED WITH AROMATIC BANA106 INHIBITOR (4-(ACETYLAMINO)-5-AMINO-3- HYDROXYBENZOIC ACID)
;
PDB 1IVD unspecified 
;INFLUENZA A SUBTYPE N2 NEURAMINIDASE ( SIALIDASE) COMPLEXED WITH AROMATIC BANA105 INHIBITOR (4-(ACETYLAMINO)-3-HYDROXY-5- NITROBENZOIC ACID)
;
PDB 1IVE unspecified 
'INFLUENZA A SUBTYPE N2 NEURAMINIDASE ( SIALIDASE) COMPLEXED WITH AROMATIC BANA108 INHIBITOR (4-(ACETYLAMINO)-3-AMINOBENZOIC ACID )' 
PDB 1IVF unspecified 
'INFLUENZA A SUBTYPE N2 NEURAMINIDASE ( SIALIDASE) COMPLEXED WITH DANA INHIBITOR (2- DEOXY-2,3-DIDEHYDRO-D-N-ACETYLNEURAMINIC ACID)' 
PDB 1IVG unspecified 'INFLUENZA A SUBTYPE N2 NEURAMINIDASE ( SIALIDASE)' 
PDB 1KIT unspecified 'VIBRIO CHOLERAE NEURAMINIDASE' 
PDB 1L7F unspecified 'CRYSTAL STRUCTURE OF INFLUENZA VIRUS NEURAMINIDASE INCOMPLEX WITH BCX-1812' 
PDB 1L7G unspecified 'CRYSTAL STRUCTURE OF E119G MUTANT INFLUENZA VIRUSNEURAMINIDASE IN COMPLEX WITH BCX-1812' 
PDB 1L7H unspecified 'CRYSTAL STRUCTURE OF R292K MUTANT INFLUENZA VIRUSNEURAMINIDASE IN COMPLEX WITH BCX-1812' 
PDB 1MWE unspecified 
;THE X-RAY STRUCTURE OF A COMPLEX OF TERN N9 INFLUENZA VIRUS NEURAMINIDASE COMPLEXED WITH SIALIC ACID AT 4 DEGREES C REVEALING A SECOND SIALIC ACID BINDING SITE
;
PDB 1NCA unspecified 'N9 NEURAMINIDASE-NC41 COMPLEX WITH FAB' 
PDB 1NCB unspecified 'N9 NEURAMINIDASE-NC41 MUTANT WITH ASN 329 REPLACED BY ASP (N329D) COMPLEX WITH FAB' 
PDB 1NCC unspecified 'N9 NEURAMINIDASE-NC41 MUTANT WITH ILE 368 REPLACED BY ARG (I368R) COMPLEX WITH FAB' 
PDB 1NCD unspecified 'N9 NEURAMINIDASE-NC41 COMPLEX WITH FAB' 
PDB 1NMA unspecified 
;MOL_ID: 1; MOLECULE: N9 NEURAMINIDASE; CHAIN : N; EC: 3.2.1.18; MUTATION: WILD TYPE ; MOL_ID: 2; MOLECULE: FAB NC10; CHAIN: L , H; OTHER_DETAILS: RESOLUTION OF 3.0 ANGSTROMS
;
PDB 1NMB unspecified 
;MOL_ID: 1; MOLECULE: N9 NEURAMINIDASE; CHAIN : N; EC: 3.2.1.18; MUTATION: WILD TYPE ; MOL_ID: 2; MOLECULE: FAB NC10; CHAIN: L , H; OTHER_DETAILS: RESOLUTION OF 2.5 ANGSTROMS
;
PDB 1NMC unspecified 
;COMPLEX BETWEEN NC10 ANTI-INFLUENZA VIRUS NEURAMINIDASE SINGLE CHAIN ANTIBODY WITH A 15 RESIDUE LINKER AND INFLUENZA VIRUS NEURAMINIDASE
;
PDB 1NN2 unspecified NEURAMINIDASE 
PDB 1NNA unspecified 'NEURAMINIDASE (SIALIDASE)' 
PDB 1NNB unspecified 'NEURAMINIDASE (SIALIDASE) COMPLEXED WITH 2- DEOXY-2,3-DEHYDRO-N-ACETYL NEURAMINIC ACID' 
PDB 1NNC unspecified 'INFLUENZA VIRUS NEURAMINIDASE SUBTYPE N9 (TERN ) COMPLEXED WITH 4-GUANIDINO-NEU5AC2EN INHIBITOR' 
PDB 1NSB unspecified 'NEURAMINIDASE (SIALIDASE)' 
PDB 1NSC unspecified 'NEURAMINIDASE (SIALIDASE) COMPLEX WITH N- ACETYL NEURAMINIC ACID (SIALIC ACID)' 
PDB 1NSD unspecified 'NEURAMINIDASE (SIALIDASE) COMPLEX WITH 2,3- DEHYDRO-2-DEOXY-N-ACETYL NEURAMINIC ACID ( DANA)' 
PDB 1USR unspecified 'NEWCASTLE DISEASE VIRUS HEMAGGLUTININ- NEURAMINIDASE COMPLEXED WITH THIOSIALOSIDE' 
PDB 1USX unspecified 'CRYSTAL STRUCTURE OF THE NEWCASTLE DISEASE VIRUS HEMAGGLUTININ-NEURAMINIDASE COMPLEXED WITH THIOSIALOSIDE' 
PDB 1V2I unspecified 'STRUCTURE OF THE HEMAGGLUTININ-NEURAMINIDASE FROM HUMANPARAINFLUENZA VIRUS TYPE III' 
PDB 1V3B unspecified 'STRUCTURE OF THE HEMAGGLUTININ-NEURAMINIDASE FROM HUMANPARAINFLUENZA VIRUS TYPE III' 
PDB 1V3C unspecified 'STRUCTURE OF THE HEMAGGLUTININ-NEURAMINIDASE FROM HUMANPARAINFLUENZA VIRUS TYPE III: COMPLEX WITH NEU5AC' 
PDB 1V3D unspecified 'STRUCTURE OF THE HEMAGGLUTININ-NEURAMINIDASE FROM HUMANPARAINFLUENZA VIRUS TYPE III: COMPLEX WITH NEU5AC2EN' 
PDB 1V3E unspecified 'STRUCTURE OF THE HEMAGGLUTININ-NEURAMINIDASE FROM HUMANPARAINFLUENZA VIRUS TYPE III: COMPLEX WITH ZANAMAVIR' 
PDB 1VCJ unspecified 
;INFLUENZA B VIRUS NEURAMINIDASE COMPLEXED WITH 1-(4-CARBOXY-2-(3-PENTYLAMINO)PHENYL)-5 -AMINOMETHYL-5-HYDROXYMETHYL-PYRROLIDIN-2-ONE
;
PDB 1W1X unspecified 
;STRUCTURE OF NEURAMINIDASE FROM ENGLISH DUCK SUBTYPE N6 COMPLEXED WITH 30 MM SIALIC ACID (NANA, NEU5AC), CRYSTAL SOAKED FOR 3 HOURS AT 277 K.
;
PDB 1W20 unspecified 
;STRUCTURE OF NEURAMINIDASE FROM ENGLISH DUCK SUBTYPE N6 COMPLEXED WITH 30 MM SIALIC ACID (NANA, NEU5AC), CRYSTAL SOAKED FOR 3 HOURS AT 291 K
;
PDB 1W21 unspecified 
;STRUCTURE OF NEURAMINIDASE FROM ENGLISH DUCK SUBTYPE N6 COMPLEXED WITH 30 MM SIALIC ACID (NANA, NEU5AC), CRYSTAL SOAKED FOR 43 HOURS AT 291 K.
;
PDB 1W8N unspecified 
'CONTRIBUTION OF THE ACTIVE SITE ASPARTIC ACID TO CATALYSIS IN THE BACTERIAL NEURAMINIDASE FROM MICROMONOSPORA VIRIDIFACIENS.' 
PDB 1W8O unspecified 
'CONTRIBUTION OF THE ACTIVE SITE ASPARTIC ACID TO CATALYSIS IN THE BACTERIAL NEURAMINIDASE FROM MICROMONOSPORA VIRIDIFACIENS' 
PDB 1XOE unspecified 
;N9 TERN INFLUENZA NEURAMINIDASE COMPLEXED WITH (2R,4R,5R)-5-(1-ACETYLAMINO-3-METHYL- BUTYL-PYRROLIDINE-2, 4-DICAROBYXYLIC ACID 4 -METHYL ESTERDASE COMPLEXED WITH
;
PDB 1XOG unspecified 'N9 TERN INFLUENZA NEURAMINIDASE COMPLEXED WITH A 2,5-DISUBSTITUTED TETRAHYDROFURAN-5- CARBOXYLIC ACID' 
PDB 1Z4V unspecified 'PARAINFLUENZA VIRUS 5 (SV5) HEMAGGLUTININ- NEURAMINIDASE(HN) WITH LIGAND DANA (SOAKED WITH DANA, PH 7.0)' 
PDB 1Z4W unspecified 'PARAINFLUENZA VIRUS 5 (SV5) HEMAGGLUTININ- NEURAMINIDASE(HN) WITH LIGAND DANA (SOAKED WITH DANA, PH8.0)' 
PDB 1Z4X unspecified 
'PARAINFLUENZA VIRUS 5 (SV5) HEMAGGLUTININ- NEURAMINIDASE(HN) WITH LIGAND SIALYLLACTOSE ( SOAKED WITH SIALYLLACTOSE,PH8.0)' 
PDB 1Z4Y unspecified 'PARAINFLUENZA VIRUS 5 (SV5) HEMAGGLUTININ- NEURAMINIDASE(HN) (PH 8.0)' 
PDB 1Z4Z unspecified 
'PARAINFLUENZA VIRUS 5 (SV5) HEMAGGLUTININ- NEURAMINIDASE(HN) WITH LIGAND DANA(SOAKED WITH SIALIC ACID, PH7.0))' 
PDB 1Z50 unspecified 
'PARAINFLUENZA VIRUS 5 (SV5) HEMAGGLUTININ- NEURAMINIDASE(HN) WITH LIGAND DANA (SOAKED WITH SIALIC ACID, PH 8.0)' 
PDB 2BAT unspecified 'NEURAMINIDASE N2 COMPLEX WITH SIALIC ACID (N -ACTYL NEURAMINIC ACID)' 
PDB 2QWA unspecified 'THE X-RAY STRUCTURE OF A DRUG RESISTANT VARIANT R292K OF TERN N9 INFLUENZA VIRUS NEURAMINIDASE' 
PDB 2QWB unspecified 
'THE X-RAY STRUCTURE OF A COMPLEX OF SIALIC ACID AND A DRUG RESISTANT VARIANT R292K OF TERN N9 INFLUENZA VIRUS NEURAMINIDASE' 
PDB 2QWC unspecified 
'THE X-RAY STRUCTURE OF A COMPLEX OF NEU5AC2EN AND A DRUG RESISTANT VARIANT R292K OF TERN N9 INFLUENZA VIRUS NEURAMINIDASE' 
PDB 2QWD unspecified 
'THE X-RAY STRUCTURE OF A COMPLEX OF 4- AMINO-NEU5AC2EN AND A DRUG RESISTANT VARIANT R292K OF TERN N9 INFLUENZA VIRUS NEURAMINIDASE' 
PDB 2QWE unspecified 
;THE X-RAY STRUCTURE OF A COMPLEX OF 4- GUANIDINO-NEU5AC2EN AND A DRUG RESISTANT VARIANT R292K OF TERN N9 INFLUENZA VIRUS NEURAMINIDASE
;
PDB 2QWF unspecified 
;THE X-RAY STRUCTURE OF A COMPLEX OF N- ACETYL-4-GUANIDINO-6- METHYL(PROPYL) CARBOXAMIDE-4,5-DIHYDRO-2H-PYRAN-2- CARBOXYLIC ACID AND A DRUG RESISTANT VARIANT R292K OF TERN N9 INFLUENZA VIRUS NEURAMINIDASE
;
PDB 2QWG unspecified 
;THE X-RAY STRUCTURE OF A COMPLEX OF 5- N-ACETYL-4-AMINO-6- DIETHYLCARBOXAMIDE-4,5 -DIHYDRO-2H-PYRAN-2-CARBOXYLIC ACID AND A DRUG RESISTANT VARIANT R292K OF TERN N9 INFLUENZA VIRUS NEURAMINIDASE
;
PDB 2QWH unspecified 
;THE X-RAY STRUCTURE OF A COMPLEX OF 5- N-ACETYL-5-AMINO-3- (1-ETHYLPROPOXY)-1- CYCLOHEXENE-1-CARBOXYLIC ACID (GS4071) AND A DRUG RESISTANT VARIANT R292K OF TERN N9 INFLUENZA VIRUS NEURAMINIDASE
;
PDB 2QWI unspecified 
;THE X-RAY STRUCTURE OF A COMPLEX OF N- ACETYL-4-GUANIDINO-6- METHYL(PROPYL) CARBOXAMIDE-4,5-DIHYDRO-2H-PYRAN-2- CARBOXYLIC ACID AND WILDTYPE TERN N9 INFLUENZA VIRUS NEURAMINIDASE
;
PDB 2QWJ unspecified 
;THE X-RAY STRUCTURE OF A COMPLEX OF 5- N-ACETYL-4-AMINO-6- DIETHYLCARBOXAMIDE-4,5 -DIHYDRO-2H-PYRAN-2-CARBOXYLIC ACID AND A DRUG RESISTANT VARIANT R292K OF TERN N9 INFLUENZA VIRUS NEURAMINIDASE
;
PDB 2QWK unspecified 
;THE X-RAY STRUCTURE OF A COMPLEX OF 5- N-ACETYL-5-AMINO-3- (1-ETHYLPROPOXY)-1- CYCLOHEXENE-1-CARBOXYLIC ACID (GS4071) AND WILDTYPE TERN N9 INFLUENZA VIRUS NEURAMINIDASE
;
PDB 2SIL unspecified 'SIALIDASE (NEURAMINIDASE)' 
PDB 2SIM unspecified 'SIALIDASE (NEURAMINIDASE)' 
PDB 3NN9 unspecified 'NEURAMINIDASE N9 (SIALIDASE) (MUTANT WITH ASN 329 REPLACED BY ASP) (N329D)' 
PDB 4NN9 unspecified 'NEURAMINIDASE N9 (SIALIDASE) (MUTANT WITH ILE 368 REPLACED BY ARG) (I368R)' 
PDB 5NN9 unspecified 'NEURAMINIDASE N9 (SIALIDASE) (MUTANT WITH ALA 369 REPLACED BY ASP) (A369D)' 
PDB 6NN9 unspecified 'NEURAMINIDASE N9 (SIALIDASE) (MUTANT WITH LYS 432 REPLACED BY ASN) (K432N)' 
PDB 7NN9 unspecified 'NATIVE INFLUENZA VIRUS NEURAMINIDASE SUBTYPE N9 (TERN)' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        1V0Z 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.SG_entry                        . 
_pdbx_database_status.recvd_initial_deposition_date   2004-03-12 
_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 
'Rudino-Pinera, E.' 1 
'Tunnah, P.'        2 
'Crennell, S.J.'    3 
'Webster, R.G.'     4 
'Laver, W.G.'       5 
'Garman, E.F.'      6 
# 
_citation.id                        primary 
_citation.title                     
'The Crystal Structure of Influenza Type a Virus Neuraminidase of the N6 Subtype at 1.85 A Resolution' 
_citation.journal_abbrev            'To be Published' 
_citation.journal_volume            ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.year                      ? 
_citation.journal_id_ASTM           ? 
_citation.country                   ? 
_citation.journal_id_ISSN           ? 
_citation.journal_id_CSD            0353 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_DOI      ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Rudino-Pinera, E.' 1 
primary 'Crennell, S.J.'    2 
primary 'Webster, R.G.'     3 
primary 'Laver, W.G.'       4 
primary 'Garman, E.F.'      5 
# 
_cell.entry_id           1V0Z 
_cell.length_a           106.482 
_cell.length_b           73.755 
_cell.length_c           106.809 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.37 
_cell.angle_gamma        90.00 
_cell.Z_PDB              8 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         1V0Z 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
# 
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 NEURAMINIDASE           43011.531 4    3.2.1.18 ? ? ? 
2 non-polymer syn 'CALCIUM ION'           40.078    4    ?        ? ? ? 
3 non-polymer syn GLYCEROL                92.094    4    ?        ? ? ? 
4 non-polymer man N-ACETYL-D-GLUCOSAMINE  221.208   20   ?        ? ? ? 
5 non-polymer man ALPHA-D-MANNOSE         180.156   14   ?        ? ? ? 
6 non-polymer man BETA-D-MANNOSE          180.156   4    ?        ? ? ? 
7 non-polymer syn 'DI(HYDROXYETHYL)ETHER' 106.120   1    ?        ? ? ? 
8 water       nat water                   18.015    1798 ?        ? ? ? 
# 
_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       
;RTFLNLTKPLCEVNSWHILSKDNAIRIGEDAHILVTREPYLSCDPQGCRMFALSQGTTLRGRHANGTIHDRSPFRALISW
EMGQAPSPYNTRVECIGWSSTSCHDGMSRMSICMSGPNNNASAVVWYGGRPITEIPSWAGNILRTQESECVCHKGVCPVV
MTDGPANNRAATKIIYFKEGKIQKIEELAGNAQHIEECSCYGAGGVIKCICRDNWKGANRPVITIDPEMMTHTSKYLCSK
VLTDTSRPNDPTNGNCDAPITGGSPDPGVKGFAFLDGENSWLGRTISKDSRSGYEMLKVPNAETDIQSGPISNQVIVNNQ
NWSGYSGAFIDYWANKECFNPCFYVELIRGRPKESSVLWTSNSIVALCGSKKRLGSWSWHDGAEIIYFE
;
_entity_poly.pdbx_seq_one_letter_code_can   
;RTFLNLTKPLCEVNSWHILSKDNAIRIGEDAHILVTREPYLSCDPQGCRMFALSQGTTLRGRHANGTIHDRSPFRALISW
EMGQAPSPYNTRVECIGWSSTSCHDGMSRMSICMSGPNNNASAVVWYGGRPITEIPSWAGNILRTQESECVCHKGVCPVV
MTDGPANNRAATKIIYFKEGKIQKIEELAGNAQHIEECSCYGAGGVIKCICRDNWKGANRPVITIDPEMMTHTSKYLCSK
VLTDTSRPNDPTNGNCDAPITGGSPDPGVKGFAFLDGENSWLGRTISKDSRSGYEMLKVPNAETDIQSGPISNQVIVNNQ
NWSGYSGAFIDYWANKECFNPCFYVELIRGRPKESSVLWTSNSIVALCGSKKRLGSWSWHDGAEIIYFE
;
_entity_poly.pdbx_strand_id                 A,B,C,D 
_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   ARG n 
1 2   THR n 
1 3   PHE n 
1 4   LEU n 
1 5   ASN n 
1 6   LEU n 
1 7   THR n 
1 8   LYS n 
1 9   PRO n 
1 10  LEU n 
1 11  CYS n 
1 12  GLU n 
1 13  VAL n 
1 14  ASN n 
1 15  SER n 
1 16  TRP n 
1 17  HIS n 
1 18  ILE n 
1 19  LEU n 
1 20  SER n 
1 21  LYS n 
1 22  ASP n 
1 23  ASN n 
1 24  ALA n 
1 25  ILE n 
1 26  ARG n 
1 27  ILE n 
1 28  GLY n 
1 29  GLU n 
1 30  ASP n 
1 31  ALA n 
1 32  HIS n 
1 33  ILE n 
1 34  LEU n 
1 35  VAL n 
1 36  THR n 
1 37  ARG n 
1 38  GLU n 
1 39  PRO n 
1 40  TYR n 
1 41  LEU n 
1 42  SER n 
1 43  CYS n 
1 44  ASP n 
1 45  PRO n 
1 46  GLN n 
1 47  GLY n 
1 48  CYS n 
1 49  ARG n 
1 50  MET n 
1 51  PHE n 
1 52  ALA n 
1 53  LEU n 
1 54  SER n 
1 55  GLN n 
1 56  GLY n 
1 57  THR n 
1 58  THR n 
1 59  LEU n 
1 60  ARG n 
1 61  GLY n 
1 62  ARG n 
1 63  HIS n 
1 64  ALA n 
1 65  ASN n 
1 66  GLY n 
1 67  THR n 
1 68  ILE n 
1 69  HIS n 
1 70  ASP n 
1 71  ARG n 
1 72  SER n 
1 73  PRO n 
1 74  PHE n 
1 75  ARG n 
1 76  ALA n 
1 77  LEU n 
1 78  ILE n 
1 79  SER n 
1 80  TRP n 
1 81  GLU n 
1 82  MET n 
1 83  GLY n 
1 84  GLN n 
1 85  ALA n 
1 86  PRO n 
1 87  SER n 
1 88  PRO n 
1 89  TYR n 
1 90  ASN n 
1 91  THR n 
1 92  ARG n 
1 93  VAL n 
1 94  GLU n 
1 95  CYS n 
1 96  ILE n 
1 97  GLY n 
1 98  TRP n 
1 99  SER n 
1 100 SER n 
1 101 THR n 
1 102 SER n 
1 103 CYS n 
1 104 HIS n 
1 105 ASP n 
1 106 GLY n 
1 107 MET n 
1 108 SER n 
1 109 ARG n 
1 110 MET n 
1 111 SER n 
1 112 ILE n 
1 113 CYS n 
1 114 MET n 
1 115 SER n 
1 116 GLY n 
1 117 PRO n 
1 118 ASN n 
1 119 ASN n 
1 120 ASN n 
1 121 ALA n 
1 122 SER n 
1 123 ALA n 
1 124 VAL n 
1 125 VAL n 
1 126 TRP n 
1 127 TYR n 
1 128 GLY n 
1 129 GLY n 
1 130 ARG n 
1 131 PRO n 
1 132 ILE n 
1 133 THR n 
1 134 GLU n 
1 135 ILE n 
1 136 PRO n 
1 137 SER n 
1 138 TRP n 
1 139 ALA n 
1 140 GLY n 
1 141 ASN n 
1 142 ILE n 
1 143 LEU n 
1 144 ARG n 
1 145 THR n 
1 146 GLN n 
1 147 GLU n 
1 148 SER n 
1 149 GLU n 
1 150 CYS n 
1 151 VAL n 
1 152 CYS n 
1 153 HIS n 
1 154 LYS n 
1 155 GLY n 
1 156 VAL n 
1 157 CYS n 
1 158 PRO n 
1 159 VAL n 
1 160 VAL n 
1 161 MET n 
1 162 THR n 
1 163 ASP n 
1 164 GLY n 
1 165 PRO n 
1 166 ALA n 
1 167 ASN n 
1 168 ASN n 
1 169 ARG n 
1 170 ALA n 
1 171 ALA n 
1 172 THR n 
1 173 LYS n 
1 174 ILE n 
1 175 ILE n 
1 176 TYR n 
1 177 PHE n 
1 178 LYS n 
1 179 GLU n 
1 180 GLY n 
1 181 LYS n 
1 182 ILE n 
1 183 GLN n 
1 184 LYS n 
1 185 ILE n 
1 186 GLU n 
1 187 GLU n 
1 188 LEU n 
1 189 ALA n 
1 190 GLY n 
1 191 ASN n 
1 192 ALA n 
1 193 GLN n 
1 194 HIS n 
1 195 ILE n 
1 196 GLU n 
1 197 GLU n 
1 198 CYS n 
1 199 SER n 
1 200 CYS n 
1 201 TYR n 
1 202 GLY n 
1 203 ALA n 
1 204 GLY n 
1 205 GLY n 
1 206 VAL n 
1 207 ILE n 
1 208 LYS n 
1 209 CYS n 
1 210 ILE n 
1 211 CYS n 
1 212 ARG n 
1 213 ASP n 
1 214 ASN n 
1 215 TRP n 
1 216 LYS n 
1 217 GLY n 
1 218 ALA n 
1 219 ASN n 
1 220 ARG n 
1 221 PRO n 
1 222 VAL n 
1 223 ILE n 
1 224 THR n 
1 225 ILE n 
1 226 ASP n 
1 227 PRO n 
1 228 GLU n 
1 229 MET n 
1 230 MET n 
1 231 THR n 
1 232 HIS n 
1 233 THR n 
1 234 SER n 
1 235 LYS n 
1 236 TYR n 
1 237 LEU n 
1 238 CYS n 
1 239 SER n 
1 240 LYS n 
1 241 VAL n 
1 242 LEU n 
1 243 THR n 
1 244 ASP n 
1 245 THR n 
1 246 SER n 
1 247 ARG n 
1 248 PRO n 
1 249 ASN n 
1 250 ASP n 
1 251 PRO n 
1 252 THR n 
1 253 ASN n 
1 254 GLY n 
1 255 ASN n 
1 256 CYS n 
1 257 ASP n 
1 258 ALA n 
1 259 PRO n 
1 260 ILE n 
1 261 THR n 
1 262 GLY n 
1 263 GLY n 
1 264 SER n 
1 265 PRO n 
1 266 ASP n 
1 267 PRO n 
1 268 GLY n 
1 269 VAL n 
1 270 LYS n 
1 271 GLY n 
1 272 PHE n 
1 273 ALA n 
1 274 PHE n 
1 275 LEU n 
1 276 ASP n 
1 277 GLY n 
1 278 GLU n 
1 279 ASN n 
1 280 SER n 
1 281 TRP n 
1 282 LEU n 
1 283 GLY n 
1 284 ARG n 
1 285 THR n 
1 286 ILE n 
1 287 SER n 
1 288 LYS n 
1 289 ASP n 
1 290 SER n 
1 291 ARG n 
1 292 SER n 
1 293 GLY n 
1 294 TYR n 
1 295 GLU n 
1 296 MET n 
1 297 LEU n 
1 298 LYS n 
1 299 VAL n 
1 300 PRO n 
1 301 ASN n 
1 302 ALA n 
1 303 GLU n 
1 304 THR n 
1 305 ASP n 
1 306 ILE n 
1 307 GLN n 
1 308 SER n 
1 309 GLY n 
1 310 PRO n 
1 311 ILE n 
1 312 SER n 
1 313 ASN n 
1 314 GLN n 
1 315 VAL n 
1 316 ILE n 
1 317 VAL n 
1 318 ASN n 
1 319 ASN n 
1 320 GLN n 
1 321 ASN n 
1 322 TRP n 
1 323 SER n 
1 324 GLY n 
1 325 TYR n 
1 326 SER n 
1 327 GLY n 
1 328 ALA n 
1 329 PHE n 
1 330 ILE n 
1 331 ASP n 
1 332 TYR n 
1 333 TRP n 
1 334 ALA n 
1 335 ASN n 
1 336 LYS n 
1 337 GLU n 
1 338 CYS n 
1 339 PHE n 
1 340 ASN n 
1 341 PRO n 
1 342 CYS n 
1 343 PHE n 
1 344 TYR n 
1 345 VAL n 
1 346 GLU n 
1 347 LEU n 
1 348 ILE n 
1 349 ARG n 
1 350 GLY n 
1 351 ARG n 
1 352 PRO n 
1 353 LYS n 
1 354 GLU n 
1 355 SER n 
1 356 SER n 
1 357 VAL n 
1 358 LEU n 
1 359 TRP n 
1 360 THR n 
1 361 SER n 
1 362 ASN n 
1 363 SER n 
1 364 ILE n 
1 365 VAL n 
1 366 ALA n 
1 367 LEU n 
1 368 CYS n 
1 369 GLY n 
1 370 SER n 
1 371 LYS n 
1 372 LYS n 
1 373 ARG n 
1 374 LEU n 
1 375 GLY n 
1 376 SER n 
1 377 TRP n 
1 378 SER n 
1 379 TRP n 
1 380 HIS n 
1 381 ASP n 
1 382 GLY n 
1 383 ALA n 
1 384 GLU n 
1 385 ILE n 
1 386 ILE n 
1 387 TYR n 
1 388 PHE n 
1 389 GLU n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      ? 
_entity_src_gen.pdbx_beg_seq_num                   ? 
_entity_src_gen.pdbx_end_seq_num                   ? 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'INFLUENZA A VIRUS' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     11320 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'GALLUS GALLUS' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     9031 
_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                    Q6XV27_9INFA 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   ? 
_struct_ref.pdbx_align_begin           ? 
_struct_ref.pdbx_db_accession          Q6XV27 
_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 1V0Z A 1 ? 389 ? Q6XV27 82 ? 470 ? 88 476 
2 1 1V0Z B 1 ? 389 ? Q6XV27 82 ? 470 ? 88 476 
3 1 1V0Z C 1 ? 389 ? Q6XV27 82 ? 470 ? 88 476 
4 1 1V0Z D 1 ? 389 ? Q6XV27 82 ? 470 ? 88 476 
# 
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 
BMA D-saccharide        . BETA-D-MANNOSE          ?                               'C6 H12 O6'      180.156 
CA  non-polymer         . 'CALCIUM ION'           ?                               'Ca 2'           40.078  
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  
GOL non-polymer         . GLYCEROL                'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'       92.094  
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 
MAN D-saccharide        . ALPHA-D-MANNOSE         ?                               'C6 H12 O6'      180.156 
MET 'L-peptide linking' y METHIONINE              ?                               'C5 H11 N O2 S'  149.211 
NAG D-saccharide        . N-ACETYL-D-GLUCOSAMINE  ?                               'C8 H15 N O6'    221.208 
PEG non-polymer         . 'DI(HYDROXYETHYL)ETHER' ?                               'C4 H10 O3'      106.120 
PHE 'L-peptide linking' y PHENYLALANINE           ?                               'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE                 ?                               'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE                  ?                               'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE               ?                               'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN              ?                               'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE                ?                               'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE                  ?                               'C5 H11 N O2'    117.146 
# 
_exptl.entry_id          1V0Z 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.48 
_exptl_crystal.density_percent_sol   50.48 
_exptl_crystal.description           ? 
_exptl_crystal.preparation           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          ? 
_exptl_crystal_grow.temp            ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.pdbx_details    '20 PERCENT (W/V) PEG 3350, 150 MM NACL' 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100.0 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               'IMAGE PLATE' 
_diffrn_detector.type                   MARRESEARCH 
_diffrn_detector.pdbx_collection_date   1995-11-24 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.488 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'SRS BEAMLINE PX7.2' 
_diffrn_source.pdbx_synchrotron_site       SRS 
_diffrn_source.pdbx_synchrotron_beamline   PX7.2 
_diffrn_source.pdbx_wavelength             1.488 
_diffrn_source.pdbx_wavelength_list        ? 
# 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.entry_id                     1V0Z 
_reflns.observed_criterion_sigma_I   0.000 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             19.960 
_reflns.d_resolution_high            1.840 
_reflns.number_obs                   127094 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         100.0 
_reflns.pdbx_Rmerge_I_obs            0.07000 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        7.8000 
_reflns.B_iso_Wilson_estimate        18.10 
_reflns.pdbx_redundancy              6.700 
_reflns.pdbx_CC_half                 ? 
_reflns.pdbx_Rpim_I_all              ? 
_reflns.pdbx_Rrim_I_all              ? 
# 
_reflns_shell.pdbx_diffrn_id         1 
_reflns_shell.pdbx_ordinal           1 
_reflns_shell.d_res_high             1.84 
_reflns_shell.d_res_low              1.89 
_reflns_shell.percent_possible_all   100.0 
_reflns_shell.Rmerge_I_obs           0.16000 
_reflns_shell.pdbx_Rsym_value        ? 
_reflns_shell.meanI_over_sigI_obs    3.400 
_reflns_shell.pdbx_redundancy        2.10 
_reflns_shell.number_measured_obs    ? 
_reflns_shell.number_unique_all      ? 
_reflns_shell.number_unique_obs      ? 
_reflns_shell.pdbx_CC_half           ? 
_reflns_shell.pdbx_Rpim_I_all        ? 
_reflns_shell.pdbx_Rrim_I_all        ? 
# 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.entry_id                                 1V0Z 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     127094 
_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                             19.96 
_refine.ls_d_res_high                            1.84 
_refine.ls_percent_reflns_obs                    100.0 
_refine.ls_R_factor_obs                          0.151 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.149 
_refine.ls_R_factor_R_free                       0.190 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.000 
_refine.ls_number_reflns_R_free                  6696 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.963 
_refine.correlation_coeff_Fo_to_Fc_free          0.942 
_refine.B_iso_mean                               15.07 
_refine.aniso_B[1][1]                            -1.02000 
_refine.aniso_B[2][2]                            2.34000 
_refine.aniso_B[3][3]                            -1.31000 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            0.04000 
_refine.aniso_B[2][3]                            0.00000 
_refine.solvent_model_details                    'BABINET MODEL WITH 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                                  ? 
_refine.pdbx_starting_model                      'PDB ENTRY 1NNA' 
_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                       0.126 
_refine.pdbx_overall_ESU_R_Free                  0.119 
_refine.overall_SU_ML                            0.072 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             2.321 
_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        12036 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         513 
_refine_hist.number_atoms_solvent             1798 
_refine_hist.number_atoms_total               14347 
_refine_hist.d_res_high                       1.84 
_refine_hist.d_res_low                        19.96 
# 
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             0.013  0.021  ? 12862 'X-RAY DIFFRACTION' ? 
r_bond_other_d               ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          1.428  1.975  ? 17494 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       7.180  5.000  ? 1552  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       34.186 23.913 ? 552   'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       12.534 15.000 ? 2004  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       16.132 15.000 ? 84    'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.101  0.200  ? 1938  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.005  0.020  ? 9604  'X-RAY DIFFRACTION' ? 
r_gen_planes_other           ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_nbd_refined                0.215  0.200  ? 6209  'X-RAY DIFFRACTION' ? 
r_nbd_other                  ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_nbtor_refined              0.306  0.200  ? 8618  'X-RAY DIFFRACTION' ? 
r_nbtor_other                ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_refined        0.142  0.200  ? 1482  '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       0.188  0.200  ? 46    'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_other         ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_refined     0.145  0.200  ? 35    '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                  0.656  1.500  ? 7996  'X-RAY DIFFRACTION' ? 
r_mcbond_other               ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_mcangle_it                 1.038  2.000  ? 12480 'X-RAY DIFFRACTION' ? 
r_mcangle_other              ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_scbond_it                  1.828  3.000  ? 5671  'X-RAY DIFFRACTION' ? 
r_scbond_other               ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_scangle_it                 2.840  4.500  ? 5014  '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                       1.84 
_refine_ls_shell.d_res_low                        1.89 
_refine_ls_shell.number_reflns_R_work             8240 
_refine_ls_shell.R_factor_R_work                  0.1950 
_refine_ls_shell.percent_reflns_obs               ? 
_refine_ls_shell.R_factor_R_free                  0.2570 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             429 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.number_reflns_obs                ? 
# 
_struct.entry_id                  1V0Z 
_struct.title                     'Structure of Neuraminidase from English duck subtype N6' 
_struct.pdbx_descriptor           'NEURAMINIDASE (E.C.3.2.1.18)' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        1V0Z 
_struct_keywords.pdbx_keywords   HYDROLASE 
_struct_keywords.text            'GLYCOSIDASE, HYDROLASE' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A  N N 1 ? 
B  N N 1 ? 
C  N N 1 ? 
D  N N 1 ? 
E  N N 2 ? 
F  N N 3 ? 
G  N N 4 ? 
H  N N 4 ? 
I  N N 4 ? 
J  N N 4 ? 
K  N N 5 ? 
L  N N 6 ? 
M  N N 5 ? 
N  N N 4 ? 
O  N N 5 ? 
P  N N 5 ? 
Q  N N 4 ? 
R  N N 5 ? 
S  N N 4 ? 
T  N N 4 ? 
U  N N 6 ? 
V  N N 5 ? 
W  N N 5 ? 
X  N N 5 ? 
Y  N N 5 ? 
Z  N N 2 ? 
AA N N 3 ? 
BA N N 4 ? 
CA N N 4 ? 
DA N N 5 ? 
EA N N 6 ? 
FA N N 4 ? 
GA N N 5 ? 
HA N N 5 ? 
IA N N 4 ? 
JA N N 2 ? 
KA N N 7 ? 
LA N N 3 ? 
MA N N 4 ? 
NA N N 4 ? 
OA N N 4 ? 
PA N N 4 ? 
QA N N 4 ? 
RA N N 6 ? 
SA N N 5 ? 
TA N N 2 ? 
UA N N 3 ? 
VA N N 4 ? 
WA N N 4 ? 
XA N N 4 ? 
YA N N 5 ? 
ZA N N 8 ? 
AB N N 8 ? 
BB N N 8 ? 
CB N N 8 ? 
# 
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  ASN A 23  ? GLU A 29  ? ASN A 110 GLU A 116 1 ? 7 
HELX_P HELX_P2  2  GLY A 61  ? ASN A 65  ? GLY A 148 ASN A 152 5 ? 5 
HELX_P HELX_P3  3  PRO A 117 ? ASN A 120 ? PRO A 204 ASN A 207 5 ? 4 
HELX_P HELX_P4  4  GLU A 384 ? GLU A 389 ? GLU A 471 GLU A 476 5 ? 6 
HELX_P HELX_P5  5  ASN B 23  ? GLU B 29  ? ASN B 110 GLU B 116 1 ? 7 
HELX_P HELX_P6  6  GLY B 61  ? ASN B 65  ? GLY B 148 ASN B 152 5 ? 5 
HELX_P HELX_P7  7  PRO B 117 ? ASN B 120 ? PRO B 204 ASN B 207 5 ? 4 
HELX_P HELX_P8  8  GLU B 384 ? GLU B 389 ? GLU B 471 GLU B 476 5 ? 6 
HELX_P HELX_P9  9  ASN C 23  ? GLU C 29  ? ASN C 110 GLU C 116 1 ? 7 
HELX_P HELX_P10 10 GLY C 61  ? ASN C 65  ? GLY C 148 ASN C 152 5 ? 5 
HELX_P HELX_P11 11 GLU C 384 ? GLU C 389 ? GLU C 471 GLU C 476 5 ? 6 
HELX_P HELX_P12 12 ASN D 23  ? GLU D 29  ? ASN D 110 GLU D 116 1 ? 7 
HELX_P HELX_P13 13 GLY D 61  ? ASN D 65  ? GLY D 148 ASN D 152 5 ? 5 
HELX_P HELX_P14 14 GLU D 384 ? GLU D 389 ? GLU D 471 GLU D 476 5 ? 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 11  SG  ? ? ? 1_555 A  CYS 338 SG ? ? A CYS 98  A CYS 425  1_555 ? ? ? ? ? ? ? 2.064 ? 
disulf2  disulf ?    ? A  CYS 43  SG  ? ? ? 1_555 A  CYS 48  SG ? ? A CYS 130 A CYS 135  1_555 ? ? ? ? ? ? ? 2.028 ? 
disulf3  disulf ?    ? A  CYS 95  SG  ? ? ? 1_555 A  CYS 113 SG ? ? A CYS 182 A CYS 200  1_555 ? ? ? ? ? ? ? 2.041 ? 
disulf4  disulf ?    ? A  CYS 103 SG  ? ? ? 1_555 A  CYS 150 SG ? ? A CYS 190 A CYS 237  1_555 ? ? ? ? ? ? ? 2.036 ? 
disulf5  disulf ?    ? A  CYS 152 SG  ? ? ? 1_555 A  CYS 157 SG ? ? A CYS 239 A CYS 244  1_555 ? ? ? ? ? ? ? 2.049 ? 
disulf6  disulf ?    ? A  CYS 198 SG  ? ? ? 1_555 A  CYS 211 SG ? ? A CYS 285 A CYS 298  1_555 ? ? ? ? ? ? ? 2.094 ? 
disulf7  disulf ?    ? A  CYS 200 SG  ? ? ? 1_555 A  CYS 209 SG ? ? A CYS 287 A CYS 296  1_555 ? ? ? ? ? ? ? 2.067 ? 
disulf8  disulf ?    ? A  CYS 238 SG  ? ? ? 1_555 A  CYS 256 SG ? ? A CYS 325 A CYS 343  1_555 ? ? ? ? ? ? ? 2.051 ? 
disulf9  disulf ?    ? A  CYS 342 SG  ? ? ? 1_555 A  CYS 368 SG ? ? A CYS 429 A CYS 455  1_555 ? ? ? ? ? ? ? 2.055 ? 
disulf10 disulf ?    ? B  CYS 11  SG  ? ? ? 1_555 B  CYS 338 SG ? ? B CYS 98  B CYS 425  1_555 ? ? ? ? ? ? ? 2.055 ? 
disulf11 disulf ?    ? B  CYS 43  SG  ? ? ? 1_555 B  CYS 48  SG ? ? B CYS 130 B CYS 135  1_555 ? ? ? ? ? ? ? 2.027 ? 
disulf12 disulf ?    ? B  CYS 95  SG  ? ? ? 1_555 B  CYS 113 SG ? ? B CYS 182 B CYS 200  1_555 ? ? ? ? ? ? ? 2.048 ? 
disulf13 disulf ?    ? B  CYS 103 SG  ? ? ? 1_555 B  CYS 150 SG ? ? B CYS 190 B CYS 237  1_555 ? ? ? ? ? ? ? 2.036 ? 
disulf14 disulf ?    ? B  CYS 152 SG  ? ? ? 1_555 B  CYS 157 SG ? ? B CYS 239 B CYS 244  1_555 ? ? ? ? ? ? ? 2.039 ? 
disulf15 disulf ?    ? B  CYS 198 SG  ? ? ? 1_555 B  CYS 211 SG ? ? B CYS 285 B CYS 298  1_555 ? ? ? ? ? ? ? 2.081 ? 
disulf16 disulf ?    ? B  CYS 200 SG  ? ? ? 1_555 B  CYS 209 SG ? ? B CYS 287 B CYS 296  1_555 ? ? ? ? ? ? ? 2.047 ? 
disulf17 disulf ?    ? B  CYS 238 SG  ? ? ? 1_555 B  CYS 256 SG ? ? B CYS 325 B CYS 343  1_555 ? ? ? ? ? ? ? 2.039 ? 
disulf18 disulf ?    ? B  CYS 342 SG  ? ? ? 1_555 B  CYS 368 SG ? ? B CYS 429 B CYS 455  1_555 ? ? ? ? ? ? ? 2.049 ? 
disulf19 disulf ?    ? C  CYS 11  SG  ? ? ? 1_555 C  CYS 338 SG ? ? C CYS 98  C CYS 425  1_555 ? ? ? ? ? ? ? 2.064 ? 
disulf20 disulf ?    ? C  CYS 43  SG  ? ? ? 1_555 C  CYS 48  SG ? ? C CYS 130 C CYS 135  1_555 ? ? ? ? ? ? ? 2.038 ? 
disulf21 disulf ?    ? C  CYS 95  SG  ? ? ? 1_555 C  CYS 113 SG ? ? C CYS 182 C CYS 200  1_555 ? ? ? ? ? ? ? 2.066 ? 
disulf22 disulf ?    ? C  CYS 103 SG  ? ? ? 1_555 C  CYS 150 SG ? ? C CYS 190 C CYS 237  1_555 ? ? ? ? ? ? ? 2.032 ? 
disulf23 disulf ?    ? C  CYS 152 SG  ? ? ? 1_555 C  CYS 157 SG ? ? C CYS 239 C CYS 244  1_555 ? ? ? ? ? ? ? 2.027 ? 
disulf24 disulf ?    ? C  CYS 198 SG  ? ? ? 1_555 C  CYS 211 SG ? ? C CYS 285 C CYS 298  1_555 ? ? ? ? ? ? ? 2.071 ? 
disulf25 disulf ?    ? C  CYS 200 SG  ? ? ? 1_555 C  CYS 209 SG ? ? C CYS 287 C CYS 296  1_555 ? ? ? ? ? ? ? 2.063 ? 
disulf26 disulf ?    ? C  CYS 238 SG  ? ? ? 1_555 C  CYS 256 SG ? ? C CYS 325 C CYS 343  1_555 ? ? ? ? ? ? ? 2.041 ? 
disulf27 disulf ?    ? C  CYS 342 SG  ? ? ? 1_555 C  CYS 368 SG ? ? C CYS 429 C CYS 455  1_555 ? ? ? ? ? ? ? 2.039 ? 
disulf28 disulf ?    ? D  CYS 11  SG  ? ? ? 1_555 D  CYS 338 SG ? ? D CYS 98  D CYS 425  1_555 ? ? ? ? ? ? ? 2.054 ? 
disulf29 disulf ?    ? D  CYS 43  SG  ? ? ? 1_555 D  CYS 48  SG ? ? D CYS 130 D CYS 135  1_555 ? ? ? ? ? ? ? 2.039 ? 
disulf30 disulf ?    ? D  CYS 95  SG  ? ? ? 1_555 D  CYS 113 SG ? ? D CYS 182 D CYS 200  1_555 ? ? ? ? ? ? ? 2.033 ? 
disulf31 disulf ?    ? D  CYS 103 SG  ? ? ? 1_555 D  CYS 150 SG ? ? D CYS 190 D CYS 237  1_555 ? ? ? ? ? ? ? 2.040 ? 
disulf32 disulf ?    ? D  CYS 152 SG  ? ? ? 1_555 D  CYS 157 SG ? ? D CYS 239 D CYS 244  1_555 ? ? ? ? ? ? ? 2.033 ? 
disulf33 disulf ?    ? D  CYS 198 SG  ? ? ? 1_555 D  CYS 211 SG ? ? D CYS 285 D CYS 298  1_555 ? ? ? ? ? ? ? 2.087 ? 
disulf34 disulf ?    ? D  CYS 200 SG  ? ? ? 1_555 D  CYS 209 SG ? ? D CYS 287 D CYS 296  1_555 ? ? ? ? ? ? ? 2.045 ? 
disulf35 disulf ?    ? D  CYS 238 SG  ? ? ? 1_555 D  CYS 256 SG ? ? D CYS 325 D CYS 343  1_555 ? ? ? ? ? ? ? 2.041 ? 
disulf36 disulf ?    ? D  CYS 342 SG  ? ? ? 1_555 D  CYS 368 SG ? ? D CYS 429 D CYS 455  1_555 ? ? ? ? ? ? ? 2.031 ? 
covale1  covale one  ? A  ASN 5   ND2 ? ? ? 1_555 G  NAG .   C1 ? ? A ASN 92  A NAG 503  1_555 ? ? ? ? ? ? ? 1.436 ? 
covale2  covale one  ? A  ASN 65  ND2 ? ? ? 1_555 I  NAG .   C1 ? ? A ASN 152 A NAG 505  1_555 ? ? ? ? ? ? ? 1.441 ? 
covale3  covale one  ? A  ASN 120 ND2 ? ? ? 1_555 S  NAG .   C1 ? ? A ASN 207 A NAG 515  1_555 ? ? ? ? ? ? ? 1.450 ? 
metalc1  metalc ?    ? A  ASP 213 O   ? ? ? 1_555 E  CA  .   CA ? ? A ASP 300 A CA  501  1_555 ? ? ? ? ? ? ? 2.349 ? 
metalc2  metalc ?    ? A  GLY 217 O   ? ? ? 1_555 E  CA  .   CA ? ? A GLY 304 A CA  501  1_555 ? ? ? ? ? ? ? 2.437 ? 
metalc3  metalc ?    ? A  ASP 244 OD2 ? ? ? 1_555 E  CA  .   CA ? ? A ASP 331 A CA  501  1_555 ? ? ? ? ? ? ? 2.394 ? 
metalc4  metalc ?    ? A  PRO 267 O   ? ? ? 1_555 E  CA  .   CA ? ? A PRO 354 A CA  501  1_555 ? ? ? ? ? ? ? 2.458 ? 
metalc5  metalc ?    ? B  ASP 213 O   ? ? ? 1_555 Z  CA  .   CA ? ? B ASP 300 B CA  501  1_555 ? ? ? ? ? ? ? 2.326 ? 
metalc6  metalc ?    ? B  GLY 217 O   ? ? ? 1_555 Z  CA  .   CA ? ? B GLY 304 B CA  501  1_555 ? ? ? ? ? ? ? 2.412 ? 
metalc7  metalc ?    ? B  ASP 244 OD2 ? ? ? 1_555 Z  CA  .   CA ? ? B ASP 331 B CA  501  1_555 ? ? ? ? ? ? ? 2.446 ? 
metalc8  metalc ?    ? B  PRO 267 O   ? ? ? 1_555 Z  CA  .   CA ? ? B PRO 354 B CA  501  1_555 ? ? ? ? ? ? ? 2.497 ? 
metalc9  metalc ?    ? C  ASP 213 O   ? ? ? 1_555 JA CA  .   CA ? ? C ASP 300 C CA  502  1_555 ? ? ? ? ? ? ? 2.305 ? 
metalc10 metalc ?    ? C  GLY 217 O   ? ? ? 1_555 JA CA  .   CA ? ? C GLY 304 C CA  502  1_555 ? ? ? ? ? ? ? 2.307 ? 
metalc11 metalc ?    ? C  ASP 244 OD2 ? ? ? 1_555 JA CA  .   CA ? ? C ASP 331 C CA  502  1_555 ? ? ? ? ? ? ? 2.454 ? 
metalc12 metalc ?    ? C  PRO 267 O   ? ? ? 1_555 JA CA  .   CA ? ? C PRO 354 C CA  502  1_555 ? ? ? ? ? ? ? 2.576 ? 
metalc13 metalc ?    ? D  ASP 213 O   ? ? ? 1_555 TA CA  .   CA ? ? D ASP 300 D CA  504  1_555 ? ? ? ? ? ? ? 2.335 ? 
metalc14 metalc ?    ? D  GLY 217 O   ? ? ? 1_555 TA CA  .   CA ? ? D GLY 304 D CA  504  1_555 ? ? ? ? ? ? ? 2.361 ? 
metalc15 metalc ?    ? D  ASP 244 OD2 ? ? ? 1_555 TA CA  .   CA ? ? D ASP 331 D CA  504  1_555 ? ? ? ? ? ? ? 2.486 ? 
metalc16 metalc ?    ? D  PRO 267 O   ? ? ? 1_555 TA CA  .   CA ? ? D PRO 354 D CA  504  1_555 ? ? ? ? ? ? ? 2.354 ? 
metalc17 metalc ?    ? E  CA  .   CA  ? ? ? 1_555 ZA HOH .   O  ? ? A CA  501 A HOH 2420 1_555 ? ? ? ? ? ? ? 2.338 ? 
metalc18 metalc ?    ? E  CA  .   CA  ? ? ? 1_555 ZA HOH .   O  ? ? A CA  501 A HOH 2519 1_555 ? ? ? ? ? ? ? 3.014 ? 
covale4  covale both ? G  NAG .   O4  ? ? ? 1_555 H  NAG .   C1 ? ? A NAG 503 A NAG 504  1_555 ? ? ? ? ? ? ? 1.436 ? 
covale5  covale one  ? K  MAN .   C1  ? ? ? 1_555 L  BMA .   O6 ? ? A MAN 507 A BMA 510  1_555 ? ? ? ? ? ? ? 1.342 ? 
covale6  covale both ? L  BMA .   C1  ? ? ? 1_555 N  NAG .   O4 ? ? A BMA 510 A NAG 512  1_555 ? ? ? ? ? ? ? 1.444 ? 
covale7  covale one  ? L  BMA .   O3  ? ? ? 1_555 M  MAN .   C1 ? ? A BMA 510 A MAN 511  1_555 ? ? ? ? ? ? ? 1.337 ? 
covale8  covale both ? S  NAG .   O4  ? ? ? 1_555 T  NAG .   C1 ? ? A NAG 515 A NAG 516  1_555 ? ? ? ? ? ? ? 1.440 ? 
covale9  covale both ? T  NAG .   O4  ? ? ? 1_555 U  BMA .   C1 ? ? A NAG 516 A BMA 517  1_555 ? ? ? ? ? ? ? 1.438 ? 
covale10 covale one  ? U  BMA .   O3  ? ? ? 1_555 V  MAN .   C1 ? ? A BMA 517 A MAN 518  1_555 ? ? ? ? ? ? ? 1.344 ? 
covale11 covale one  ? U  BMA .   O6  ? ? ? 1_555 X  MAN .   C1 ? ? A BMA 517 A MAN 520  1_555 ? ? ? ? ? ? ? 1.337 ? 
covale12 covale one  ? V  MAN .   O2  ? ? ? 1_555 W  MAN .   C1 ? ? A MAN 518 A MAN 519  1_555 ? ? ? ? ? ? ? 1.330 ? 
metalc19 metalc ?    ? Z  CA  .   CA  ? ? ? 1_555 AB HOH .   O  ? ? B CA  501 B HOH 763  1_555 ? ? ? ? ? ? ? 2.657 ? 
metalc20 metalc ?    ? Z  CA  .   CA  ? ? ? 1_555 AB HOH .   O  ? ? B CA  501 B HOH 738  1_555 ? ? ? ? ? ? ? 2.301 ? 
covale13 covale one  ? DA MAN .   C1  ? ? ? 1_555 EA BMA .   O6 ? ? B MAN 505 B BMA 507  1_555 ? ? ? ? ? ? ? 1.335 ? 
covale14 covale both ? EA BMA .   C1  ? ? ? 1_555 FA NAG .   O4 ? ? B BMA 507 B NAG 508  1_555 ? ? ? ? ? ? ? 1.425 ? 
metalc21 metalc ?    ? JA CA  .   CA  ? ? ? 1_555 BB HOH .   O  ? ? C CA  502 C HOH 684  1_555 ? ? ? ? ? ? ? 2.371 ? 
metalc22 metalc ?    ? JA CA  .   CA  ? ? ? 1_555 BB HOH .   O  ? ? C CA  502 C HOH 745  1_555 ? ? ? ? ? ? ? 3.012 ? 
covale15 covale both ? OA NAG .   O4  ? ? ? 1_555 PA NAG .   C1 ? ? C NAG 507 C NAG 508  1_555 ? ? ? ? ? ? ? 1.423 ? 
covale16 covale one  ? RA BMA .   O6  ? ? ? 1_555 SA MAN .   C1 ? ? D BMA 502 D MAN 503  1_555 ? ? ? ? ? ? ? 1.342 ? 
metalc23 metalc ?    ? TA CA  .   CA  ? ? ? 1_555 CB HOH .   O  ? ? D CA  504 D HOH 720  1_555 ? ? ? ? ? ? ? 2.798 ? 
metalc24 metalc ?    ? TA CA  .   CA  ? ? ? 1_555 CB HOH .   O  ? ? D CA  504 D HOH 654  1_555 ? ? ? ? ? ? ? 2.394 ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
metalc ? ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1  THR 245 A . ? THR 332 A SER 246 A ? SER 333 A 1 6.50  
2  SER 264 A . ? SER 351 A PRO 265 A ? PRO 352 A 1 1.51  
3  ARG 351 A . ? ARG 438 A PRO 352 A ? PRO 439 A 1 -1.15 
4  THR 245 B . ? THR 332 B SER 246 B ? SER 333 B 1 3.42  
5  SER 264 B . ? SER 351 B PRO 265 B ? PRO 352 B 1 -0.54 
6  ARG 351 B . ? ARG 438 B PRO 352 B ? PRO 439 B 1 1.95  
7  THR 245 C . ? THR 332 C SER 246 C ? SER 333 C 1 4.50  
8  SER 264 C . ? SER 351 C PRO 265 C ? PRO 352 C 1 3.82  
9  ARG 351 C . ? ARG 438 C PRO 352 C ? PRO 439 C 1 0.56  
10 THR 245 D . ? THR 332 D SER 246 D ? SER 333 D 1 3.35  
11 SER 264 D . ? SER 351 D PRO 265 D ? PRO 352 D 1 4.21  
12 ARG 351 D . ? ARG 438 D PRO 352 D ? PRO 439 D 1 -0.50 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA ? 4 ? 
AB ? 4 ? 
AC ? 4 ? 
AD ? 3 ? 
AE ? 4 ? 
AF ? 4 ? 
BA ? 4 ? 
BB ? 4 ? 
BC ? 4 ? 
BD ? 3 ? 
BE ? 4 ? 
BF ? 4 ? 
CA ? 4 ? 
CB ? 4 ? 
CC ? 4 ? 
CD ? 3 ? 
CE ? 4 ? 
CF ? 4 ? 
DA ? 4 ? 
DB ? 4 ? 
DC ? 4 ? 
DD ? 3 ? 
DE ? 4 ? 
DF ? 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 
AB 1 2 ? anti-parallel 
AB 2 3 ? anti-parallel 
AB 3 4 ? anti-parallel 
AC 1 2 ? anti-parallel 
AC 2 3 ? anti-parallel 
AC 3 4 ? anti-parallel 
AD 1 2 ? anti-parallel 
AD 2 3 ? anti-parallel 
AE 1 2 ? anti-parallel 
AE 2 3 ? anti-parallel 
AE 3 4 ? anti-parallel 
AF 1 2 ? anti-parallel 
AF 2 3 ? anti-parallel 
AF 3 4 ? anti-parallel 
BA 1 2 ? anti-parallel 
BA 2 3 ? anti-parallel 
BA 3 4 ? anti-parallel 
BB 1 2 ? anti-parallel 
BB 2 3 ? anti-parallel 
BB 3 4 ? anti-parallel 
BC 1 2 ? anti-parallel 
BC 2 3 ? anti-parallel 
BC 3 4 ? anti-parallel 
BD 1 2 ? anti-parallel 
BD 2 3 ? anti-parallel 
BE 1 2 ? anti-parallel 
BE 2 3 ? anti-parallel 
BE 3 4 ? anti-parallel 
BF 1 2 ? anti-parallel 
BF 2 3 ? anti-parallel 
BF 3 4 ? anti-parallel 
CA 1 2 ? anti-parallel 
CA 2 3 ? anti-parallel 
CA 3 4 ? anti-parallel 
CB 1 2 ? anti-parallel 
CB 2 3 ? anti-parallel 
CB 3 4 ? anti-parallel 
CC 1 2 ? anti-parallel 
CC 2 3 ? anti-parallel 
CC 3 4 ? anti-parallel 
CD 1 2 ? anti-parallel 
CD 2 3 ? anti-parallel 
CE 1 2 ? anti-parallel 
CE 2 3 ? anti-parallel 
CE 3 4 ? anti-parallel 
CF 1 2 ? anti-parallel 
CF 2 3 ? anti-parallel 
CF 3 4 ? anti-parallel 
DA 1 2 ? anti-parallel 
DA 2 3 ? anti-parallel 
DA 3 4 ? anti-parallel 
DB 1 2 ? anti-parallel 
DB 2 3 ? anti-parallel 
DB 3 4 ? anti-parallel 
DC 1 2 ? anti-parallel 
DC 2 3 ? anti-parallel 
DC 3 4 ? anti-parallel 
DD 1 2 ? anti-parallel 
DD 2 3 ? anti-parallel 
DE 1 2 ? anti-parallel 
DE 2 3 ? anti-parallel 
DE 3 4 ? anti-parallel 
DF 1 2 ? anti-parallel 
DF 2 3 ? anti-parallel 
DF 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 SER A 15  ? LYS A 21  ? SER A 102 LYS A 108 
AA 2 THR A 360 ? SER A 370 ? THR A 447 SER A 457 
AA 3 PRO A 341 ? GLY A 350 ? PRO A 428 GLY A 437 
AA 4 SER A 326 ? ILE A 330 ? SER A 413 ILE A 417 
AB 1 LEU A 34  ? ASP A 44  ? LEU A 121 ASP A 131 
AB 2 GLY A 47  ? THR A 58  ? GLY A 134 THR A 145 
AB 3 ALA A 76  ? GLU A 81  ? ALA A 163 GLU A 168 
AB 4 ARG A 92  ? ILE A 96  ? ARG A 179 ILE A 183 
AC 1 SER A 99  ? HIS A 104 ? SER A 186 HIS A 191 
AC 2 ARG A 109 ? SER A 115 ? ARG A 196 SER A 202 
AC 3 SER A 122 ? TYR A 127 ? SER A 209 TYR A 214 
AC 4 ARG A 130 ? PRO A 136 ? ARG A 217 PRO A 223 
AD 1 CYS A 157 ? ASP A 163 ? CYS A 244 ASP A 250 
AD 2 ALA A 171 ? LYS A 178 ? ALA A 258 LYS A 265 
AD 3 LYS A 181 ? GLU A 187 ? LYS A 268 GLU A 274 
AE 1 GLU A 196 ? ALA A 203 ? GLU A 283 ALA A 290 
AE 2 VAL A 206 ? ARG A 212 ? VAL A 293 ARG A 299 
AE 3 PRO A 221 ? ASP A 226 ? PRO A 308 ASP A 313 
AE 4 THR A 231 ? TYR A 236 ? THR A 318 TYR A 323 
AF 1 ALA A 273 ? PHE A 274 ? ALA A 360 PHE A 361 
AF 2 TRP A 281 ? ARG A 284 ? TRP A 368 ARG A 371 
AF 3 SER A 292 ? LYS A 298 ? SER A 379 LYS A 385 
AF 4 SER A 312 ? TRP A 322 ? SER A 399 TRP A 409 
BA 1 SER B 15  ? LYS B 21  ? SER B 102 LYS B 108 
BA 2 THR B 360 ? SER B 370 ? THR B 447 SER B 457 
BA 3 PRO B 341 ? GLY B 350 ? PRO B 428 GLY B 437 
BA 4 SER B 326 ? ILE B 330 ? SER B 413 ILE B 417 
BB 1 LEU B 34  ? CYS B 43  ? LEU B 121 CYS B 130 
BB 2 CYS B 48  ? THR B 58  ? CYS B 135 THR B 145 
BB 3 ALA B 76  ? GLU B 81  ? ALA B 163 GLU B 168 
BB 4 ARG B 92  ? ILE B 96  ? ARG B 179 ILE B 183 
BC 1 SER B 99  ? HIS B 104 ? SER B 186 HIS B 191 
BC 2 ARG B 109 ? SER B 115 ? ARG B 196 SER B 202 
BC 3 SER B 122 ? TYR B 127 ? SER B 209 TYR B 214 
BC 4 ARG B 130 ? PRO B 136 ? ARG B 217 PRO B 223 
BD 1 CYS B 157 ? ASP B 163 ? CYS B 244 ASP B 250 
BD 2 ALA B 171 ? LYS B 178 ? ALA B 258 LYS B 265 
BD 3 LYS B 181 ? GLU B 187 ? LYS B 268 GLU B 274 
BE 1 GLU B 196 ? ALA B 203 ? GLU B 283 ALA B 290 
BE 2 VAL B 206 ? ARG B 212 ? VAL B 293 ARG B 299 
BE 3 PRO B 221 ? ASP B 226 ? PRO B 308 ASP B 313 
BE 4 THR B 231 ? TYR B 236 ? THR B 318 TYR B 323 
BF 1 ALA B 273 ? PHE B 274 ? ALA B 360 PHE B 361 
BF 2 TRP B 281 ? ARG B 284 ? TRP B 368 ARG B 371 
BF 3 SER B 292 ? LYS B 298 ? SER B 379 LYS B 385 
BF 4 SER B 312 ? TRP B 322 ? SER B 399 TRP B 409 
CA 1 SER C 15  ? LYS C 21  ? SER C 102 LYS C 108 
CA 2 THR C 360 ? SER C 370 ? THR C 447 SER C 457 
CA 3 PRO C 341 ? GLY C 350 ? PRO C 428 GLY C 437 
CA 4 SER C 326 ? ILE C 330 ? SER C 413 ILE C 417 
CB 1 LEU C 34  ? ASP C 44  ? LEU C 121 ASP C 131 
CB 2 GLY C 47  ? THR C 58  ? GLY C 134 THR C 145 
CB 3 ALA C 76  ? GLU C 81  ? ALA C 163 GLU C 168 
CB 4 ARG C 92  ? ILE C 96  ? ARG C 179 ILE C 183 
CC 1 SER C 99  ? HIS C 104 ? SER C 186 HIS C 191 
CC 2 ARG C 109 ? SER C 115 ? ARG C 196 SER C 202 
CC 3 SER C 122 ? TYR C 127 ? SER C 209 TYR C 214 
CC 4 ARG C 130 ? PRO C 136 ? ARG C 217 PRO C 223 
CD 1 CYS C 157 ? ASP C 163 ? CYS C 244 ASP C 250 
CD 2 ALA C 171 ? LYS C 178 ? ALA C 258 LYS C 265 
CD 3 LYS C 181 ? GLU C 187 ? LYS C 268 GLU C 274 
CE 1 GLU C 196 ? ALA C 203 ? GLU C 283 ALA C 290 
CE 2 VAL C 206 ? ARG C 212 ? VAL C 293 ARG C 299 
CE 3 PRO C 221 ? ASP C 226 ? PRO C 308 ASP C 313 
CE 4 THR C 231 ? TYR C 236 ? THR C 318 TYR C 323 
CF 1 ALA C 273 ? PHE C 274 ? ALA C 360 PHE C 361 
CF 2 TRP C 281 ? ARG C 284 ? TRP C 368 ARG C 371 
CF 3 SER C 292 ? LYS C 298 ? SER C 379 LYS C 385 
CF 4 SER C 312 ? TRP C 322 ? SER C 399 TRP C 409 
DA 1 SER D 15  ? LYS D 21  ? SER D 102 LYS D 108 
DA 2 THR D 360 ? SER D 370 ? THR D 447 SER D 457 
DA 3 PRO D 341 ? GLY D 350 ? PRO D 428 GLY D 437 
DA 4 SER D 326 ? ILE D 330 ? SER D 413 ILE D 417 
DB 1 LEU D 34  ? ASP D 44  ? LEU D 121 ASP D 131 
DB 2 GLY D 47  ? THR D 58  ? GLY D 134 THR D 145 
DB 3 ALA D 76  ? GLU D 81  ? ALA D 163 GLU D 168 
DB 4 ARG D 92  ? ILE D 96  ? ARG D 179 ILE D 183 
DC 1 SER D 99  ? HIS D 104 ? SER D 186 HIS D 191 
DC 2 ARG D 109 ? SER D 115 ? ARG D 196 SER D 202 
DC 3 SER D 122 ? TYR D 127 ? SER D 209 TYR D 214 
DC 4 ARG D 130 ? PRO D 136 ? ARG D 217 PRO D 223 
DD 1 CYS D 157 ? ASP D 163 ? CYS D 244 ASP D 250 
DD 2 ALA D 171 ? LYS D 178 ? ALA D 258 LYS D 265 
DD 3 LYS D 181 ? GLU D 187 ? LYS D 268 GLU D 274 
DE 1 GLU D 196 ? ALA D 203 ? GLU D 283 ALA D 290 
DE 2 VAL D 206 ? ARG D 212 ? VAL D 293 ARG D 299 
DE 3 PRO D 221 ? ASP D 226 ? PRO D 308 ASP D 313 
DE 4 THR D 231 ? TYR D 236 ? THR D 318 TYR D 323 
DF 1 ALA D 273 ? PHE D 274 ? ALA D 360 PHE D 361 
DF 2 TRP D 281 ? ARG D 284 ? TRP D 368 ARG D 371 
DF 3 SER D 292 ? LYS D 298 ? SER D 379 LYS D 385 
DF 4 SER D 312 ? TRP D 322 ? SER D 399 TRP D 409 
# 
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 LEU A 19  ? N LEU A 106 O ALA A 366 ? O ALA A 453 
AA 2 3 N GLY A 369 ? N GLY A 456 O PRO A 341 ? O PRO A 428 
AA 3 4 N TYR A 344 ? N TYR A 431 O GLY A 327 ? O GLY A 414 
AB 1 2 N ASP A 44  ? N ASP A 131 O GLY A 47  ? O GLY A 134 
AB 2 3 N SER A 54  ? N SER A 141 O ALA A 76  ? O ALA A 163 
AB 3 4 N SER A 79  ? N SER A 166 O ARG A 92  ? O ARG A 179 
AC 1 2 N CYS A 103 ? N CYS A 190 O MET A 110 ? O MET A 197 
AC 2 3 N SER A 115 ? N SER A 202 O SER A 122 ? O SER A 209 
AC 3 4 N TYR A 127 ? N TYR A 214 O ARG A 130 ? O ARG A 217 
AD 1 2 N ASP A 163 ? N ASP A 250 O ALA A 171 ? O ALA A 258 
AD 2 3 N LYS A 178 ? N LYS A 265 O LYS A 181 ? O LYS A 268 
AE 1 2 N ALA A 203 ? N ALA A 290 O VAL A 206 ? O VAL A 293 
AE 2 3 N CYS A 211 ? N CYS A 298 O PRO A 221 ? O PRO A 308 
AE 3 4 N ASP A 226 ? N ASP A 313 O THR A 231 ? O THR A 318 
AF 1 2 N PHE A 274 ? N PHE A 361 O TRP A 281 ? O TRP A 368 
AF 2 3 N ARG A 284 ? N ARG A 371 O GLU A 295 ? O GLU A 382 
AF 3 4 N LYS A 298 ? N LYS A 385 O SER A 312 ? O SER A 399 
BA 1 2 N LEU B 19  ? N LEU B 106 O ALA B 366 ? O ALA B 453 
BA 2 3 N GLY B 369 ? N GLY B 456 O PRO B 341 ? O PRO B 428 
BA 3 4 N TYR B 344 ? N TYR B 431 O GLY B 327 ? O GLY B 414 
BB 1 2 N SER B 42  ? N SER B 129 O ARG B 49  ? O ARG B 136 
BB 2 3 N SER B 54  ? N SER B 141 O ALA B 76  ? O ALA B 163 
BB 3 4 N SER B 79  ? N SER B 166 O ARG B 92  ? O ARG B 179 
BC 1 2 N CYS B 103 ? N CYS B 190 O MET B 110 ? O MET B 197 
BC 2 3 N SER B 115 ? N SER B 202 O SER B 122 ? O SER B 209 
BC 3 4 N TYR B 127 ? N TYR B 214 O ARG B 130 ? O ARG B 217 
BD 1 2 N ASP B 163 ? N ASP B 250 O ALA B 171 ? O ALA B 258 
BD 2 3 N LYS B 178 ? N LYS B 265 O LYS B 181 ? O LYS B 268 
BE 1 2 N ALA B 203 ? N ALA B 290 O VAL B 206 ? O VAL B 293 
BE 2 3 N CYS B 211 ? N CYS B 298 O PRO B 221 ? O PRO B 308 
BE 3 4 N ASP B 226 ? N ASP B 313 O THR B 231 ? O THR B 318 
BF 1 2 N PHE B 274 ? N PHE B 361 O TRP B 281 ? O TRP B 368 
BF 2 3 N ARG B 284 ? N ARG B 371 O GLU B 295 ? O GLU B 382 
BF 3 4 N LYS B 298 ? N LYS B 385 O SER B 312 ? O SER B 399 
CA 1 2 N LEU C 19  ? N LEU C 106 O ALA C 366 ? O ALA C 453 
CA 2 3 N GLY C 369 ? N GLY C 456 O PRO C 341 ? O PRO C 428 
CA 3 4 N TYR C 344 ? N TYR C 431 O GLY C 327 ? O GLY C 414 
CB 1 2 N ASP C 44  ? N ASP C 131 O GLY C 47  ? O GLY C 134 
CB 2 3 N SER C 54  ? N SER C 141 O ALA C 76  ? O ALA C 163 
CB 3 4 N SER C 79  ? N SER C 166 O ARG C 92  ? O ARG C 179 
CC 1 2 N CYS C 103 ? N CYS C 190 O MET C 110 ? O MET C 197 
CC 2 3 N SER C 115 ? N SER C 202 O SER C 122 ? O SER C 209 
CC 3 4 N TYR C 127 ? N TYR C 214 O ARG C 130 ? O ARG C 217 
CD 1 2 N ASP C 163 ? N ASP C 250 O ALA C 171 ? O ALA C 258 
CD 2 3 N LYS C 178 ? N LYS C 265 O LYS C 181 ? O LYS C 268 
CE 1 2 N ALA C 203 ? N ALA C 290 O VAL C 206 ? O VAL C 293 
CE 2 3 N CYS C 211 ? N CYS C 298 O PRO C 221 ? O PRO C 308 
CE 3 4 N ASP C 226 ? N ASP C 313 O THR C 231 ? O THR C 318 
CF 1 2 N PHE C 274 ? N PHE C 361 O TRP C 281 ? O TRP C 368 
CF 2 3 N ARG C 284 ? N ARG C 371 O GLU C 295 ? O GLU C 382 
CF 3 4 N LYS C 298 ? N LYS C 385 O SER C 312 ? O SER C 399 
DA 1 2 N LEU D 19  ? N LEU D 106 O ALA D 366 ? O ALA D 453 
DA 2 3 N GLY D 369 ? N GLY D 456 O PRO D 341 ? O PRO D 428 
DA 3 4 N TYR D 344 ? N TYR D 431 O GLY D 327 ? O GLY D 414 
DB 1 2 N ASP D 44  ? N ASP D 131 O GLY D 47  ? O GLY D 134 
DB 2 3 N SER D 54  ? N SER D 141 O ALA D 76  ? O ALA D 163 
DB 3 4 N SER D 79  ? N SER D 166 O ARG D 92  ? O ARG D 179 
DC 1 2 N CYS D 103 ? N CYS D 190 O MET D 110 ? O MET D 197 
DC 2 3 N SER D 115 ? N SER D 202 O SER D 122 ? O SER D 209 
DC 3 4 N TYR D 127 ? N TYR D 214 O ARG D 130 ? O ARG D 217 
DD 1 2 N ASP D 163 ? N ASP D 250 O ALA D 171 ? O ALA D 258 
DD 2 3 N LYS D 178 ? N LYS D 265 O LYS D 181 ? O LYS D 268 
DE 1 2 N ALA D 203 ? N ALA D 290 O VAL D 206 ? O VAL D 293 
DE 2 3 N CYS D 211 ? N CYS D 298 O PRO D 221 ? O PRO D 308 
DE 3 4 N ASP D 226 ? N ASP D 313 O THR D 231 ? O THR D 318 
DF 1 2 N PHE D 274 ? N PHE D 361 O TRP D 281 ? O TRP D 368 
DF 2 3 N ARG D 284 ? N ARG D 371 O GLU D 295 ? O GLU D 382 
DF 3 4 N LYS D 298 ? N LYS D 385 O SER D 312 ? O SER D 399 
# 
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 ? ? ? ? 4  'BINDING SITE FOR RESIDUE NAG A1479' 
AC2 Software ? ? ? ? 1  'BINDING SITE FOR RESIDUE NAG A1480' 
AC3 Software ? ? ? ? 6  'BINDING SITE FOR RESIDUE NAG A1481' 
AC4 Software ? ? ? ? 1  'BINDING SITE FOR RESIDUE NAG A1482' 
AC5 Software ? ? ? ? 7  'BINDING SITE FOR RESIDUE MAN A1483' 
AC6 Software ? ? ? ? 8  'BINDING SITE FOR RESIDUE BMA A1486' 
AC7 Software ? ? ? ? 1  'BINDING SITE FOR RESIDUE MAN A1487' 
AC8 Software ? ? ? ? 6  'BINDING SITE FOR RESIDUE NAG A1495' 
AC9 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE MAN A1484' 
BC1 Software ? ? ? ? 8  'BINDING SITE FOR RESIDUE MAN A1485' 
BC2 Software ? ? ? ? 7  'BINDING SITE FOR RESIDUE NAG A1488' 
BC3 Software ? ? ? ? 8  'BINDING SITE FOR RESIDUE NAG A1489' 
BC4 Software ? ? ? ? 8  'BINDING SITE FOR RESIDUE BMA A1490' 
BC5 Software ? ? ? ? 6  'BINDING SITE FOR RESIDUE MAN A1491' 
BC6 Software ? ? ? ? 3  'BINDING SITE FOR RESIDUE MAN A1492' 
BC7 Software ? ? ? ? 7  'BINDING SITE FOR RESIDUE MAN A1493' 
BC8 Software ? ? ? ? 9  'BINDING SITE FOR RESIDUE MAN A1494' 
BC9 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE NAG B1479' 
CC1 Software ? ? ? ? 6  'BINDING SITE FOR RESIDUE NAG B1480' 
CC2 Software ? ? ? ? 1  'BINDING SITE FOR RESIDUE NAG B1481' 
CC3 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE NAG B1482' 
CC4 Software ? ? ? ? 6  'BINDING SITE FOR RESIDUE MAN B1483' 
CC5 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE BMA B1486' 
CC6 Software ? ? ? ? 7  'BINDING SITE FOR RESIDUE NAG B1487' 
CC7 Software ? ? ? ? 6  'BINDING SITE FOR RESIDUE MAN B1484' 
CC8 Software ? ? ? ? 6  'BINDING SITE FOR RESIDUE MAN B1485' 
CC9 Software ? ? ? ? 3  'BINDING SITE FOR RESIDUE NAG C1480' 
DC1 Software ? ? ? ? 8  'BINDING SITE FOR RESIDUE NAG C1481' 
DC2 Software ? ? ? ? 3  'BINDING SITE FOR RESIDUE NAG C1482' 
DC3 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE NAG C1483' 
DC4 Software ? ? ? ? 6  'BINDING SITE FOR RESIDUE NAG C1484' 
DC5 Software ? ? ? ? 6  'BINDING SITE FOR RESIDUE MAN C1485' 
DC6 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE BMA C1486' 
DC7 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE MAN C1487' 
DC8 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE NAG D1479' 
DC9 Software ? ? ? ? 7  'BINDING SITE FOR RESIDUE NAG D1480' 
EC1 Software ? ? ? ? 7  'BINDING SITE FOR RESIDUE NAG D1481' 
EC2 Software ? ? ? ? 6  'BINDING SITE FOR RESIDUE MAN D1483' 
EC3 Software ? ? ? ? 6  'BINDING SITE FOR RESIDUE CA A1477'  
EC4 Software ? ? ? ? 6  'BINDING SITE FOR RESIDUE CA B1477'  
EC5 Software ? ? ? ? 6  'BINDING SITE FOR RESIDUE CA C1477'  
EC6 Software ? ? ? ? 6  'BINDING SITE FOR RESIDUE CA D1477'  
EC7 Software ? ? ? ? 7  'BINDING SITE FOR RESIDUE GOL A1478' 
EC8 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE GOL B1478' 
EC9 Software ? ? ? ? 12 'BINDING SITE FOR RESIDUE PEG C1478' 
FC1 Software ? ? ? ? 7  'BINDING SITE FOR RESIDUE GOL C1479' 
FC2 Software ? ? ? ? 6  'BINDING SITE FOR RESIDUE GOL D1478' 
# 
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 4  ASN A  5   ? ASN A 92   . ? 1_555 ? 
2   AC1 4  LYS A  154 ? LYS A 241  . ? 1_555 ? 
3   AC1 4  NAG H  .   ? NAG A 504  . ? 1_555 ? 
4   AC1 4  HOH ZA .   ? HOH A 2610 . ? 1_555 ? 
5   AC2 1  NAG G  .   ? NAG A 503  . ? 1_555 ? 
6   AC3 6  ASN A  65  ? ASN A 152  . ? 1_555 ? 
7   AC3 6  LEU A  358 ? LEU A 445  . ? 1_555 ? 
8   AC3 6  NAG IA .   ? NAG C 501  . ? 1_555 ? 
9   AC3 6  HOH ZA .   ? HOH A 2409 . ? 1_555 ? 
10  AC3 6  HOH ZA .   ? HOH A 2509 . ? 1_555 ? 
11  AC3 6  TYR C  387 ? TYR C 474  . ? 1_555 ? 
12  AC4 1  NAG I  .   ? NAG A 505  . ? 1_555 ? 
13  AC5 7  LEU A  297 ? LEU A 384  . ? 1_555 ? 
14  AC5 7  PRO A  310 ? PRO A 397  . ? 1_555 ? 
15  AC5 7  ASN A  313 ? ASN A 400  . ? 1_555 ? 
16  AC5 7  MAN O  .   ? MAN A 508  . ? 1_555 ? 
17  AC5 7  MAN P  .   ? MAN A 509  . ? 1_555 ? 
18  AC5 7  BMA L  .   ? BMA A 510  . ? 1_555 ? 
19  AC5 7  HOH ZA .   ? HOH A 2515 . ? 1_555 ? 
20  AC6 8  ILE A  311 ? ILE A 398  . ? 1_555 ? 
21  AC6 8  SER A  312 ? SER A 399  . ? 1_555 ? 
22  AC6 8  ASN A  313 ? ASN A 400  . ? 1_555 ? 
23  AC6 8  MAN K  .   ? MAN A 507  . ? 1_555 ? 
24  AC6 8  MAN M  .   ? MAN A 511  . ? 1_555 ? 
25  AC6 8  NAG N  .   ? NAG A 512  . ? 1_555 ? 
26  AC6 8  HOH ZA .   ? HOH A 2625 . ? 1_555 ? 
27  AC6 8  HOH ZA .   ? HOH A 2575 . ? 1_555 ? 
28  AC7 1  BMA L  .   ? BMA A 510  . ? 1_555 ? 
29  AC8 6  SER A  15  ? SER A 102  . ? 1_555 ? 
30  AC8 6  SER A  312 ? SER A 399  . ? 1_555 ? 
31  AC8 6  ASN A  313 ? ASN A 400  . ? 1_555 ? 
32  AC8 6  BMA L  .   ? BMA A 510  . ? 1_555 ? 
33  AC8 6  HOH ZA .   ? HOH A 2604 . ? 1_555 ? 
34  AC8 6  NAG J  .   ? NAG A 506  . ? 1_555 ? 
35  AC9 5  ASP A  250 ? ASP A 337  . ? 1_555 ? 
36  AC9 5  ARG A  284 ? ARG A 371  . ? 1_555 ? 
37  AC9 5  MAN K  .   ? MAN A 507  . ? 1_555 ? 
38  AC9 5  HOH ZA .   ? HOH A 2464 . ? 1_555 ? 
39  AC9 5  HOH ZA .   ? HOH A 2387 . ? 1_555 ? 
40  BC1 8  GLU A  295 ? GLU A 382  . ? 1_555 ? 
41  BC1 8  LEU A  297 ? LEU A 384  . ? 1_555 ? 
42  BC1 8  ASN A  313 ? ASN A 400  . ? 1_555 ? 
43  BC1 8  VAL A  315 ? VAL A 402  . ? 1_555 ? 
44  BC1 8  MAN K  .   ? MAN A 507  . ? 1_555 ? 
45  BC1 8  HOH ZA .   ? HOH A 2414 . ? 1_555 ? 
46  BC1 8  HOH ZA .   ? HOH A 2310 . ? 1_555 ? 
47  BC1 8  HOH ZA .   ? HOH A 2476 . ? 1_555 ? 
48  BC2 7  ASN A  120 ? ASN A 207  . ? 1_555 ? 
49  BC2 7  NAG T  .   ? NAG A 516  . ? 1_555 ? 
50  BC2 7  HOH ZA .   ? HOH A 2634 . ? 1_555 ? 
51  BC2 7  HOH ZA .   ? HOH A 2314 . ? 1_555 ? 
52  BC2 7  ARG C  373 ? ARG C 460  . ? 1_555 ? 
53  BC2 7  LEU C  374 ? LEU C 461  . ? 1_555 ? 
54  BC2 7  GLY C  375 ? GLY C 462  . ? 1_555 ? 
55  BC3 8  NAG S  .   ? NAG A 515  . ? 1_555 ? 
56  BC3 8  BMA U  .   ? BMA A 517  . ? 1_555 ? 
57  BC3 8  MAN V  .   ? MAN A 518  . ? 1_555 ? 
58  BC3 8  HOH ZA .   ? HOH A 2421 . ? 1_555 ? 
59  BC3 8  ASN C  14  ? ASN C 101  . ? 1_555 ? 
60  BC3 8  SER C  312 ? SER C 399  . ? 1_555 ? 
61  BC3 8  ASN C  313 ? ASN C 400  . ? 1_555 ? 
62  BC3 8  HOH BB .   ? HOH C 603  . ? 1_555 ? 
63  BC4 8  NAG T  .   ? NAG A 516  . ? 1_555 ? 
64  BC4 8  MAN V  .   ? MAN A 518  . ? 1_555 ? 
65  BC4 8  MAN X  .   ? MAN A 520  . ? 1_555 ? 
66  BC4 8  HOH ZA .   ? HOH A 2360 . ? 1_555 ? 
67  BC4 8  HOH ZA .   ? HOH A 2335 . ? 1_555 ? 
68  BC4 8  ILE C  311 ? ILE C 398  . ? 1_555 ? 
69  BC4 8  SER C  312 ? SER C 399  . ? 1_555 ? 
70  BC4 8  ASN C  313 ? ASN C 400  . ? 1_555 ? 
71  BC5 6  NAG T  .   ? NAG A 516  . ? 1_555 ? 
72  BC5 6  BMA U  .   ? BMA A 517  . ? 1_555 ? 
73  BC5 6  MAN W  .   ? MAN A 519  . ? 1_555 ? 
74  BC5 6  HOH ZA .   ? HOH A 2533 . ? 1_555 ? 
75  BC5 6  HOH ZA .   ? HOH A 2479 . ? 1_555 ? 
76  BC5 6  HOH ZA .   ? HOH A 2532 . ? 1_555 ? 
77  BC6 3  MAN V  .   ? MAN A 518  . ? 1_555 ? 
78  BC6 3  HOH ZA .   ? HOH A 2646 . ? 1_555 ? 
79  BC6 3  HOH ZA .   ? HOH A 2345 . ? 1_555 ? 
80  BC7 7  BMA U  .   ? BMA A 517  . ? 1_555 ? 
81  BC7 7  MAN Y  .   ? MAN A 521  . ? 1_555 ? 
82  BC7 7  LEU C  297 ? LEU C 384  . ? 1_555 ? 
83  BC7 7  PRO C  310 ? PRO C 397  . ? 1_555 ? 
84  BC7 7  ASN C  313 ? ASN C 400  . ? 1_555 ? 
85  BC7 7  MAN R  .   ? MAN A 514  . ? 1_555 ? 
86  BC7 7  HOH BB .   ? HOH C 878  . ? 1_555 ? 
87  BC8 9  MAN X  .   ? MAN A 520  . ? 1_555 ? 
88  BC8 9  HOH ZA .   ? HOH A 2321 . ? 1_555 ? 
89  BC8 9  HOH ZA .   ? HOH A 2489 . ? 1_555 ? 
90  BC8 9  HOH ZA .   ? HOH A 2599 . ? 1_555 ? 
91  BC8 9  HOH ZA .   ? HOH A 2308 . ? 1_555 ? 
92  BC8 9  GLU C  295 ? GLU C 382  . ? 1_555 ? 
93  BC8 9  LEU C  297 ? LEU C 384  . ? 1_555 ? 
94  BC8 9  ASN C  313 ? ASN C 400  . ? 1_555 ? 
95  BC8 9  VAL C  315 ? VAL C 402  . ? 1_555 ? 
96  BC9 4  THR B  2   ? THR B 89   . ? 1_555 ? 
97  BC9 4  ASN B  5   ? ASN B 92   . ? 1_555 ? 
98  BC9 4  HOH AB .   ? HOH B 649  . ? 1_555 ? 
99  BC9 4  HOH AB .   ? HOH B 893  . ? 1_555 ? 
100 CC1 6  TYR A  387 ? TYR A 474  . ? 1_555 ? 
101 CC1 6  ASN B  65  ? ASN B 152  . ? 1_555 ? 
102 CC1 6  LEU B  358 ? LEU B 445  . ? 1_555 ? 
103 CC1 6  NAG Q  .   ? NAG A 513  . ? 1_555 ? 
104 CC1 6  HOH AB .   ? HOH B 746  . ? 1_555 ? 
105 CC1 6  HOH AB .   ? HOH B 785  . ? 1_555 ? 
106 CC2 1  NAG CA .   ? NAG B 504  . ? 1_555 ? 
107 CC3 5  LEU A  374 ? LEU A 461  . ? 1_555 ? 
108 CC3 5  NAG N  .   ? NAG A 512  . ? 1_555 ? 
109 CC3 5  ASN B  119 ? ASN B 206  . ? 1_555 ? 
110 CC3 5  ASN B  120 ? ASN B 207  . ? 1_555 ? 
111 CC3 5  HOH ZA .   ? HOH A 2305 . ? 1_555 ? 
112 CC4 6  PRO B  310 ? PRO B 397  . ? 1_555 ? 
113 CC4 6  ASN B  313 ? ASN B 400  . ? 1_555 ? 
114 CC4 6  MAN GA .   ? MAN B 506  . ? 1_555 ? 
115 CC4 6  MAN HA .   ? MAN B 509  . ? 1_555 ? 
116 CC4 6  BMA EA .   ? BMA B 507  . ? 1_555 ? 
117 CC4 6  HOH AB .   ? HOH B 706  . ? 1_555 ? 
118 CC5 5  ILE B  311 ? ILE B 398  . ? 1_555 ? 
119 CC5 5  SER B  312 ? SER B 399  . ? 1_555 ? 
120 CC5 5  ASN B  313 ? ASN B 400  . ? 1_555 ? 
121 CC5 5  MAN DA .   ? MAN B 505  . ? 1_555 ? 
122 CC5 5  NAG FA .   ? NAG B 508  . ? 1_555 ? 
123 CC6 7  ASN B  14  ? ASN B 101  . ? 1_555 ? 
124 CC6 7  SER B  312 ? SER B 399  . ? 1_555 ? 
125 CC6 7  ASN B  313 ? ASN B 400  . ? 1_555 ? 
126 CC6 7  BMA EA .   ? BMA B 507  . ? 1_555 ? 
127 CC6 7  HOH AB .   ? HOH B 731  . ? 1_555 ? 
128 CC6 7  HOH AB .   ? HOH B 705  . ? 1_555 ? 
129 CC6 7  NAG XA .   ? NAG D 508  . ? 1_555 ? 
130 CC7 6  ASP B  250 ? ASP B 337  . ? 1_555 ? 
131 CC7 6  ARG B  284 ? ARG B 371  . ? 1_555 ? 
132 CC7 6  MAN DA .   ? MAN B 505  . ? 1_555 ? 
133 CC7 6  HOH AB .   ? HOH B 626  . ? 1_555 ? 
134 CC7 6  HOH AB .   ? HOH B 818  . ? 1_555 ? 
135 CC7 6  HOH AB .   ? HOH B 656  . ? 1_555 ? 
136 CC8 6  GLU B  295 ? GLU B 382  . ? 1_555 ? 
137 CC8 6  ASN B  313 ? ASN B 400  . ? 1_555 ? 
138 CC8 6  VAL B  315 ? VAL B 402  . ? 1_555 ? 
139 CC8 6  MAN DA .   ? MAN B 505  . ? 1_555 ? 
140 CC8 6  HOH AB .   ? HOH B 648  . ? 1_555 ? 
141 CC8 6  HOH AB .   ? HOH B 748  . ? 1_555 ? 
142 CC9 3  THR C  2   ? THR C 89   . ? 1_555 ? 
143 CC9 3  PHE C  3   ? PHE C 90   . ? 1_555 ? 
144 CC9 3  ASN C  5   ? ASN C 92   . ? 1_555 ? 
145 DC1 8  ASN C  65  ? ASN C 152  . ? 1_555 ? 
146 DC1 8  NAG QA .   ? NAG D 501  . ? 1_555 ? 
147 DC1 8  HOH BB .   ? HOH C 721  . ? 1_555 ? 
148 DC1 8  HOH BB .   ? HOH C 888  . ? 1_555 ? 
149 DC1 8  HOH BB .   ? HOH C 777  . ? 1_555 ? 
150 DC1 8  HOH BB .   ? HOH C 904  . ? 1_555 ? 
151 DC1 8  TYR D  387 ? TYR D 474  . ? 1_555 ? 
152 DC1 8  HOH CB .   ? HOH D 629  . ? 1_555 ? 
153 DC2 3  NAG NA .   ? NAG C 506  . ? 1_555 ? 
154 DC2 3  HOH CB .   ? HOH D 816  . ? 1_555 ? 
155 DC2 3  ILE D  386 ? ILE D 473  . ? 1_555 ? 
156 DC3 5  ASN C  120 ? ASN C 207  . ? 1_555 ? 
157 DC3 5  NAG PA .   ? NAG C 508  . ? 1_555 ? 
158 DC3 5  LEU D  374 ? LEU D 461  . ? 1_555 ? 
159 DC3 5  GLY D  375 ? GLY D 462  . ? 1_555 ? 
160 DC3 5  SER D  376 ? SER D 463  . ? 1_555 ? 
161 DC4 6  NAG OA .   ? NAG C 507  . ? 1_555 ? 
162 DC4 6  BMA RA .   ? BMA D 502  . ? 1_555 ? 
163 DC4 6  ASN D  14  ? ASN D 101  . ? 1_555 ? 
164 DC4 6  SER D  312 ? SER D 399  . ? 1_555 ? 
165 DC4 6  ASN D  313 ? ASN D 400  . ? 1_555 ? 
166 DC4 6  ARG D  373 ? ARG D 460  . ? 1_555 ? 
167 DC5 6  MAN X  .   ? MAN A 520  . ? 1_555 ? 
168 DC5 6  ASP C  250 ? ASP C 337  . ? 1_555 ? 
169 DC5 6  ARG C  284 ? ARG C 371  . ? 1_555 ? 
170 DC5 6  HOH ZA .   ? HOH A 2592 . ? 1_555 ? 
171 DC5 6  HOH ZA .   ? HOH A 2591 . ? 1_555 ? 
172 DC5 6  HOH ZA .   ? HOH A 2483 . ? 1_555 ? 
173 DC6 5  NAG PA .   ? NAG C 508  . ? 1_555 ? 
174 DC6 5  MAN SA .   ? MAN D 503  . ? 1_555 ? 
175 DC6 5  ILE D  311 ? ILE D 398  . ? 1_555 ? 
176 DC6 5  SER D  312 ? SER D 399  . ? 1_555 ? 
177 DC6 5  ASN D  313 ? ASN D 400  . ? 1_555 ? 
178 DC7 5  BMA RA .   ? BMA D 502  . ? 1_555 ? 
179 DC7 5  LEU D  297 ? LEU D 384  . ? 1_555 ? 
180 DC7 5  ASN D  313 ? ASN D 400  . ? 1_555 ? 
181 DC7 5  MAN YA .   ? MAN D 509  . ? 1_555 ? 
182 DC7 5  HOH CB .   ? HOH D 729  . ? 1_555 ? 
183 DC8 5  PHE D  3   ? PHE D 90   . ? 1_555 ? 
184 DC8 5  ASN D  5   ? ASN D 92   . ? 1_555 ? 
185 DC8 5  THR D  7   ? THR D 94   . ? 1_555 ? 
186 DC8 5  LYS D  154 ? LYS D 241  . ? 1_555 ? 
187 DC8 5  HOH CB .   ? HOH D 609  . ? 1_555 ? 
188 DC9 7  TYR B  387 ? TYR B 474  . ? 1_555 ? 
189 DC9 7  ASN D  65  ? ASN D 152  . ? 1_555 ? 
190 DC9 7  LEU D  358 ? LEU D 445  . ? 1_555 ? 
191 DC9 7  HOH CB .   ? HOH D 652  . ? 1_555 ? 
192 DC9 7  HOH CB .   ? HOH D 873  . ? 1_555 ? 
193 DC9 7  HOH CB .   ? HOH D 803  . ? 1_555 ? 
194 DC9 7  HOH CB .   ? HOH D 809  . ? 1_555 ? 
195 EC1 7  LEU B  374 ? LEU B 461  . ? 1_555 ? 
196 EC1 7  GLY B  375 ? GLY B 462  . ? 1_555 ? 
197 EC1 7  SER B  376 ? SER B 463  . ? 1_555 ? 
198 EC1 7  NAG FA .   ? NAG B 508  . ? 1_555 ? 
199 EC1 7  HOH AB .   ? HOH B 823  . ? 1_555 ? 
200 EC1 7  ASN D  120 ? ASN D 207  . ? 1_555 ? 
201 EC1 7  HOH CB .   ? HOH D 896  . ? 1_555 ? 
202 EC2 6  MAN SA .   ? MAN D 503  . ? 1_555 ? 
203 EC2 6  ILE D  286 ? ILE D 373  . ? 1_555 ? 
204 EC2 6  HOH CB .   ? HOH D 605  . ? 1_555 ? 
205 EC2 6  HOH CB .   ? HOH D 862  . ? 1_555 ? 
206 EC2 6  HOH CB .   ? HOH D 783  . ? 1_555 ? 
207 EC2 6  HOH CB .   ? HOH D 601  . ? 1_555 ? 
208 EC3 6  ASP A  213 ? ASP A 300  . ? 1_555 ? 
209 EC3 6  GLY A  217 ? GLY A 304  . ? 1_555 ? 
210 EC3 6  ASP A  244 ? ASP A 331  . ? 1_555 ? 
211 EC3 6  PRO A  267 ? PRO A 354  . ? 1_555 ? 
212 EC3 6  HOH ZA .   ? HOH A 2420 . ? 1_555 ? 
213 EC3 6  HOH ZA .   ? HOH A 2519 . ? 1_555 ? 
214 EC4 6  ASP B  213 ? ASP B 300  . ? 1_555 ? 
215 EC4 6  GLY B  217 ? GLY B 304  . ? 1_555 ? 
216 EC4 6  ASP B  244 ? ASP B 331  . ? 1_555 ? 
217 EC4 6  PRO B  267 ? PRO B 354  . ? 1_555 ? 
218 EC4 6  HOH AB .   ? HOH B 738  . ? 1_555 ? 
219 EC4 6  HOH AB .   ? HOH B 763  . ? 1_555 ? 
220 EC5 6  ASP C  213 ? ASP C 300  . ? 1_555 ? 
221 EC5 6  GLY C  217 ? GLY C 304  . ? 1_555 ? 
222 EC5 6  ASP C  244 ? ASP C 331  . ? 1_555 ? 
223 EC5 6  PRO C  267 ? PRO C 354  . ? 1_555 ? 
224 EC5 6  HOH BB .   ? HOH C 684  . ? 1_555 ? 
225 EC5 6  HOH BB .   ? HOH C 745  . ? 1_555 ? 
226 EC6 6  ASP D  213 ? ASP D 300  . ? 1_555 ? 
227 EC6 6  GLY D  217 ? GLY D 304  . ? 1_555 ? 
228 EC6 6  ASP D  244 ? ASP D 331  . ? 1_555 ? 
229 EC6 6  PRO D  267 ? PRO D 354  . ? 1_555 ? 
230 EC6 6  HOH CB .   ? HOH D 654  . ? 1_555 ? 
231 EC6 6  HOH CB .   ? HOH D 720  . ? 1_555 ? 
232 EC7 7  GLN A  55  ? GLN A 142  . ? 1_555 ? 
233 EC7 7  HIS A  63  ? HIS A 150  . ? 1_555 ? 
234 EC7 7  ASN A  65  ? ASN A 152  . ? 1_555 ? 
235 EC7 7  SER A  72  ? SER A 159  . ? 1_555 ? 
236 EC7 7  HOH ZA .   ? HOH A 2454 . ? 1_555 ? 
237 EC7 7  HOH ZA .   ? HOH A 2553 . ? 1_555 ? 
238 EC7 7  ARG C  26  ? ARG C 113  . ? 1_555 ? 
239 EC8 5  ARG A  26  ? ARG A 113  . ? 1_555 ? 
240 EC8 5  GLN B  55  ? GLN B 142  . ? 1_555 ? 
241 EC8 5  HIS B  63  ? HIS B 150  . ? 1_555 ? 
242 EC8 5  ASN B  65  ? ASN B 152  . ? 1_555 ? 
243 EC8 5  SER B  72  ? SER B 159  . ? 1_555 ? 
244 EC9 12 PRO A  131 ? PRO A 218  . ? 1_555 ? 
245 EC9 12 ILE A  132 ? ILE A 219  . ? 1_555 ? 
246 EC9 12 GLU A  134 ? GLU A 221  . ? 1_555 ? 
247 EC9 12 HIS C  17  ? HIS C 104  . ? 1_555 ? 
248 EC9 12 LYS C  336 ? LYS C 423  . ? 1_555 ? 
249 EC9 12 ASN C  340 ? ASN C 427  . ? 1_555 ? 
250 EC9 12 CYS C  342 ? CYS C 429  . ? 1_555 ? 
251 EC9 12 CYS C  368 ? CYS C 455  . ? 1_555 ? 
252 EC9 12 GLY C  369 ? GLY C 456  . ? 1_555 ? 
253 EC9 12 HOH BB .   ? HOH C 629  . ? 1_555 ? 
254 EC9 12 HOH BB .   ? HOH C 903  . ? 1_555 ? 
255 EC9 12 HOH BB .   ? HOH C 687  . ? 1_555 ? 
256 FC1 7  GLN C  55  ? GLN C 142  . ? 1_555 ? 
257 FC1 7  HIS C  63  ? HIS C 150  . ? 1_555 ? 
258 FC1 7  ASN C  65  ? ASN C 152  . ? 1_555 ? 
259 FC1 7  SER C  72  ? SER C 159  . ? 1_555 ? 
260 FC1 7  PHE C  74  ? PHE C 161  . ? 1_555 ? 
261 FC1 7  HOH BB .   ? HOH C 711  . ? 1_555 ? 
262 FC1 7  ARG D  26  ? ARG D 113  . ? 1_555 ? 
263 FC2 6  ARG B  26  ? ARG B 113  . ? 1_555 ? 
264 FC2 6  GLN D  55  ? GLN D 142  . ? 1_555 ? 
265 FC2 6  HIS D  63  ? HIS D 150  . ? 1_555 ? 
266 FC2 6  SER D  72  ? SER D 159  . ? 1_555 ? 
267 FC2 6  HOH CB .   ? HOH D 699  . ? 1_555 ? 
268 FC2 6  HOH CB .   ? HOH D 911  . ? 1_555 ? 
# 
_database_PDB_matrix.entry_id          1V0Z 
_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                    1V0Z 
_atom_sites.fract_transf_matrix[1][1]   0.009391 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000060 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.013558 
_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]   0.009363 
_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  
CA 
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1     N  N   . ARG A  1 1   ? 32.248  -26.059 63.787  1.00 26.29  ? 88   ARG A N   1 
ATOM   2     C  CA  . ARG A  1 1   ? 32.394  -25.061 62.689  1.00 26.09  ? 88   ARG A CA  1 
ATOM   3     C  C   . ARG A  1 1   ? 33.051  -25.654 61.444  1.00 24.57  ? 88   ARG A C   1 
ATOM   4     O  O   . ARG A  1 1   ? 33.897  -26.539 61.528  1.00 24.30  ? 88   ARG A O   1 
ATOM   5     C  CB  . ARG A  1 1   ? 33.220  -23.860 63.159  1.00 26.36  ? 88   ARG A CB  1 
ATOM   6     C  CG  . ARG A  1 1   ? 32.443  -22.748 63.869  1.00 28.27  ? 88   ARG A CG  1 
ATOM   7     C  CD  . ARG A  1 1   ? 33.419  -21.686 64.437  1.00 29.00  ? 88   ARG A CD  1 
ATOM   8     N  NE  . ARG A  1 1   ? 34.360  -22.283 65.402  1.00 35.51  ? 88   ARG A NE  1 
ATOM   9     C  CZ  . ARG A  1 1   ? 35.670  -22.494 65.213  1.00 37.42  ? 88   ARG A CZ  1 
ATOM   10    N  NH1 . ARG A  1 1   ? 36.275  -22.138 64.089  1.00 39.39  ? 88   ARG A NH1 1 
ATOM   11    N  NH2 . ARG A  1 1   ? 36.392  -23.061 66.176  1.00 38.86  ? 88   ARG A NH2 1 
ATOM   12    N  N   . THR A  1 2   ? 32.665  -25.135 60.287  1.00 22.46  ? 89   THR A N   1 
ATOM   13    C  CA  . THR A  1 2   ? 33.297  -25.487 59.026  1.00 20.65  ? 89   THR A CA  1 
ATOM   14    C  C   . THR A  1 2   ? 33.511  -24.200 58.213  1.00 18.80  ? 89   THR A C   1 
ATOM   15    O  O   . THR A  1 2   ? 32.881  -23.176 58.499  1.00 17.45  ? 89   THR A O   1 
ATOM   16    C  CB  . THR A  1 2   ? 32.421  -26.470 58.200  1.00 21.14  ? 89   THR A CB  1 
ATOM   17    O  OG1 . THR A  1 2   ? 31.144  -25.876 57.949  1.00 22.24  ? 89   THR A OG1 1 
ATOM   18    C  CG2 . THR A  1 2   ? 32.196  -27.781 58.947  1.00 22.49  ? 89   THR A CG2 1 
ATOM   19    N  N   . PHE A  1 3   ? 34.387  -24.250 57.207  1.00 16.53  ? 90   PHE A N   1 
ATOM   20    C  CA  . PHE A  1 3   ? 34.488  -23.160 56.249  1.00 15.63  ? 90   PHE A CA  1 
ATOM   21    C  C   . PHE A  1 3   ? 33.148  -23.032 55.505  1.00 14.97  ? 90   PHE A C   1 
ATOM   22    O  O   . PHE A  1 3   ? 32.591  -24.029 55.033  1.00 13.12  ? 90   PHE A O   1 
ATOM   23    C  CB  . PHE A  1 3   ? 35.597  -23.402 55.221  1.00 16.01  ? 90   PHE A CB  1 
ATOM   24    C  CG  . PHE A  1 3   ? 36.994  -23.188 55.747  1.00 16.84  ? 90   PHE A CG  1 
ATOM   25    C  CD1 . PHE A  1 3   ? 37.967  -24.163 55.556  1.00 18.86  ? 90   PHE A CD1 1 
ATOM   26    C  CD2 . PHE A  1 3   ? 37.346  -22.014 56.424  1.00 16.50  ? 90   PHE A CD2 1 
ATOM   27    C  CE1 . PHE A  1 3   ? 39.266  -23.984 56.039  1.00 19.20  ? 90   PHE A CE1 1 
ATOM   28    C  CE2 . PHE A  1 3   ? 38.651  -21.826 56.905  1.00 18.95  ? 90   PHE A CE2 1 
ATOM   29    C  CZ  . PHE A  1 3   ? 39.604  -22.813 56.715  1.00 18.71  ? 90   PHE A CZ  1 
ATOM   30    N  N   . LEU A  1 4   ? 32.643  -21.804 55.413  1.00 13.98  ? 91   LEU A N   1 
ATOM   31    C  CA  . LEU A  1 4   ? 31.493  -21.495 54.577  1.00 13.05  ? 91   LEU A CA  1 
ATOM   32    C  C   . LEU A  1 4   ? 31.816  -21.753 53.094  1.00 13.43  ? 91   LEU A C   1 
ATOM   33    O  O   . LEU A  1 4   ? 32.912  -21.400 52.621  1.00 12.86  ? 91   LEU A O   1 
ATOM   34    C  CB  . LEU A  1 4   ? 31.157  -19.995 54.747  1.00 13.13  ? 91   LEU A CB  1 
ATOM   35    C  CG  . LEU A  1 4   ? 30.107  -19.393 53.802  1.00 11.69  ? 91   LEU A CG  1 
ATOM   36    C  CD1 . LEU A  1 4   ? 28.719  -19.957 54.170  1.00 11.40  ? 91   LEU A CD1 1 
ATOM   37    C  CD2 . LEU A  1 4   ? 30.117  -17.850 53.837  1.00 12.66  ? 91   LEU A CD2 1 
ATOM   38    N  N   . ASN A  1 5   ? 30.872  -22.346 52.358  1.00 13.51  ? 92   ASN A N   1 
ATOM   39    C  CA  . ASN A  1 5   ? 30.912  -22.264 50.886  1.00 13.94  ? 92   ASN A CA  1 
ATOM   40    C  C   . ASN A  1 5   ? 29.649  -21.601 50.319  1.00 14.07  ? 92   ASN A C   1 
ATOM   41    O  O   . ASN A  1 5   ? 28.606  -21.549 50.980  1.00 13.31  ? 92   ASN A O   1 
ATOM   42    C  CB  . ASN A  1 5   ? 31.170  -23.631 50.234  1.00 14.45  ? 92   ASN A CB  1 
ATOM   43    C  CG  . ASN A  1 5   ? 30.028  -24.584 50.419  1.00 16.14  ? 92   ASN A CG  1 
ATOM   44    O  OD1 . ASN A  1 5   ? 28.892  -24.313 49.980  1.00 16.28  ? 92   ASN A OD1 1 
ATOM   45    N  ND2 . ASN A  1 5   ? 30.313  -25.714 51.065  1.00 18.26  ? 92   ASN A ND2 1 
ATOM   46    N  N   . LEU A  1 6   ? 29.746  -21.137 49.084  1.00 13.72  ? 93   LEU A N   1 
ATOM   47    C  CA  . LEU A  1 6   ? 28.735  -20.249 48.526  1.00 14.55  ? 93   LEU A CA  1 
ATOM   48    C  C   . LEU A  1 6   ? 27.843  -20.958 47.522  1.00 15.14  ? 93   LEU A C   1 
ATOM   49    O  O   . LEU A  1 6   ? 27.340  -20.337 46.594  1.00 15.50  ? 93   LEU A O   1 
ATOM   50    C  CB  . LEU A  1 6   ? 29.425  -19.057 47.863  1.00 13.92  ? 93   LEU A CB  1 
ATOM   51    C  CG  . LEU A  1 6   ? 30.344  -18.225 48.752  1.00 13.24  ? 93   LEU A CG  1 
ATOM   52    C  CD1 . LEU A  1 6   ? 31.054  -17.151 47.902  1.00 12.52  ? 93   LEU A CD1 1 
ATOM   53    C  CD2 . LEU A  1 6   ? 29.535  -17.589 49.920  1.00 13.43  ? 93   LEU A CD2 1 
ATOM   54    N  N   . THR A  1 7   ? 27.644  -22.257 47.704  1.00 15.97  ? 94   THR A N   1 
ATOM   55    C  CA  . THR A  1 7   ? 26.936  -23.015 46.669  1.00 17.16  ? 94   THR A CA  1 
ATOM   56    C  C   . THR A  1 7   ? 25.449  -22.587 46.508  1.00 17.31  ? 94   THR A C   1 
ATOM   57    O  O   . THR A  1 7   ? 24.923  -22.606 45.386  1.00 19.42  ? 94   THR A O   1 
ATOM   58    C  CB  . THR A  1 7   ? 27.186  -24.558 46.776  1.00 17.33  ? 94   THR A CB  1 
ATOM   59    O  OG1 . THR A  1 7   ? 26.789  -25.036 48.067  1.00 18.71  ? 94   THR A OG1 1 
ATOM   60    C  CG2 . THR A  1 7   ? 28.680  -24.866 46.565  1.00 17.70  ? 94   THR A CG2 1 
ATOM   61    N  N   . LYS A  1 8   ? 24.805  -22.141 47.589  1.00 15.28  ? 95   LYS A N   1 
ATOM   62    C  CA  . LYS A  1 8   ? 23.365  -21.786 47.558  1.00 14.63  ? 95   LYS A CA  1 
ATOM   63    C  C   . LYS A  1 8   ? 23.008  -20.649 46.571  1.00 13.91  ? 95   LYS A C   1 
ATOM   64    O  O   . LYS A  1 8   ? 23.833  -19.771 46.300  1.00 13.76  ? 95   LYS A O   1 
ATOM   65    C  CB  . LYS A  1 8   ? 22.848  -21.426 48.973  1.00 13.47  ? 95   LYS A CB  1 
ATOM   66    C  CG  . LYS A  1 8   ? 22.882  -22.579 49.996  1.00 14.15  ? 95   LYS A CG  1 
ATOM   67    C  CD  . LYS A  1 8   ? 22.442  -22.142 51.392  1.00 14.47  ? 95   LYS A CD  1 
ATOM   68    C  CE  . LYS A  1 8   ? 22.651  -23.270 52.420  1.00 15.86  ? 95   LYS A CE  1 
ATOM   69    N  NZ  . LYS A  1 8   ? 21.935  -23.050 53.708  1.00 14.57  ? 95   LYS A NZ  1 
ATOM   70    N  N   . PRO A  1 9   ? 21.775  -20.666 46.026  1.00 13.48  ? 96   PRO A N   1 
ATOM   71    C  CA  . PRO A  1 9   ? 21.330  -19.566 45.159  1.00 12.99  ? 96   PRO A CA  1 
ATOM   72    C  C   . PRO A  1 9   ? 20.828  -18.382 45.993  1.00 12.59  ? 96   PRO A C   1 
ATOM   73    O  O   . PRO A  1 9   ? 20.592  -18.549 47.185  1.00 12.88  ? 96   PRO A O   1 
ATOM   74    C  CB  . PRO A  1 9   ? 20.161  -20.191 44.381  1.00 12.36  ? 96   PRO A CB  1 
ATOM   75    C  CG  . PRO A  1 9   ? 19.580  -21.180 45.331  1.00 13.80  ? 96   PRO A CG  1 
ATOM   76    C  CD  . PRO A  1 9   ? 20.729  -21.703 46.184  1.00 13.51  ? 96   PRO A CD  1 
ATOM   77    N  N   . LEU A  1 10  ? 20.667  -17.208 45.386  1.00 12.54  ? 97   LEU A N   1 
ATOM   78    C  CA  . LEU A  1 10  ? 20.009  -16.090 46.066  1.00 13.11  ? 97   LEU A CA  1 
ATOM   79    C  C   . LEU A  1 10  ? 18.516  -16.384 46.195  1.00 13.18  ? 97   LEU A C   1 
ATOM   80    O  O   . LEU A  1 10  ? 17.904  -16.951 45.271  1.00 12.91  ? 97   LEU A O   1 
ATOM   81    C  CB  . LEU A  1 10  ? 20.185  -14.774 45.306  1.00 13.12  ? 97   LEU A CB  1 
ATOM   82    C  CG  . LEU A  1 10  ? 21.467  -13.960 45.340  1.00 15.02  ? 97   LEU A CG  1 
ATOM   83    C  CD1 . LEU A  1 10  ? 21.138  -12.567 44.725  1.00 13.27  ? 97   LEU A CD1 1 
ATOM   84    C  CD2 . LEU A  1 10  ? 22.029  -13.853 46.771  1.00 13.20  ? 97   LEU A CD2 1 
ATOM   85    N  N   . CYS A  1 11  ? 17.948  -16.030 47.346  1.00 12.70  ? 98   CYS A N   1 
ATOM   86    C  CA  . CYS A  1 11  ? 16.494  -16.063 47.565  1.00 13.04  ? 98   CYS A CA  1 
ATOM   87    C  C   . CYS A  1 11  ? 15.794  -15.087 46.649  1.00 12.83  ? 98   CYS A C   1 
ATOM   88    O  O   . CYS A  1 11  ? 16.352  -14.055 46.303  1.00 11.96  ? 98   CYS A O   1 
ATOM   89    C  CB  . CYS A  1 11  ? 16.147  -15.678 49.009  1.00 13.19  ? 98   CYS A CB  1 
ATOM   90    S  SG  . CYS A  1 11  ? 16.909  -16.741 50.265  1.00 14.37  ? 98   CYS A SG  1 
ATOM   91    N  N   . GLU A  1 12  ? 14.561  -15.431 46.266  1.00 13.24  ? 99   GLU A N   1 
ATOM   92    C  CA  . GLU A  1 12  ? 13.673  -14.492 45.578  1.00 13.51  ? 99   GLU A CA  1 
ATOM   93    C  C   . GLU A  1 12  ? 13.378  -13.291 46.489  1.00 12.18  ? 99   GLU A C   1 
ATOM   94    O  O   . GLU A  1 12  ? 13.099  -13.472 47.675  1.00 12.60  ? 99   GLU A O   1 
ATOM   95    C  CB  . GLU A  1 12  ? 12.370  -15.205 45.223  1.00 13.40  ? 99   GLU A CB  1 
ATOM   96    C  CG  . GLU A  1 12  ? 11.291  -14.306 44.620  1.00 14.37  ? 99   GLU A CG  1 
ATOM   97    C  CD  . GLU A  1 12  ? 10.018  -15.078 44.294  1.00 16.29  ? 99   GLU A CD  1 
ATOM   98    O  OE1 . GLU A  1 12  ? 9.007   -14.430 43.986  1.00 17.95  ? 99   GLU A OE1 1 
ATOM   99    O  OE2 . GLU A  1 12  ? 10.022  -16.330 44.351  1.00 19.16  ? 99   GLU A OE2 1 
ATOM   100   N  N   . VAL A  1 13  ? 13.426  -12.081 45.937  1.00 11.55  ? 100  VAL A N   1 
ATOM   101   C  CA  . VAL A  1 13  ? 13.136  -10.856 46.697  1.00 11.02  ? 100  VAL A CA  1 
ATOM   102   C  C   . VAL A  1 13  ? 12.085  -10.029 45.959  1.00 11.39  ? 100  VAL A C   1 
ATOM   103   O  O   . VAL A  1 13  ? 12.274  -9.647  44.794  1.00 11.13  ? 100  VAL A O   1 
ATOM   104   C  CB  . VAL A  1 13  ? 14.438  -10.026 46.959  1.00 10.93  ? 100  VAL A CB  1 
ATOM   105   C  CG1 . VAL A  1 13  ? 14.154  -8.682  47.653  1.00 10.53  ? 100  VAL A CG1 1 
ATOM   106   C  CG2 . VAL A  1 13  ? 15.439  -10.864 47.771  1.00 8.60   ? 100  VAL A CG2 1 
ATOM   107   N  N   . ASN A  1 14  ? 10.969  -9.787  46.651  1.00 10.86  ? 101  ASN A N   1 
ATOM   108   C  CA  . ASN A  1 14  ? 9.883   -8.961  46.140  1.00 11.24  ? 101  ASN A CA  1 
ATOM   109   C  C   . ASN A  1 14  ? 9.724   -7.639  46.879  1.00 11.51  ? 101  ASN A C   1 
ATOM   110   O  O   . ASN A  1 14  ? 9.219   -6.664  46.321  1.00 11.91  ? 101  ASN A O   1 
ATOM   111   C  CB  . ASN A  1 14  ? 8.579   -9.771  46.097  1.00 11.64  ? 101  ASN A CB  1 
ATOM   112   C  CG  . ASN A  1 14  ? 8.684   -10.949 45.156  1.00 11.51  ? 101  ASN A CG  1 
ATOM   113   O  OD1 . ASN A  1 14  ? 9.139   -10.792 44.021  1.00 12.66  ? 101  ASN A OD1 1 
ATOM   114   N  ND2 . ASN A  1 14  ? 8.325   -12.144 45.633  1.00 10.88  ? 101  ASN A ND2 1 
ATOM   115   N  N   . SER A  1 15  ? 10.215  -7.598  48.116  1.00 11.33  ? 102  SER A N   1 
ATOM   116   C  CA  . SER A  1 15  ? 10.280  -6.350  48.882  1.00 11.34  ? 102  SER A CA  1 
ATOM   117   C  C   . SER A  1 15  ? 11.348  -6.507  49.969  1.00 10.99  ? 102  SER A C   1 
ATOM   118   O  O   . SER A  1 15  ? 12.006  -7.560  50.056  1.00 10.48  ? 102  SER A O   1 
ATOM   119   C  CB  . SER A  1 15  ? 8.904   -6.019  49.497  1.00 11.21  ? 102  SER A CB  1 
ATOM   120   O  OG  . SER A  1 15  ? 8.474   -7.055  50.373  1.00 12.69  ? 102  SER A OG  1 
ATOM   121   N  N   . TRP A  1 16  ? 11.493  -5.482  50.808  1.00 10.65  ? 103  TRP A N   1 
ATOM   122   C  CA  . TRP A  1 16  ? 12.559  -5.447  51.819  1.00 10.34  ? 103  TRP A CA  1 
ATOM   123   C  C   . TRP A  1 16  ? 11.985  -5.225  53.230  1.00 10.32  ? 103  TRP A C   1 
ATOM   124   O  O   . TRP A  1 16  ? 11.186  -4.300  53.434  1.00 10.66  ? 103  TRP A O   1 
ATOM   125   C  CB  . TRP A  1 16  ? 13.587  -4.351  51.463  1.00 10.86  ? 103  TRP A CB  1 
ATOM   126   C  CG  . TRP A  1 16  ? 14.192  -4.573  50.083  1.00 9.36   ? 103  TRP A CG  1 
ATOM   127   C  CD1 . TRP A  1 16  ? 13.693  -4.142  48.879  1.00 10.76  ? 103  TRP A CD1 1 
ATOM   128   C  CD2 . TRP A  1 16  ? 15.358  -5.345  49.786  1.00 10.42  ? 103  TRP A CD2 1 
ATOM   129   N  NE1 . TRP A  1 16  ? 14.496  -4.590  47.838  1.00 11.19  ? 103  TRP A NE1 1 
ATOM   130   C  CE2 . TRP A  1 16  ? 15.520  -5.339  48.367  1.00 10.87  ? 103  TRP A CE2 1 
ATOM   131   C  CE3 . TRP A  1 16  ? 16.285  -6.053  50.576  1.00 9.29   ? 103  TRP A CE3 1 
ATOM   132   C  CZ2 . TRP A  1 16  ? 16.583  -6.000  47.730  1.00 10.25  ? 103  TRP A CZ2 1 
ATOM   133   C  CZ3 . TRP A  1 16  ? 17.343  -6.709  49.939  1.00 11.62  ? 103  TRP A CZ3 1 
ATOM   134   C  CH2 . TRP A  1 16  ? 17.490  -6.665  48.530  1.00 10.38  ? 103  TRP A CH2 1 
ATOM   135   N  N   . HIS A  1 17  ? 12.374  -6.089  54.173  1.00 9.63   ? 104  HIS A N   1 
ATOM   136   C  CA  . HIS A  1 17  ? 11.947  -5.986  55.580  1.00 9.55   ? 104  HIS A CA  1 
ATOM   137   C  C   . HIS A  1 17  ? 13.021  -5.324  56.463  1.00 9.46   ? 104  HIS A C   1 
ATOM   138   O  O   . HIS A  1 17  ? 14.211  -5.492  56.222  1.00 8.53   ? 104  HIS A O   1 
ATOM   139   C  CB  . HIS A  1 17  ? 11.519  -7.360  56.153  1.00 9.65   ? 104  HIS A CB  1 
ATOM   140   C  CG  . HIS A  1 17  ? 12.655  -8.251  56.577  1.00 10.40  ? 104  HIS A CG  1 
ATOM   141   N  ND1 . HIS A  1 17  ? 13.363  -8.057  57.746  1.00 10.01  ? 104  HIS A ND1 1 
ATOM   142   C  CD2 . HIS A  1 17  ? 13.170  -9.370  56.010  1.00 11.38  ? 104  HIS A CD2 1 
ATOM   143   C  CE1 . HIS A  1 17  ? 14.281  -9.005  57.869  1.00 12.91  ? 104  HIS A CE1 1 
ATOM   144   N  NE2 . HIS A  1 17  ? 14.190  -9.810  56.823  1.00 11.97  ? 104  HIS A NE2 1 
ATOM   145   N  N   . ILE A  1 18  ? 12.596  -4.588  57.496  1.00 9.31   ? 105  ILE A N   1 
ATOM   146   C  CA  . ILE A  1 18  ? 13.555  -3.958  58.412  1.00 8.31   ? 105  ILE A CA  1 
ATOM   147   C  C   . ILE A  1 18  ? 14.333  -5.040  59.203  1.00 8.99   ? 105  ILE A C   1 
ATOM   148   O  O   . ILE A  1 18  ? 13.726  -5.953  59.766  1.00 8.72   ? 105  ILE A O   1 
ATOM   149   C  CB  . ILE A  1 18  ? 12.855  -2.923  59.355  1.00 8.89   ? 105  ILE A CB  1 
ATOM   150   C  CG1 . ILE A  1 18  ? 13.896  -2.185  60.196  1.00 7.98   ? 105  ILE A CG1 1 
ATOM   151   C  CG2 . ILE A  1 18  ? 11.771  -3.594  60.213  1.00 7.38   ? 105  ILE A CG2 1 
ATOM   152   C  CD1 . ILE A  1 18  ? 14.776  -1.184  59.371  1.00 7.94   ? 105  ILE A CD1 1 
ATOM   153   N  N   . LEU A  1 19  ? 15.665  -4.951  59.196  1.00 8.45   ? 106  LEU A N   1 
ATOM   154   C  CA  . LEU A  1 19  ? 16.524  -5.840  59.991  1.00 8.99   ? 106  LEU A CA  1 
ATOM   155   C  C   . LEU A  1 19  ? 17.050  -5.150  61.248  1.00 9.17   ? 106  LEU A C   1 
ATOM   156   O  O   . LEU A  1 19  ? 16.961  -5.711  62.347  1.00 9.92   ? 106  LEU A O   1 
ATOM   157   C  CB  . LEU A  1 19  ? 17.707  -6.356  59.164  1.00 8.75   ? 106  LEU A CB  1 
ATOM   158   C  CG  . LEU A  1 19  ? 18.671  -7.330  59.833  1.00 9.79   ? 106  LEU A CG  1 
ATOM   159   C  CD1 . LEU A  1 19  ? 18.105  -8.772  59.783  1.00 8.53   ? 106  LEU A CD1 1 
ATOM   160   C  CD2 . LEU A  1 19  ? 20.081  -7.238  59.154  1.00 9.50   ? 106  LEU A CD2 1 
ATOM   161   N  N   . SER A  1 20  ? 17.609  -3.943  61.088  1.00 9.11   ? 107  SER A N   1 
ATOM   162   C  CA  . SER A  1 20  ? 18.174  -3.219  62.224  1.00 8.92   ? 107  SER A CA  1 
ATOM   163   C  C   . SER A  1 20  ? 18.223  -1.727  61.960  1.00 8.15   ? 107  SER A C   1 
ATOM   164   O  O   . SER A  1 20  ? 18.273  -1.294  60.805  1.00 8.55   ? 107  SER A O   1 
ATOM   165   C  CB  . SER A  1 20  ? 19.588  -3.727  62.581  1.00 9.14   ? 107  SER A CB  1 
ATOM   166   O  OG  . SER A  1 20  ? 19.935  -3.283  63.892  1.00 9.37   ? 107  SER A OG  1 
ATOM   167   N  N   . LYS A  1 21  ? 18.236  -0.950  63.043  1.00 8.24   ? 108  LYS A N   1 
ATOM   168   C  CA  . LYS A  1 21  ? 18.483  0.488   62.974  1.00 9.09   ? 108  LYS A CA  1 
ATOM   169   C  C   . LYS A  1 21  ? 19.076  0.871   64.320  1.00 8.85   ? 108  LYS A C   1 
ATOM   170   O  O   . LYS A  1 21  ? 18.573  0.415   65.361  1.00 8.90   ? 108  LYS A O   1 
ATOM   171   C  CB  . LYS A  1 21  ? 17.164  1.255   62.741  1.00 9.01   ? 108  LYS A CB  1 
ATOM   172   C  CG  . LYS A  1 21  ? 17.342  2.702   62.243  1.00 10.10  ? 108  LYS A CG  1 
ATOM   173   C  CD  . LYS A  1 21  ? 16.000  3.453   62.292  1.00 9.68   ? 108  LYS A CD  1 
ATOM   174   C  CE  . LYS A  1 21  ? 16.067  4.772   61.557  1.00 11.47  ? 108  LYS A CE  1 
ATOM   175   N  NZ  . LYS A  1 21  ? 16.916  5.735   62.310  1.00 11.41  ? 108  LYS A NZ  1 
ATOM   176   N  N   . ASP A  1 22  ? 20.151  1.658   64.317  1.00 8.69   ? 109  ASP A N   1 
ATOM   177   C  CA  . ASP A  1 22  ? 20.802  1.998   65.603  1.00 8.89   ? 109  ASP A CA  1 
ATOM   178   C  C   . ASP A  1 22  ? 20.470  3.380   66.178  1.00 8.64   ? 109  ASP A C   1 
ATOM   179   O  O   . ASP A  1 22  ? 20.737  3.647   67.359  1.00 8.86   ? 109  ASP A O   1 
ATOM   180   C  CB  . ASP A  1 22  ? 22.328  1.738   65.567  1.00 8.00   ? 109  ASP A CB  1 
ATOM   181   C  CG  . ASP A  1 22  ? 23.101  2.726   64.679  1.00 10.68  ? 109  ASP A CG  1 
ATOM   182   O  OD1 . ASP A  1 22  ? 22.483  3.518   63.937  1.00 10.14  ? 109  ASP A OD1 1 
ATOM   183   O  OD2 . ASP A  1 22  ? 24.359  2.703   64.723  1.00 11.44  ? 109  ASP A OD2 1 
ATOM   184   N  N   . ASN A  1 23  ? 19.882  4.260   65.373  1.00 8.71   ? 110  ASN A N   1 
ATOM   185   C  CA  . ASN A  1 23  ? 19.500  5.595   65.878  1.00 8.40   ? 110  ASN A CA  1 
ATOM   186   C  C   . ASN A  1 23  ? 20.646  6.299   66.608  1.00 8.63   ? 110  ASN A C   1 
ATOM   187   O  O   . ASN A  1 23  ? 20.432  6.964   67.634  1.00 7.90   ? 110  ASN A O   1 
ATOM   188   C  CB  . ASN A  1 23  ? 18.265  5.480   66.782  1.00 9.09   ? 110  ASN A CB  1 
ATOM   189   C  CG  . ASN A  1 23  ? 17.066  4.927   66.041  1.00 10.71  ? 110  ASN A CG  1 
ATOM   190   O  OD1 . ASN A  1 23  ? 16.539  5.586   65.151  1.00 10.22  ? 110  ASN A OD1 1 
ATOM   191   N  ND2 . ASN A  1 23  ? 16.657  3.699   66.377  1.00 8.25   ? 110  ASN A ND2 1 
ATOM   192   N  N   . ALA A  1 24  ? 21.855  6.152   66.062  1.00 7.72   ? 111  ALA A N   1 
ATOM   193   C  CA  . ALA A  1 24  ? 23.072  6.537   66.768  1.00 8.05   ? 111  ALA A CA  1 
ATOM   194   C  C   . ALA A  1 24  ? 23.145  8.039   67.068  1.00 8.15   ? 111  ALA A C   1 
ATOM   195   O  O   . ALA A  1 24  ? 23.589  8.435   68.152  1.00 8.22   ? 111  ALA A O   1 
ATOM   196   C  CB  . ALA A  1 24  ? 24.312  6.075   66.008  1.00 7.90   ? 111  ALA A CB  1 
ATOM   197   N  N   . ILE A  1 25  ? 22.728  8.858   66.105  1.00 8.24   ? 112  ILE A N   1 
ATOM   198   C  CA  . ILE A  1 25  ? 22.803  10.319  66.257  1.00 8.39   ? 112  ILE A CA  1 
ATOM   199   C  C   . ILE A  1 25  ? 21.754  10.830  67.271  1.00 8.48   ? 112  ILE A C   1 
ATOM   200   O  O   . ILE A  1 25  ? 22.058  11.667  68.108  1.00 8.38   ? 112  ILE A O   1 
ATOM   201   C  CB  . ILE A  1 25  ? 22.700  11.049  64.864  1.00 8.56   ? 112  ILE A CB  1 
ATOM   202   C  CG1 . ILE A  1 25  ? 23.734  10.504  63.851  1.00 8.13   ? 112  ILE A CG1 1 
ATOM   203   C  CG2 . ILE A  1 25  ? 22.788  12.623  64.998  1.00 8.16   ? 112  ILE A CG2 1 
ATOM   204   C  CD1 . ILE A  1 25  ? 25.240  10.715  64.218  1.00 9.51   ? 112  ILE A CD1 1 
ATOM   205   N  N   . ARG A  1 26  ? 20.531  10.305  67.206  1.00 8.02   ? 113  ARG A N   1 
ATOM   206   C  CA  . ARG A  1 26  ? 19.508  10.616  68.205  1.00 8.25   ? 113  ARG A CA  1 
ATOM   207   C  C   . ARG A  1 26  ? 20.017  10.356  69.633  1.00 8.03   ? 113  ARG A C   1 
ATOM   208   O  O   . ARG A  1 26  ? 19.994  11.231  70.508  1.00 8.60   ? 113  ARG A O   1 
ATOM   209   C  CB  . ARG A  1 26  ? 18.269  9.772   67.925  1.00 7.64   ? 113  ARG A CB  1 
ATOM   210   C  CG  . ARG A  1 26  ? 17.465  10.255  66.725  1.00 8.02   ? 113  ARG A CG  1 
ATOM   211   C  CD  . ARG A  1 26  ? 16.232  9.395   66.484  1.00 8.94   ? 113  ARG A CD  1 
ATOM   212   N  NE  . ARG A  1 26  ? 15.405  9.202   67.683  1.00 10.00  ? 113  ARG A NE  1 
ATOM   213   C  CZ  . ARG A  1 26  ? 14.393  9.991   68.043  1.00 9.47   ? 113  ARG A CZ  1 
ATOM   214   N  NH1 . ARG A  1 26  ? 14.077  11.063  67.308  1.00 11.41  ? 113  ARG A NH1 1 
ATOM   215   N  NH2 . ARG A  1 26  ? 13.700  9.720   69.150  1.00 10.04  ? 113  ARG A NH2 1 
ATOM   216   N  N   . ILE A  1 27  ? 20.499  9.142   69.841  1.00 8.81   ? 114  ILE A N   1 
ATOM   217   C  CA  . ILE A  1 27  ? 20.984  8.698   71.145  1.00 8.12   ? 114  ILE A CA  1 
ATOM   218   C  C   . ILE A  1 27  ? 22.236  9.477   71.540  1.00 7.92   ? 114  ILE A C   1 
ATOM   219   O  O   . ILE A  1 27  ? 22.325  9.977   72.662  1.00 8.46   ? 114  ILE A O   1 
ATOM   220   C  CB  . ILE A  1 27  ? 21.226  7.155   71.132  1.00 7.29   ? 114  ILE A CB  1 
ATOM   221   C  CG1 . ILE A  1 27  ? 19.875  6.412   71.006  1.00 7.08   ? 114  ILE A CG1 1 
ATOM   222   C  CG2 . ILE A  1 27  ? 21.994  6.701   72.392  1.00 6.64   ? 114  ILE A CG2 1 
ATOM   223   C  CD1 . ILE A  1 27  ? 20.024  4.880   70.656  1.00 8.07   ? 114  ILE A CD1 1 
ATOM   224   N  N   . GLY A  1 28  ? 23.182  9.597   70.606  1.00 8.10   ? 115  GLY A N   1 
ATOM   225   C  CA  . GLY A  1 28  ? 24.463  10.288  70.845  1.00 8.36   ? 115  GLY A CA  1 
ATOM   226   C  C   . GLY A  1 28  ? 24.389  11.786  71.126  1.00 9.27   ? 115  GLY A C   1 
ATOM   227   O  O   . GLY A  1 28  ? 25.391  12.392  71.526  1.00 9.47   ? 115  GLY A O   1 
ATOM   228   N  N   . GLU A  1 29  ? 23.205  12.379  70.942  1.00 9.83   ? 116  GLU A N   1 
ATOM   229   C  CA  . GLU A  1 29  ? 22.972  13.763  71.361  1.00 10.85  ? 116  GLU A CA  1 
ATOM   230   C  C   . GLU A  1 29  ? 23.188  13.930  72.885  1.00 11.95  ? 116  GLU A C   1 
ATOM   231   O  O   . GLU A  1 29  ? 23.513  15.042  73.359  1.00 11.40  ? 116  GLU A O   1 
ATOM   232   C  CB  . GLU A  1 29  ? 21.557  14.231  70.931  1.00 9.83   ? 116  GLU A CB  1 
ATOM   233   C  CG  . GLU A  1 29  ? 21.242  15.732  71.168  1.00 11.96  ? 116  GLU A CG  1 
ATOM   234   C  CD  . GLU A  1 29  ? 20.858  16.064  72.592  1.00 12.05  ? 116  GLU A CD  1 
ATOM   235   O  OE1 . GLU A  1 29  ? 21.189  17.176  73.039  1.00 11.97  ? 116  GLU A OE1 1 
ATOM   236   O  OE2 . GLU A  1 29  ? 20.251  15.211  73.286  1.00 13.00  ? 116  GLU A OE2 1 
ATOM   237   N  N   . ASP A  1 30  ? 23.006  12.846  73.653  1.00 13.07  ? 117  ASP A N   1 
ATOM   238   C  CA  . ASP A  1 30  ? 23.138  12.949  75.113  1.00 15.30  ? 117  ASP A CA  1 
ATOM   239   C  C   . ASP A  1 30  ? 23.769  11.724  75.796  1.00 15.63  ? 117  ASP A C   1 
ATOM   240   O  O   . ASP A  1 30  ? 23.876  11.673  77.022  1.00 19.06  ? 117  ASP A O   1 
ATOM   241   C  CB  . ASP A  1 30  ? 21.783  13.293  75.775  1.00 16.04  ? 117  ASP A CB  1 
ATOM   242   C  CG  . ASP A  1 30  ? 21.947  13.939  77.175  1.00 18.72  ? 117  ASP A CG  1 
ATOM   243   O  OD1 . ASP A  1 30  ? 20.956  14.413  77.773  1.00 23.60  ? 117  ASP A OD1 1 
ATOM   244   O  OD2 . ASP A  1 30  ? 23.077  13.994  77.688  1.00 21.04  ? 117  ASP A OD2 1 
ATOM   245   N  N   . ALA A  1 31  ? 24.152  10.726  75.021  1.00 13.75  ? 118  ALA A N   1 
ATOM   246   C  CA  . ALA A  1 31  ? 24.834  9.561   75.570  1.00 12.50  ? 118  ALA A CA  1 
ATOM   247   C  C   . ALA A  1 31  ? 26.225  9.560   74.938  1.00 11.33  ? 118  ALA A C   1 
ATOM   248   O  O   . ALA A  1 31  ? 26.468  10.317  73.998  1.00 11.68  ? 118  ALA A O   1 
ATOM   249   C  CB  . ALA A  1 31  ? 24.062  8.296   75.243  1.00 11.69  ? 118  ALA A CB  1 
ATOM   250   N  N   . HIS A  1 32  ? 27.137  8.749   75.463  1.00 10.31  ? 119  HIS A N   1 
ATOM   251   C  CA  . HIS A  1 32  ? 28.510  8.752   74.973  1.00 9.79   ? 119  HIS A CA  1 
ATOM   252   C  C   . HIS A  1 32  ? 28.594  7.849   73.741  1.00 9.39   ? 119  HIS A C   1 
ATOM   253   O  O   . HIS A  1 32  ? 28.799  6.649   73.870  1.00 9.38   ? 119  HIS A O   1 
ATOM   254   C  CB  . HIS A  1 32  ? 29.488  8.284   76.064  1.00 9.74   ? 119  HIS A CB  1 
ATOM   255   C  CG  . HIS A  1 32  ? 29.481  9.126   77.311  1.00 10.34  ? 119  HIS A CG  1 
ATOM   256   N  ND1 . HIS A  1 32  ? 29.812  8.613   78.549  1.00 10.23  ? 119  HIS A ND1 1 
ATOM   257   C  CD2 . HIS A  1 32  ? 29.197  10.438  77.510  1.00 9.60   ? 119  HIS A CD2 1 
ATOM   258   C  CE1 . HIS A  1 32  ? 29.744  9.577   79.455  1.00 10.45  ? 119  HIS A CE1 1 
ATOM   259   N  NE2 . HIS A  1 32  ? 29.380  10.695  78.853  1.00 8.61   ? 119  HIS A NE2 1 
ATOM   260   N  N   . ILE A  1 33  ? 28.430  8.433   72.553  1.00 8.38   ? 120  ILE A N   1 
ATOM   261   C  CA  . ILE A  1 33  ? 28.444  7.677   71.298  1.00 8.69   ? 120  ILE A CA  1 
ATOM   262   C  C   . ILE A  1 33  ? 29.591  8.190   70.419  1.00 8.17   ? 120  ILE A C   1 
ATOM   263   O  O   . ILE A  1 33  ? 29.758  9.409   70.233  1.00 8.45   ? 120  ILE A O   1 
ATOM   264   C  CB  . ILE A  1 33  ? 27.088  7.809   70.544  1.00 8.66   ? 120  ILE A CB  1 
ATOM   265   C  CG1 . ILE A  1 33  ? 25.924  7.324   71.444  1.00 8.57   ? 120  ILE A CG1 1 
ATOM   266   C  CG2 . ILE A  1 33  ? 27.140  7.132   69.150  1.00 7.61   ? 120  ILE A CG2 1 
ATOM   267   C  CD1 . ILE A  1 33  ? 26.011  5.816   71.834  1.00 6.23   ? 120  ILE A CD1 1 
ATOM   268   N  N   . LEU A  1 34  ? 30.363  7.246   69.895  1.00 8.52   ? 121  LEU A N   1 
ATOM   269   C  CA  . LEU A  1 34  ? 31.529  7.532   69.067  1.00 8.43   ? 121  LEU A CA  1 
ATOM   270   C  C   . LEU A  1 34  ? 31.113  8.101   67.708  1.00 8.69   ? 121  LEU A C   1 
ATOM   271   O  O   . LEU A  1 34  ? 30.121  7.649   67.116  1.00 8.71   ? 121  LEU A O   1 
ATOM   272   C  CB  . LEU A  1 34  ? 32.347  6.250   68.854  1.00 8.80   ? 121  LEU A CB  1 
ATOM   273   C  CG  . LEU A  1 34  ? 33.014  5.683   70.106  1.00 8.37   ? 121  LEU A CG  1 
ATOM   274   C  CD1 . LEU A  1 34  ? 33.536  4.270   69.800  1.00 9.48   ? 121  LEU A CD1 1 
ATOM   275   C  CD2 . LEU A  1 34  ? 34.166  6.615   70.579  1.00 9.41   ? 121  LEU A CD2 1 
ATOM   276   N  N   . VAL A  1 35  ? 31.866  9.103   67.243  1.00 8.13   ? 122  VAL A N   1 
ATOM   277   C  CA  . VAL A  1 35  ? 31.739  9.591   65.872  1.00 7.97   ? 122  VAL A CA  1 
ATOM   278   C  C   . VAL A  1 35  ? 32.256  8.503   64.933  1.00 8.21   ? 122  VAL A C   1 
ATOM   279   O  O   . VAL A  1 35  ? 33.334  7.918   65.158  1.00 8.38   ? 122  VAL A O   1 
ATOM   280   C  CB  . VAL A  1 35  ? 32.520  10.920  65.637  1.00 8.14   ? 122  VAL A CB  1 
ATOM   281   C  CG1 . VAL A  1 35  ? 32.424  11.369  64.163  1.00 6.51   ? 122  VAL A CG1 1 
ATOM   282   C  CG2 . VAL A  1 35  ? 32.014  12.014  66.556  1.00 7.26   ? 122  VAL A CG2 1 
ATOM   283   N  N   . THR A  1 36  ? 31.475  8.225   63.893  1.00 7.87   ? 123  THR A N   1 
ATOM   284   C  CA  . THR A  1 36  ? 31.839  7.237   62.897  1.00 7.39   ? 123  THR A CA  1 
ATOM   285   C  C   . THR A  1 36  ? 31.588  7.768   61.489  1.00 7.79   ? 123  THR A C   1 
ATOM   286   O  O   . THR A  1 36  ? 31.074  8.886   61.310  1.00 7.00   ? 123  THR A O   1 
ATOM   287   C  CB  . THR A  1 36  ? 31.031  5.906   63.098  1.00 7.58   ? 123  THR A CB  1 
ATOM   288   O  OG1 . THR A  1 36  ? 29.633  6.175   62.974  1.00 6.53   ? 123  THR A OG1 1 
ATOM   289   C  CG2 . THR A  1 36  ? 31.290  5.282   64.490  1.00 6.65   ? 123  THR A CG2 1 
ATOM   290   N  N   . ARG A  1 37  ? 31.962  6.943   60.507  1.00 7.69   ? 124  ARG A N   1 
ATOM   291   C  CA  . ARG A  1 37  ? 31.441  6.968   59.121  1.00 8.53   ? 124  ARG A CA  1 
ATOM   292   C  C   . ARG A  1 37  ? 31.908  5.668   58.479  1.00 8.80   ? 124  ARG A C   1 
ATOM   293   O  O   . ARG A  1 37  ? 32.597  4.879   59.135  1.00 8.21   ? 124  ARG A O   1 
ATOM   294   C  CB  . ARG A  1 37  ? 31.913  8.206   58.315  1.00 8.16   ? 124  ARG A CB  1 
ATOM   295   C  CG  . ARG A  1 37  ? 30.866  9.340   58.216  1.00 9.63   ? 124  ARG A CG  1 
ATOM   296   C  CD  . ARG A  1 37  ? 30.981  10.076  56.861  1.00 9.32   ? 124  ARG A CD  1 
ATOM   297   N  NE  . ARG A  1 37  ? 30.607  9.163   55.774  1.00 9.54   ? 124  ARG A NE  1 
ATOM   298   C  CZ  . ARG A  1 37  ? 31.113  9.172   54.536  1.00 10.31  ? 124  ARG A CZ  1 
ATOM   299   N  NH1 . ARG A  1 37  ? 30.696  8.261   53.659  1.00 9.09   ? 124  ARG A NH1 1 
ATOM   300   N  NH2 . ARG A  1 37  ? 32.040  10.050  54.165  1.00 7.51   ? 124  ARG A NH2 1 
ATOM   301   N  N   . GLU A  1 38  ? 31.527  5.453   57.217  1.00 8.64   ? 125  GLU A N   1 
ATOM   302   C  CA  . GLU A  1 38  ? 31.848  4.233   56.469  1.00 8.66   ? 125  GLU A CA  1 
ATOM   303   C  C   . GLU A  1 38  ? 31.391  2.947   57.203  1.00 8.69   ? 125  GLU A C   1 
ATOM   304   O  O   . GLU A  1 38  ? 32.198  2.034   57.425  1.00 9.27   ? 125  GLU A O   1 
ATOM   305   C  CB  . GLU A  1 38  ? 33.364  4.178   56.117  1.00 9.46   ? 125  GLU A CB  1 
ATOM   306   C  CG  . GLU A  1 38  ? 33.887  5.353   55.256  1.00 8.64   ? 125  GLU A CG  1 
ATOM   307   C  CD  . GLU A  1 38  ? 34.175  6.644   56.013  1.00 10.17  ? 125  GLU A CD  1 
ATOM   308   O  OE1 . GLU A  1 38  ? 34.080  7.708   55.374  1.00 10.53  ? 125  GLU A OE1 1 
ATOM   309   O  OE2 . GLU A  1 38  ? 34.545  6.621   57.209  1.00 8.69   ? 125  GLU A OE2 1 
ATOM   310   N  N   . PRO A  1 39  ? 30.098  2.872   57.582  1.00 8.76   ? 126  PRO A N   1 
ATOM   311   C  CA  . PRO A  1 39  ? 29.668  1.704   58.303  1.00 8.74   ? 126  PRO A CA  1 
ATOM   312   C  C   . PRO A  1 39  ? 29.340  0.516   57.388  1.00 9.14   ? 126  PRO A C   1 
ATOM   313   O  O   . PRO A  1 39  ? 29.303  0.650   56.156  1.00 9.66   ? 126  PRO A O   1 
ATOM   314   C  CB  . PRO A  1 39  ? 28.398  2.186   59.005  1.00 8.58   ? 126  PRO A CB  1 
ATOM   315   C  CG  . PRO A  1 39  ? 27.733  3.068   57.927  1.00 8.29   ? 126  PRO A CG  1 
ATOM   316   C  CD  . PRO A  1 39  ? 28.984  3.825   57.376  1.00 8.51   ? 126  PRO A CD  1 
ATOM   317   N  N   . TYR A  1 40  ? 29.106  -0.630  58.009  1.00 8.64   ? 127  TYR A N   1 
ATOM   318   C  CA  . TYR A  1 40  ? 28.548  -1.800  57.338  1.00 8.83   ? 127  TYR A CA  1 
ATOM   319   C  C   . TYR A  1 40  ? 28.094  -2.819  58.359  1.00 8.71   ? 127  TYR A C   1 
ATOM   320   O  O   . TYR A  1 40  ? 28.165  -2.544  59.566  1.00 9.86   ? 127  TYR A O   1 
ATOM   321   C  CB  . TYR A  1 40  ? 29.524  -2.420  56.326  1.00 8.05   ? 127  TYR A CB  1 
ATOM   322   C  CG  . TYR A  1 40  ? 30.944  -2.715  56.796  1.00 8.98   ? 127  TYR A CG  1 
ATOM   323   C  CD1 . TYR A  1 40  ? 31.913  -1.714  56.821  1.00 7.57   ? 127  TYR A CD1 1 
ATOM   324   C  CD2 . TYR A  1 40  ? 31.346  -4.025  57.096  1.00 7.89   ? 127  TYR A CD2 1 
ATOM   325   C  CE1 . TYR A  1 40  ? 33.228  -1.979  57.197  1.00 7.21   ? 127  TYR A CE1 1 
ATOM   326   C  CE2 . TYR A  1 40  ? 32.683  -4.307  57.460  1.00 7.63   ? 127  TYR A CE2 1 
ATOM   327   C  CZ  . TYR A  1 40  ? 33.609  -3.273  57.515  1.00 8.78   ? 127  TYR A CZ  1 
ATOM   328   O  OH  . TYR A  1 40  ? 34.929  -3.517  57.844  1.00 8.15   ? 127  TYR A OH  1 
ATOM   329   N  N   . LEU A  1 41  ? 27.580  -3.962  57.877  1.00 8.10   ? 128  LEU A N   1 
ATOM   330   C  CA  . LEU A  1 41  ? 27.289  -5.098  58.732  1.00 8.01   ? 128  LEU A CA  1 
ATOM   331   C  C   . LEU A  1 41  ? 27.993  -6.314  58.166  1.00 7.59   ? 128  LEU A C   1 
ATOM   332   O  O   . LEU A  1 41  ? 28.230  -6.413  56.940  1.00 6.94   ? 128  LEU A O   1 
ATOM   333   C  CB  . LEU A  1 41  ? 25.791  -5.420  58.807  1.00 7.64   ? 128  LEU A CB  1 
ATOM   334   C  CG  . LEU A  1 41  ? 24.610  -4.511  59.231  1.00 11.85  ? 128  LEU A CG  1 
ATOM   335   C  CD1 . LEU A  1 41  ? 23.811  -5.000  60.458  1.00 10.28  ? 128  LEU A CD1 1 
ATOM   336   C  CD2 . LEU A  1 41  ? 24.815  -3.024  59.187  1.00 11.55  ? 128  LEU A CD2 1 
ATOM   337   N  N   . SER A  1 42  ? 28.319  -7.246  59.057  1.00 7.46   ? 129  SER A N   1 
ATOM   338   C  CA  . SER A  1 42  ? 28.869  -8.535  58.643  1.00 8.59   ? 129  SER A CA  1 
ATOM   339   C  C   . SER A  1 42  ? 28.418  -9.600  59.646  1.00 8.67   ? 129  SER A C   1 
ATOM   340   O  O   . SER A  1 42  ? 28.342  -9.337  60.862  1.00 8.41   ? 129  SER A O   1 
ATOM   341   C  CB  . SER A  1 42  ? 30.417  -8.477  58.549  1.00 8.14   ? 129  SER A CB  1 
ATOM   342   O  OG  . SER A  1 42  ? 30.953  -9.737  58.112  1.00 9.96   ? 129  SER A OG  1 
ATOM   343   N  N   . CYS A  1 43  ? 28.145  -10.793 59.139  1.00 9.44   ? 130  CYS A N   1 
ATOM   344   C  CA  . CYS A  1 43  ? 27.586  -11.865 59.954  1.00 10.35  ? 130  CYS A CA  1 
ATOM   345   C  C   . CYS A  1 43  ? 28.583  -13.004 60.166  1.00 11.16  ? 130  CYS A C   1 
ATOM   346   O  O   . CYS A  1 43  ? 29.635  -13.062 59.527  1.00 10.84  ? 130  CYS A O   1 
ATOM   347   C  CB  . CYS A  1 43  ? 26.278  -12.390 59.332  1.00 10.87  ? 130  CYS A CB  1 
ATOM   348   S  SG  . CYS A  1 43  ? 25.054  -11.061 58.985  1.00 12.83  ? 130  CYS A SG  1 
ATOM   349   N  N   . ASP A  1 44  ? 28.237  -13.898 61.087  1.00 11.30  ? 131  ASP A N   1 
ATOM   350   C  CA  . ASP A  1 44  ? 29.014  -15.103 61.352  1.00 12.39  ? 131  ASP A CA  1 
ATOM   351   C  C   . ASP A  1 44  ? 28.047  -16.188 61.829  1.00 12.45  ? 131  ASP A C   1 
ATOM   352   O  O   . ASP A  1 44  ? 26.825  -15.960 61.876  1.00 12.71  ? 131  ASP A O   1 
ATOM   353   C  CB  . ASP A  1 44  ? 30.142  -14.822 62.362  1.00 12.26  ? 131  ASP A CB  1 
ATOM   354   C  CG  . ASP A  1 44  ? 29.629  -14.423 63.736  1.00 14.91  ? 131  ASP A CG  1 
ATOM   355   O  OD1 . ASP A  1 44  ? 30.349  -13.695 64.448  1.00 20.52  ? 131  ASP A OD1 1 
ATOM   356   O  OD2 . ASP A  1 44  ? 28.505  -14.806 64.116  1.00 16.01  ? 131  ASP A OD2 1 
ATOM   357   N  N   . PRO A  1 45  ? 28.556  -17.393 62.126  1.00 12.45  ? 132  PRO A N   1 
ATOM   358   C  CA  . PRO A  1 45  ? 27.620  -18.446 62.553  1.00 12.82  ? 132  PRO A CA  1 
ATOM   359   C  C   . PRO A  1 45  ? 26.686  -18.091 63.734  1.00 13.80  ? 132  PRO A C   1 
ATOM   360   O  O   . PRO A  1 45  ? 25.607  -18.694 63.853  1.00 14.99  ? 132  PRO A O   1 
ATOM   361   C  CB  . PRO A  1 45  ? 28.552  -19.619 62.908  1.00 12.23  ? 132  PRO A CB  1 
ATOM   362   C  CG  . PRO A  1 45  ? 29.754  -19.411 62.007  1.00 12.30  ? 132  PRO A CG  1 
ATOM   363   C  CD  . PRO A  1 45  ? 29.943  -17.895 62.022  1.00 12.90  ? 132  PRO A CD  1 
ATOM   364   N  N   . GLN A  1 46  ? 27.077  -17.132 64.572  1.00 13.79  ? 133  GLN A N   1 
ATOM   365   C  CA  . GLN A  1 46  ? 26.272  -16.769 65.747  1.00 15.37  ? 133  GLN A CA  1 
ATOM   366   C  C   . GLN A  1 46  ? 25.269  -15.620 65.530  1.00 15.16  ? 133  GLN A C   1 
ATOM   367   O  O   . GLN A  1 46  ? 24.276  -15.501 66.250  1.00 14.81  ? 133  GLN A O   1 
ATOM   368   C  CB  . GLN A  1 46  ? 27.173  -16.456 66.935  1.00 15.85  ? 133  GLN A CB  1 
ATOM   369   C  CG  . GLN A  1 46  ? 27.633  -17.704 67.676  1.00 21.00  ? 133  GLN A CG  1 
ATOM   370   C  CD  . GLN A  1 46  ? 28.580  -18.568 66.860  1.00 25.37  ? 133  GLN A CD  1 
ATOM   371   O  OE1 . GLN A  1 46  ? 29.606  -18.091 66.358  1.00 29.79  ? 133  GLN A OE1 1 
ATOM   372   N  NE2 . GLN A  1 46  ? 28.239  -19.858 66.717  1.00 28.72  ? 133  GLN A NE2 1 
ATOM   373   N  N   . GLY A  1 47  ? 25.514  -14.776 64.539  1.00 14.13  ? 134  GLY A N   1 
ATOM   374   C  CA  . GLY A  1 47  ? 24.613  -13.652 64.327  1.00 13.78  ? 134  GLY A CA  1 
ATOM   375   C  C   . GLY A  1 47  ? 25.227  -12.638 63.406  1.00 13.41  ? 134  GLY A C   1 
ATOM   376   O  O   . GLY A  1 47  ? 26.080  -12.982 62.565  1.00 13.58  ? 134  GLY A O   1 
ATOM   377   N  N   . CYS A  1 48  ? 24.807  -11.387 63.562  1.00 12.08  ? 135  CYS A N   1 
ATOM   378   C  CA  . CYS A  1 48  ? 25.357  -10.324 62.727  1.00 11.68  ? 135  CYS A CA  1 
ATOM   379   C  C   . CYS A  1 48  ? 25.825  -9.192  63.618  1.00 10.91  ? 135  CYS A C   1 
ATOM   380   O  O   . CYS A  1 48  ? 25.294  -8.996  64.731  1.00 10.37  ? 135  CYS A O   1 
ATOM   381   C  CB  . CYS A  1 48  ? 24.314  -9.821  61.720  1.00 11.53  ? 135  CYS A CB  1 
ATOM   382   S  SG  . CYS A  1 48  ? 23.735  -11.083 60.525  1.00 15.65  ? 135  CYS A SG  1 
ATOM   383   N  N   . ARG A  1 49  ? 26.830  -8.458  63.140  1.00 9.80   ? 136  ARG A N   1 
ATOM   384   C  CA  . ARG A  1 49  ? 27.348  -7.298  63.876  1.00 9.24   ? 136  ARG A CA  1 
ATOM   385   C  C   . ARG A  1 49  ? 27.425  -6.059  63.000  1.00 9.02   ? 136  ARG A C   1 
ATOM   386   O  O   . ARG A  1 49  ? 27.523  -6.149  61.774  1.00 8.35   ? 136  ARG A O   1 
ATOM   387   C  CB  . ARG A  1 49  ? 28.731  -7.610  64.492  1.00 9.98   ? 136  ARG A CB  1 
ATOM   388   C  CG  . ARG A  1 49  ? 28.639  -8.608  65.665  1.00 9.24   ? 136  ARG A CG  1 
ATOM   389   C  CD  . ARG A  1 49  ? 30.005  -9.143  66.055  1.00 12.39  ? 136  ARG A CD  1 
ATOM   390   N  NE  . ARG A  1 49  ? 30.925  -8.141  66.608  1.00 10.79  ? 136  ARG A NE  1 
ATOM   391   C  CZ  . ARG A  1 49  ? 30.839  -7.652  67.845  1.00 11.12  ? 136  ARG A CZ  1 
ATOM   392   N  NH1 . ARG A  1 49  ? 29.854  -8.027  68.649  1.00 10.30  ? 136  ARG A NH1 1 
ATOM   393   N  NH2 . ARG A  1 49  ? 31.730  -6.785  68.277  1.00 12.13  ? 136  ARG A NH2 1 
ATOM   394   N  N   . MET A  1 50  ? 27.356  -4.892  63.634  1.00 7.88   ? 137  MET A N   1 
ATOM   395   C  CA  . MET A  1 50  ? 27.607  -3.636  62.923  1.00 7.93   ? 137  MET A CA  1 
ATOM   396   C  C   . MET A  1 50  ? 29.090  -3.270  63.000  1.00 7.79   ? 137  MET A C   1 
ATOM   397   O  O   . MET A  1 50  ? 29.757  -3.571  63.998  1.00 7.79   ? 137  MET A O   1 
ATOM   398   C  CB  . MET A  1 50  ? 26.767  -2.516  63.526  1.00 7.16   ? 137  MET A CB  1 
ATOM   399   C  CG  . MET A  1 50  ? 25.277  -2.636  63.129  1.00 8.34   ? 137  MET A CG  1 
ATOM   400   S  SD  . MET A  1 50  ? 24.239  -1.500  64.069  1.00 8.38   ? 137  MET A SD  1 
ATOM   401   C  CE  . MET A  1 50  ? 22.789  -1.570  62.999  1.00 7.02   ? 137  MET A CE  1 
ATOM   402   N  N   . PHE A  1 51  ? 29.581  -2.636  61.940  1.00 8.43   ? 138  PHE A N   1 
ATOM   403   C  CA  . PHE A  1 51  ? 30.985  -2.210  61.781  1.00 8.14   ? 138  PHE A CA  1 
ATOM   404   C  C   . PHE A  1 51  ? 31.007  -0.759  61.321  1.00 8.16   ? 138  PHE A C   1 
ATOM   405   O  O   . PHE A  1 51  ? 30.083  -0.313  60.628  1.00 8.14   ? 138  PHE A O   1 
ATOM   406   C  CB  . PHE A  1 51  ? 31.715  -3.061  60.724  1.00 8.59   ? 138  PHE A CB  1 
ATOM   407   C  CG  . PHE A  1 51  ? 31.965  -4.482  61.146  1.00 8.77   ? 138  PHE A CG  1 
ATOM   408   C  CD1 . PHE A  1 51  ? 30.903  -5.396  61.235  1.00 9.14   ? 138  PHE A CD1 1 
ATOM   409   C  CD2 . PHE A  1 51  ? 33.264  -4.914  61.443  1.00 9.67   ? 138  PHE A CD2 1 
ATOM   410   C  CE1 . PHE A  1 51  ? 31.115  -6.716  61.627  1.00 9.66   ? 138  PHE A CE1 1 
ATOM   411   C  CE2 . PHE A  1 51  ? 33.502  -6.233  61.824  1.00 8.88   ? 138  PHE A CE2 1 
ATOM   412   C  CZ  . PHE A  1 51  ? 32.436  -7.135  61.940  1.00 10.16  ? 138  PHE A CZ  1 
ATOM   413   N  N   . ALA A  1 52  ? 32.058  -0.028  61.692  1.00 7.58   ? 139  ALA A N   1 
ATOM   414   C  CA  . ALA A  1 52  ? 32.298  1.341   61.174  1.00 7.89   ? 139  ALA A CA  1 
ATOM   415   C  C   . ALA A  1 52  ? 33.692  1.814   61.534  1.00 8.52   ? 139  ALA A C   1 
ATOM   416   O  O   . ALA A  1 52  ? 34.364  1.219   62.407  1.00 8.68   ? 139  ALA A O   1 
ATOM   417   C  CB  . ALA A  1 52  ? 31.254  2.359   61.707  1.00 7.33   ? 139  ALA A CB  1 
ATOM   418   N  N   . LEU A  1 53  ? 34.120  2.876   60.858  1.00 8.77   ? 140  LEU A N   1 
ATOM   419   C  CA  . LEU A  1 53  ? 35.369  3.557   61.198  1.00 8.39   ? 140  LEU A CA  1 
ATOM   420   C  C   . LEU A  1 53  ? 35.111  4.655   62.217  1.00 8.85   ? 140  LEU A C   1 
ATOM   421   O  O   . LEU A  1 53  ? 34.531  5.708   61.910  1.00 8.86   ? 140  LEU A O   1 
ATOM   422   C  CB  . LEU A  1 53  ? 36.089  4.111   59.948  1.00 8.35   ? 140  LEU A CB  1 
ATOM   423   C  CG  . LEU A  1 53  ? 36.458  3.056   58.886  1.00 8.20   ? 140  LEU A CG  1 
ATOM   424   C  CD1 . LEU A  1 53  ? 36.948  3.703   57.592  1.00 7.81   ? 140  LEU A CD1 1 
ATOM   425   C  CD2 . LEU A  1 53  ? 37.505  2.052   59.428  1.00 9.46   ? 140  LEU A CD2 1 
ATOM   426   N  N   . SER A  1 54  ? 35.532  4.389   63.447  1.00 8.96   ? 141  SER A N   1 
ATOM   427   C  CA  . SER A  1 54  ? 35.514  5.406   64.485  1.00 8.65   ? 141  SER A CA  1 
ATOM   428   C  C   . SER A  1 54  ? 36.457  6.560   64.108  1.00 8.58   ? 141  SER A C   1 
ATOM   429   O  O   . SER A  1 54  ? 37.418  6.371   63.340  1.00 8.10   ? 141  SER A O   1 
ATOM   430   C  CB  . SER A  1 54  ? 35.931  4.799   65.827  1.00 9.13   ? 141  SER A CB  1 
ATOM   431   O  OG  . SER A  1 54  ? 35.886  5.773   66.855  1.00 8.96   ? 141  SER A OG  1 
ATOM   432   N  N   . GLN A  1 55  ? 36.132  7.736   64.635  1.00 8.18   ? 142  GLN A N   1 
ATOM   433   C  CA  . GLN A  1 55  ? 36.988  8.933   64.595  1.00 8.87   ? 142  GLN A CA  1 
ATOM   434   C  C   . GLN A  1 55  ? 37.739  9.155   65.917  1.00 9.04   ? 142  GLN A C   1 
ATOM   435   O  O   . GLN A  1 55  ? 38.465  10.127  66.070  1.00 8.06   ? 142  GLN A O   1 
ATOM   436   C  CB  . GLN A  1 55  ? 36.156  10.149  64.215  1.00 8.59   ? 142  GLN A CB  1 
ATOM   437   C  CG  . GLN A  1 55  ? 35.658  10.166  62.744  1.00 8.02   ? 142  GLN A CG  1 
ATOM   438   C  CD  . GLN A  1 55  ? 36.719  10.647  61.747  1.00 9.67   ? 142  GLN A CD  1 
ATOM   439   O  OE1 . GLN A  1 55  ? 37.910  10.678  62.052  1.00 9.23   ? 142  GLN A OE1 1 
ATOM   440   N  NE2 . GLN A  1 55  ? 36.279  11.011  60.536  1.00 8.56   ? 142  GLN A NE2 1 
ATOM   441   N  N   . GLY A  1 56  ? 37.604  8.213   66.858  1.00 9.70   ? 143  GLY A N   1 
ATOM   442   C  CA  . GLY A  1 56  ? 38.299  8.331   68.156  1.00 9.18   ? 143  GLY A CA  1 
ATOM   443   C  C   . GLY A  1 56  ? 37.906  9.534   68.995  1.00 8.93   ? 143  GLY A C   1 
ATOM   444   O  O   . GLY A  1 56  ? 38.764  10.202  69.562  1.00 8.39   ? 143  GLY A O   1 
ATOM   445   N  N   . THR A  1 57  ? 36.596  9.795   69.065  1.00 8.83   ? 144  THR A N   1 
ATOM   446   C  CA  . THR A  1 57  ? 36.009  10.877  69.851  1.00 9.07   ? 144  THR A CA  1 
ATOM   447   C  C   . THR A  1 57  ? 34.517  10.569  69.949  1.00 9.23   ? 144  THR A C   1 
ATOM   448   O  O   . THR A  1 57  ? 33.959  9.896   69.056  1.00 8.43   ? 144  THR A O   1 
ATOM   449   C  CB  . THR A  1 57  ? 36.228  12.310  69.191  1.00 8.27   ? 144  THR A CB  1 
ATOM   450   O  OG1 . THR A  1 57  ? 35.581  13.317  69.982  1.00 10.61  ? 144  THR A OG1 1 
ATOM   451   C  CG2 . THR A  1 57  ? 35.651  12.365  67.773  1.00 8.98   ? 144  THR A CG2 1 
ATOM   452   N  N   . THR A  1 58  ? 33.875  11.073  71.007  1.00 9.28   ? 145  THR A N   1 
ATOM   453   C  CA  . THR A  1 58  ? 32.409  11.065  71.079  1.00 9.51   ? 145  THR A CA  1 
ATOM   454   C  C   . THR A  1 58  ? 31.787  12.176  70.235  1.00 9.28   ? 145  THR A C   1 
ATOM   455   O  O   . THR A  1 58  ? 32.460  13.151  69.895  1.00 8.66   ? 145  THR A O   1 
ATOM   456   C  CB  . THR A  1 58  ? 31.849  11.152  72.510  1.00 9.84   ? 145  THR A CB  1 
ATOM   457   O  OG1 . THR A  1 58  ? 32.271  12.371  73.114  1.00 10.20  ? 145  THR A OG1 1 
ATOM   458   C  CG2 . THR A  1 58  ? 32.276  9.942   73.360  1.00 10.51  ? 145  THR A CG2 1 
ATOM   459   N  N   . LEU A  1 59  ? 30.512  11.996  69.882  1.00 8.57   ? 146  LEU A N   1 
ATOM   460   C  CA  . LEU A  1 59  ? 29.764  12.949  69.059  1.00 9.51   ? 146  LEU A CA  1 
ATOM   461   C  C   . LEU A  1 59  ? 29.609  14.335  69.733  1.00 9.54   ? 146  LEU A C   1 
ATOM   462   O  O   . LEU A  1 59  ? 29.728  15.375  69.081  1.00 9.73   ? 146  LEU A O   1 
ATOM   463   C  CB  . LEU A  1 59  ? 28.378  12.365  68.725  1.00 9.20   ? 146  LEU A CB  1 
ATOM   464   C  CG  . LEU A  1 59  ? 27.485  13.145  67.742  1.00 9.56   ? 146  LEU A CG  1 
ATOM   465   C  CD1 . LEU A  1 59  ? 28.085  13.232  66.344  1.00 8.01   ? 146  LEU A CD1 1 
ATOM   466   C  CD2 . LEU A  1 59  ? 26.085  12.492  67.668  1.00 9.59   ? 146  LEU A CD2 1 
ATOM   467   N  N   . ARG A  1 60  ? 29.328  14.328  71.034  1.00 9.34   ? 147  ARG A N   1 
ATOM   468   C  CA  . ARG A  1 60  ? 29.156  15.582  71.796  1.00 8.95   ? 147  ARG A CA  1 
ATOM   469   C  C   . ARG A  1 60  ? 30.488  16.162  72.295  1.00 9.61   ? 147  ARG A C   1 
ATOM   470   O  O   . ARG A  1 60  ? 30.516  17.299  72.785  1.00 9.61   ? 147  ARG A O   1 
ATOM   471   C  CB  . ARG A  1 60  ? 28.203  15.365  72.977  1.00 8.45   ? 147  ARG A CB  1 
ATOM   472   C  CG  . ARG A  1 60  ? 26.728  15.481  72.596  1.00 8.50   ? 147  ARG A CG  1 
ATOM   473   C  CD  . ARG A  1 60  ? 26.418  16.829  71.897  1.00 7.30   ? 147  ARG A CD  1 
ATOM   474   N  NE  . ARG A  1 60  ? 25.003  17.183  72.005  1.00 8.39   ? 147  ARG A NE  1 
ATOM   475   C  CZ  . ARG A  1 60  ? 24.516  18.390  71.721  1.00 10.04  ? 147  ARG A CZ  1 
ATOM   476   N  NH1 . ARG A  1 60  ? 25.323  19.342  71.247  1.00 8.54   ? 147  ARG A NH1 1 
ATOM   477   N  NH2 . ARG A  1 60  ? 23.214  18.637  71.869  1.00 8.02   ? 147  ARG A NH2 1 
ATOM   478   N  N   . GLY A  1 61  ? 31.565  15.375  72.186  1.00 9.14   ? 148  GLY A N   1 
ATOM   479   C  CA  . GLY A  1 61  ? 32.897  15.781  72.642  1.00 9.33   ? 148  GLY A CA  1 
ATOM   480   C  C   . GLY A  1 61  ? 33.480  16.886  71.764  1.00 8.89   ? 148  GLY A C   1 
ATOM   481   O  O   . GLY A  1 61  ? 33.101  17.036  70.581  1.00 8.38   ? 148  GLY A O   1 
ATOM   482   N  N   . ARG A  1 62  ? 34.405  17.671  72.320  1.00 8.80   ? 149  ARG A N   1 
ATOM   483   C  CA  . ARG A  1 62  ? 35.007  18.771  71.537  1.00 9.76   ? 149  ARG A CA  1 
ATOM   484   C  C   . ARG A  1 62  ? 35.854  18.276  70.369  1.00 10.15  ? 149  ARG A C   1 
ATOM   485   O  O   . ARG A  1 62  ? 36.019  19.003  69.373  1.00 10.59  ? 149  ARG A O   1 
ATOM   486   C  CB  . ARG A  1 62  ? 35.797  19.750  72.433  1.00 9.18   ? 149  ARG A CB  1 
ATOM   487   C  CG  . ARG A  1 62  ? 34.879  20.520  73.348  1.00 11.62  ? 149  ARG A CG  1 
ATOM   488   C  CD  . ARG A  1 62  ? 35.620  21.355  74.364  1.00 16.18  ? 149  ARG A CD  1 
ATOM   489   N  NE  . ARG A  1 62  ? 34.678  22.250  75.048  1.00 16.45  ? 149  ARG A NE  1 
ATOM   490   C  CZ  . ARG A  1 62  ? 34.914  22.851  76.208  1.00 21.55  ? 149  ARG A CZ  1 
ATOM   491   N  NH1 . ARG A  1 62  ? 36.076  22.681  76.830  1.00 20.90  ? 149  ARG A NH1 1 
ATOM   492   N  NH2 . ARG A  1 62  ? 33.981  23.638  76.745  1.00 23.24  ? 149  ARG A NH2 1 
ATOM   493   N  N   . HIS A  1 63  ? 36.374  17.050  70.471  1.00 10.29  ? 150  HIS A N   1 
ATOM   494   C  CA  . HIS A  1 63  ? 37.166  16.459  69.384  1.00 9.76   ? 150  HIS A CA  1 
ATOM   495   C  C   . HIS A  1 63  ? 36.308  16.055  68.169  1.00 9.82   ? 150  HIS A C   1 
ATOM   496   O  O   . HIS A  1 63  ? 36.853  15.678  67.128  1.00 9.93   ? 150  HIS A O   1 
ATOM   497   C  CB  . HIS A  1 63  ? 38.069  15.304  69.875  1.00 9.92   ? 150  HIS A CB  1 
ATOM   498   C  CG  . HIS A  1 63  ? 39.039  15.707  70.955  1.00 8.87   ? 150  HIS A CG  1 
ATOM   499   N  ND1 . HIS A  1 63  ? 40.267  16.286  70.693  1.00 12.13  ? 150  HIS A ND1 1 
ATOM   500   C  CD2 . HIS A  1 63  ? 38.940  15.634  72.304  1.00 7.23   ? 150  HIS A CD2 1 
ATOM   501   C  CE1 . HIS A  1 63  ? 40.889  16.531  71.835  1.00 6.97   ? 150  HIS A CE1 1 
ATOM   502   N  NE2 . HIS A  1 63  ? 40.114  16.127  72.826  1.00 9.62   ? 150  HIS A NE2 1 
ATOM   503   N  N   . ALA A  1 64  ? 34.978  16.172  68.275  1.00 9.38   ? 151  ALA A N   1 
ATOM   504   C  CA  . ALA A  1 64  ? 34.126  15.890  67.110  1.00 9.98   ? 151  ALA A CA  1 
ATOM   505   C  C   . ALA A  1 64  ? 34.313  16.989  66.053  1.00 10.47  ? 151  ALA A C   1 
ATOM   506   O  O   . ALA A  1 64  ? 34.050  16.783  64.869  1.00 9.84   ? 151  ALA A O   1 
ATOM   507   C  CB  . ALA A  1 64  ? 32.646  15.741  67.499  1.00 9.00   ? 151  ALA A CB  1 
ATOM   508   N  N   . ASN A  1 65  ? 34.749  18.164  66.506  1.00 11.50  ? 152  ASN A N   1 
ATOM   509   C  CA  . ASN A  1 65  ? 35.095  19.260  65.604  1.00 12.37  ? 152  ASN A CA  1 
ATOM   510   C  C   . ASN A  1 65  ? 36.186  18.834  64.628  1.00 12.29  ? 152  ASN A C   1 
ATOM   511   O  O   . ASN A  1 65  ? 37.268  18.445  65.041  1.00 12.69  ? 152  ASN A O   1 
ATOM   512   C  CB  . ASN A  1 65  ? 35.501  20.481  66.451  1.00 12.32  ? 152  ASN A CB  1 
ATOM   513   C  CG  . ASN A  1 65  ? 36.017  21.650  65.633  1.00 13.97  ? 152  ASN A CG  1 
ATOM   514   O  OD1 . ASN A  1 65  ? 35.794  21.748  64.418  1.00 14.22  ? 152  ASN A OD1 1 
ATOM   515   N  ND2 . ASN A  1 65  ? 36.742  22.536  66.315  1.00 15.61  ? 152  ASN A ND2 1 
ATOM   516   N  N   . GLY A  1 66  ? 35.876  18.894  63.324  1.00 12.19  ? 153  GLY A N   1 
ATOM   517   C  CA  . GLY A  1 66  ? 36.828  18.556  62.271  1.00 11.70  ? 153  GLY A CA  1 
ATOM   518   C  C   . GLY A  1 66  ? 36.741  17.134  61.730  1.00 11.58  ? 153  GLY A C   1 
ATOM   519   O  O   . GLY A  1 66  ? 37.590  16.722  60.943  1.00 10.73  ? 153  GLY A O   1 
ATOM   520   N  N   . THR A  1 67  ? 35.699  16.393  62.122  1.00 11.23  ? 154  THR A N   1 
ATOM   521   C  CA  . THR A  1 67  ? 35.548  14.991  61.718  1.00 11.16  ? 154  THR A CA  1 
ATOM   522   C  C   . THR A  1 67  ? 35.051  14.780  60.276  1.00 11.69  ? 154  THR A C   1 
ATOM   523   O  O   . THR A  1 67  ? 34.831  13.641  59.846  1.00 11.66  ? 154  THR A O   1 
ATOM   524   C  CB  . THR A  1 67  ? 34.708  14.172  62.757  1.00 11.01  ? 154  THR A CB  1 
ATOM   525   O  OG1 . THR A  1 67  ? 33.545  14.921  63.149  1.00 10.37  ? 154  THR A OG1 1 
ATOM   526   C  CG2 . THR A  1 67  ? 35.564  13.873  63.995  1.00 10.43  ? 154  THR A CG2 1 
ATOM   527   N  N   . ILE A  1 68  ? 34.885  15.877  59.525  1.00 12.69  ? 155  ILE A N   1 
ATOM   528   C  CA  . ILE A  1 68  ? 34.754  15.788  58.069  1.00 13.16  ? 155  ILE A CA  1 
ATOM   529   C  C   . ILE A  1 68  ? 35.996  15.087  57.471  1.00 13.25  ? 155  ILE A C   1 
ATOM   530   O  O   . ILE A  1 68  ? 35.901  14.352  56.480  1.00 12.70  ? 155  ILE A O   1 
ATOM   531   C  CB  . ILE A  1 68  ? 34.536  17.212  57.412  1.00 13.65  ? 155  ILE A CB  1 
ATOM   532   C  CG1 . ILE A  1 68  ? 34.211  17.103  55.911  1.00 15.48  ? 155  ILE A CG1 1 
ATOM   533   C  CG2 . ILE A  1 68  ? 35.766  18.092  57.581  1.00 14.25  ? 155  ILE A CG2 1 
ATOM   534   C  CD1 . ILE A  1 68  ? 32.977  16.344  55.597  1.00 17.69  ? 155  ILE A CD1 1 
ATOM   535   N  N   . HIS A  1 69  ? 37.146  15.305  58.111  1.00 13.27  ? 156  HIS A N   1 
ATOM   536   C  CA  . HIS A  1 69  ? 38.430  14.792  57.653  1.00 13.44  ? 156  HIS A CA  1 
ATOM   537   C  C   . HIS A  1 69  ? 38.402  13.260  57.654  1.00 13.23  ? 156  HIS A C   1 
ATOM   538   O  O   . HIS A  1 69  ? 38.027  12.630  58.656  1.00 11.88  ? 156  HIS A O   1 
ATOM   539   C  CB  . HIS A  1 69  ? 39.535  15.366  58.543  1.00 14.84  ? 156  HIS A CB  1 
ATOM   540   C  CG  . HIS A  1 69  ? 40.923  15.158  58.018  1.00 18.87  ? 156  HIS A CG  1 
ATOM   541   N  ND1 . HIS A  1 69  ? 41.444  15.894  56.975  1.00 23.21  ? 156  HIS A ND1 1 
ATOM   542   C  CD2 . HIS A  1 69  ? 41.917  14.330  58.428  1.00 21.60  ? 156  HIS A CD2 1 
ATOM   543   C  CE1 . HIS A  1 69  ? 42.689  15.503  56.741  1.00 22.44  ? 156  HIS A CE1 1 
ATOM   544   N  NE2 . HIS A  1 69  ? 43.001  14.558  57.612  1.00 23.07  ? 156  HIS A NE2 1 
ATOM   545   N  N   . ASP A  1 70  ? 38.779  12.669  56.521  1.00 13.15  ? 157  ASP A N   1 
ATOM   546   C  CA  . ASP A  1 70  ? 38.686  11.218  56.307  1.00 13.38  ? 157  ASP A CA  1 
ATOM   547   C  C   . ASP A  1 70  ? 39.777  10.374  56.986  1.00 13.47  ? 157  ASP A C   1 
ATOM   548   O  O   . ASP A  1 70  ? 39.508  9.248   57.403  1.00 12.81  ? 157  ASP A O   1 
ATOM   549   C  CB  . ASP A  1 70  ? 38.732  10.873  54.811  1.00 13.90  ? 157  ASP A CB  1 
ATOM   550   C  CG  . ASP A  1 70  ? 37.515  11.365  54.038  1.00 16.69  ? 157  ASP A CG  1 
ATOM   551   O  OD1 . ASP A  1 70  ? 36.369  11.162  54.485  1.00 15.84  ? 157  ASP A OD1 1 
ATOM   552   O  OD2 . ASP A  1 70  ? 37.718  11.933  52.949  1.00 20.02  ? 157  ASP A OD2 1 
ATOM   553   N  N   . ARG A  1 71  ? 41.010  10.870  57.045  1.00 12.42  ? 158  ARG A N   1 
ATOM   554   C  CA  . ARG A  1 71  ? 42.105  10.009  57.479  1.00 13.24  ? 158  ARG A CA  1 
ATOM   555   C  C   . ARG A  1 71  ? 42.913  10.647  58.594  1.00 13.25  ? 158  ARG A C   1 
ATOM   556   O  O   . ARG A  1 71  ? 43.375  11.784  58.462  1.00 13.35  ? 158  ARG A O   1 
ATOM   557   C  CB  . ARG A  1 71  ? 43.030  9.644   56.293  1.00 13.08  ? 158  ARG A CB  1 
ATOM   558   C  CG  . ARG A  1 71  ? 42.372  8.809   55.187  1.00 13.30  ? 158  ARG A CG  1 
ATOM   559   C  CD  . ARG A  1 71  ? 43.287  8.677   53.960  1.00 14.06  ? 158  ARG A CD  1 
ATOM   560   N  NE  . ARG A  1 71  ? 43.553  9.990   53.361  1.00 11.66  ? 158  ARG A NE  1 
ATOM   561   C  CZ  . ARG A  1 71  ? 42.721  10.657  52.563  1.00 13.86  ? 158  ARG A CZ  1 
ATOM   562   N  NH1 . ARG A  1 71  ? 41.539  10.166  52.217  1.00 13.57  ? 158  ARG A NH1 1 
ATOM   563   N  NH2 . ARG A  1 71  ? 43.087  11.847  52.093  1.00 16.64  ? 158  ARG A NH2 1 
ATOM   564   N  N   . SER A  1 72  ? 43.087  9.912   59.695  1.00 12.47  ? 159  SER A N   1 
ATOM   565   C  CA  . SER A  1 72  ? 43.897  10.395  60.822  1.00 11.74  ? 159  SER A CA  1 
ATOM   566   C  C   . SER A  1 72  ? 44.468  9.186   61.578  1.00 10.73  ? 159  SER A C   1 
ATOM   567   O  O   . SER A  1 72  ? 43.985  8.055   61.395  1.00 10.13  ? 159  SER A O   1 
ATOM   568   C  CB  . SER A  1 72  ? 43.050  11.226  61.783  1.00 12.20  ? 159  SER A CB  1 
ATOM   569   O  OG  . SER A  1 72  ? 42.318  10.342  62.636  1.00 11.14  ? 159  SER A OG  1 
ATOM   570   N  N   . PRO A  1 73  ? 45.484  9.411   62.434  1.00 9.62   ? 160  PRO A N   1 
ATOM   571   C  CA  . PRO A  1 73  ? 45.956  8.285   63.270  1.00 9.42   ? 160  PRO A CA  1 
ATOM   572   C  C   . PRO A  1 73  ? 44.991  7.897   64.404  1.00 9.50   ? 160  PRO A C   1 
ATOM   573   O  O   . PRO A  1 73  ? 45.339  7.016   65.203  1.00 9.55   ? 160  PRO A O   1 
ATOM   574   C  CB  . PRO A  1 73  ? 47.280  8.810   63.886  1.00 8.85   ? 160  PRO A CB  1 
ATOM   575   C  CG  . PRO A  1 73  ? 47.609  10.080  63.125  1.00 9.21   ? 160  PRO A CG  1 
ATOM   576   C  CD  . PRO A  1 73  ? 46.266  10.644  62.690  1.00 9.77   ? 160  PRO A CD  1 
ATOM   577   N  N   . PHE A  1 74  ? 43.818  8.541   64.471  1.00 9.39   ? 161  PHE A N   1 
ATOM   578   C  CA  . PHE A  1 74  ? 42.845  8.352   65.596  1.00 8.90   ? 161  PHE A CA  1 
ATOM   579   C  C   . PHE A  1 74  ? 41.624  7.518   65.176  1.00 8.70   ? 161  PHE A C   1 
ATOM   580   O  O   . PHE A  1 74  ? 40.715  7.275   65.983  1.00 8.04   ? 161  PHE A O   1 
ATOM   581   C  CB  . PHE A  1 74  ? 42.429  9.706   66.187  1.00 9.28   ? 161  PHE A CB  1 
ATOM   582   C  CG  . PHE A  1 74  ? 43.531  10.720  66.149  1.00 10.80  ? 161  PHE A CG  1 
ATOM   583   C  CD1 . PHE A  1 74  ? 43.371  11.918  65.464  1.00 11.63  ? 161  PHE A CD1 1 
ATOM   584   C  CD2 . PHE A  1 74  ? 44.777  10.428  66.721  1.00 10.02  ? 161  PHE A CD2 1 
ATOM   585   C  CE1 . PHE A  1 74  ? 44.435  12.856  65.399  1.00 12.30  ? 161  PHE A CE1 1 
ATOM   586   C  CE2 . PHE A  1 74  ? 45.835  11.348  66.661  1.00 10.99  ? 161  PHE A CE2 1 
ATOM   587   C  CZ  . PHE A  1 74  ? 45.663  12.560  65.986  1.00 10.94  ? 161  PHE A CZ  1 
ATOM   588   N  N   . ARG A  1 75  ? 41.635  7.058   63.918  1.00 7.78   ? 162  ARG A N   1 
ATOM   589   C  CA  . ARG A  1 75  ? 40.574  6.187   63.398  1.00 8.28   ? 162  ARG A CA  1 
ATOM   590   C  C   . ARG A  1 75  ? 40.860  4.707   63.601  1.00 7.67   ? 162  ARG A C   1 
ATOM   591   O  O   . ARG A  1 75  ? 42.017  4.287   63.654  1.00 7.66   ? 162  ARG A O   1 
ATOM   592   C  CB  . ARG A  1 75  ? 40.305  6.483   61.900  1.00 8.54   ? 162  ARG A CB  1 
ATOM   593   C  CG  . ARG A  1 75  ? 39.930  7.935   61.623  1.00 7.68   ? 162  ARG A CG  1 
ATOM   594   C  CD  . ARG A  1 75  ? 39.112  8.083   60.323  1.00 7.25   ? 162  ARG A CD  1 
ATOM   595   N  NE  . ARG A  1 75  ? 37.703  7.725   60.518  1.00 9.30   ? 162  ARG A NE  1 
ATOM   596   C  CZ  . ARG A  1 75  ? 36.745  7.854   59.599  1.00 8.76   ? 162  ARG A CZ  1 
ATOM   597   N  NH1 . ARG A  1 75  ? 37.026  8.349   58.383  1.00 8.83   ? 162  ARG A NH1 1 
ATOM   598   N  NH2 . ARG A  1 75  ? 35.494  7.497   59.900  1.00 10.98  ? 162  ARG A NH2 1 
ATOM   599   N  N   . ALA A  1 76  ? 39.796  3.919   63.763  1.00 7.65   ? 163  ALA A N   1 
ATOM   600   C  CA  . ALA A  1 76  ? 39.906  2.452   63.876  1.00 7.18   ? 163  ALA A CA  1 
ATOM   601   C  C   . ALA A  1 76  ? 38.621  1.795   63.424  1.00 7.18   ? 163  ALA A C   1 
ATOM   602   O  O   . ALA A  1 76  ? 37.539  2.388   63.503  1.00 7.39   ? 163  ALA A O   1 
ATOM   603   C  CB  . ALA A  1 76  ? 40.218  2.024   65.335  1.00 7.34   ? 163  ALA A CB  1 
ATOM   604   N  N   . LEU A  1 77  ? 38.731  0.564   62.944  1.00 6.62   ? 164  LEU A N   1 
ATOM   605   C  CA  . LEU A  1 77  ? 37.532  -0.222  62.641  1.00 7.60   ? 164  LEU A CA  1 
ATOM   606   C  C   . LEU A  1 77  ? 37.023  -0.805  63.973  1.00 7.89   ? 164  LEU A C   1 
ATOM   607   O  O   . LEU A  1 77  ? 37.765  -1.473  64.681  1.00 8.07   ? 164  LEU A O   1 
ATOM   608   C  CB  . LEU A  1 77  ? 37.848  -1.332  61.634  1.00 7.54   ? 164  LEU A CB  1 
ATOM   609   C  CG  . LEU A  1 77  ? 36.700  -2.312  61.367  1.00 7.23   ? 164  LEU A CG  1 
ATOM   610   C  CD1 . LEU A  1 77  ? 35.485  -1.594  60.683  1.00 6.55   ? 164  LEU A CD1 1 
ATOM   611   C  CD2 . LEU A  1 77  ? 37.198  -3.553  60.554  1.00 8.02   ? 164  LEU A CD2 1 
ATOM   612   N  N   . ILE A  1 78  ? 35.779  -0.489  64.308  1.00 7.94   ? 165  ILE A N   1 
ATOM   613   C  CA  . ILE A  1 78  ? 35.110  -0.972  65.517  1.00 8.49   ? 165  ILE A CA  1 
ATOM   614   C  C   . ILE A  1 78  ? 33.904  -1.828  65.091  1.00 8.79   ? 165  ILE A C   1 
ATOM   615   O  O   . ILE A  1 78  ? 33.318  -1.593  64.025  1.00 9.09   ? 165  ILE A O   1 
ATOM   616   C  CB  . ILE A  1 78  ? 34.622  0.197   66.420  1.00 8.94   ? 165  ILE A CB  1 
ATOM   617   C  CG1 . ILE A  1 78  ? 33.847  1.262   65.615  1.00 8.64   ? 165  ILE A CG1 1 
ATOM   618   C  CG2 . ILE A  1 78  ? 35.819  0.830   67.187  1.00 9.14   ? 165  ILE A CG2 1 
ATOM   619   C  CD1 . ILE A  1 78  ? 32.889  2.180   66.488  1.00 9.10   ? 165  ILE A CD1 1 
ATOM   620   N  N   . SER A  1 79  ? 33.570  -2.837  65.891  1.00 8.70   ? 166  SER A N   1 
ATOM   621   C  CA  . SER A  1 79  ? 32.369  -3.615  65.666  1.00 8.27   ? 166  SER A CA  1 
ATOM   622   C  C   . SER A  1 79  ? 31.560  -3.676  66.958  1.00 8.08   ? 166  SER A C   1 
ATOM   623   O  O   . SER A  1 79  ? 32.101  -3.553  68.061  1.00 8.19   ? 166  SER A O   1 
ATOM   624   C  CB  . SER A  1 79  ? 32.690  -5.032  65.147  1.00 8.69   ? 166  SER A CB  1 
ATOM   625   O  OG  . SER A  1 79  ? 33.414  -5.784  66.118  1.00 8.10   ? 166  SER A OG  1 
ATOM   626   N  N   . TRP A  1 80  ? 30.264  -3.892  66.818  1.00 8.29   ? 167  TRP A N   1 
ATOM   627   C  CA  . TRP A  1 80  ? 29.401  -3.995  67.992  1.00 8.24   ? 167  TRP A CA  1 
ATOM   628   C  C   . TRP A  1 80  ? 28.136  -4.802  67.684  1.00 8.57   ? 167  TRP A C   1 
ATOM   629   O  O   . TRP A  1 80  ? 27.837  -5.074  66.527  1.00 8.89   ? 167  TRP A O   1 
ATOM   630   C  CB  . TRP A  1 80  ? 29.077  -2.586  68.520  1.00 7.79   ? 167  TRP A CB  1 
ATOM   631   C  CG  . TRP A  1 80  ? 28.276  -1.691  67.587  1.00 8.00   ? 167  TRP A CG  1 
ATOM   632   C  CD1 . TRP A  1 80  ? 26.918  -1.502  67.616  1.00 7.94   ? 167  TRP A CD1 1 
ATOM   633   C  CD2 . TRP A  1 80  ? 28.772  -0.860  66.526  1.00 8.64   ? 167  TRP A CD2 1 
ATOM   634   N  NE1 . TRP A  1 80  ? 26.537  -0.613  66.629  1.00 7.04   ? 167  TRP A NE1 1 
ATOM   635   C  CE2 . TRP A  1 80  ? 27.653  -0.190  65.960  1.00 8.07   ? 167  TRP A CE2 1 
ATOM   636   C  CE3 . TRP A  1 80  ? 30.059  -0.598  66.005  1.00 8.39   ? 167  TRP A CE3 1 
ATOM   637   C  CZ2 . TRP A  1 80  ? 27.768  0.723   64.892  1.00 7.78   ? 167  TRP A CZ2 1 
ATOM   638   C  CZ3 . TRP A  1 80  ? 30.183  0.316   64.939  1.00 8.02   ? 167  TRP A CZ3 1 
ATOM   639   C  CH2 . TRP A  1 80  ? 29.027  0.954   64.381  1.00 8.66   ? 167  TRP A CH2 1 
ATOM   640   N  N   . GLU A  1 81  ? 27.416  -5.206  68.728  1.00 9.19   ? 168  GLU A N   1 
ATOM   641   C  CA  . GLU A  1 81  ? 26.192  -6.007  68.574  1.00 9.52   ? 168  GLU A CA  1 
ATOM   642   C  C   . GLU A  1 81  ? 25.160  -5.244  67.745  1.00 9.20   ? 168  GLU A C   1 
ATOM   643   O  O   . GLU A  1 81  ? 24.867  -4.067  68.026  1.00 8.73   ? 168  GLU A O   1 
ATOM   644   C  CB  . GLU A  1 81  ? 25.629  -6.349  69.946  1.00 10.25  ? 168  GLU A CB  1 
ATOM   645   C  CG  . GLU A  1 81  ? 24.447  -7.297  69.920  1.00 13.28  ? 168  GLU A CG  1 
ATOM   646   C  CD  . GLU A  1 81  ? 24.003  -7.649  71.336  1.00 18.78  ? 168  GLU A CD  1 
ATOM   647   O  OE1 . GLU A  1 81  ? 24.797  -8.288  72.065  1.00 18.69  ? 168  GLU A OE1 1 
ATOM   648   O  OE2 . GLU A  1 81  ? 22.881  -7.254  71.723  1.00 19.66  ? 168  GLU A OE2 1 
ATOM   649   N  N   . MET A  1 82  ? 24.620  -5.918  66.732  1.00 8.62   ? 169  MET A N   1 
ATOM   650   C  CA  . MET A  1 82  ? 23.714  -5.287  65.775  1.00 9.67   ? 169  MET A CA  1 
ATOM   651   C  C   . MET A  1 82  ? 22.564  -4.590  66.505  1.00 8.65   ? 169  MET A C   1 
ATOM   652   O  O   . MET A  1 82  ? 21.926  -5.187  67.384  1.00 8.67   ? 169  MET A O   1 
ATOM   653   C  CB  . MET A  1 82  ? 23.176  -6.332  64.790  1.00 8.65   ? 169  MET A CB  1 
ATOM   654   C  CG  . MET A  1 82  ? 22.222  -5.775  63.746  1.00 8.57   ? 169  MET A CG  1 
ATOM   655   S  SD  . MET A  1 82  ? 21.666  -7.057  62.574  1.00 11.68  ? 169  MET A SD  1 
ATOM   656   C  CE  . MET A  1 82  ? 20.540  -7.997  63.585  1.00 10.78  ? 169  MET A CE  1 
ATOM   657   N  N   . GLY A  1 83  ? 22.324  -3.326  66.158  1.00 9.36   ? 170  GLY A N   1 
ATOM   658   C  CA  . GLY A  1 83  ? 21.172  -2.574  66.704  1.00 9.60   ? 170  GLY A CA  1 
ATOM   659   C  C   . GLY A  1 83  ? 21.514  -1.620  67.827  1.00 9.71   ? 170  GLY A C   1 
ATOM   660   O  O   . GLY A  1 83  ? 20.898  -0.549  67.937  1.00 10.34  ? 170  GLY A O   1 
ATOM   661   N  N   . GLN A  1 84  ? 22.509  -1.978  68.645  1.00 9.89   ? 171  GLN A N   1 
ATOM   662   C  CA  . GLN A  1 84  ? 23.039  -1.017  69.609  1.00 10.19  ? 171  GLN A CA  1 
ATOM   663   C  C   . GLN A  1 84  ? 23.689  0.156   68.868  1.00 8.95   ? 171  GLN A C   1 
ATOM   664   O  O   . GLN A  1 84  ? 24.064  0.038   67.687  1.00 8.73   ? 171  GLN A O   1 
ATOM   665   C  CB  . GLN A  1 84  ? 24.057  -1.646  70.572  1.00 9.13   ? 171  GLN A CB  1 
ATOM   666   C  CG  . GLN A  1 84  ? 23.479  -2.669  71.569  1.00 11.92  ? 171  GLN A CG  1 
ATOM   667   C  CD  . GLN A  1 84  ? 24.558  -3.468  72.273  1.00 13.44  ? 171  GLN A CD  1 
ATOM   668   O  OE1 . GLN A  1 84  ? 25.741  -3.103  72.258  1.00 13.22  ? 171  GLN A OE1 1 
ATOM   669   N  NE2 . GLN A  1 84  ? 24.164  -4.598  72.867  1.00 18.97  ? 171  GLN A NE2 1 
ATOM   670   N  N   . ALA A  1 85  ? 23.821  1.291   69.552  1.00 9.27   ? 172  ALA A N   1 
ATOM   671   C  CA  . ALA A  1 85  ? 24.640  2.381   69.006  1.00 8.67   ? 172  ALA A CA  1 
ATOM   672   C  C   . ALA A  1 85  ? 26.101  2.203   69.466  1.00 8.90   ? 172  ALA A C   1 
ATOM   673   O  O   . ALA A  1 85  ? 26.356  1.586   70.510  1.00 9.31   ? 172  ALA A O   1 
ATOM   674   C  CB  . ALA A  1 85  ? 24.089  3.738   69.413  1.00 8.31   ? 172  ALA A CB  1 
ATOM   675   N  N   . PRO A  1 86  ? 27.072  2.724   68.678  1.00 8.74   ? 173  PRO A N   1 
ATOM   676   C  CA  . PRO A  1 86  ? 28.481  2.495   69.044  1.00 8.03   ? 173  PRO A CA  1 
ATOM   677   C  C   . PRO A  1 86  ? 28.988  3.431   70.144  1.00 7.97   ? 173  PRO A C   1 
ATOM   678   O  O   . PRO A  1 86  ? 29.070  4.634   69.926  1.00 7.74   ? 173  PRO A O   1 
ATOM   679   C  CB  . PRO A  1 86  ? 29.229  2.698   67.720  1.00 8.13   ? 173  PRO A CB  1 
ATOM   680   C  CG  . PRO A  1 86  ? 28.361  3.647   66.927  1.00 8.29   ? 173  PRO A CG  1 
ATOM   681   C  CD  . PRO A  1 86  ? 26.930  3.438   67.387  1.00 9.03   ? 173  PRO A CD  1 
ATOM   682   N  N   . SER A  1 87  ? 29.297  2.882   71.316  1.00 8.02   ? 174  SER A N   1 
ATOM   683   C  CA  . SER A  1 87  ? 29.841  3.693   72.415  1.00 7.97   ? 174  SER A CA  1 
ATOM   684   C  C   . SER A  1 87  ? 31.268  3.214   72.716  1.00 7.67   ? 174  SER A C   1 
ATOM   685   O  O   . SER A  1 87  ? 31.694  2.180   72.173  1.00 7.35   ? 174  SER A O   1 
ATOM   686   C  CB  . SER A  1 87  ? 28.952  3.572   73.659  1.00 8.06   ? 174  SER A CB  1 
ATOM   687   O  OG  . SER A  1 87  ? 29.150  2.320   74.301  1.00 9.55   ? 174  SER A OG  1 
ATOM   688   N  N   . PRO A  1 88  ? 32.015  3.955   73.555  1.00 8.14   ? 175  PRO A N   1 
ATOM   689   C  CA  . PRO A  1 88  ? 33.329  3.478   73.997  1.00 8.75   ? 175  PRO A CA  1 
ATOM   690   C  C   . PRO A  1 88  ? 33.255  2.228   74.872  1.00 8.66   ? 175  PRO A C   1 
ATOM   691   O  O   . PRO A  1 88  ? 34.276  1.638   75.162  1.00 9.99   ? 175  PRO A O   1 
ATOM   692   C  CB  . PRO A  1 88  ? 33.869  4.636   74.853  1.00 8.43   ? 175  PRO A CB  1 
ATOM   693   C  CG  . PRO A  1 88  ? 33.083  5.838   74.422  1.00 9.02   ? 175  PRO A CG  1 
ATOM   694   C  CD  . PRO A  1 88  ? 31.722  5.308   74.085  1.00 8.95   ? 175  PRO A CD  1 
ATOM   695   N  N   . TYR A  1 89  ? 32.057  1.865   75.300  1.00 8.78   ? 176  TYR A N   1 
ATOM   696   C  CA  . TYR A  1 89  ? 31.869  0.813   76.287  1.00 9.38   ? 176  TYR A CA  1 
ATOM   697   C  C   . TYR A  1 89  ? 31.380  -0.506  75.674  1.00 9.67   ? 176  TYR A C   1 
ATOM   698   O  O   . TYR A  1 89  ? 31.444  -1.548  76.340  1.00 10.59  ? 176  TYR A O   1 
ATOM   699   C  CB  . TYR A  1 89  ? 30.898  1.279   77.386  1.00 8.71   ? 176  TYR A CB  1 
ATOM   700   C  CG  . TYR A  1 89  ? 31.081  2.735   77.858  1.00 8.91   ? 176  TYR A CG  1 
ATOM   701   C  CD1 . TYR A  1 89  ? 30.004  3.628   77.857  1.00 6.44   ? 176  TYR A CD1 1 
ATOM   702   C  CD2 . TYR A  1 89  ? 32.329  3.208   78.300  1.00 7.62   ? 176  TYR A CD2 1 
ATOM   703   C  CE1 . TYR A  1 89  ? 30.160  4.977   78.282  1.00 8.29   ? 176  TYR A CE1 1 
ATOM   704   C  CE2 . TYR A  1 89  ? 32.489  4.547   78.732  1.00 8.83   ? 176  TYR A CE2 1 
ATOM   705   C  CZ  . TYR A  1 89  ? 31.412  5.420   78.709  1.00 8.70   ? 176  TYR A CZ  1 
ATOM   706   O  OH  . TYR A  1 89  ? 31.585  6.733   79.142  1.00 8.55   ? 176  TYR A OH  1 
ATOM   707   N  N   . ASN A  1 90  ? 30.871  -0.477  74.437  1.00 9.55   ? 177  ASN A N   1 
ATOM   708   C  CA  . ASN A  1 90  ? 30.302  -1.710  73.835  1.00 9.36   ? 177  ASN A CA  1 
ATOM   709   C  C   . ASN A  1 90  ? 30.917  -2.107  72.491  1.00 9.36   ? 177  ASN A C   1 
ATOM   710   O  O   . ASN A  1 90  ? 30.363  -2.944  71.774  1.00 9.06   ? 177  ASN A O   1 
ATOM   711   C  CB  . ASN A  1 90  ? 28.776  -1.581  73.681  1.00 9.26   ? 177  ASN A CB  1 
ATOM   712   C  CG  . ASN A  1 90  ? 28.389  -0.670  72.516  1.00 10.28  ? 177  ASN A CG  1 
ATOM   713   O  OD1 . ASN A  1 90  ? 29.087  0.309   72.246  1.00 9.39   ? 177  ASN A OD1 1 
ATOM   714   N  ND2 . ASN A  1 90  ? 27.313  -1.018  71.797  1.00 8.98   ? 177  ASN A ND2 1 
ATOM   715   N  N   . THR A  1 91  ? 32.050  -1.504  72.151  1.00 9.06   ? 178  THR A N   1 
ATOM   716   C  CA  . THR A  1 91  ? 32.635  -1.671  70.833  1.00 9.48   ? 178  THR A CA  1 
ATOM   717   C  C   . THR A  1 91  ? 33.955  -2.427  70.887  1.00 10.04  ? 178  THR A C   1 
ATOM   718   O  O   . THR A  1 91  ? 34.765  -2.231  71.799  1.00 10.86  ? 178  THR A O   1 
ATOM   719   C  CB  . THR A  1 91  ? 32.857  -0.319  70.113  1.00 9.28   ? 178  THR A CB  1 
ATOM   720   O  OG1 . THR A  1 91  ? 33.473  0.621   71.017  1.00 9.86   ? 178  THR A OG1 1 
ATOM   721   C  CG2 . THR A  1 91  ? 31.532  0.230   69.537  1.00 8.55   ? 178  THR A CG2 1 
ATOM   722   N  N   . ARG A  1 92  ? 34.177  -3.273  69.892  1.00 9.75   ? 179  ARG A N   1 
ATOM   723   C  CA  . ARG A  1 92  ? 35.418  -4.027  69.771  1.00 11.04  ? 179  ARG A CA  1 
ATOM   724   C  C   . ARG A  1 92  ? 36.294  -3.393  68.685  1.00 10.64  ? 179  ARG A C   1 
ATOM   725   O  O   . ARG A  1 92  ? 35.826  -3.209  67.552  1.00 10.26  ? 179  ARG A O   1 
ATOM   726   C  CB  . ARG A  1 92  ? 35.083  -5.481  69.406  1.00 11.23  ? 179  ARG A CB  1 
ATOM   727   C  CG  . ARG A  1 92  ? 36.283  -6.351  69.026  1.00 12.01  ? 179  ARG A CG  1 
ATOM   728   C  CD  . ARG A  1 92  ? 35.835  -7.772  68.658  1.00 14.53  ? 179  ARG A CD  1 
ATOM   729   N  NE  . ARG A  1 92  ? 35.003  -8.389  69.696  1.00 23.15  ? 179  ARG A NE  1 
ATOM   730   C  CZ  . ARG A  1 92  ? 34.055  -9.306  69.482  1.00 25.38  ? 179  ARG A CZ  1 
ATOM   731   N  NH1 . ARG A  1 92  ? 33.793  -9.755  68.260  1.00 26.49  ? 179  ARG A NH1 1 
ATOM   732   N  NH2 . ARG A  1 92  ? 33.357  -9.784  70.503  1.00 29.58  ? 179  ARG A NH2 1 
ATOM   733   N  N   . VAL A  1 93  ? 37.557  -3.090  69.012  1.00 10.30  ? 180  VAL A N   1 
ATOM   734   C  CA  . VAL A  1 93  ? 38.503  -2.611  67.990  1.00 10.08  ? 180  VAL A CA  1 
ATOM   735   C  C   . VAL A  1 93  ? 39.001  -3.805  67.182  1.00 10.65  ? 180  VAL A C   1 
ATOM   736   O  O   . VAL A  1 93  ? 39.640  -4.729  67.725  1.00 10.29  ? 180  VAL A O   1 
ATOM   737   C  CB  . VAL A  1 93  ? 39.689  -1.786  68.574  1.00 10.49  ? 180  VAL A CB  1 
ATOM   738   C  CG1 . VAL A  1 93  ? 40.621  -1.272  67.435  1.00 8.66   ? 180  VAL A CG1 1 
ATOM   739   C  CG2 . VAL A  1 93  ? 39.165  -0.614  69.393  1.00 10.61  ? 180  VAL A CG2 1 
ATOM   740   N  N   . GLU A  1 94  ? 38.638  -3.797  65.903  1.00 10.37  ? 181  GLU A N   1 
ATOM   741   C  CA  . GLU A  1 94  ? 39.008  -4.835  64.951  1.00 10.25  ? 181  GLU A CA  1 
ATOM   742   C  C   . GLU A  1 94  ? 40.429  -4.640  64.429  1.00 9.95   ? 181  GLU A C   1 
ATOM   743   O  O   . GLU A  1 94  ? 41.149  -5.614  64.221  1.00 10.13  ? 181  GLU A O   1 
ATOM   744   C  CB  . GLU A  1 94  ? 38.039  -4.829  63.746  1.00 10.29  ? 181  GLU A CB  1 
ATOM   745   C  CG  . GLU A  1 94  ? 36.579  -5.246  64.079  1.00 10.92  ? 181  GLU A CG  1 
ATOM   746   C  CD  . GLU A  1 94  ? 36.411  -6.743  64.372  1.00 12.88  ? 181  GLU A CD  1 
ATOM   747   O  OE1 . GLU A  1 94  ? 37.139  -7.566  63.767  1.00 11.46  ? 181  GLU A OE1 1 
ATOM   748   O  OE2 . GLU A  1 94  ? 35.500  -7.095  65.166  1.00 12.52  ? 181  GLU A OE2 1 
ATOM   749   N  N   . CYS A  1 95  ? 40.777  -3.384  64.151  1.00 8.95   ? 182  CYS A N   1 
ATOM   750   C  CA  . CYS A  1 95  ? 42.081  -3.000  63.634  1.00 9.23   ? 182  CYS A CA  1 
ATOM   751   C  C   . CYS A  1 95  ? 42.173  -1.472  63.625  1.00 9.53   ? 182  CYS A C   1 
ATOM   752   O  O   . CYS A  1 95  ? 41.145  -0.780  63.801  1.00 8.91   ? 182  CYS A O   1 
ATOM   753   C  CB  . CYS A  1 95  ? 42.397  -3.651  62.261  1.00 9.46   ? 182  CYS A CB  1 
ATOM   754   S  SG  . CYS A  1 95  ? 41.078  -3.627  61.019  1.00 11.22  ? 182  CYS A SG  1 
ATOM   755   N  N   . ILE A  1 96  ? 43.392  -0.955  63.441  1.00 8.99   ? 183  ILE A N   1 
ATOM   756   C  CA  . ILE A  1 96  ? 43.628  0.496   63.422  1.00 8.53   ? 183  ILE A CA  1 
ATOM   757   C  C   . ILE A  1 96  ? 43.783  1.025   62.010  1.00 8.83   ? 183  ILE A C   1 
ATOM   758   O  O   . ILE A  1 96  ? 44.603  0.524   61.236  1.00 9.40   ? 183  ILE A O   1 
ATOM   759   C  CB  . ILE A  1 96  ? 44.865  0.888   64.296  1.00 8.36   ? 183  ILE A CB  1 
ATOM   760   C  CG1 . ILE A  1 96  ? 44.793  0.184   65.678  1.00 8.76   ? 183  ILE A CG1 1 
ATOM   761   C  CG2 . ILE A  1 96  ? 45.039  2.422   64.367  1.00 8.93   ? 183  ILE A CG2 1 
ATOM   762   C  CD1 . ILE A  1 96  ? 43.540  0.555   66.524  1.00 7.80   ? 183  ILE A CD1 1 
ATOM   763   N  N   . GLY A  1 97  ? 43.002  2.055   61.682  1.00 9.26   ? 184  GLY A N   1 
ATOM   764   C  CA  . GLY A  1 97  ? 43.125  2.704   60.382  1.00 9.71   ? 184  GLY A CA  1 
ATOM   765   C  C   . GLY A  1 97  ? 41.870  3.392   59.878  1.00 9.19   ? 184  GLY A C   1 
ATOM   766   O  O   . GLY A  1 97  ? 40.886  3.575   60.628  1.00 7.58   ? 184  GLY A O   1 
ATOM   767   N  N   . TRP A  1 98  ? 41.908  3.756   58.593  1.00 8.79   ? 185  TRP A N   1 
ATOM   768   C  CA  . TRP A  1 98  ? 40.921  4.643   57.993  1.00 9.11   ? 185  TRP A CA  1 
ATOM   769   C  C   . TRP A  1 98  ? 40.281  4.140   56.694  1.00 9.13   ? 185  TRP A C   1 
ATOM   770   O  O   . TRP A  1 98  ? 39.627  4.910   55.991  1.00 9.10   ? 185  TRP A O   1 
ATOM   771   C  CB  . TRP A  1 98  ? 41.500  6.079   57.816  1.00 9.25   ? 185  TRP A CB  1 
ATOM   772   C  CG  . TRP A  1 98  ? 42.962  6.139   57.287  1.00 9.50   ? 185  TRP A CG  1 
ATOM   773   C  CD1 . TRP A  1 98  ? 44.041  6.645   57.943  1.00 8.81   ? 185  TRP A CD1 1 
ATOM   774   C  CD2 . TRP A  1 98  ? 43.444  5.688   56.004  1.00 9.16   ? 185  TRP A CD2 1 
ATOM   775   N  NE1 . TRP A  1 98  ? 45.176  6.536   57.155  1.00 9.00   ? 185  TRP A NE1 1 
ATOM   776   C  CE2 . TRP A  1 98  ? 44.838  5.955   55.964  1.00 9.38   ? 185  TRP A CE2 1 
ATOM   777   C  CE3 . TRP A  1 98  ? 42.834  5.086   54.886  1.00 7.82   ? 185  TRP A CE3 1 
ATOM   778   C  CZ2 . TRP A  1 98  ? 45.644  5.646   54.834  1.00 10.54  ? 185  TRP A CZ2 1 
ATOM   779   C  CZ3 . TRP A  1 98  ? 43.640  4.772   53.755  1.00 9.66   ? 185  TRP A CZ3 1 
ATOM   780   C  CH2 . TRP A  1 98  ? 45.024  5.053   53.752  1.00 8.77   ? 185  TRP A CH2 1 
ATOM   781   N  N   . SER A  1 99  ? 40.462  2.854   56.393  1.00 8.78   ? 186  SER A N   1 
ATOM   782   C  CA  . SER A  1 99  ? 39.729  2.168   55.339  1.00 9.39   ? 186  SER A CA  1 
ATOM   783   C  C   . SER A  1 99  ? 39.720  0.695   55.763  1.00 8.75   ? 186  SER A C   1 
ATOM   784   O  O   . SER A  1 99  ? 40.713  0.224   56.343  1.00 9.82   ? 186  SER A O   1 
ATOM   785   C  CB  . SER A  1 99  ? 40.441  2.369   53.977  1.00 8.21   ? 186  SER A CB  1 
ATOM   786   O  OG  . SER A  1 99  ? 39.787  1.656   52.947  1.00 8.88   ? 186  SER A OG  1 
ATOM   787   N  N   . SER A  1 100 ? 38.619  -0.036  55.536  1.00 8.83   ? 187  SER A N   1 
ATOM   788   C  CA  . SER A  1 100 ? 38.536  -1.407  56.051  1.00 8.60   ? 187  SER A CA  1 
ATOM   789   C  C   . SER A  1 100 ? 37.660  -2.354  55.234  1.00 8.14   ? 187  SER A C   1 
ATOM   790   O  O   . SER A  1 100 ? 36.849  -1.930  54.404  1.00 8.23   ? 187  SER A O   1 
ATOM   791   C  CB  . SER A  1 100 ? 38.021  -1.416  57.520  1.00 8.55   ? 187  SER A CB  1 
ATOM   792   O  OG  . SER A  1 100 ? 36.595  -1.292  57.577  1.00 8.73   ? 187  SER A OG  1 
ATOM   793   N  N   . THR A  1 101 ? 37.812  -3.641  55.515  1.00 8.14   ? 188  THR A N   1 
ATOM   794   C  CA  . THR A  1 101 ? 36.822  -4.631  55.170  1.00 8.07   ? 188  THR A CA  1 
ATOM   795   C  C   . THR A  1 101 ? 36.913  -5.712  56.261  1.00 8.47   ? 188  THR A C   1 
ATOM   796   O  O   . THR A  1 101 ? 37.871  -5.728  57.067  1.00 9.09   ? 188  THR A O   1 
ATOM   797   C  CB  . THR A  1 101 ? 37.070  -5.254  53.747  1.00 8.73   ? 188  THR A CB  1 
ATOM   798   O  OG1 . THR A  1 101 ? 35.988  -6.148  53.390  1.00 7.77   ? 188  THR A OG1 1 
ATOM   799   C  CG2 . THR A  1 101 ? 38.381  -6.053  53.719  1.00 8.31   ? 188  THR A CG2 1 
ATOM   800   N  N   . SER A  1 102 ? 35.934  -6.607  56.282  1.00 7.77   ? 189  SER A N   1 
ATOM   801   C  CA  . SER A  1 102 ? 35.906  -7.711  57.245  1.00 7.76   ? 189  SER A CA  1 
ATOM   802   C  C   . SER A  1 102 ? 34.938  -8.785  56.756  1.00 8.24   ? 189  SER A C   1 
ATOM   803   O  O   . SER A  1 102 ? 33.951  -8.465  56.092  1.00 8.17   ? 189  SER A O   1 
ATOM   804   C  CB  . SER A  1 102 ? 35.482  -7.216  58.644  1.00 7.55   ? 189  SER A CB  1 
ATOM   805   O  OG  . SER A  1 102 ? 35.578  -8.248  59.612  1.00 7.28   ? 189  SER A OG  1 
ATOM   806   N  N   . CYS A  1 103 ? 35.229  -10.046 57.082  1.00 8.41   ? 190  CYS A N   1 
ATOM   807   C  CA  . CYS A  1 103 ? 34.343  -11.166 56.753  1.00 9.18   ? 190  CYS A CA  1 
ATOM   808   C  C   . CYS A  1 103 ? 34.723  -12.400 57.552  1.00 8.92   ? 190  CYS A C   1 
ATOM   809   O  O   . CYS A  1 103 ? 35.869  -12.545 57.979  1.00 9.76   ? 190  CYS A O   1 
ATOM   810   C  CB  . CYS A  1 103 ? 34.338  -11.462 55.248  1.00 9.43   ? 190  CYS A CB  1 
ATOM   811   S  SG  . CYS A  1 103 ? 35.991  -11.595 54.432  1.00 10.91  ? 190  CYS A SG  1 
ATOM   812   N  N   . HIS A  1 104 ? 33.744  -13.266 57.781  1.00 9.63   ? 191  HIS A N   1 
ATOM   813   C  CA  . HIS A  1 104 ? 33.938  -14.486 58.541  1.00 9.07   ? 191  HIS A CA  1 
ATOM   814   C  C   . HIS A  1 104 ? 33.962  -15.649 57.547  1.00 10.04  ? 191  HIS A C   1 
ATOM   815   O  O   . HIS A  1 104 ? 33.115  -15.736 56.651  1.00 9.81   ? 191  HIS A O   1 
ATOM   816   C  CB  . HIS A  1 104 ? 32.796  -14.658 59.550  1.00 9.35   ? 191  HIS A CB  1 
ATOM   817   C  CG  . HIS A  1 104 ? 33.126  -15.572 60.690  1.00 8.33   ? 191  HIS A CG  1 
ATOM   818   N  ND1 . HIS A  1 104 ? 33.077  -16.949 60.580  1.00 9.89   ? 191  HIS A ND1 1 
ATOM   819   C  CD2 . HIS A  1 104 ? 33.491  -15.308 61.971  1.00 7.80   ? 191  HIS A CD2 1 
ATOM   820   C  CE1 . HIS A  1 104 ? 33.407  -17.491 61.741  1.00 9.49   ? 191  HIS A CE1 1 
ATOM   821   N  NE2 . HIS A  1 104 ? 33.658  -16.517 62.604  1.00 9.24   ? 191  HIS A NE2 1 
ATOM   822   N  N   . ASP A  1 105 ? 34.947  -16.534 57.678  1.00 10.28  ? 192  ASP A N   1 
ATOM   823   C  CA  . ASP A  1 105 ? 35.059  -17.655 56.736  1.00 10.84  ? 192  ASP A CA  1 
ATOM   824   C  C   . ASP A  1 105 ? 34.315  -18.913 57.192  1.00 10.93  ? 192  ASP A C   1 
ATOM   825   O  O   . ASP A  1 105 ? 34.444  -19.985 56.563  1.00 11.75  ? 192  ASP A O   1 
ATOM   826   C  CB  . ASP A  1 105 ? 36.541  -17.947 56.417  1.00 10.82  ? 192  ASP A CB  1 
ATOM   827   C  CG  . ASP A  1 105 ? 37.319  -18.494 57.615  1.00 11.67  ? 192  ASP A CG  1 
ATOM   828   O  OD1 . ASP A  1 105 ? 36.707  -18.926 58.625  1.00 10.41  ? 192  ASP A OD1 1 
ATOM   829   O  OD2 . ASP A  1 105 ? 38.563  -18.517 57.518  1.00 12.03  ? 192  ASP A OD2 1 
ATOM   830   N  N   . GLY A  1 106 ? 33.544  -18.783 58.277  1.00 11.08  ? 193  GLY A N   1 
ATOM   831   C  CA  . GLY A  1 106 ? 32.892  -19.921 58.940  1.00 11.42  ? 193  GLY A CA  1 
ATOM   832   C  C   . GLY A  1 106 ? 33.633  -20.386 60.188  1.00 11.98  ? 193  GLY A C   1 
ATOM   833   O  O   . GLY A  1 106 ? 33.019  -20.948 61.109  1.00 13.35  ? 193  GLY A O   1 
ATOM   834   N  N   . MET A  1 107 ? 34.950  -20.195 60.196  1.00 11.63  ? 194  MET A N   1 
ATOM   835   C  CA  . MET A  1 107 ? 35.818  -20.589 61.316  1.00 11.95  ? 194  MET A CA  1 
ATOM   836   C  C   . MET A  1 107 ? 36.172  -19.385 62.189  1.00 11.50  ? 194  MET A C   1 
ATOM   837   O  O   . MET A  1 107 ? 35.924  -19.399 63.410  1.00 12.17  ? 194  MET A O   1 
ATOM   838   C  CB  . MET A  1 107 ? 37.117  -21.225 60.803  1.00 11.95  ? 194  MET A CB  1 
ATOM   839   C  CG  . MET A  1 107 ? 36.930  -22.528 59.992  1.00 15.02  ? 194  MET A CG  1 
ATOM   840   S  SD  . MET A  1 107 ? 36.047  -23.774 60.931  1.00 22.84  ? 194  MET A SD  1 
ATOM   841   C  CE  . MET A  1 107 ? 37.333  -24.327 62.046  1.00 20.51  ? 194  MET A CE  1 
ATOM   842   N  N   . SER A  1 108 ? 36.765  -18.368 61.557  1.00 10.40  ? 195  SER A N   1 
ATOM   843   C  CA  . SER A  1 108 ? 37.144  -17.110 62.223  1.00 10.92  ? 195  SER A CA  1 
ATOM   844   C  C   . SER A  1 108 ? 36.890  -15.889 61.339  1.00 10.64  ? 195  SER A C   1 
ATOM   845   O  O   . SER A  1 108 ? 36.679  -16.011 60.118  1.00 11.40  ? 195  SER A O   1 
ATOM   846   C  CB  . SER A  1 108 ? 38.636  -17.137 62.624  1.00 10.46  ? 195  SER A CB  1 
ATOM   847   O  OG  . SER A  1 108 ? 38.863  -18.134 63.592  1.00 13.77  ? 195  SER A OG  1 
ATOM   848   N  N   . ARG A  1 109 ? 36.933  -14.712 61.958  1.00 10.73  ? 196  ARG A N   1 
ATOM   849   C  CA  . ARG A  1 109 ? 36.785  -13.449 61.240  1.00 10.09  ? 196  ARG A CA  1 
ATOM   850   C  C   . ARG A  1 109 ? 38.123  -12.885 60.766  1.00 10.33  ? 196  ARG A C   1 
ATOM   851   O  O   . ARG A  1 109 ? 39.093  -12.832 61.534  1.00 10.28  ? 196  ARG A O   1 
ATOM   852   C  CB  . ARG A  1 109 ? 36.066  -12.418 62.127  1.00 9.84   ? 196  ARG A CB  1 
ATOM   853   C  CG  . ARG A  1 109 ? 35.948  -11.022 61.476  1.00 8.53   ? 196  ARG A CG  1 
ATOM   854   C  CD  . ARG A  1 109 ? 34.870  -10.187 62.192  1.00 10.14  ? 196  ARG A CD  1 
ATOM   855   N  NE  . ARG A  1 109 ? 33.529  -10.750 61.960  1.00 9.97   ? 196  ARG A NE  1 
ATOM   856   C  CZ  . ARG A  1 109 ? 32.837  -10.664 60.820  1.00 10.34  ? 196  ARG A CZ  1 
ATOM   857   N  NH1 . ARG A  1 109 ? 31.631  -11.235 60.732  1.00 8.55   ? 196  ARG A NH1 1 
ATOM   858   N  NH2 . ARG A  1 109 ? 33.332  -10.023 59.763  1.00 8.16   ? 196  ARG A NH2 1 
ATOM   859   N  N   . MET A  1 110 ? 38.177  -12.514 59.486  1.00 9.54   ? 197  MET A N   1 
ATOM   860   C  CA  . MET A  1 110 ? 39.265  -11.706 58.954  1.00 10.47  ? 197  MET A CA  1 
ATOM   861   C  C   . MET A  1 110 ? 38.849  -10.226 58.922  1.00 10.56  ? 197  MET A C   1 
ATOM   862   O  O   . MET A  1 110 ? 37.776  -9.882  58.429  1.00 9.63   ? 197  MET A O   1 
ATOM   863   C  CB  . MET A  1 110 ? 39.660  -12.168 57.532  1.00 10.82  ? 197  MET A CB  1 
ATOM   864   C  CG  . MET A  1 110 ? 40.819  -11.367 56.943  1.00 11.98  ? 197  MET A CG  1 
ATOM   865   S  SD  . MET A  1 110 ? 41.271  -11.788 55.251  1.00 11.13  ? 197  MET A SD  1 
ATOM   866   C  CE  . MET A  1 110 ? 39.848  -11.306 54.278  1.00 11.30  ? 197  MET A CE  1 
ATOM   867   N  N   . SER A  1 111 ? 39.707  -9.362  59.473  1.00 10.00  ? 198  SER A N   1 
ATOM   868   C  CA  . SER A  1 111 ? 39.523  -7.913  59.380  1.00 10.14  ? 198  SER A CA  1 
ATOM   869   C  C   . SER A  1 111 ? 40.795  -7.241  58.848  1.00 10.75  ? 198  SER A C   1 
ATOM   870   O  O   . SER A  1 111 ? 41.908  -7.627  59.216  1.00 11.53  ? 198  SER A O   1 
ATOM   871   C  CB  . SER A  1 111 ? 39.168  -7.330  60.749  1.00 10.02  ? 198  SER A CB  1 
ATOM   872   O  OG  . SER A  1 111 ? 37.887  -7.775  61.173  1.00 10.70  ? 198  SER A OG  1 
ATOM   873   N  N   . ILE A  1 112 ? 40.619  -6.247  57.983  1.00 9.98   ? 199  ILE A N   1 
ATOM   874   C  CA  . ILE A  1 112 ? 41.737  -5.540  57.339  1.00 9.97   ? 199  ILE A CA  1 
ATOM   875   C  C   . ILE A  1 112 ? 41.529  -4.036  57.464  1.00 10.02  ? 199  ILE A C   1 
ATOM   876   O  O   . ILE A  1 112 ? 40.456  -3.527  57.141  1.00 9.71   ? 199  ILE A O   1 
ATOM   877   C  CB  . ILE A  1 112 ? 41.843  -5.898  55.821  1.00 9.63   ? 199  ILE A CB  1 
ATOM   878   C  CG1 . ILE A  1 112 ? 41.909  -7.407  55.615  1.00 9.18   ? 199  ILE A CG1 1 
ATOM   879   C  CG2 . ILE A  1 112 ? 43.062  -5.193  55.144  1.00 9.01   ? 199  ILE A CG2 1 
ATOM   880   C  CD1 . ILE A  1 112 ? 41.881  -7.775  54.115  1.00 10.66  ? 199  ILE A CD1 1 
ATOM   881   N  N   . CYS A  1 113 ? 42.563  -3.334  57.926  1.00 9.81   ? 200  CYS A N   1 
ATOM   882   C  CA  . CYS A  1 113 ? 42.568  -1.876  58.031  1.00 10.63  ? 200  CYS A CA  1 
ATOM   883   C  C   . CYS A  1 113 ? 43.824  -1.312  57.353  1.00 10.29  ? 200  CYS A C   1 
ATOM   884   O  O   . CYS A  1 113 ? 44.938  -1.796  57.605  1.00 10.77  ? 200  CYS A O   1 
ATOM   885   C  CB  . CYS A  1 113 ? 42.596  -1.435  59.503  1.00 10.77  ? 200  CYS A CB  1 
ATOM   886   S  SG  . CYS A  1 113 ? 41.069  -1.674  60.427  1.00 13.31  ? 200  CYS A SG  1 
ATOM   887   N  N   . MET A  1 114 ? 43.640  -0.286  56.526  1.00 10.58  ? 201  MET A N   1 
ATOM   888   C  CA  . MET A  1 114 ? 44.750  0.547   56.049  1.00 10.90  ? 201  MET A CA  1 
ATOM   889   C  C   . MET A  1 114 ? 44.979  1.775   56.954  1.00 10.86  ? 201  MET A C   1 
ATOM   890   O  O   . MET A  1 114 ? 44.037  2.426   57.381  1.00 9.59   ? 201  MET A O   1 
ATOM   891   C  CB  . MET A  1 114 ? 44.488  1.049   54.623  1.00 11.00  ? 201  MET A CB  1 
ATOM   892   C  CG  . MET A  1 114 ? 44.645  -0.023  53.550  1.00 11.38  ? 201  MET A CG  1 
ATOM   893   S  SD  . MET A  1 114 ? 43.411  -1.353  53.601  1.00 11.47  ? 201  MET A SD  1 
ATOM   894   C  CE  . MET A  1 114 ? 43.756  -2.055  51.976  1.00 12.16  ? 201  MET A CE  1 
ATOM   895   N  N   . SER A  1 115 ? 46.246  2.092   57.218  1.00 10.84  ? 202  SER A N   1 
ATOM   896   C  CA  . SER A  1 115 ? 46.586  3.301   57.937  1.00 11.45  ? 202  SER A CA  1 
ATOM   897   C  C   . SER A  1 115 ? 47.878  3.892   57.367  1.00 11.57  ? 202  SER A C   1 
ATOM   898   O  O   . SER A  1 115 ? 48.503  3.280   56.474  1.00 11.26  ? 202  SER A O   1 
ATOM   899   C  CB  . SER A  1 115 ? 46.742  2.999   59.438  1.00 12.14  ? 202  SER A CB  1 
ATOM   900   O  OG  . SER A  1 115 ? 48.043  2.457   59.690  1.00 14.26  ? 202  SER A OG  1 
ATOM   901   N  N   . GLY A  1 116 ? 48.282  5.052   57.885  1.00 10.97  ? 203  GLY A N   1 
ATOM   902   C  CA  . GLY A  1 116 ? 49.538  5.689   57.477  1.00 11.28  ? 203  GLY A CA  1 
ATOM   903   C  C   . GLY A  1 116 ? 49.259  6.936   56.663  1.00 11.82  ? 203  GLY A C   1 
ATOM   904   O  O   . GLY A  1 116 ? 48.096  7.291   56.470  1.00 11.62  ? 203  GLY A O   1 
ATOM   905   N  N   . PRO A  1 117 ? 50.325  7.607   56.175  1.00 12.01  ? 204  PRO A N   1 
ATOM   906   C  CA  . PRO A  1 117 ? 50.204  8.815   55.367  1.00 11.92  ? 204  PRO A CA  1 
ATOM   907   C  C   . PRO A  1 117 ? 49.804  8.436   53.940  1.00 11.89  ? 204  PRO A C   1 
ATOM   908   O  O   . PRO A  1 117 ? 49.914  7.258   53.547  1.00 10.88  ? 204  PRO A O   1 
ATOM   909   C  CB  . PRO A  1 117 ? 51.633  9.374   55.374  1.00 11.97  ? 204  PRO A CB  1 
ATOM   910   C  CG  . PRO A  1 117 ? 52.483  8.193   55.471  1.00 10.99  ? 204  PRO A CG  1 
ATOM   911   C  CD  . PRO A  1 117 ? 51.739  7.190   56.319  1.00 12.02  ? 204  PRO A CD  1 
ATOM   912   N  N   . ASN A  1 118 ? 49.336  9.416   53.175  1.00 13.14  ? 205  ASN A N   1 
ATOM   913   C  CA  . ASN A  1 118 ? 48.820  9.150   51.824  1.00 13.62  ? 205  ASN A CA  1 
ATOM   914   C  C   . ASN A  1 118 ? 49.839  8.444   50.936  1.00 13.74  ? 205  ASN A C   1 
ATOM   915   O  O   . ASN A  1 118 ? 49.496  7.527   50.176  1.00 13.86  ? 205  ASN A O   1 
ATOM   916   C  CB  . ASN A  1 118 ? 48.350  10.453  51.164  1.00 14.37  ? 205  ASN A CB  1 
ATOM   917   C  CG  . ASN A  1 118 ? 47.148  11.073  51.864  1.00 15.25  ? 205  ASN A CG  1 
ATOM   918   O  OD1 . ASN A  1 118 ? 46.495  10.454  52.723  1.00 14.78  ? 205  ASN A OD1 1 
ATOM   919   N  ND2 . ASN A  1 118 ? 46.845  12.305  51.495  1.00 19.95  ? 205  ASN A ND2 1 
ATOM   920   N  N   . ASN A  1 119 ? 51.103  8.837   51.073  1.00 13.78  ? 206  ASN A N   1 
ATOM   921   C  CA  . ASN A  1 119 ? 52.148  8.353   50.184  1.00 14.34  ? 206  ASN A CA  1 
ATOM   922   C  C   . ASN A  1 119 ? 52.829  7.074   50.652  1.00 13.99  ? 206  ASN A C   1 
ATOM   923   O  O   . ASN A  1 119 ? 53.758  6.611   50.003  1.00 13.95  ? 206  ASN A O   1 
ATOM   924   C  CB  . ASN A  1 119 ? 53.193  9.463   49.887  1.00 14.10  ? 206  ASN A CB  1 
ATOM   925   C  CG  . ASN A  1 119 ? 54.087  9.788   51.086  1.00 16.42  ? 206  ASN A CG  1 
ATOM   926   O  OD1 . ASN A  1 119 ? 53.899  9.260   52.186  1.00 17.73  ? 206  ASN A OD1 1 
ATOM   927   N  ND2 . ASN A  1 119 ? 55.073  10.675  50.872  1.00 16.66  ? 206  ASN A ND2 1 
ATOM   928   N  N   . ASN A  1 120 ? 52.359  6.496   51.762  1.00 13.48  ? 207  ASN A N   1 
ATOM   929   C  CA  . ASN A  1 120 ? 53.089  5.404   52.402  1.00 14.03  ? 207  ASN A CA  1 
ATOM   930   C  C   . ASN A  1 120 ? 52.174  4.578   53.303  1.00 12.15  ? 207  ASN A C   1 
ATOM   931   O  O   . ASN A  1 120 ? 52.564  4.194   54.388  1.00 11.77  ? 207  ASN A O   1 
ATOM   932   C  CB  . ASN A  1 120 ? 54.242  6.002   53.227  1.00 14.43  ? 207  ASN A CB  1 
ATOM   933   C  CG  . ASN A  1 120 ? 55.545  5.215   53.124  1.00 19.43  ? 207  ASN A CG  1 
ATOM   934   O  OD1 . ASN A  1 120 ? 55.675  4.241   52.361  1.00 22.19  ? 207  ASN A OD1 1 
ATOM   935   N  ND2 . ASN A  1 120 ? 56.530  5.647   53.939  1.00 25.51  ? 207  ASN A ND2 1 
ATOM   936   N  N   . ALA A  1 121 ? 50.945  4.320   52.853  1.00 11.41  ? 208  ALA A N   1 
ATOM   937   C  CA  . ALA A  1 121 ? 49.976  3.629   53.685  1.00 11.18  ? 208  ALA A CA  1 
ATOM   938   C  C   . ALA A  1 121 ? 50.282  2.139   53.694  1.00 11.11  ? 208  ALA A C   1 
ATOM   939   O  O   . ALA A  1 121 ? 51.041  1.645   52.866  1.00 12.36  ? 208  ALA A O   1 
ATOM   940   C  CB  . ALA A  1 121 ? 48.535  3.887   53.180  1.00 10.34  ? 208  ALA A CB  1 
ATOM   941   N  N   . SER A  1 122 ? 49.662  1.411   54.606  1.00 11.22  ? 209  SER A N   1 
ATOM   942   C  CA  . SER A  1 122 ? 49.835  -0.037  54.637  1.00 11.18  ? 209  SER A CA  1 
ATOM   943   C  C   . SER A  1 122 ? 48.605  -0.690  55.224  1.00 11.18  ? 209  SER A C   1 
ATOM   944   O  O   . SER A  1 122 ? 47.955  -0.110  56.103  1.00 9.89   ? 209  SER A O   1 
ATOM   945   C  CB  . SER A  1 122 ? 51.073  -0.426  55.466  1.00 11.67  ? 209  SER A CB  1 
ATOM   946   O  OG  . SER A  1 122 ? 50.957  0.067   56.790  1.00 13.63  ? 209  SER A OG  1 
ATOM   947   N  N   . ALA A  1 123 ? 48.322  -1.910  54.758  1.00 10.56  ? 210  ALA A N   1 
ATOM   948   C  CA  . ALA A  1 123 ? 47.254  -2.733  55.307  1.00 11.08  ? 210  ALA A CA  1 
ATOM   949   C  C   . ALA A  1 123 ? 47.801  -3.725  56.340  1.00 10.57  ? 210  ALA A C   1 
ATOM   950   O  O   . ALA A  1 123 ? 48.875  -4.299  56.158  1.00 11.47  ? 210  ALA A O   1 
ATOM   951   C  CB  . ALA A  1 123 ? 46.513  -3.482  54.188  1.00 10.70  ? 210  ALA A CB  1 
ATOM   952   N  N   . VAL A  1 124 ? 47.069  -3.887  57.439  1.00 9.73   ? 211  VAL A N   1 
ATOM   953   C  CA  . VAL A  1 124 ? 47.321  -4.972  58.383  1.00 9.37   ? 211  VAL A CA  1 
ATOM   954   C  C   . VAL A  1 124 ? 46.108  -5.916  58.340  1.00 9.33   ? 211  VAL A C   1 
ATOM   955   O  O   . VAL A  1 124 ? 44.947  -5.469  58.467  1.00 8.26   ? 211  VAL A O   1 
ATOM   956   C  CB  . VAL A  1 124 ? 47.607  -4.444  59.816  1.00 9.23   ? 211  VAL A CB  1 
ATOM   957   C  CG1 . VAL A  1 124 ? 47.856  -5.625  60.778  1.00 10.21  ? 211  VAL A CG1 1 
ATOM   958   C  CG2 . VAL A  1 124 ? 48.818  -3.433  59.806  1.00 9.24   ? 211  VAL A CG2 1 
ATOM   959   N  N   . VAL A  1 125 ? 46.394  -7.200  58.107  1.00 9.40   ? 212  VAL A N   1 
ATOM   960   C  CA  . VAL A  1 125 ? 45.371  -8.238  57.921  1.00 9.75   ? 212  VAL A CA  1 
ATOM   961   C  C   . VAL A  1 125 ? 45.302  -9.080  59.191  1.00 9.56   ? 212  VAL A C   1 
ATOM   962   O  O   . VAL A  1 125 ? 46.302  -9.671  59.609  1.00 9.28   ? 212  VAL A O   1 
ATOM   963   C  CB  . VAL A  1 125 ? 45.682  -9.158  56.681  1.00 9.94   ? 212  VAL A CB  1 
ATOM   964   C  CG1 . VAL A  1 125 ? 44.630  -10.290 56.541  1.00 9.52   ? 212  VAL A CG1 1 
ATOM   965   C  CG2 . VAL A  1 125 ? 45.800  -8.347  55.372  1.00 9.45   ? 212  VAL A CG2 1 
ATOM   966   N  N   . TRP A  1 126 ? 44.131  -9.092  59.826  1.00 9.22   ? 213  TRP A N   1 
ATOM   967   C  CA  . TRP A  1 126 ? 43.937  -9.772  61.086  1.00 9.33   ? 213  TRP A CA  1 
ATOM   968   C  C   . TRP A  1 126 ? 43.067  -10.992 60.836  1.00 9.85   ? 213  TRP A C   1 
ATOM   969   O  O   . TRP A  1 126 ? 42.193  -10.941 59.967  1.00 10.14  ? 213  TRP A O   1 
ATOM   970   C  CB  . TRP A  1 126 ? 43.191  -8.843  62.066  1.00 9.08   ? 213  TRP A CB  1 
ATOM   971   C  CG  . TRP A  1 126 ? 43.966  -7.644  62.515  1.00 10.50  ? 213  TRP A CG  1 
ATOM   972   C  CD1 . TRP A  1 126 ? 44.361  -6.568  61.752  1.00 11.06  ? 213  TRP A CD1 1 
ATOM   973   C  CD2 . TRP A  1 126 ? 44.401  -7.370  63.848  1.00 10.16  ? 213  TRP A CD2 1 
ATOM   974   N  NE1 . TRP A  1 126 ? 45.018  -5.646  62.536  1.00 9.69   ? 213  TRP A NE1 1 
ATOM   975   C  CE2 . TRP A  1 126 ? 45.058  -6.114  63.825  1.00 9.96   ? 213  TRP A CE2 1 
ATOM   976   C  CE3 . TRP A  1 126 ? 44.293  -8.062  65.066  1.00 11.63  ? 213  TRP A CE3 1 
ATOM   977   C  CZ2 . TRP A  1 126 ? 45.617  -5.536  64.970  1.00 10.78  ? 213  TRP A CZ2 1 
ATOM   978   C  CZ3 . TRP A  1 126 ? 44.856  -7.479  66.219  1.00 10.57  ? 213  TRP A CZ3 1 
ATOM   979   C  CH2 . TRP A  1 126 ? 45.507  -6.226  66.151  1.00 9.66   ? 213  TRP A CH2 1 
ATOM   980   N  N   . TYR A  1 127 ? 43.281  -12.067 61.603  1.00 10.03  ? 214  TYR A N   1 
ATOM   981   C  CA  . TYR A  1 127 ? 42.445  -13.271 61.542  1.00 10.59  ? 214  TYR A CA  1 
ATOM   982   C  C   . TYR A  1 127 ? 42.278  -13.858 62.943  1.00 10.93  ? 214  TYR A C   1 
ATOM   983   O  O   . TYR A  1 127 ? 43.268  -14.113 63.643  1.00 10.57  ? 214  TYR A O   1 
ATOM   984   C  CB  . TYR A  1 127 ? 43.077  -14.323 60.616  1.00 10.67  ? 214  TYR A CB  1 
ATOM   985   C  CG  . TYR A  1 127 ? 42.227  -15.556 60.352  1.00 11.99  ? 214  TYR A CG  1 
ATOM   986   C  CD1 . TYR A  1 127 ? 42.544  -16.788 60.943  1.00 11.16  ? 214  TYR A CD1 1 
ATOM   987   C  CD2 . TYR A  1 127 ? 41.111  -15.497 59.502  1.00 10.69  ? 214  TYR A CD2 1 
ATOM   988   C  CE1 . TYR A  1 127 ? 41.772  -17.941 60.701  1.00 12.28  ? 214  TYR A CE1 1 
ATOM   989   C  CE2 . TYR A  1 127 ? 40.329  -16.643 59.259  1.00 9.86   ? 214  TYR A CE2 1 
ATOM   990   C  CZ  . TYR A  1 127 ? 40.661  -17.854 59.846  1.00 10.73  ? 214  TYR A CZ  1 
ATOM   991   O  OH  . TYR A  1 127 ? 39.894  -18.983 59.602  1.00 10.74  ? 214  TYR A OH  1 
ATOM   992   N  N   . GLY A  1 128 ? 41.032  -14.072 63.359  1.00 11.11  ? 215  GLY A N   1 
ATOM   993   C  CA  . GLY A  1 128 ? 40.779  -14.591 64.701  1.00 12.09  ? 215  GLY A CA  1 
ATOM   994   C  C   . GLY A  1 128 ? 41.286  -13.642 65.785  1.00 11.94  ? 215  GLY A C   1 
ATOM   995   O  O   . GLY A  1 128 ? 41.691  -14.085 66.859  1.00 12.75  ? 215  GLY A O   1 
ATOM   996   N  N   . GLY A  1 129 ? 41.301  -12.345 65.491  1.00 11.76  ? 216  GLY A N   1 
ATOM   997   C  CA  . GLY A  1 129 ? 41.734  -11.314 66.450  1.00 11.50  ? 216  GLY A CA  1 
ATOM   998   C  C   . GLY A  1 129 ? 43.234  -11.117 66.628  1.00 12.11  ? 216  GLY A C   1 
ATOM   999   O  O   . GLY A  1 129 ? 43.663  -10.399 67.541  1.00 12.22  ? 216  GLY A O   1 
ATOM   1000  N  N   . ARG A  1 130 ? 44.027  -11.715 65.740  1.00 11.97  ? 217  ARG A N   1 
ATOM   1001  C  CA  . ARG A  1 130 ? 45.491  -11.612 65.772  1.00 12.77  ? 217  ARG A CA  1 
ATOM   1002  C  C   . ARG A  1 130 ? 45.975  -11.053 64.417  1.00 12.26  ? 217  ARG A C   1 
ATOM   1003  O  O   . ARG A  1 130 ? 45.371  -11.382 63.372  1.00 12.58  ? 217  ARG A O   1 
ATOM   1004  C  CB  . ARG A  1 130 ? 46.109  -13.006 66.071  1.00 12.56  ? 217  ARG A CB  1 
ATOM   1005  C  CG  . ARG A  1 130 ? 45.818  -13.531 67.510  1.00 14.12  ? 217  ARG A CG  1 
ATOM   1006  C  CD  . ARG A  1 130 ? 46.537  -14.853 67.957  1.00 14.81  ? 217  ARG A CD  1 
ATOM   1007  N  NE  . ARG A  1 130 ? 46.916  -14.702 69.372  1.00 15.88  ? 217  ARG A NE  1 
ATOM   1008  C  CZ  . ARG A  1 130 ? 46.321  -15.228 70.449  1.00 18.89  ? 217  ARG A CZ  1 
ATOM   1009  N  NH1 . ARG A  1 130 ? 46.791  -14.910 71.681  1.00 14.92  ? 217  ARG A NH1 1 
ATOM   1010  N  NH2 . ARG A  1 130 ? 45.276  -16.051 70.324  1.00 16.91  ? 217  ARG A NH2 1 
ATOM   1011  N  N   . PRO A  1 131 ? 47.045  -10.210 64.410  1.00 12.24  ? 218  PRO A N   1 
ATOM   1012  C  CA  . PRO A  1 131 ? 47.599  -9.766  63.112  1.00 12.46  ? 218  PRO A CA  1 
ATOM   1013  C  C   . PRO A  1 131 ? 48.364  -10.901 62.397  1.00 12.32  ? 218  PRO A C   1 
ATOM   1014  O  O   . PRO A  1 131 ? 49.160  -11.612 63.018  1.00 11.82  ? 218  PRO A O   1 
ATOM   1015  C  CB  . PRO A  1 131 ? 48.565  -8.636  63.480  1.00 12.46  ? 218  PRO A CB  1 
ATOM   1016  C  CG  . PRO A  1 131 ? 48.974  -8.907  64.900  1.00 12.24  ? 218  PRO A CG  1 
ATOM   1017  C  CD  . PRO A  1 131 ? 47.809  -9.675  65.562  1.00 12.10  ? 218  PRO A CD  1 
ATOM   1018  N  N   . ILE A  1 132 ? 48.115  -11.062 61.104  1.00 12.00  ? 219  ILE A N   1 
ATOM   1019  C  CA  . ILE A  1 132 ? 48.710  -12.168 60.335  1.00 12.22  ? 219  ILE A CA  1 
ATOM   1020  C  C   . ILE A  1 132 ? 49.684  -11.678 59.249  1.00 13.16  ? 219  ILE A C   1 
ATOM   1021  O  O   . ILE A  1 132 ? 50.815  -12.192 59.122  1.00 12.96  ? 219  ILE A O   1 
ATOM   1022  C  CB  . ILE A  1 132 ? 47.606  -13.068 59.693  1.00 11.95  ? 219  ILE A CB  1 
ATOM   1023  C  CG1 . ILE A  1 132 ? 46.550  -13.480 60.742  1.00 12.12  ? 219  ILE A CG1 1 
ATOM   1024  C  CG2 . ILE A  1 132 ? 48.224  -14.279 58.908  1.00 11.48  ? 219  ILE A CG2 1 
ATOM   1025  C  CD1 . ILE A  1 132 ? 47.059  -14.366 61.913  1.00 12.39  ? 219  ILE A CD1 1 
ATOM   1026  N  N   . THR A  1 133 ? 49.229  -10.710 58.460  1.00 12.55  ? 220  THR A N   1 
ATOM   1027  C  CA  . THR A  1 133 ? 49.930  -10.251 57.267  1.00 13.36  ? 220  THR A CA  1 
ATOM   1028  C  C   . THR A  1 133 ? 49.914  -8.718  57.210  1.00 12.98  ? 220  THR A C   1 
ATOM   1029  O  O   . THR A  1 133 ? 48.975  -8.083  57.687  1.00 11.94  ? 220  THR A O   1 
ATOM   1030  C  CB  . THR A  1 133 ? 49.235  -10.843 55.987  1.00 13.21  ? 220  THR A CB  1 
ATOM   1031  O  OG1 . THR A  1 133 ? 49.274  -12.276 56.050  1.00 14.07  ? 220  THR A OG1 1 
ATOM   1032  C  CG2 . THR A  1 133 ? 49.914  -10.381 54.710  1.00 15.46  ? 220  THR A CG2 1 
ATOM   1033  N  N   . GLU A  1 134 ? 50.964  -8.134  56.630  1.00 12.95  ? 221  GLU A N   1 
ATOM   1034  C  CA  . GLU A  1 134 ? 50.988  -6.697  56.333  1.00 12.95  ? 221  GLU A CA  1 
ATOM   1035  C  C   . GLU A  1 134 ? 51.271  -6.501  54.845  1.00 13.24  ? 221  GLU A C   1 
ATOM   1036  O  O   . GLU A  1 134 ? 52.000  -7.300  54.244  1.00 12.37  ? 221  GLU A O   1 
ATOM   1037  C  CB  . GLU A  1 134 ? 52.020  -5.955  57.207  1.00 12.85  ? 221  GLU A CB  1 
ATOM   1038  C  CG  . GLU A  1 134 ? 52.018  -6.358  58.703  1.00 14.80  ? 221  GLU A CG  1 
ATOM   1039  C  CD  . GLU A  1 134 ? 52.674  -7.706  58.946  1.00 17.11  ? 221  GLU A CD  1 
ATOM   1040  O  OE1 . GLU A  1 134 ? 52.070  -8.537  59.639  1.00 19.77  ? 221  GLU A OE1 1 
ATOM   1041  O  OE2 . GLU A  1 134 ? 53.778  -7.962  58.421  1.00 19.04  ? 221  GLU A OE2 1 
ATOM   1042  N  N   . ILE A  1 135 ? 50.679  -5.454  54.266  1.00 12.93  ? 222  ILE A N   1 
ATOM   1043  C  CA  . ILE A  1 135 ? 50.793  -5.145  52.831  1.00 13.26  ? 222  ILE A CA  1 
ATOM   1044  C  C   . ILE A  1 135 ? 51.106  -3.668  52.632  1.00 13.04  ? 222  ILE A C   1 
ATOM   1045  O  O   . ILE A  1 135 ? 50.265  -2.797  52.901  1.00 13.38  ? 222  ILE A O   1 
ATOM   1046  C  CB  . ILE A  1 135 ? 49.489  -5.465  52.031  1.00 13.25  ? 222  ILE A CB  1 
ATOM   1047  C  CG1 . ILE A  1 135 ? 49.073  -6.934  52.200  1.00 12.22  ? 222  ILE A CG1 1 
ATOM   1048  C  CG2 . ILE A  1 135 ? 49.667  -5.120  50.531  1.00 14.14  ? 222  ILE A CG2 1 
ATOM   1049  C  CD1 . ILE A  1 135 ? 47.574  -7.197  51.845  1.00 13.08  ? 222  ILE A CD1 1 
ATOM   1050  N  N   . PRO A  1 136 ? 52.317  -3.370  52.130  1.00 12.73  ? 223  PRO A N   1 
ATOM   1051  C  CA  . PRO A  1 136 ? 52.681  -1.995  51.835  1.00 12.41  ? 223  PRO A CA  1 
ATOM   1052  C  C   . PRO A  1 136 ? 51.994  -1.472  50.573  1.00 12.79  ? 223  PRO A C   1 
ATOM   1053  O  O   . PRO A  1 136 ? 51.696  -2.239  49.652  1.00 12.54  ? 223  PRO A O   1 
ATOM   1054  C  CB  . PRO A  1 136 ? 54.200  -2.067  51.626  1.00 12.56  ? 223  PRO A CB  1 
ATOM   1055  C  CG  . PRO A  1 136 ? 54.445  -3.447  51.147  1.00 12.85  ? 223  PRO A CG  1 
ATOM   1056  C  CD  . PRO A  1 136 ? 53.397  -4.322  51.800  1.00 13.00  ? 223  PRO A CD  1 
ATOM   1057  N  N   . SER A  1 137 ? 51.745  -0.168  50.563  1.00 12.61  ? 224  SER A N   1 
ATOM   1058  C  CA  . SER A  1 137 ? 51.256  0.538   49.390  1.00 12.97  ? 224  SER A CA  1 
ATOM   1059  C  C   . SER A  1 137 ? 52.121  0.197   48.176  1.00 13.23  ? 224  SER A C   1 
ATOM   1060  O  O   . SER A  1 137 ? 53.348  0.144   48.275  1.00 12.19  ? 224  SER A O   1 
ATOM   1061  C  CB  . SER A  1 137 ? 51.282  2.041   49.667  1.00 13.54  ? 224  SER A CB  1 
ATOM   1062  O  OG  . SER A  1 137 ? 50.924  2.797   48.519  1.00 14.48  ? 224  SER A OG  1 
ATOM   1063  N  N   . TRP A  1 138 ? 51.467  -0.067  47.047  1.00 13.55  ? 225  TRP A N   1 
ATOM   1064  C  CA  . TRP A  1 138 ? 52.158  -0.345  45.792  1.00 14.77  ? 225  TRP A CA  1 
ATOM   1065  C  C   . TRP A  1 138 ? 52.230  0.844   44.819  1.00 15.16  ? 225  TRP A C   1 
ATOM   1066  O  O   . TRP A  1 138 ? 53.078  0.871   43.903  1.00 15.85  ? 225  TRP A O   1 
ATOM   1067  C  CB  . TRP A  1 138 ? 51.564  -1.570  45.094  1.00 14.25  ? 225  TRP A CB  1 
ATOM   1068  C  CG  . TRP A  1 138 ? 50.047  -1.581  44.889  1.00 14.55  ? 225  TRP A CG  1 
ATOM   1069  C  CD1 . TRP A  1 138 ? 49.339  -0.958  43.892  1.00 15.34  ? 225  TRP A CD1 1 
ATOM   1070  C  CD2 . TRP A  1 138 ? 49.076  -2.305  45.676  1.00 14.33  ? 225  TRP A CD2 1 
ATOM   1071  N  NE1 . TRP A  1 138 ? 47.986  -1.248  44.013  1.00 15.57  ? 225  TRP A NE1 1 
ATOM   1072  C  CE2 . TRP A  1 138 ? 47.799  -2.067  45.099  1.00 14.33  ? 225  TRP A CE2 1 
ATOM   1073  C  CE3 . TRP A  1 138 ? 49.163  -3.133  46.802  1.00 12.62  ? 225  TRP A CE3 1 
ATOM   1074  C  CZ2 . TRP A  1 138 ? 46.619  -2.622  45.626  1.00 14.27  ? 225  TRP A CZ2 1 
ATOM   1075  C  CZ3 . TRP A  1 138 ? 47.984  -3.686  47.331  1.00 14.81  ? 225  TRP A CZ3 1 
ATOM   1076  C  CH2 . TRP A  1 138 ? 46.729  -3.426  46.737  1.00 14.09  ? 225  TRP A CH2 1 
ATOM   1077  N  N   . ALA A  1 139 ? 51.361  1.821   45.003  1.00 14.88  ? 226  ALA A N   1 
ATOM   1078  C  CA  . ALA A  1 139 ? 51.329  2.961   44.100  1.00 15.11  ? 226  ALA A CA  1 
ATOM   1079  C  C   . ALA A  1 139 ? 51.526  4.282   44.835  1.00 15.15  ? 226  ALA A C   1 
ATOM   1080  O  O   . ALA A  1 139 ? 51.498  5.340   44.220  1.00 15.88  ? 226  ALA A O   1 
ATOM   1081  C  CB  . ALA A  1 139 ? 50.020  2.962   43.257  1.00 14.55  ? 226  ALA A CB  1 
ATOM   1082  N  N   . GLY A  1 140 ? 51.729  4.224   46.152  1.00 15.12  ? 227  GLY A N   1 
ATOM   1083  C  CA  . GLY A  1 140 ? 52.018  5.437   46.936  1.00 14.57  ? 227  GLY A CA  1 
ATOM   1084  C  C   . GLY A  1 140 ? 50.930  6.500   47.003  1.00 14.44  ? 227  GLY A C   1 
ATOM   1085  O  O   . GLY A  1 140 ? 51.231  7.683   47.146  1.00 13.74  ? 227  GLY A O   1 
ATOM   1086  N  N   . ASN A  1 141 ? 49.656  6.088   46.941  1.00 13.92  ? 228  ASN A N   1 
ATOM   1087  C  CA  . ASN A  1 141 ? 48.549  7.050   46.913  1.00 14.55  ? 228  ASN A CA  1 
ATOM   1088  C  C   . ASN A  1 141 ? 47.279  6.488   47.535  1.00 13.75  ? 228  ASN A C   1 
ATOM   1089  O  O   . ASN A  1 141 ? 46.341  6.085   46.823  1.00 14.19  ? 228  ASN A O   1 
ATOM   1090  C  CB  . ASN A  1 141 ? 48.291  7.581   45.478  1.00 15.02  ? 228  ASN A CB  1 
ATOM   1091  C  CG  . ASN A  1 141 ? 47.390  8.837   45.447  1.00 17.29  ? 228  ASN A CG  1 
ATOM   1092  O  OD1 . ASN A  1 141 ? 46.778  9.232   46.457  1.00 17.74  ? 228  ASN A OD1 1 
ATOM   1093  N  ND2 . ASN A  1 141 ? 47.307  9.467   44.261  1.00 18.80  ? 228  ASN A ND2 1 
ATOM   1094  N  N   . ILE A  1 142 ? 47.273  6.461   48.869  1.00 12.50  ? 229  ILE A N   1 
ATOM   1095  C  CA  . ILE A  1 142 ? 46.105  6.067   49.664  1.00 12.07  ? 229  ILE A CA  1 
ATOM   1096  C  C   . ILE A  1 142 ? 45.636  4.645   49.336  1.00 11.56  ? 229  ILE A C   1 
ATOM   1097  O  O   . ILE A  1 142 ? 44.527  4.440   48.817  1.00 12.10  ? 229  ILE A O   1 
ATOM   1098  C  CB  . ILE A  1 142 ? 44.919  7.086   49.541  1.00 11.82  ? 229  ILE A CB  1 
ATOM   1099  C  CG1 . ILE A  1 142 ? 45.420  8.537   49.667  1.00 11.84  ? 229  ILE A CG1 1 
ATOM   1100  C  CG2 . ILE A  1 142 ? 43.802  6.797   50.597  1.00 10.54  ? 229  ILE A CG2 1 
ATOM   1101  C  CD1 . ILE A  1 142 ? 44.315  9.601   49.438  1.00 12.56  ? 229  ILE A CD1 1 
ATOM   1102  N  N   . LEU A  1 143 ? 46.477  3.668   49.648  1.00 11.12  ? 230  LEU A N   1 
ATOM   1103  C  CA  . LEU A  1 143 ? 46.064  2.261   49.622  1.00 11.24  ? 230  LEU A CA  1 
ATOM   1104  C  C   . LEU A  1 143 ? 44.754  2.118   50.406  1.00 11.08  ? 230  LEU A C   1 
ATOM   1105  O  O   . LEU A  1 143 ? 44.645  2.641   51.524  1.00 11.20  ? 230  LEU A O   1 
ATOM   1106  C  CB  . LEU A  1 143 ? 47.166  1.381   50.224  1.00 11.80  ? 230  LEU A CB  1 
ATOM   1107  C  CG  . LEU A  1 143 ? 46.819  -0.101  50.382  1.00 11.37  ? 230  LEU A CG  1 
ATOM   1108  C  CD1 . LEU A  1 143 ? 46.523  -0.742  49.022  1.00 12.76  ? 230  LEU A CD1 1 
ATOM   1109  C  CD2 . LEU A  1 143 ? 47.928  -0.831  51.148  1.00 10.98  ? 230  LEU A CD2 1 
ATOM   1110  N  N   . ARG A  1 144 ? 43.762  1.432   49.819  1.00 10.29  ? 231  ARG A N   1 
ATOM   1111  C  CA  . ARG A  1 144 ? 42.382  1.498   50.326  1.00 10.45  ? 231  ARG A CA  1 
ATOM   1112  C  C   . ARG A  1 144 ? 41.519  0.342   49.851  1.00 9.70   ? 231  ARG A C   1 
ATOM   1113  O  O   . ARG A  1 144 ? 41.892  -0.368  48.927  1.00 9.21   ? 231  ARG A O   1 
ATOM   1114  C  CB  . ARG A  1 144 ? 41.733  2.849   49.954  1.00 9.90   ? 231  ARG A CB  1 
ATOM   1115  C  CG  . ARG A  1 144 ? 41.614  3.121   48.434  1.00 9.79   ? 231  ARG A CG  1 
ATOM   1116  C  CD  . ARG A  1 144 ? 41.311  4.560   48.201  1.00 11.02  ? 231  ARG A CD  1 
ATOM   1117  N  NE  . ARG A  1 144 ? 41.154  4.914   46.789  1.00 12.82  ? 231  ARG A NE  1 
ATOM   1118  C  CZ  . ARG A  1 144 ? 42.146  5.330   46.000  1.00 13.62  ? 231  ARG A CZ  1 
ATOM   1119  N  NH1 . ARG A  1 144 ? 43.400  5.420   46.468  1.00 10.91  ? 231  ARG A NH1 1 
ATOM   1120  N  NH2 . ARG A  1 144 ? 41.878  5.653   44.741  1.00 10.45  ? 231  ARG A NH2 1 
ATOM   1121  N  N   . THR A  1 145 ? 40.364  0.139   50.496  1.00 10.04  ? 232  THR A N   1 
ATOM   1122  C  CA  . THR A  1 145 ? 39.573  -1.058  50.216  1.00 9.53   ? 232  THR A CA  1 
ATOM   1123  C  C   . THR A  1 145 ? 38.057  -0.800  50.305  1.00 9.85   ? 232  THR A C   1 
ATOM   1124  O  O   . THR A  1 145 ? 37.596  0.340   50.132  1.00 9.59   ? 232  THR A O   1 
ATOM   1125  C  CB  . THR A  1 145 ? 40.104  -2.295  51.042  1.00 9.52   ? 232  THR A CB  1 
ATOM   1126  O  OG1 . THR A  1 145 ? 39.528  -3.520  50.570  1.00 8.72   ? 232  THR A OG1 1 
ATOM   1127  C  CG2 . THR A  1 145 ? 39.883  -2.139  52.549  1.00 9.17   ? 232  THR A CG2 1 
ATOM   1128  N  N   . GLN A  1 146 ? 37.298  -1.870  50.553  1.00 9.40   ? 233  GLN A N   1 
ATOM   1129  C  CA  . GLN A  1 146 ? 35.861  -1.888  50.238  1.00 9.78   ? 233  GLN A CA  1 
ATOM   1130  C  C   . GLN A  1 146 ? 34.935  -0.954  51.067  1.00 9.47   ? 233  GLN A C   1 
ATOM   1131  O  O   . GLN A  1 146 ? 33.976  -0.363  50.523  1.00 10.42  ? 233  GLN A O   1 
ATOM   1132  C  CB  . GLN A  1 146 ? 35.370  -3.332  50.311  1.00 9.29   ? 233  GLN A CB  1 
ATOM   1133  C  CG  . GLN A  1 146 ? 35.993  -4.223  49.231  1.00 9.69   ? 233  GLN A CG  1 
ATOM   1134  C  CD  . GLN A  1 146 ? 35.543  -5.649  49.321  1.00 12.14  ? 233  GLN A CD  1 
ATOM   1135  O  OE1 . GLN A  1 146 ? 34.546  -5.959  49.975  1.00 13.74  ? 233  GLN A OE1 1 
ATOM   1136  N  NE2 . GLN A  1 146 ? 36.281  -6.533  48.685  1.00 9.38   ? 233  GLN A NE2 1 
ATOM   1137  N  N   . GLU A  1 147 ? 35.217  -0.833  52.367  1.00 9.09   ? 234  GLU A N   1 
ATOM   1138  C  CA  . GLU A  1 147 ? 34.295  -0.232  53.348  1.00 8.83   ? 234  GLU A CA  1 
ATOM   1139  C  C   . GLU A  1 147 ? 32.956  -0.979  53.489  1.00 9.79   ? 234  GLU A C   1 
ATOM   1140  O  O   . GLU A  1 147 ? 31.952  -0.369  53.906  1.00 9.21   ? 234  GLU A O   1 
ATOM   1141  C  CB  . GLU A  1 147 ? 34.005  1.273   53.077  1.00 8.98   ? 234  GLU A CB  1 
ATOM   1142  C  CG  . GLU A  1 147 ? 35.139  2.124   52.487  1.00 9.04   ? 234  GLU A CG  1 
ATOM   1143  C  CD  . GLU A  1 147 ? 36.408  2.185   53.328  1.00 10.32  ? 234  GLU A CD  1 
ATOM   1144  O  OE1 . GLU A  1 147 ? 37.388  2.809   52.839  1.00 10.49  ? 234  GLU A OE1 1 
ATOM   1145  O  OE2 . GLU A  1 147 ? 36.452  1.615   54.443  1.00 10.10  ? 234  GLU A OE2 1 
ATOM   1146  N  N   . SER A  1 148 ? 32.936  -2.266  53.105  1.00 9.56   ? 235  SER A N   1 
ATOM   1147  C  CA  . SER A  1 148 ? 31.852  -3.185  53.489  1.00 10.05  ? 235  SER A CA  1 
ATOM   1148  C  C   . SER A  1 148 ? 32.410  -4.599  53.474  1.00 9.84   ? 235  SER A C   1 
ATOM   1149  O  O   . SER A  1 148 ? 33.599  -4.800  53.172  1.00 10.08  ? 235  SER A O   1 
ATOM   1150  C  CB  . SER A  1 148 ? 30.600  -3.053  52.608  1.00 9.69   ? 235  SER A CB  1 
ATOM   1151  O  OG  . SER A  1 148 ? 30.891  -3.360  51.260  1.00 10.53  ? 235  SER A OG  1 
ATOM   1152  N  N   . GLU A  1 149 ? 31.575  -5.576  53.814  1.00 9.93   ? 236  GLU A N   1 
ATOM   1153  C  CA  . GLU A  1 149 ? 32.086  -6.922  54.081  1.00 9.70   ? 236  GLU A CA  1 
ATOM   1154  C  C   . GLU A  1 149 ? 32.701  -7.600  52.832  1.00 9.51   ? 236  GLU A C   1 
ATOM   1155  O  O   . GLU A  1 149 ? 32.259  -7.385  51.687  1.00 9.07   ? 236  GLU A O   1 
ATOM   1156  C  CB  . GLU A  1 149 ? 31.027  -7.795  54.760  1.00 10.61  ? 236  GLU A CB  1 
ATOM   1157  C  CG  . GLU A  1 149 ? 29.972  -8.421  53.844  1.00 8.93   ? 236  GLU A CG  1 
ATOM   1158  C  CD  . GLU A  1 149 ? 29.257  -9.598  54.512  1.00 10.63  ? 236  GLU A CD  1 
ATOM   1159  O  OE1 . GLU A  1 149 ? 29.490  -9.838  55.725  1.00 7.76   ? 236  GLU A OE1 1 
ATOM   1160  O  OE2 . GLU A  1 149 ? 28.453  -10.267 53.820  1.00 9.35   ? 236  GLU A OE2 1 
ATOM   1161  N  N   . CYS A  1 150 ? 33.765  -8.356  53.056  1.00 9.77   ? 237  CYS A N   1 
ATOM   1162  C  CA  . CYS A  1 150 ? 34.248  -9.265  52.034  1.00 9.64   ? 237  CYS A CA  1 
ATOM   1163  C  C   . CYS A  1 150 ? 33.395  -10.538 52.100  1.00 10.52  ? 237  CYS A C   1 
ATOM   1164  O  O   . CYS A  1 150 ? 32.400  -10.586 52.843  1.00 9.62   ? 237  CYS A O   1 
ATOM   1165  C  CB  . CYS A  1 150 ? 35.759  -9.537  52.167  1.00 9.94   ? 237  CYS A CB  1 
ATOM   1166  S  SG  . CYS A  1 150 ? 36.432  -9.685  53.880  1.00 10.03  ? 237  CYS A SG  1 
ATOM   1167  N  N   . VAL A  1 151 ? 33.770  -11.562 51.332  1.00 11.11  ? 238  VAL A N   1 
ATOM   1168  C  CA  . VAL A  1 151 ? 32.969  -12.802 51.230  1.00 11.40  ? 238  VAL A CA  1 
ATOM   1169  C  C   . VAL A  1 151 ? 33.963  -13.978 51.108  1.00 11.53  ? 238  VAL A C   1 
ATOM   1170  O  O   . VAL A  1 151 ? 34.972  -13.837 50.429  1.00 11.94  ? 238  VAL A O   1 
ATOM   1171  C  CB  . VAL A  1 151 ? 32.036  -12.781 49.972  1.00 11.63  ? 238  VAL A CB  1 
ATOM   1172  C  CG1 . VAL A  1 151 ? 31.082  -13.962 49.996  1.00 11.88  ? 238  VAL A CG1 1 
ATOM   1173  C  CG2 . VAL A  1 151 ? 31.258  -11.442 49.860  1.00 12.17  ? 238  VAL A CG2 1 
ATOM   1174  N  N   . CYS A  1 152 ? 33.677  -15.110 51.757  1.00 11.23  ? 239  CYS A N   1 
ATOM   1175  C  CA  . CYS A  1 152 ? 34.593  -16.267 51.767  1.00 11.18  ? 239  CYS A CA  1 
ATOM   1176  C  C   . CYS A  1 152 ? 33.966  -17.527 51.176  1.00 11.48  ? 239  CYS A C   1 
ATOM   1177  O  O   . CYS A  1 152 ? 32.753  -17.772 51.335  1.00 11.25  ? 239  CYS A O   1 
ATOM   1178  C  CB  . CYS A  1 152 ? 35.069  -16.582 53.192  1.00 11.08  ? 239  CYS A CB  1 
ATOM   1179  S  SG  . CYS A  1 152 ? 35.792  -15.166 54.060  1.00 12.02  ? 239  CYS A SG  1 
ATOM   1180  N  N   . HIS A  1 153 ? 34.817  -18.335 50.529  1.00 11.23  ? 240  HIS A N   1 
ATOM   1181  C  CA  . HIS A  1 153 ? 34.402  -19.606 49.940  1.00 11.13  ? 240  HIS A CA  1 
ATOM   1182  C  C   . HIS A  1 153 ? 35.491  -20.665 50.129  1.00 11.37  ? 240  HIS A C   1 
ATOM   1183  O  O   . HIS A  1 153 ? 36.607  -20.529 49.589  1.00 11.03  ? 240  HIS A O   1 
ATOM   1184  C  CB  . HIS A  1 153 ? 34.055  -19.457 48.450  1.00 11.09  ? 240  HIS A CB  1 
ATOM   1185  C  CG  . HIS A  1 153 ? 33.574  -20.726 47.816  1.00 11.92  ? 240  HIS A CG  1 
ATOM   1186  N  ND1 . HIS A  1 153 ? 34.386  -21.533 47.042  1.00 14.43  ? 240  HIS A ND1 1 
ATOM   1187  C  CD2 . HIS A  1 153 ? 32.358  -21.330 47.840  1.00 11.29  ? 240  HIS A CD2 1 
ATOM   1188  C  CE1 . HIS A  1 153 ? 33.697  -22.590 46.639  1.00 9.59   ? 240  HIS A CE1 1 
ATOM   1189  N  NE2 . HIS A  1 153 ? 32.462  -22.486 47.101  1.00 12.88  ? 240  HIS A NE2 1 
ATOM   1190  N  N   . LYS A  1 154 ? 35.146  -21.688 50.913  1.00 10.95  ? 241  LYS A N   1 
ATOM   1191  C  CA  . LYS A  1 154 ? 36.030  -22.810 51.247  1.00 11.88  ? 241  LYS A CA  1 
ATOM   1192  C  C   . LYS A  1 154 ? 37.390  -22.333 51.759  1.00 12.28  ? 241  LYS A C   1 
ATOM   1193  O  O   . LYS A  1 154 ? 38.441  -22.852 51.348  1.00 12.82  ? 241  LYS A O   1 
ATOM   1194  C  CB  . LYS A  1 154 ? 36.188  -23.771 50.053  1.00 11.66  ? 241  LYS A CB  1 
ATOM   1195  C  CG  . LYS A  1 154 ? 34.858  -24.373 49.577  1.00 12.26  ? 241  LYS A CG  1 
ATOM   1196  C  CD  . LYS A  1 154 ? 35.050  -25.355 48.414  1.00 12.65  ? 241  LYS A CD  1 
ATOM   1197  C  CE  . LYS A  1 154 ? 35.776  -26.637 48.821  1.00 13.83  ? 241  LYS A CE  1 
ATOM   1198  N  NZ  . LYS A  1 154 ? 35.163  -27.386 49.978  1.00 15.03  ? 241  LYS A NZ  1 
ATOM   1199  N  N   . GLY A  1 155 ? 37.356  -21.326 52.635  1.00 11.72  ? 242  GLY A N   1 
ATOM   1200  C  CA  . GLY A  1 155 ? 38.567  -20.747 53.215  1.00 12.43  ? 242  GLY A CA  1 
ATOM   1201  C  C   . GLY A  1 155 ? 39.162  -19.544 52.498  1.00 12.02  ? 242  GLY A C   1 
ATOM   1202  O  O   . GLY A  1 155 ? 39.969  -18.815 53.087  1.00 12.03  ? 242  GLY A O   1 
ATOM   1203  N  N   . VAL A  1 156 ? 38.785  -19.343 51.234  1.00 12.13  ? 243  VAL A N   1 
ATOM   1204  C  CA  . VAL A  1 156 ? 39.330  -18.248 50.417  1.00 13.20  ? 243  VAL A CA  1 
ATOM   1205  C  C   . VAL A  1 156 ? 38.423  -17.020 50.406  1.00 12.98  ? 243  VAL A C   1 
ATOM   1206  O  O   . VAL A  1 156 ? 37.253  -17.081 50.001  1.00 13.38  ? 243  VAL A O   1 
ATOM   1207  C  CB  . VAL A  1 156 ? 39.677  -18.709 48.956  1.00 12.65  ? 243  VAL A CB  1 
ATOM   1208  C  CG1 . VAL A  1 156 ? 40.122  -17.503 48.075  1.00 14.28  ? 243  VAL A CG1 1 
ATOM   1209  C  CG2 . VAL A  1 156 ? 40.782  -19.780 48.998  1.00 15.09  ? 243  VAL A CG2 1 
ATOM   1210  N  N   . CYS A  1 157 ? 38.978  -15.912 50.878  1.00 12.58  ? 244  CYS A N   1 
ATOM   1211  C  CA  . CYS A  1 157 ? 38.250  -14.656 50.977  1.00 12.13  ? 244  CYS A CA  1 
ATOM   1212  C  C   . CYS A  1 157 ? 38.940  -13.624 50.070  1.00 11.59  ? 244  CYS A C   1 
ATOM   1213  O  O   . CYS A  1 157 ? 39.972  -13.041 50.456  1.00 11.55  ? 244  CYS A O   1 
ATOM   1214  C  CB  . CYS A  1 157 ? 38.221  -14.149 52.435  1.00 11.57  ? 244  CYS A CB  1 
ATOM   1215  S  SG  . CYS A  1 157 ? 37.807  -15.350 53.736  1.00 12.85  ? 244  CYS A SG  1 
ATOM   1216  N  N   . PRO A  1 158 ? 38.371  -13.371 48.874  1.00 11.29  ? 245  PRO A N   1 
ATOM   1217  C  CA  . PRO A  1 158 ? 38.943  -12.305 48.042  1.00 10.65  ? 245  PRO A CA  1 
ATOM   1218  C  C   . PRO A  1 158 ? 38.579  -10.899 48.545  1.00 10.50  ? 245  PRO A C   1 
ATOM   1219  O  O   . PRO A  1 158 ? 37.469  -10.674 49.078  1.00 10.54  ? 245  PRO A O   1 
ATOM   1220  C  CB  . PRO A  1 158 ? 38.310  -12.544 46.654  1.00 11.33  ? 245  PRO A CB  1 
ATOM   1221  C  CG  . PRO A  1 158 ? 37.587  -13.873 46.750  1.00 11.19  ? 245  PRO A CG  1 
ATOM   1222  C  CD  . PRO A  1 158 ? 37.226  -14.010 48.209  1.00 11.62  ? 245  PRO A CD  1 
ATOM   1223  N  N   . VAL A  1 159 ? 39.510  -9.964  48.370  1.00 9.34   ? 246  VAL A N   1 
ATOM   1224  C  CA  . VAL A  1 159 ? 39.319  -8.577  48.762  1.00 8.91   ? 246  VAL A CA  1 
ATOM   1225  C  C   . VAL A  1 159 ? 39.788  -7.669  47.610  1.00 9.69   ? 246  VAL A C   1 
ATOM   1226  O  O   . VAL A  1 159 ? 40.874  -7.855  47.083  1.00 10.23  ? 246  VAL A O   1 
ATOM   1227  C  CB  . VAL A  1 159 ? 40.111  -8.251  50.075  1.00 8.78   ? 246  VAL A CB  1 
ATOM   1228  C  CG1 . VAL A  1 159 ? 40.100  -6.747  50.428  1.00 8.08   ? 246  VAL A CG1 1 
ATOM   1229  C  CG2 . VAL A  1 159 ? 39.609  -9.100  51.267  1.00 7.74   ? 246  VAL A CG2 1 
ATOM   1230  N  N   . VAL A  1 160 ? 38.984  -6.671  47.249  1.00 9.98   ? 247  VAL A N   1 
ATOM   1231  C  CA  . VAL A  1 160 ? 39.364  -5.694  46.211  1.00 9.57   ? 247  VAL A CA  1 
ATOM   1232  C  C   . VAL A  1 160 ? 39.989  -4.462  46.875  1.00 10.22  ? 247  VAL A C   1 
ATOM   1233  O  O   . VAL A  1 160 ? 39.411  -3.893  47.814  1.00 9.39   ? 247  VAL A O   1 
ATOM   1234  C  CB  . VAL A  1 160 ? 38.124  -5.253  45.382  1.00 9.79   ? 247  VAL A CB  1 
ATOM   1235  C  CG1 . VAL A  1 160 ? 38.547  -4.376  44.191  1.00 9.80   ? 247  VAL A CG1 1 
ATOM   1236  C  CG2 . VAL A  1 160 ? 37.301  -6.473  44.935  1.00 9.64   ? 247  VAL A CG2 1 
ATOM   1237  N  N   . MET A  1 161 ? 41.188  -4.084  46.416  1.00 10.19  ? 248  MET A N   1 
ATOM   1238  C  CA  . MET A  1 161 ? 41.920  -2.927  46.941  1.00 10.78  ? 248  MET A CA  1 
ATOM   1239  C  C   . MET A  1 161 ? 42.351  -2.000  45.804  1.00 10.76  ? 248  MET A C   1 
ATOM   1240  O  O   . MET A  1 161 ? 42.575  -2.464  44.690  1.00 10.67  ? 248  MET A O   1 
ATOM   1241  C  CB  . MET A  1 161 ? 43.167  -3.398  47.686  1.00 10.34  ? 248  MET A CB  1 
ATOM   1242  C  CG  . MET A  1 161 ? 42.879  -4.276  48.892  1.00 10.66  ? 248  MET A CG  1 
ATOM   1243  S  SD  . MET A  1 161 ? 44.430  -4.765  49.671  1.00 12.19  ? 248  MET A SD  1 
ATOM   1244  C  CE  . MET A  1 161 ? 43.847  -5.988  50.828  1.00 10.92  ? 248  MET A CE  1 
ATOM   1245  N  N   . THR A  1 162 ? 42.447  -0.703  46.079  1.00 11.55  ? 249  THR A N   1 
ATOM   1246  C  CA  . THR A  1 162 ? 42.864  0.283   45.082  1.00 11.59  ? 249  THR A CA  1 
ATOM   1247  C  C   . THR A  1 162 ? 43.979  1.143   45.707  1.00 11.90  ? 249  THR A C   1 
ATOM   1248  O  O   . THR A  1 162 ? 43.925  1.461   46.900  1.00 11.39  ? 249  THR A O   1 
ATOM   1249  C  CB  . THR A  1 162 ? 41.662  1.145   44.611  1.00 11.62  ? 249  THR A CB  1 
ATOM   1250  O  OG1 . THR A  1 162 ? 40.697  0.285   43.983  1.00 12.77  ? 249  THR A OG1 1 
ATOM   1251  C  CG2 . THR A  1 162 ? 42.094  2.238   43.601  1.00 11.87  ? 249  THR A CG2 1 
ATOM   1252  N  N   . ASP A  1 163 ? 44.991  1.477   44.902  1.00 11.84  ? 250  ASP A N   1 
ATOM   1253  C  CA  . ASP A  1 163 ? 46.061  2.390   45.300  1.00 12.66  ? 250  ASP A CA  1 
ATOM   1254  C  C   . ASP A  1 163 ? 46.324  3.273   44.063  1.00 13.16  ? 250  ASP A C   1 
ATOM   1255  O  O   . ASP A  1 163 ? 46.492  2.757   42.959  1.00 13.05  ? 250  ASP A O   1 
ATOM   1256  C  CB  . ASP A  1 163 ? 47.293  1.567   45.699  1.00 12.73  ? 250  ASP A CB  1 
ATOM   1257  C  CG  . ASP A  1 163 ? 48.361  2.377   46.459  1.00 12.36  ? 250  ASP A CG  1 
ATOM   1258  O  OD1 . ASP A  1 163 ? 49.244  1.739   47.066  1.00 12.73  ? 250  ASP A OD1 1 
ATOM   1259  O  OD2 . ASP A  1 163 ? 48.339  3.621   46.447  1.00 13.07  ? 250  ASP A OD2 1 
ATOM   1260  N  N   . GLY A  1 164 ? 46.326  4.585   44.240  1.00 14.03  ? 251  GLY A N   1 
ATOM   1261  C  CA  . GLY A  1 164 ? 46.452  5.519   43.111  1.00 15.32  ? 251  GLY A CA  1 
ATOM   1262  C  C   . GLY A  1 164 ? 45.410  6.625   43.122  1.00 15.64  ? 251  GLY A C   1 
ATOM   1263  O  O   . GLY A  1 164 ? 44.635  6.728   44.075  1.00 16.44  ? 251  GLY A O   1 
ATOM   1264  N  N   . PRO A  1 165 ? 45.376  7.460   42.056  1.00 16.26  ? 252  PRO A N   1 
ATOM   1265  C  CA  . PRO A  1 165 ? 44.471  8.608   41.975  1.00 16.76  ? 252  PRO A CA  1 
ATOM   1266  C  C   . PRO A  1 165 ? 43.001  8.197   42.129  1.00 17.34  ? 252  PRO A C   1 
ATOM   1267  O  O   . PRO A  1 165 ? 42.602  7.101   41.691  1.00 17.47  ? 252  PRO A O   1 
ATOM   1268  C  CB  . PRO A  1 165 ? 44.720  9.160   40.559  1.00 16.36  ? 252  PRO A CB  1 
ATOM   1269  C  CG  . PRO A  1 165 ? 46.123  8.718   40.242  1.00 16.41  ? 252  PRO A CG  1 
ATOM   1270  C  CD  . PRO A  1 165 ? 46.236  7.355   40.855  1.00 16.06  ? 252  PRO A CD  1 
ATOM   1271  N  N   . ALA A  1 166 ? 42.241  9.063   42.789  1.00 18.20  ? 253  ALA A N   1 
ATOM   1272  C  CA  . ALA A  1 166 ? 40.775  8.949   42.890  1.00 19.49  ? 253  ALA A CA  1 
ATOM   1273  C  C   . ALA A  1 166 ? 40.063  9.491   41.637  1.00 20.11  ? 253  ALA A C   1 
ATOM   1274  O  O   . ALA A  1 166 ? 38.881  9.205   41.405  1.00 20.60  ? 253  ALA A O   1 
ATOM   1275  C  CB  . ALA A  1 166 ? 40.277  9.688   44.139  1.00 19.69  ? 253  ALA A CB  1 
ATOM   1276  N  N   . ASN A  1 167 ? 40.799  10.241  40.821  1.00 20.56  ? 254  ASN A N   1 
ATOM   1277  C  CA  . ASN A  1 167 ? 40.232  11.032  39.732  1.00 20.62  ? 254  ASN A CA  1 
ATOM   1278  C  C   . ASN A  1 167 ? 40.863  10.710  38.368  1.00 21.23  ? 254  ASN A C   1 
ATOM   1279  O  O   . ASN A  1 167 ? 40.796  11.512  37.425  1.00 21.14  ? 254  ASN A O   1 
ATOM   1280  C  CB  . ASN A  1 167 ? 40.406  12.518  40.064  1.00 20.78  ? 254  ASN A CB  1 
ATOM   1281  C  CG  . ASN A  1 167 ? 41.878  12.900  40.266  1.00 22.01  ? 254  ASN A CG  1 
ATOM   1282  O  OD1 . ASN A  1 167 ? 42.782  12.127  39.942  1.00 22.84  ? 254  ASN A OD1 1 
ATOM   1283  N  ND2 . ASN A  1 167 ? 42.115  14.095  40.809  1.00 24.61  ? 254  ASN A ND2 1 
ATOM   1284  N  N   . ASN A  1 168 ? 41.492  9.543   38.284  1.00 20.78  ? 255  ASN A N   1 
ATOM   1285  C  CA  . ASN A  1 168 ? 42.107  9.072   37.056  1.00 22.04  ? 255  ASN A CA  1 
ATOM   1286  C  C   . ASN A  1 168 ? 42.435  7.593   37.219  1.00 21.56  ? 255  ASN A C   1 
ATOM   1287  O  O   . ASN A  1 168 ? 42.065  7.004   38.241  1.00 21.27  ? 255  ASN A O   1 
ATOM   1288  C  CB  . ASN A  1 168 ? 43.356  9.896   36.703  1.00 22.11  ? 255  ASN A CB  1 
ATOM   1289  C  CG  . ASN A  1 168 ? 43.563  10.010  35.201  1.00 24.32  ? 255  ASN A CG  1 
ATOM   1290  O  OD1 . ASN A  1 168 ? 44.078  9.089   34.565  1.00 24.28  ? 255  ASN A OD1 1 
ATOM   1291  N  ND2 . ASN A  1 168 ? 43.127  11.133  34.621  1.00 27.11  ? 255  ASN A ND2 1 
ATOM   1292  N  N   . ARG A  1 169 ? 43.100  6.994   36.224  1.00 21.44  ? 256  ARG A N   1 
ATOM   1293  C  CA  . ARG A  1 169 ? 43.469  5.579   36.276  1.00 21.98  ? 256  ARG A CA  1 
ATOM   1294  C  C   . ARG A  1 169 ? 44.282  5.272   37.543  1.00 20.66  ? 256  ARG A C   1 
ATOM   1295  O  O   . ARG A  1 169 ? 45.191  6.015   37.907  1.00 20.63  ? 256  ARG A O   1 
ATOM   1296  C  CB  . ARG A  1 169 ? 44.221  5.128   35.010  1.00 21.77  ? 256  ARG A CB  1 
ATOM   1297  C  CG  . ARG A  1 169 ? 44.313  3.594   34.888  1.00 24.46  ? 256  ARG A CG  1 
ATOM   1298  C  CD  . ARG A  1 169 ? 44.595  3.037   33.461  1.00 25.52  ? 256  ARG A CD  1 
ATOM   1299  N  NE  . ARG A  1 169 ? 43.680  3.507   32.402  1.00 31.89  ? 256  ARG A NE  1 
ATOM   1300  C  CZ  . ARG A  1 169 ? 42.384  3.184   32.254  1.00 34.07  ? 256  ARG A CZ  1 
ATOM   1301  N  NH1 . ARG A  1 169 ? 41.743  2.380   33.111  1.00 31.97  ? 256  ARG A NH1 1 
ATOM   1302  N  NH2 . ARG A  1 169 ? 41.709  3.697   31.223  1.00 35.82  ? 256  ARG A NH2 1 
ATOM   1303  N  N   . ALA A  1 170 ? 43.925  4.182   38.221  1.00 19.40  ? 257  ALA A N   1 
ATOM   1304  C  CA  . ALA A  1 170 ? 44.571  3.807   39.472  1.00 17.45  ? 257  ALA A CA  1 
ATOM   1305  C  C   . ALA A  1 170 ? 44.967  2.336   39.400  1.00 17.00  ? 257  ALA A C   1 
ATOM   1306  O  O   . ALA A  1 170 ? 44.623  1.663   38.423  1.00 17.73  ? 257  ALA A O   1 
ATOM   1307  C  CB  . ALA A  1 170 ? 43.638  4.087   40.652  1.00 17.51  ? 257  ALA A CB  1 
ATOM   1308  N  N   . ALA A  1 171 ? 45.706  1.843   40.401  1.00 15.82  ? 258  ALA A N   1 
ATOM   1309  C  CA  . ALA A  1 171 ? 46.127  0.431   40.455  1.00 14.28  ? 258  ALA A CA  1 
ATOM   1310  C  C   . ALA A  1 171 ? 45.273  -0.427  41.423  1.00 14.56  ? 258  ALA A C   1 
ATOM   1311  O  O   . ALA A  1 171 ? 45.487  -0.426  42.648  1.00 13.76  ? 258  ALA A O   1 
ATOM   1312  C  CB  . ALA A  1 171 ? 47.638  0.335   40.823  1.00 14.71  ? 258  ALA A CB  1 
ATOM   1313  N  N   . THR A  1 172 ? 44.316  -1.161  40.858  1.00 13.17  ? 259  THR A N   1 
ATOM   1314  C  CA  . THR A  1 172 ? 43.418  -1.983  41.634  1.00 13.15  ? 259  THR A CA  1 
ATOM   1315  C  C   . THR A  1 172 ? 43.891  -3.430  41.557  1.00 12.26  ? 259  THR A C   1 
ATOM   1316  O  O   . THR A  1 172 ? 44.341  -3.899  40.499  1.00 12.43  ? 259  THR A O   1 
ATOM   1317  C  CB  . THR A  1 172 ? 41.943  -1.823  41.135  1.00 12.35  ? 259  THR A CB  1 
ATOM   1318  O  OG1 . THR A  1 172 ? 41.473  -0.511  41.476  1.00 12.84  ? 259  THR A OG1 1 
ATOM   1319  C  CG2 . THR A  1 172 ? 41.037  -2.866  41.745  1.00 14.04  ? 259  THR A CG2 1 
ATOM   1320  N  N   . LYS A  1 173 ? 43.819  -4.112  42.692  1.00 12.86  ? 260  LYS A N   1 
ATOM   1321  C  CA  . LYS A  1 173 ? 44.219  -5.515  42.817  1.00 12.98  ? 260  LYS A CA  1 
ATOM   1322  C  C   . LYS A  1 173 ? 43.175  -6.332  43.570  1.00 13.75  ? 260  LYS A C   1 
ATOM   1323  O  O   . LYS A  1 173 ? 42.481  -5.829  44.472  1.00 14.13  ? 260  LYS A O   1 
ATOM   1324  C  CB  . LYS A  1 173 ? 45.568  -5.643  43.552  1.00 13.69  ? 260  LYS A CB  1 
ATOM   1325  C  CG  . LYS A  1 173 ? 46.747  -4.972  42.860  1.00 13.45  ? 260  LYS A CG  1 
ATOM   1326  C  CD  . LYS A  1 173 ? 48.064  -5.296  43.564  1.00 14.06  ? 260  LYS A CD  1 
ATOM   1327  C  CE  . LYS A  1 173 ? 49.241  -4.482  42.995  1.00 18.03  ? 260  LYS A CE  1 
ATOM   1328  N  NZ  . LYS A  1 173 ? 49.311  -4.449  41.509  1.00 20.22  ? 260  LYS A NZ  1 
ATOM   1329  N  N   . ILE A  1 174 ? 43.057  -7.595  43.186  1.00 13.65  ? 261  ILE A N   1 
ATOM   1330  C  CA  . ILE A  1 174 ? 42.301  -8.550  43.963  1.00 14.12  ? 261  ILE A CA  1 
ATOM   1331  C  C   . ILE A  1 174 ? 43.262  -9.449  44.704  1.00 14.71  ? 261  ILE A C   1 
ATOM   1332  O  O   . ILE A  1 174 ? 44.107  -10.142 44.094  1.00 14.97  ? 261  ILE A O   1 
ATOM   1333  C  CB  . ILE A  1 174 ? 41.390  -9.430  43.088  1.00 14.03  ? 261  ILE A CB  1 
ATOM   1334  C  CG1 . ILE A  1 174 ? 40.634  -8.573  42.053  1.00 15.68  ? 261  ILE A CG1 1 
ATOM   1335  C  CG2 . ILE A  1 174 ? 40.516  -10.350 43.961  1.00 13.51  ? 261  ILE A CG2 1 
ATOM   1336  C  CD1 . ILE A  1 174 ? 39.547  -7.746  42.590  1.00 18.45  ? 261  ILE A CD1 1 
ATOM   1337  N  N   . ILE A  1 175 ? 43.123  -9.464  46.027  1.00 14.31  ? 262  ILE A N   1 
ATOM   1338  C  CA  . ILE A  1 175 ? 43.963  -10.319 46.840  1.00 14.15  ? 262  ILE A CA  1 
ATOM   1339  C  C   . ILE A  1 175 ? 43.122  -11.401 47.516  1.00 13.49  ? 262  ILE A C   1 
ATOM   1340  O  O   . ILE A  1 175 ? 42.059  -11.128 48.111  1.00 13.42  ? 262  ILE A O   1 
ATOM   1341  C  CB  . ILE A  1 175 ? 44.826  -9.504  47.847  1.00 14.52  ? 262  ILE A CB  1 
ATOM   1342  C  CG1 . ILE A  1 175 ? 45.617  -8.423  47.091  1.00 15.33  ? 262  ILE A CG1 1 
ATOM   1343  C  CG2 . ILE A  1 175 ? 45.773  -10.434 48.604  1.00 14.80  ? 262  ILE A CG2 1 
ATOM   1344  C  CD1 . ILE A  1 175 ? 46.416  -7.453  47.985  1.00 15.19  ? 262  ILE A CD1 1 
ATOM   1345  N  N   . TYR A  1 176 ? 43.601  -12.630 47.391  1.00 12.48  ? 263  TYR A N   1 
ATOM   1346  C  CA  . TYR A  1 176 ? 42.870  -13.792 47.844  1.00 13.09  ? 263  TYR A CA  1 
ATOM   1347  C  C   . TYR A  1 176 ? 43.528  -14.266 49.130  1.00 13.62  ? 263  TYR A C   1 
ATOM   1348  O  O   . TYR A  1 176 ? 44.715  -14.616 49.127  1.00 13.87  ? 263  TYR A O   1 
ATOM   1349  C  CB  . TYR A  1 176 ? 42.916  -14.885 46.769  1.00 11.90  ? 263  TYR A CB  1 
ATOM   1350  C  CG  . TYR A  1 176 ? 42.286  -14.473 45.463  1.00 12.40  ? 263  TYR A CG  1 
ATOM   1351  C  CD1 . TYR A  1 176 ? 43.010  -13.778 44.502  1.00 11.60  ? 263  TYR A CD1 1 
ATOM   1352  C  CD2 . TYR A  1 176 ? 40.947  -14.770 45.196  1.00 11.53  ? 263  TYR A CD2 1 
ATOM   1353  C  CE1 . TYR A  1 176 ? 42.405  -13.385 43.280  1.00 12.36  ? 263  TYR A CE1 1 
ATOM   1354  C  CE2 . TYR A  1 176 ? 40.344  -14.387 43.998  1.00 10.51  ? 263  TYR A CE2 1 
ATOM   1355  C  CZ  . TYR A  1 176 ? 41.067  -13.714 43.049  1.00 10.97  ? 263  TYR A CZ  1 
ATOM   1356  O  OH  . TYR A  1 176 ? 40.454  -13.351 41.865  1.00 12.94  ? 263  TYR A OH  1 
ATOM   1357  N  N   . PHE A  1 177 ? 42.774  -14.218 50.231  1.00 13.22  ? 264  PHE A N   1 
ATOM   1358  C  CA  . PHE A  1 177 ? 43.296  -14.592 51.545  1.00 12.71  ? 264  PHE A CA  1 
ATOM   1359  C  C   . PHE A  1 177 ? 42.752  -15.933 52.028  1.00 12.69  ? 264  PHE A C   1 
ATOM   1360  O  O   . PHE A  1 177 ? 41.600  -16.283 51.749  1.00 11.65  ? 264  PHE A O   1 
ATOM   1361  C  CB  . PHE A  1 177 ? 42.946  -13.515 52.597  1.00 12.10  ? 264  PHE A CB  1 
ATOM   1362  C  CG  . PHE A  1 177 ? 43.556  -12.157 52.338  1.00 12.39  ? 264  PHE A CG  1 
ATOM   1363  C  CD1 . PHE A  1 177 ? 42.816  -11.155 51.706  1.00 12.20  ? 264  PHE A CD1 1 
ATOM   1364  C  CD2 . PHE A  1 177 ? 44.853  -11.860 52.779  1.00 12.27  ? 264  PHE A CD2 1 
ATOM   1365  C  CE1 . PHE A  1 177 ? 43.361  -9.884  51.492  1.00 11.08  ? 264  PHE A CE1 1 
ATOM   1366  C  CE2 . PHE A  1 177 ? 45.405  -10.603 52.558  1.00 12.15  ? 264  PHE A CE2 1 
ATOM   1367  C  CZ  . PHE A  1 177 ? 44.664  -9.613  51.926  1.00 10.82  ? 264  PHE A CZ  1 
ATOM   1368  N  N   . LYS A  1 178 ? 43.577  -16.672 52.775  1.00 12.33  ? 265  LYS A N   1 
ATOM   1369  C  CA  . LYS A  1 178 ? 43.114  -17.805 53.547  1.00 12.45  ? 265  LYS A CA  1 
ATOM   1370  C  C   . LYS A  1 178 ? 43.785  -17.794 54.921  1.00 12.54  ? 265  LYS A C   1 
ATOM   1371  O  O   . LYS A  1 178 ? 45.020  -17.796 55.013  1.00 12.41  ? 265  LYS A O   1 
ATOM   1372  C  CB  . LYS A  1 178 ? 43.398  -19.138 52.831  1.00 13.09  ? 265  LYS A CB  1 
ATOM   1373  C  CG  . LYS A  1 178 ? 43.004  -20.357 53.674  1.00 15.41  ? 265  LYS A CG  1 
ATOM   1374  C  CD  . LYS A  1 178 ? 42.814  -21.603 52.831  1.00 20.44  ? 265  LYS A CD  1 
ATOM   1375  C  CE  . LYS A  1 178 ? 42.857  -22.842 53.711  1.00 25.90  ? 265  LYS A CE  1 
ATOM   1376  N  NZ  . LYS A  1 178 ? 42.614  -24.107 52.950  1.00 28.77  ? 265  LYS A NZ  1 
ATOM   1377  N  N   . GLU A  1 179 ? 42.973  -17.813 55.976  1.00 12.37  ? 266  GLU A N   1 
ATOM   1378  C  CA  . GLU A  1 179 ? 43.460  -17.661 57.366  1.00 12.96  ? 266  GLU A CA  1 
ATOM   1379  C  C   . GLU A  1 179 ? 44.368  -16.442 57.514  1.00 12.43  ? 266  GLU A C   1 
ATOM   1380  O  O   . GLU A  1 179 ? 45.345  -16.458 58.271  1.00 11.59  ? 266  GLU A O   1 
ATOM   1381  C  CB  . GLU A  1 179 ? 44.122  -18.949 57.868  1.00 13.23  ? 266  GLU A CB  1 
ATOM   1382  C  CG  . GLU A  1 179 ? 43.099  -20.048 58.116  1.00 13.93  ? 266  GLU A CG  1 
ATOM   1383  C  CD  . GLU A  1 179 ? 43.704  -21.439 58.357  1.00 17.42  ? 266  GLU A CD  1 
ATOM   1384  O  OE1 . GLU A  1 179 ? 44.894  -21.675 58.033  1.00 21.59  ? 266  GLU A OE1 1 
ATOM   1385  O  OE2 . GLU A  1 179 ? 42.965  -22.306 58.849  1.00 21.37  ? 266  GLU A OE2 1 
ATOM   1386  N  N   . GLY A  1 180 ? 44.015  -15.388 56.770  1.00 11.57  ? 267  GLY A N   1 
ATOM   1387  C  CA  . GLY A  1 180 ? 44.739  -14.120 56.775  1.00 11.87  ? 267  GLY A CA  1 
ATOM   1388  C  C   . GLY A  1 180 ? 46.057  -14.094 56.008  1.00 12.37  ? 267  GLY A C   1 
ATOM   1389  O  O   . GLY A  1 180 ? 46.750  -13.061 56.015  1.00 10.60  ? 267  GLY A O   1 
ATOM   1390  N  N   . LYS A  1 181 ? 46.379  -15.221 55.339  1.00 12.78  ? 268  LYS A N   1 
ATOM   1391  C  CA  . LYS A  1 181 ? 47.579  -15.369 54.514  1.00 13.91  ? 268  LYS A CA  1 
ATOM   1392  C  C   . LYS A  1 181 ? 47.284  -15.161 53.035  1.00 13.94  ? 268  LYS A C   1 
ATOM   1393  O  O   . LYS A  1 181 ? 46.253  -15.638 52.529  1.00 14.09  ? 268  LYS A O   1 
ATOM   1394  C  CB  . LYS A  1 181 ? 48.209  -16.754 54.742  1.00 14.22  ? 268  LYS A CB  1 
ATOM   1395  C  CG  . LYS A  1 181 ? 48.629  -16.954 56.191  1.00 17.50  ? 268  LYS A CG  1 
ATOM   1396  C  CD  . LYS A  1 181 ? 49.159  -18.357 56.446  1.00 23.36  ? 268  LYS A CD  1 
ATOM   1397  C  CE  . LYS A  1 181 ? 50.649  -18.461 56.156  1.00 29.21  ? 268  LYS A CE  1 
ATOM   1398  N  NZ  . LYS A  1 181 ? 50.951  -18.736 54.712  1.00 31.48  ? 268  LYS A NZ  1 
ATOM   1399  N  N   . ILE A  1 182 ? 48.169  -14.437 52.343  1.00 13.67  ? 269  ILE A N   1 
ATOM   1400  C  CA  . ILE A  1 182 ? 47.988  -14.163 50.908  1.00 13.79  ? 269  ILE A CA  1 
ATOM   1401  C  C   . ILE A  1 182 ? 48.192  -15.449 50.095  1.00 14.60  ? 269  ILE A C   1 
ATOM   1402  O  O   . ILE A  1 182 ? 49.271  -16.059 50.178  1.00 13.86  ? 269  ILE A O   1 
ATOM   1403  C  CB  . ILE A  1 182 ? 48.942  -13.066 50.400  1.00 13.95  ? 269  ILE A CB  1 
ATOM   1404  C  CG1 . ILE A  1 182 ? 48.581  -11.708 51.029  1.00 12.91  ? 269  ILE A CG1 1 
ATOM   1405  C  CG2 . ILE A  1 182 ? 48.921  -12.976 48.850  1.00 13.64  ? 269  ILE A CG2 1 
ATOM   1406  C  CD1 . ILE A  1 182 ? 49.716  -10.704 50.966  1.00 16.28  ? 269  ILE A CD1 1 
ATOM   1407  N  N   . GLN A  1 183 ? 47.143  -15.849 49.364  1.00 14.36  ? 270  GLN A N   1 
ATOM   1408  C  CA  . GLN A  1 183 ? 47.173  -16.991 48.434  1.00 15.30  ? 270  GLN A CA  1 
ATOM   1409  C  C   . GLN A  1 183 ? 47.562  -16.592 47.010  1.00 15.70  ? 270  GLN A C   1 
ATOM   1410  O  O   . GLN A  1 183 ? 48.194  -17.383 46.290  1.00 15.96  ? 270  GLN A O   1 
ATOM   1411  C  CB  . GLN A  1 183 ? 45.828  -17.745 48.402  1.00 15.46  ? 270  GLN A CB  1 
ATOM   1412  C  CG  . GLN A  1 183 ? 45.312  -18.237 49.750  1.00 15.26  ? 270  GLN A CG  1 
ATOM   1413  C  CD  . GLN A  1 183 ? 46.365  -19.003 50.540  1.00 17.48  ? 270  GLN A CD  1 
ATOM   1414  O  OE1 . GLN A  1 183 ? 46.963  -18.477 51.491  1.00 15.56  ? 270  GLN A OE1 1 
ATOM   1415  N  NE2 . GLN A  1 183 ? 46.597  -20.251 50.151  1.00 16.28  ? 270  GLN A NE2 1 
ATOM   1416  N  N   . LYS A  1 184 ? 47.181  -15.380 46.605  1.00 15.34  ? 271  LYS A N   1 
ATOM   1417  C  CA  . LYS A  1 184 ? 47.322  -14.907 45.231  1.00 15.49  ? 271  LYS A CA  1 
ATOM   1418  C  C   . LYS A  1 184 ? 47.012  -13.416 45.196  1.00 15.45  ? 271  LYS A C   1 
ATOM   1419  O  O   . LYS A  1 184 ? 46.142  -12.940 45.947  1.00 14.24  ? 271  LYS A O   1 
ATOM   1420  C  CB  . LYS A  1 184 ? 46.337  -15.637 44.294  1.00 15.59  ? 271  LYS A CB  1 
ATOM   1421  C  CG  . LYS A  1 184 ? 46.519  -15.357 42.761  1.00 15.92  ? 271  LYS A CG  1 
ATOM   1422  C  CD  . LYS A  1 184 ? 45.539  -16.250 41.960  1.00 16.26  ? 271  LYS A CD  1 
ATOM   1423  C  CE  . LYS A  1 184 ? 45.583  -16.113 40.430  1.00 18.31  ? 271  LYS A CE  1 
ATOM   1424  N  NZ  . LYS A  1 184 ? 44.730  -17.245 39.836  1.00 18.61  ? 271  LYS A NZ  1 
ATOM   1425  N  N   . ILE A  1 185 ? 47.705  -12.700 44.313  1.00 15.12  ? 272  ILE A N   1 
ATOM   1426  C  CA  . ILE A  1 185 ? 47.432  -11.289 44.042  1.00 15.03  ? 272  ILE A CA  1 
ATOM   1427  C  C   . ILE A  1 185 ? 47.261  -11.143 42.527  1.00 15.28  ? 272  ILE A C   1 
ATOM   1428  O  O   . ILE A  1 185 ? 48.103  -11.629 41.762  1.00 13.48  ? 272  ILE A O   1 
ATOM   1429  C  CB  . ILE A  1 185 ? 48.583  -10.363 44.548  1.00 15.23  ? 272  ILE A CB  1 
ATOM   1430  C  CG1 . ILE A  1 185 ? 48.781  -10.480 46.068  1.00 16.33  ? 272  ILE A CG1 1 
ATOM   1431  C  CG2 . ILE A  1 185 ? 48.341  -8.919  44.154  1.00 14.19  ? 272  ILE A CG2 1 
ATOM   1432  C  CD1 . ILE A  1 185 ? 50.106  -9.918  46.569  1.00 16.40  ? 272  ILE A CD1 1 
ATOM   1433  N  N   . GLU A  1 186 ? 46.183  -10.475 42.108  1.00 15.01  ? 273  GLU A N   1 
ATOM   1434  C  CA  . GLU A  1 186 ? 45.907  -10.223 40.701  1.00 16.44  ? 273  GLU A CA  1 
ATOM   1435  C  C   . GLU A  1 186 ? 45.691  -8.757  40.489  1.00 16.54  ? 273  GLU A C   1 
ATOM   1436  O  O   . GLU A  1 186 ? 45.003  -8.117  41.286  1.00 17.06  ? 273  GLU A O   1 
ATOM   1437  C  CB  . GLU A  1 186 ? 44.588  -10.871 40.284  1.00 16.80  ? 273  GLU A CB  1 
ATOM   1438  C  CG  . GLU A  1 186 ? 44.538  -12.358 40.246  1.00 18.07  ? 273  GLU A CG  1 
ATOM   1439  C  CD  . GLU A  1 186 ? 43.294  -12.795 39.518  1.00 18.70  ? 273  GLU A CD  1 
ATOM   1440  O  OE1 . GLU A  1 186 ? 42.182  -12.418 39.959  1.00 16.59  ? 273  GLU A OE1 1 
ATOM   1441  O  OE2 . GLU A  1 186 ? 43.437  -13.485 38.489  1.00 19.58  ? 273  GLU A OE2 1 
ATOM   1442  N  N   . GLU A  1 187 ? 46.231  -8.232  39.393  1.00 16.13  ? 274  GLU A N   1 
ATOM   1443  C  CA  . GLU A  1 187 ? 45.873  -6.899  38.933  1.00 16.74  ? 274  GLU A CA  1 
ATOM   1444  C  C   . GLU A  1 187 ? 44.469  -6.940  38.338  1.00 15.98  ? 274  GLU A C   1 
ATOM   1445  O  O   . GLU A  1 187 ? 44.083  -7.965  37.780  1.00 15.87  ? 274  GLU A O   1 
ATOM   1446  C  CB  . GLU A  1 187 ? 46.869  -6.432  37.878  1.00 17.52  ? 274  GLU A CB  1 
ATOM   1447  C  CG  . GLU A  1 187 ? 48.247  -6.182  38.461  1.00 21.50  ? 274  GLU A CG  1 
ATOM   1448  C  CD  . GLU A  1 187 ? 49.242  -5.691  37.430  1.00 29.25  ? 274  GLU A CD  1 
ATOM   1449  O  OE1 . GLU A  1 187 ? 48.896  -5.628  36.225  1.00 30.80  ? 274  GLU A OE1 1 
ATOM   1450  O  OE2 . GLU A  1 187 ? 50.382  -5.367  37.839  1.00 33.88  ? 274  GLU A OE2 1 
ATOM   1451  N  N   . LEU A  1 188 ? 43.732  -5.834  38.455  1.00 15.58  ? 275  LEU A N   1 
ATOM   1452  C  CA  . LEU A  1 188 ? 42.389  -5.715  37.862  1.00 15.21  ? 275  LEU A CA  1 
ATOM   1453  C  C   . LEU A  1 188 ? 42.461  -5.986  36.347  1.00 15.79  ? 275  LEU A C   1 
ATOM   1454  O  O   . LEU A  1 188 ? 43.346  -5.454  35.653  1.00 15.42  ? 275  LEU A O   1 
ATOM   1455  C  CB  . LEU A  1 188 ? 41.782  -4.330  38.133  1.00 15.36  ? 275  LEU A CB  1 
ATOM   1456  C  CG  . LEU A  1 188 ? 40.433  -4.015  37.458  1.00 14.69  ? 275  LEU A CG  1 
ATOM   1457  C  CD1 . LEU A  1 188 ? 39.273  -4.779  38.097  1.00 13.94  ? 275  LEU A CD1 1 
ATOM   1458  C  CD2 . LEU A  1 188 ? 40.124  -2.501  37.438  1.00 14.04  ? 275  LEU A CD2 1 
ATOM   1459  N  N   . ALA A  1 189 ? 41.548  -6.827  35.864  1.00 15.79  ? 276  ALA A N   1 
ATOM   1460  C  CA  . ALA A  1 189 ? 41.424  -7.132  34.442  1.00 15.65  ? 276  ALA A CA  1 
ATOM   1461  C  C   . ALA A  1 189 ? 40.027  -6.731  33.974  1.00 15.78  ? 276  ALA A C   1 
ATOM   1462  O  O   . ALA A  1 189 ? 39.149  -6.433  34.799  1.00 15.82  ? 276  ALA A O   1 
ATOM   1463  C  CB  . ALA A  1 189 ? 41.675  -8.605  34.189  1.00 16.26  ? 276  ALA A CB  1 
ATOM   1464  N  N   . GLY A  1 190 ? 39.841  -6.690  32.655  1.00 15.08  ? 277  GLY A N   1 
ATOM   1465  C  CA  . GLY A  1 190 ? 38.544  -6.386  32.055  1.00 14.44  ? 277  GLY A CA  1 
ATOM   1466  C  C   . GLY A  1 190 ? 38.235  -4.942  31.706  1.00 13.82  ? 277  GLY A C   1 
ATOM   1467  O  O   . GLY A  1 190 ? 39.130  -4.097  31.594  1.00 14.22  ? 277  GLY A O   1 
ATOM   1468  N  N   . ASN A  1 191 ? 36.950  -4.663  31.509  1.00 13.04  ? 278  ASN A N   1 
ATOM   1469  C  CA  . ASN A  1 191 ? 36.510  -3.348  31.033  1.00 12.90  ? 278  ASN A CA  1 
ATOM   1470  C  C   . ASN A  1 191 ? 36.141  -2.269  32.060  1.00 12.79  ? 278  ASN A C   1 
ATOM   1471  O  O   . ASN A  1 191 ? 35.893  -1.131  31.667  1.00 12.65  ? 278  ASN A O   1 
ATOM   1472  C  CB  . ASN A  1 191 ? 35.421  -3.493  29.952  1.00 12.65  ? 278  ASN A CB  1 
ATOM   1473  C  CG  . ASN A  1 191 ? 35.970  -4.123  28.652  1.00 13.37  ? 278  ASN A CG  1 
ATOM   1474  O  OD1 . ASN A  1 191 ? 37.184  -4.060  28.369  1.00 12.43  ? 278  ASN A OD1 1 
ATOM   1475  N  ND2 . ASN A  1 191 ? 35.088  -4.756  27.885  1.00 12.16  ? 278  ASN A ND2 1 
ATOM   1476  N  N   . ALA A  1 192 ? 36.130  -2.584  33.362  1.00 13.31  ? 279  ALA A N   1 
ATOM   1477  C  CA  . ALA A  1 192 ? 35.957  -1.510  34.369  1.00 13.46  ? 279  ALA A CA  1 
ATOM   1478  C  C   . ALA A  1 192 ? 37.183  -0.610  34.332  1.00 14.30  ? 279  ALA A C   1 
ATOM   1479  O  O   . ALA A  1 192 ? 38.305  -1.112  34.384  1.00 15.44  ? 279  ALA A O   1 
ATOM   1480  C  CB  . ALA A  1 192 ? 35.740  -2.066  35.782  1.00 12.40  ? 279  ALA A CB  1 
ATOM   1481  N  N   . GLN A  1 193 ? 36.978  0.705   34.245  1.00 15.14  ? 280  GLN A N   1 
ATOM   1482  C  CA  . GLN A  1 193 ? 38.094  1.646   34.049  1.00 16.14  ? 280  GLN A CA  1 
ATOM   1483  C  C   . GLN A  1 193 ? 38.656  2.226   35.350  1.00 15.48  ? 280  GLN A C   1 
ATOM   1484  O  O   . GLN A  1 193 ? 39.752  2.826   35.373  1.00 15.31  ? 280  GLN A O   1 
ATOM   1485  C  CB  . GLN A  1 193 ? 37.696  2.759   33.081  1.00 15.68  ? 280  GLN A CB  1 
ATOM   1486  C  CG  . GLN A  1 193 ? 37.340  2.255   31.680  1.00 16.49  ? 280  GLN A CG  1 
ATOM   1487  C  CD  . GLN A  1 193 ? 37.142  3.382   30.664  1.00 18.50  ? 280  GLN A CD  1 
ATOM   1488  O  OE1 . GLN A  1 193 ? 37.453  4.545   30.939  1.00 23.55  ? 280  GLN A OE1 1 
ATOM   1489  N  NE2 . GLN A  1 193 ? 36.604  3.040   29.490  1.00 18.94  ? 280  GLN A NE2 1 
ATOM   1490  N  N   . HIS A  1 194 ? 37.909  2.044   36.439  1.00 14.67  ? 281  HIS A N   1 
ATOM   1491  C  CA  . HIS A  1 194 ? 38.302  2.587   37.736  1.00 13.85  ? 281  HIS A CA  1 
ATOM   1492  C  C   . HIS A  1 194 ? 37.427  1.938   38.786  1.00 13.51  ? 281  HIS A C   1 
ATOM   1493  O  O   . HIS A  1 194 ? 36.219  1.753   38.560  1.00 12.92  ? 281  HIS A O   1 
ATOM   1494  C  CB  . HIS A  1 194 ? 38.115  4.106   37.784  1.00 13.56  ? 281  HIS A CB  1 
ATOM   1495  C  CG  . HIS A  1 194 ? 38.654  4.744   39.028  1.00 15.11  ? 281  HIS A CG  1 
ATOM   1496  N  ND1 . HIS A  1 194 ? 39.965  5.168   39.143  1.00 15.27  ? 281  HIS A ND1 1 
ATOM   1497  C  CD2 . HIS A  1 194 ? 38.060  5.037   40.212  1.00 16.05  ? 281  HIS A CD2 1 
ATOM   1498  C  CE1 . HIS A  1 194 ? 40.150  5.703   40.340  1.00 14.31  ? 281  HIS A CE1 1 
ATOM   1499  N  NE2 . HIS A  1 194 ? 39.015  5.630   41.010  1.00 17.92  ? 281  HIS A NE2 1 
ATOM   1500  N  N   . ILE A  1 195 ? 38.039  1.624   39.929  1.00 12.71  ? 282  ILE A N   1 
ATOM   1501  C  CA  . ILE A  1 195 ? 37.372  0.857   40.977  1.00 12.00  ? 282  ILE A CA  1 
ATOM   1502  C  C   . ILE A  1 195 ? 37.580  1.467   42.358  1.00 12.50  ? 282  ILE A C   1 
ATOM   1503  O  O   . ILE A  1 195 ? 38.722  1.694   42.780  1.00 12.86  ? 282  ILE A O   1 
ATOM   1504  C  CB  . ILE A  1 195 ? 37.847  -0.642  40.959  1.00 11.86  ? 282  ILE A CB  1 
ATOM   1505  C  CG1 . ILE A  1 195 ? 37.417  -1.340  39.659  1.00 11.33  ? 282  ILE A CG1 1 
ATOM   1506  C  CG2 . ILE A  1 195 ? 37.403  -1.373  42.221  1.00 11.00  ? 282  ILE A CG2 1 
ATOM   1507  C  CD1 . ILE A  1 195 ? 35.931  -1.656  39.530  1.00 11.13  ? 282  ILE A CD1 1 
ATOM   1508  N  N   . GLU A  1 196 ? 36.473  1.739   43.053  1.00 12.53  ? 283  GLU A N   1 
ATOM   1509  C  CA  . GLU A  1 196 ? 36.504  2.158   44.468  1.00 12.49  ? 283  GLU A CA  1 
ATOM   1510  C  C   . GLU A  1 196 ? 35.439  1.386   45.234  1.00 11.53  ? 283  GLU A C   1 
ATOM   1511  O  O   . GLU A  1 196 ? 34.374  1.106   44.680  1.00 11.27  ? 283  GLU A O   1 
ATOM   1512  C  CB  . GLU A  1 196 ? 36.177  3.651   44.623  1.00 12.82  ? 283  GLU A CB  1 
ATOM   1513  C  CG  . GLU A  1 196 ? 37.054  4.632   43.844  1.00 14.77  ? 283  GLU A CG  1 
ATOM   1514  C  CD  . GLU A  1 196 ? 38.406  4.898   44.492  1.00 17.91  ? 283  GLU A CD  1 
ATOM   1515  O  OE1 . GLU A  1 196 ? 39.133  5.756   43.951  1.00 20.05  ? 283  GLU A OE1 1 
ATOM   1516  O  OE2 . GLU A  1 196 ? 38.754  4.248   45.505  1.00 17.92  ? 283  GLU A OE2 1 
ATOM   1517  N  N   . GLU A  1 197 ? 35.739  1.047   46.495  1.00 11.43  ? 284  GLU A N   1 
ATOM   1518  C  CA  . GLU A  1 197 ? 34.719  0.757   47.506  1.00 11.43  ? 284  GLU A CA  1 
ATOM   1519  C  C   . GLU A  1 197 ? 33.701  -0.313  47.088  1.00 11.03  ? 284  GLU A C   1 
ATOM   1520  O  O   . GLU A  1 197 ? 32.486  -0.088  47.103  1.00 12.05  ? 284  GLU A O   1 
ATOM   1521  C  CB  . GLU A  1 197 ? 34.003  2.065   47.906  1.00 10.78  ? 284  GLU A CB  1 
ATOM   1522  C  CG  . GLU A  1 197 ? 34.867  3.057   48.687  1.00 12.36  ? 284  GLU A CG  1 
ATOM   1523  C  CD  . GLU A  1 197 ? 34.285  4.471   48.710  1.00 11.01  ? 284  GLU A CD  1 
ATOM   1524  O  OE1 . GLU A  1 197 ? 33.307  4.753   47.971  1.00 12.00  ? 284  GLU A OE1 1 
ATOM   1525  O  OE2 . GLU A  1 197 ? 34.810  5.325   49.469  1.00 12.18  ? 284  GLU A OE2 1 
ATOM   1526  N  N   . CYS A  1 198 ? 34.195  -1.484  46.705  1.00 11.19  ? 285  CYS A N   1 
ATOM   1527  C  CA  . CYS A  1 198 ? 33.325  -2.544  46.202  1.00 10.59  ? 285  CYS A CA  1 
ATOM   1528  C  C   . CYS A  1 198 ? 32.356  -3.103  47.255  1.00 10.52  ? 285  CYS A C   1 
ATOM   1529  O  O   . CYS A  1 198 ? 32.736  -3.334  48.408  1.00 9.09   ? 285  CYS A O   1 
ATOM   1530  C  CB  . CYS A  1 198 ? 34.175  -3.679  45.639  1.00 10.45  ? 285  CYS A CB  1 
ATOM   1531  S  SG  . CYS A  1 198 ? 35.035  -3.230  44.100  1.00 12.35  ? 285  CYS A SG  1 
ATOM   1532  N  N   . SER A  1 199 ? 31.100  -3.288  46.848  1.00 9.52   ? 286  SER A N   1 
ATOM   1533  C  CA  . SER A  1 199 ? 30.118  -3.987  47.688  1.00 10.22  ? 286  SER A CA  1 
ATOM   1534  C  C   . SER A  1 199 ? 29.894  -5.390  47.138  1.00 10.43  ? 286  SER A C   1 
ATOM   1535  O  O   . SER A  1 199 ? 29.440  -5.544  45.997  1.00 10.44  ? 286  SER A O   1 
ATOM   1536  C  CB  . SER A  1 199 ? 28.812  -3.229  47.727  1.00 9.89   ? 286  SER A CB  1 
ATOM   1537  O  OG  . SER A  1 199 ? 28.998  -1.931  48.274  1.00 9.49   ? 286  SER A OG  1 
ATOM   1538  N  N   . CYS A  1 200 ? 30.203  -6.403  47.946  1.00 10.21  ? 287  CYS A N   1 
ATOM   1539  C  CA  . CYS A  1 200 ? 30.334  -7.768  47.427  1.00 11.36  ? 287  CYS A CA  1 
ATOM   1540  C  C   . CYS A  1 200 ? 29.411  -8.760  48.118  1.00 11.66  ? 287  CYS A C   1 
ATOM   1541  O  O   . CYS A  1 200 ? 29.157  -8.650  49.326  1.00 11.64  ? 287  CYS A O   1 
ATOM   1542  C  CB  . CYS A  1 200 ? 31.775  -8.296  47.543  1.00 11.22  ? 287  CYS A CB  1 
ATOM   1543  S  SG  . CYS A  1 200 ? 33.029  -7.203  46.841  1.00 12.12  ? 287  CYS A SG  1 
ATOM   1544  N  N   . TYR A  1 201 ? 28.951  -9.752  47.355  1.00 11.63  ? 288  TYR A N   1 
ATOM   1545  C  CA  . TYR A  1 201 ? 28.149  -10.855 47.922  1.00 11.65  ? 288  TYR A CA  1 
ATOM   1546  C  C   . TYR A  1 201 ? 28.361  -12.124 47.102  1.00 11.84  ? 288  TYR A C   1 
ATOM   1547  O  O   . TYR A  1 201 ? 28.743  -12.046 45.918  1.00 12.18  ? 288  TYR A O   1 
ATOM   1548  C  CB  . TYR A  1 201 ? 26.637  -10.512 47.970  1.00 11.56  ? 288  TYR A CB  1 
ATOM   1549  C  CG  . TYR A  1 201 ? 26.018  -10.554 46.594  1.00 11.78  ? 288  TYR A CG  1 
ATOM   1550  C  CD1 . TYR A  1 201 ? 26.052  -9.434  45.764  1.00 12.11  ? 288  TYR A CD1 1 
ATOM   1551  C  CD2 . TYR A  1 201 ? 25.438  -11.740 46.109  1.00 11.85  ? 288  TYR A CD2 1 
ATOM   1552  C  CE1 . TYR A  1 201 ? 25.515  -9.475  44.487  1.00 12.90  ? 288  TYR A CE1 1 
ATOM   1553  C  CE2 . TYR A  1 201 ? 24.905  -11.807 44.828  1.00 12.91  ? 288  TYR A CE2 1 
ATOM   1554  C  CZ  . TYR A  1 201 ? 24.960  -10.671 44.013  1.00 12.44  ? 288  TYR A CZ  1 
ATOM   1555  O  OH  . TYR A  1 201 ? 24.418  -10.720 42.749  1.00 13.07  ? 288  TYR A OH  1 
ATOM   1556  N  N   . GLY A  1 202 ? 28.088  -13.268 47.729  1.00 10.98  ? 289  GLY A N   1 
ATOM   1557  C  CA  . GLY A  1 202 ? 28.230  -14.575 47.099  1.00 11.75  ? 289  GLY A CA  1 
ATOM   1558  C  C   . GLY A  1 202 ? 26.943  -15.365 46.890  1.00 12.44  ? 289  GLY A C   1 
ATOM   1559  O  O   . GLY A  1 202 ? 26.012  -15.330 47.711  1.00 12.38  ? 289  GLY A O   1 
ATOM   1560  N  N   . ALA A  1 203 ? 26.896  -16.093 45.779  1.00 12.33  ? 290  ALA A N   1 
ATOM   1561  C  CA  . ALA A  1 203 ? 25.788  -17.007 45.488  1.00 12.32  ? 290  ALA A CA  1 
ATOM   1562  C  C   . ALA A  1 203 ? 26.194  -17.888 44.308  1.00 12.88  ? 290  ALA A C   1 
ATOM   1563  O  O   . ALA A  1 203 ? 26.848  -17.418 43.384  1.00 13.77  ? 290  ALA A O   1 
ATOM   1564  C  CB  . ALA A  1 203 ? 24.513  -16.237 45.138  1.00 11.87  ? 290  ALA A CB  1 
ATOM   1565  N  N   . GLY A  1 204 ? 25.804  -19.157 44.351  1.00 13.73  ? 291  GLY A N   1 
ATOM   1566  C  CA  . GLY A  1 204 ? 26.094  -20.084 43.251  1.00 15.33  ? 291  GLY A CA  1 
ATOM   1567  C  C   . GLY A  1 204 ? 27.582  -20.238 42.969  1.00 15.46  ? 291  GLY A C   1 
ATOM   1568  O  O   . GLY A  1 204 ? 27.990  -20.365 41.809  1.00 16.67  ? 291  GLY A O   1 
ATOM   1569  N  N   . GLY A  1 205 ? 28.394  -20.221 44.026  1.00 15.12  ? 292  GLY A N   1 
ATOM   1570  C  CA  . GLY A  1 205 ? 29.846  -20.365 43.900  1.00 14.45  ? 292  GLY A CA  1 
ATOM   1571  C  C   . GLY A  1 205 ? 30.587  -19.161 43.333  1.00 15.11  ? 292  GLY A C   1 
ATOM   1572  O  O   . GLY A  1 205 ? 31.801  -19.224 43.140  1.00 15.50  ? 292  GLY A O   1 
ATOM   1573  N  N   . VAL A  1 206 ? 29.870  -18.073 43.071  1.00 14.18  ? 293  VAL A N   1 
ATOM   1574  C  CA  . VAL A  1 206 ? 30.436  -16.885 42.451  1.00 15.43  ? 293  VAL A CA  1 
ATOM   1575  C  C   . VAL A  1 206 ? 30.302  -15.669 43.385  1.00 14.62  ? 293  VAL A C   1 
ATOM   1576  O  O   . VAL A  1 206 ? 29.287  -15.549 44.077  1.00 14.91  ? 293  VAL A O   1 
ATOM   1577  C  CB  . VAL A  1 206 ? 29.753  -16.645 41.070  1.00 15.59  ? 293  VAL A CB  1 
ATOM   1578  C  CG1 . VAL A  1 206 ? 29.883  -15.208 40.604  1.00 16.63  ? 293  VAL A CG1 1 
ATOM   1579  C  CG2 . VAL A  1 206 ? 30.360  -17.580 40.047  1.00 17.83  ? 293  VAL A CG2 1 
ATOM   1580  N  N   . ILE A  1 207 ? 31.325  -14.799 43.411  1.00 13.63  ? 294  ILE A N   1 
ATOM   1581  C  CA  . ILE A  1 207 ? 31.263  -13.515 44.140  1.00 13.07  ? 294  ILE A CA  1 
ATOM   1582  C  C   . ILE A  1 207 ? 31.093  -12.357 43.154  1.00 13.43  ? 294  ILE A C   1 
ATOM   1583  O  O   . ILE A  1 207 ? 31.857  -12.235 42.185  1.00 13.17  ? 294  ILE A O   1 
ATOM   1584  C  CB  . ILE A  1 207 ? 32.501  -13.318 45.077  1.00 12.82  ? 294  ILE A CB  1 
ATOM   1585  C  CG1 . ILE A  1 207 ? 32.511  -14.420 46.147  1.00 12.34  ? 294  ILE A CG1 1 
ATOM   1586  C  CG2 . ILE A  1 207 ? 32.507  -11.953 45.739  1.00 13.53  ? 294  ILE A CG2 1 
ATOM   1587  C  CD1 . ILE A  1 207 ? 33.826  -14.583 46.882  1.00 12.46  ? 294  ILE A CD1 1 
ATOM   1588  N  N   . LYS A  1 208 ? 30.072  -11.544 43.372  1.00 12.30  ? 295  LYS A N   1 
ATOM   1589  C  CA  . LYS A  1 208 ? 29.896  -10.339 42.593  1.00 13.20  ? 295  LYS A CA  1 
ATOM   1590  C  C   . LYS A  1 208 ? 30.199  -9.106  43.442  1.00 11.02  ? 295  LYS A C   1 
ATOM   1591  O  O   . LYS A  1 208 ? 29.738  -9.001  44.557  1.00 12.48  ? 295  LYS A O   1 
ATOM   1592  C  CB  . LYS A  1 208 ? 28.497  -10.275 41.988  1.00 12.89  ? 295  LYS A CB  1 
ATOM   1593  C  CG  . LYS A  1 208 ? 28.332  -11.118 40.738  1.00 14.09  ? 295  LYS A CG  1 
ATOM   1594  C  CD  . LYS A  1 208 ? 26.907  -11.187 40.293  1.00 13.29  ? 295  LYS A CD  1 
ATOM   1595  C  CE  . LYS A  1 208 ? 26.580  -12.511 39.607  1.00 12.40  ? 295  LYS A CE  1 
ATOM   1596  N  NZ  . LYS A  1 208 ? 25.336  -12.460 38.780  1.00 12.33  ? 295  LYS A NZ  1 
ATOM   1597  N  N   . CYS A  1 209 ? 31.012  -8.212  42.891  1.00 11.36  ? 296  CYS A N   1 
ATOM   1598  C  CA  . CYS A  1 209 ? 31.350  -6.950  43.554  1.00 11.62  ? 296  CYS A CA  1 
ATOM   1599  C  C   . CYS A  1 209 ? 30.857  -5.809  42.681  1.00 11.34  ? 296  CYS A C   1 
ATOM   1600  O  O   . CYS A  1 209 ? 31.230  -5.707  41.504  1.00 11.11  ? 296  CYS A O   1 
ATOM   1601  C  CB  . CYS A  1 209 ? 32.872  -6.824  43.803  1.00 11.03  ? 296  CYS A CB  1 
ATOM   1602  S  SG  . CYS A  1 209 ? 33.538  -8.021  45.012  1.00 12.85  ? 296  CYS A SG  1 
ATOM   1603  N  N   . ILE A  1 210 ? 30.005  -4.965  43.261  1.00 10.87  ? 297  ILE A N   1 
ATOM   1604  C  CA  . ILE A  1 210 ? 29.418  -3.840  42.553  1.00 10.51  ? 297  ILE A CA  1 
ATOM   1605  C  C   . ILE A  1 210 ? 30.073  -2.580  43.143  1.00 10.90  ? 297  ILE A C   1 
ATOM   1606  O  O   . ILE A  1 210 ? 29.973  -2.314  44.344  1.00 11.32  ? 297  ILE A O   1 
ATOM   1607  C  CB  . ILE A  1 210 ? 27.864  -3.835  42.700  1.00 9.95   ? 297  ILE A CB  1 
ATOM   1608  C  CG1 . ILE A  1 210 ? 27.198  -4.930  41.825  1.00 10.53  ? 297  ILE A CG1 1 
ATOM   1609  C  CG2 . ILE A  1 210 ? 27.303  -2.498  42.323  1.00 11.02  ? 297  ILE A CG2 1 
ATOM   1610  C  CD1 . ILE A  1 210 ? 27.473  -6.361  42.216  1.00 9.54   ? 297  ILE A CD1 1 
ATOM   1611  N  N   . CYS A  1 211 ? 30.761  -1.824  42.305  1.00 11.35  ? 298  CYS A N   1 
ATOM   1612  C  CA  . CYS A  1 211 ? 31.743  -0.870  42.815  1.00 11.62  ? 298  CYS A CA  1 
ATOM   1613  C  C   . CYS A  1 211 ? 31.409  0.564   42.407  1.00 12.07  ? 298  CYS A C   1 
ATOM   1614  O  O   . CYS A  1 211 ? 30.276  0.870   41.965  1.00 11.68  ? 298  CYS A O   1 
ATOM   1615  C  CB  . CYS A  1 211 ? 33.171  -1.314  42.411  1.00 11.14  ? 298  CYS A CB  1 
ATOM   1616  S  SG  . CYS A  1 211 ? 33.476  -3.083  42.710  1.00 13.48  ? 298  CYS A SG  1 
ATOM   1617  N  N   . ARG A  1 212 ? 32.380  1.448   42.581  1.00 11.22  ? 299  ARG A N   1 
ATOM   1618  C  CA  . ARG A  1 212 ? 32.193  2.871   42.326  1.00 11.90  ? 299  ARG A CA  1 
ATOM   1619  C  C   . ARG A  1 212 ? 33.306  3.244   41.361  1.00 12.67  ? 299  ARG A C   1 
ATOM   1620  O  O   . ARG A  1 212 ? 34.490  3.023   41.661  1.00 13.09  ? 299  ARG A O   1 
ATOM   1621  C  CB  . ARG A  1 212 ? 32.305  3.653   43.658  1.00 11.07  ? 299  ARG A CB  1 
ATOM   1622  C  CG  . ARG A  1 212 ? 32.547  5.169   43.556  1.00 10.92  ? 299  ARG A CG  1 
ATOM   1623  C  CD  . ARG A  1 212 ? 32.926  5.733   44.959  1.00 12.27  ? 299  ARG A CD  1 
ATOM   1624  N  NE  . ARG A  1 212 ? 33.305  7.155   44.943  1.00 10.59  ? 299  ARG A NE  1 
ATOM   1625  C  CZ  . ARG A  1 212 ? 33.342  7.929   46.028  1.00 12.27  ? 299  ARG A CZ  1 
ATOM   1626  N  NH1 . ARG A  1 212 ? 32.976  7.442   47.231  1.00 9.77   ? 299  ARG A NH1 1 
ATOM   1627  N  NH2 . ARG A  1 212 ? 33.695  9.211   45.912  1.00 11.02  ? 299  ARG A NH2 1 
ATOM   1628  N  N   . ASP A  1 213 ? 32.926  3.753   40.187  1.00 13.15  ? 300  ASP A N   1 
ATOM   1629  C  CA  . ASP A  1 213 ? 33.886  4.346   39.259  1.00 12.95  ? 300  ASP A CA  1 
ATOM   1630  C  C   . ASP A  1 213 ? 33.930  5.836   39.585  1.00 13.50  ? 300  ASP A C   1 
ATOM   1631  O  O   . ASP A  1 213 ? 32.989  6.582   39.272  1.00 13.44  ? 300  ASP A O   1 
ATOM   1632  C  CB  . ASP A  1 213 ? 33.441  4.096   37.801  1.00 13.20  ? 300  ASP A CB  1 
ATOM   1633  C  CG  . ASP A  1 213 ? 34.343  4.771   36.755  1.00 14.28  ? 300  ASP A CG  1 
ATOM   1634  O  OD1 . ASP A  1 213 ? 34.207  4.439   35.555  1.00 15.84  ? 300  ASP A OD1 1 
ATOM   1635  O  OD2 . ASP A  1 213 ? 35.166  5.647   37.102  1.00 13.66  ? 300  ASP A OD2 1 
ATOM   1636  N  N   . ASN A  1 214 ? 35.003  6.271   40.248  1.00 14.05  ? 301  ASN A N   1 
ATOM   1637  C  CA  . ASN A  1 214 ? 35.140  7.668   40.651  1.00 14.80  ? 301  ASN A CA  1 
ATOM   1638  C  C   . ASN A  1 214 ? 35.722  8.586   39.572  1.00 15.68  ? 301  ASN A C   1 
ATOM   1639  O  O   . ASN A  1 214 ? 35.774  9.823   39.748  1.00 15.91  ? 301  ASN A O   1 
ATOM   1640  C  CB  . ASN A  1 214 ? 35.982  7.779   41.928  1.00 14.62  ? 301  ASN A CB  1 
ATOM   1641  C  CG  . ASN A  1 214 ? 35.621  8.992   42.738  1.00 16.08  ? 301  ASN A CG  1 
ATOM   1642  O  OD1 . ASN A  1 214 ? 34.469  9.154   43.141  1.00 15.75  ? 301  ASN A OD1 1 
ATOM   1643  N  ND2 . ASN A  1 214 ? 36.598  9.869   42.978  1.00 15.16  ? 301  ASN A ND2 1 
ATOM   1644  N  N   . TRP A  1 215 ? 36.167  7.981   38.472  1.00 16.29  ? 302  TRP A N   1 
ATOM   1645  C  CA  . TRP A  1 215 ? 36.801  8.703   37.371  1.00 17.29  ? 302  TRP A CA  1 
ATOM   1646  C  C   . TRP A  1 215 ? 35.772  9.223   36.370  1.00 18.32  ? 302  TRP A C   1 
ATOM   1647  O  O   . TRP A  1 215 ? 35.631  10.440  36.206  1.00 18.88  ? 302  TRP A O   1 
ATOM   1648  C  CB  . TRP A  1 215 ? 37.823  7.785   36.699  1.00 18.03  ? 302  TRP A CB  1 
ATOM   1649  C  CG  . TRP A  1 215 ? 38.684  8.386   35.613  1.00 18.02  ? 302  TRP A CG  1 
ATOM   1650  C  CD1 . TRP A  1 215 ? 38.847  9.712   35.296  1.00 19.94  ? 302  TRP A CD1 1 
ATOM   1651  C  CD2 . TRP A  1 215 ? 39.555  7.657   34.744  1.00 19.50  ? 302  TRP A CD2 1 
ATOM   1652  N  NE1 . TRP A  1 215 ? 39.747  9.842   34.247  1.00 20.10  ? 302  TRP A NE1 1 
ATOM   1653  C  CE2 . TRP A  1 215 ? 40.195  8.596   33.898  1.00 19.42  ? 302  TRP A CE2 1 
ATOM   1654  C  CE3 . TRP A  1 215 ? 39.853  6.297   34.593  1.00 18.81  ? 302  TRP A CE3 1 
ATOM   1655  C  CZ2 . TRP A  1 215 ? 41.107  8.211   32.911  1.00 19.22  ? 302  TRP A CZ2 1 
ATOM   1656  C  CZ3 . TRP A  1 215 ? 40.768  5.919   33.607  1.00 19.54  ? 302  TRP A CZ3 1 
ATOM   1657  C  CH2 . TRP A  1 215 ? 41.381  6.878   32.786  1.00 18.71  ? 302  TRP A CH2 1 
ATOM   1658  N  N   . LYS A  1 216 ? 35.027  8.319   35.733  1.00 18.29  ? 303  LYS A N   1 
ATOM   1659  C  CA  . LYS A  1 216 ? 34.168  8.684   34.607  1.00 19.02  ? 303  LYS A CA  1 
ATOM   1660  C  C   . LYS A  1 216 ? 32.679  8.306   34.725  1.00 18.03  ? 303  LYS A C   1 
ATOM   1661  O  O   . LYS A  1 216 ? 31.799  9.088   34.372  1.00 17.87  ? 303  LYS A O   1 
ATOM   1662  C  CB  . LYS A  1 216 ? 34.732  8.050   33.320  1.00 19.59  ? 303  LYS A CB  1 
ATOM   1663  C  CG  . LYS A  1 216 ? 36.085  8.608   32.844  1.00 22.59  ? 303  LYS A CG  1 
ATOM   1664  C  CD  . LYS A  1 216 ? 35.978  10.062  32.372  1.00 27.44  ? 303  LYS A CD  1 
ATOM   1665  C  CE  . LYS A  1 216 ? 36.605  11.040  33.371  1.00 30.81  ? 303  LYS A CE  1 
ATOM   1666  N  NZ  . LYS A  1 216 ? 36.290  12.490  33.109  1.00 33.20  ? 303  LYS A NZ  1 
ATOM   1667  N  N   . GLY A  1 217 ? 32.425  7.094   35.205  1.00 17.28  ? 304  GLY A N   1 
ATOM   1668  C  CA  . GLY A  1 217 ? 31.116  6.446   35.070  1.00 15.89  ? 304  GLY A CA  1 
ATOM   1669  C  C   . GLY A  1 217 ? 30.092  6.735   36.154  1.00 15.36  ? 304  GLY A C   1 
ATOM   1670  O  O   . GLY A  1 217 ? 30.392  6.681   37.360  1.00 14.10  ? 304  GLY A O   1 
ATOM   1671  N  N   . ALA A  1 218 ? 28.872  7.022   35.701  1.00 14.14  ? 305  ALA A N   1 
ATOM   1672  C  CA  . ALA A  1 218 ? 27.706  7.163   36.569  1.00 13.64  ? 305  ALA A CA  1 
ATOM   1673  C  C   . ALA A  1 218 ? 27.013  5.796   36.639  1.00 13.42  ? 305  ALA A C   1 
ATOM   1674  O  O   . ALA A  1 218 ? 26.153  5.578   37.486  1.00 13.00  ? 305  ALA A O   1 
ATOM   1675  C  CB  . ALA A  1 218 ? 26.769  8.221   36.018  1.00 13.98  ? 305  ALA A CB  1 
ATOM   1676  N  N   . ASN A  1 219 ? 27.374  4.900   35.717  1.00 13.02  ? 306  ASN A N   1 
ATOM   1677  C  CA  . ASN A  1 219 ? 27.064  3.473   35.846  1.00 12.70  ? 306  ASN A CA  1 
ATOM   1678  C  C   . ASN A  1 219 ? 28.121  2.771   36.709  1.00 12.60  ? 306  ASN A C   1 
ATOM   1679  O  O   . ASN A  1 219 ? 29.281  3.182   36.733  1.00 12.71  ? 306  ASN A O   1 
ATOM   1680  C  CB  . ASN A  1 219 ? 26.913  2.784   34.468  1.00 13.36  ? 306  ASN A CB  1 
ATOM   1681  C  CG  . ASN A  1 219 ? 28.110  3.027   33.532  1.00 13.18  ? 306  ASN A CG  1 
ATOM   1682  O  OD1 . ASN A  1 219 ? 28.926  3.917   33.772  1.00 13.91  ? 306  ASN A OD1 1 
ATOM   1683  N  ND2 . ASN A  1 219 ? 28.199  2.238   32.452  1.00 11.41  ? 306  ASN A ND2 1 
ATOM   1684  N  N   . ARG A  1 220 ? 27.725  1.723   37.436  1.00 11.67  ? 307  ARG A N   1 
ATOM   1685  C  CA  . ARG A  1 220 ? 28.658  1.061   38.375  1.00 11.38  ? 307  ARG A CA  1 
ATOM   1686  C  C   . ARG A  1 220 ? 29.419  -0.113  37.774  1.00 11.61  ? 307  ARG A C   1 
ATOM   1687  O  O   . ARG A  1 220 ? 28.830  -0.949  37.098  1.00 11.27  ? 307  ARG A O   1 
ATOM   1688  C  CB  . ARG A  1 220 ? 27.931  0.577   39.640  1.00 11.18  ? 307  ARG A CB  1 
ATOM   1689  C  CG  . ARG A  1 220 ? 27.341  1.689   40.469  1.00 10.91  ? 307  ARG A CG  1 
ATOM   1690  C  CD  . ARG A  1 220 ? 26.898  1.175   41.846  1.00 8.46   ? 307  ARG A CD  1 
ATOM   1691  N  NE  . ARG A  1 220 ? 26.444  2.306   42.674  1.00 10.93  ? 307  ARG A NE  1 
ATOM   1692  C  CZ  . ARG A  1 220 ? 27.245  3.177   43.288  1.00 10.99  ? 307  ARG A CZ  1 
ATOM   1693  N  NH1 . ARG A  1 220 ? 28.573  3.073   43.199  1.00 9.93   ? 307  ARG A NH1 1 
ATOM   1694  N  NH2 . ARG A  1 220 ? 26.717  4.162   44.002  1.00 10.38  ? 307  ARG A NH2 1 
ATOM   1695  N  N   . PRO A  1 221 ? 30.743  -0.168  38.019  1.00 12.06  ? 308  PRO A N   1 
ATOM   1696  C  CA  . PRO A  1 221 ? 31.520  -1.335  37.619  1.00 12.08  ? 308  PRO A CA  1 
ATOM   1697  C  C   . PRO A  1 221 ? 31.051  -2.567  38.362  1.00 11.92  ? 308  PRO A C   1 
ATOM   1698  O  O   . PRO A  1 221 ? 30.565  -2.465  39.504  1.00 12.20  ? 308  PRO A O   1 
ATOM   1699  C  CB  . PRO A  1 221 ? 32.966  -0.987  38.062  1.00 12.05  ? 308  PRO A CB  1 
ATOM   1700  C  CG  . PRO A  1 221 ? 32.986  0.419   38.338  1.00 11.38  ? 308  PRO A CG  1 
ATOM   1701  C  CD  . PRO A  1 221 ? 31.580  0.862   38.665  1.00 12.17  ? 308  PRO A CD  1 
ATOM   1702  N  N   . VAL A  1 222 ? 31.182  -3.713  37.714  1.00 11.59  ? 309  VAL A N   1 
ATOM   1703  C  CA  . VAL A  1 222 ? 30.862  -4.991  38.316  1.00 12.01  ? 309  VAL A CA  1 
ATOM   1704  C  C   . VAL A  1 222 ? 32.049  -5.924  38.070  1.00 11.96  ? 309  VAL A C   1 
ATOM   1705  O  O   . VAL A  1 222 ? 32.470  -6.134  36.913  1.00 11.96  ? 309  VAL A O   1 
ATOM   1706  C  CB  . VAL A  1 222 ? 29.557  -5.628  37.726  1.00 12.18  ? 309  VAL A CB  1 
ATOM   1707  C  CG1 . VAL A  1 222 ? 29.293  -6.993  38.365  1.00 12.83  ? 309  VAL A CG1 1 
ATOM   1708  C  CG2 . VAL A  1 222 ? 28.332  -4.680  37.892  1.00 13.24  ? 309  VAL A CG2 1 
ATOM   1709  N  N   . ILE A  1 223 ? 32.597  -6.457  39.161  1.00 11.62  ? 310  ILE A N   1 
ATOM   1710  C  CA  . ILE A  1 223 ? 33.704  -7.422  39.124  1.00 12.37  ? 310  ILE A CA  1 
ATOM   1711  C  C   . ILE A  1 223 ? 33.144  -8.797  39.522  1.00 12.40  ? 310  ILE A C   1 
ATOM   1712  O  O   . ILE A  1 223 ? 32.511  -8.942  40.568  1.00 11.55  ? 310  ILE A O   1 
ATOM   1713  C  CB  . ILE A  1 223 ? 34.861  -7.004  40.099  1.00 12.05  ? 310  ILE A CB  1 
ATOM   1714  C  CG1 . ILE A  1 223 ? 35.480  -5.660  39.688  1.00 12.90  ? 310  ILE A CG1 1 
ATOM   1715  C  CG2 . ILE A  1 223 ? 35.926  -8.082  40.205  1.00 13.23  ? 310  ILE A CG2 1 
ATOM   1716  C  CD1 . ILE A  1 223 ? 36.492  -5.097  40.735  1.00 11.32  ? 310  ILE A CD1 1 
ATOM   1717  N  N   . THR A  1 224 ? 33.365  -9.799  38.685  1.00 12.49  ? 311  THR A N   1 
ATOM   1718  C  CA  . THR A  1 224 ? 32.893  -11.146 38.983  1.00 12.98  ? 311  THR A CA  1 
ATOM   1719  C  C   . THR A  1 224 ? 34.081  -12.034 39.322  1.00 13.41  ? 311  THR A C   1 
ATOM   1720  O  O   . THR A  1 224 ? 35.013  -12.174 38.522  1.00 13.13  ? 311  THR A O   1 
ATOM   1721  C  CB  . THR A  1 224 ? 32.050  -11.746 37.825  1.00 13.38  ? 311  THR A CB  1 
ATOM   1722  O  OG1 . THR A  1 224 ? 30.965  -10.855 37.538  1.00 12.79  ? 311  THR A OG1 1 
ATOM   1723  C  CG2 . THR A  1 224 ? 31.495  -13.152 38.217  1.00 12.52  ? 311  THR A CG2 1 
ATOM   1724  N  N   . ILE A  1 225 ? 34.037  -12.619 40.513  1.00 13.20  ? 312  ILE A N   1 
ATOM   1725  C  CA  . ILE A  1 225 ? 35.200  -13.335 41.051  1.00 13.98  ? 312  ILE A CA  1 
ATOM   1726  C  C   . ILE A  1 225 ? 34.874  -14.810 41.286  1.00 13.92  ? 312  ILE A C   1 
ATOM   1727  O  O   . ILE A  1 225 ? 33.876  -15.164 41.949  1.00 14.27  ? 312  ILE A O   1 
ATOM   1728  C  CB  . ILE A  1 225 ? 35.740  -12.722 42.378  1.00 13.05  ? 312  ILE A CB  1 
ATOM   1729  C  CG1 . ILE A  1 225 ? 36.135  -11.253 42.218  1.00 14.99  ? 312  ILE A CG1 1 
ATOM   1730  C  CG2 . ILE A  1 225 ? 36.947  -13.550 42.904  1.00 14.13  ? 312  ILE A CG2 1 
ATOM   1731  C  CD1 . ILE A  1 225 ? 36.305  -10.498 43.547  1.00 14.58  ? 312  ILE A CD1 1 
ATOM   1732  N  N   . ASP A  1 226 ? 35.725  -15.669 40.739  1.00 12.74  ? 313  ASP A N   1 
ATOM   1733  C  CA  . ASP A  1 226 ? 35.658  -17.076 41.062  1.00 13.18  ? 313  ASP A CA  1 
ATOM   1734  C  C   . ASP A  1 226 ? 36.653  -17.417 42.189  1.00 13.10  ? 313  ASP A C   1 
ATOM   1735  O  O   . ASP A  1 226 ? 37.852  -17.450 41.941  1.00 13.50  ? 313  ASP A O   1 
ATOM   1736  C  CB  . ASP A  1 226 ? 35.913  -17.910 39.799  1.00 13.44  ? 313  ASP A CB  1 
ATOM   1737  C  CG  . ASP A  1 226 ? 35.672  -19.402 40.019  1.00 12.92  ? 313  ASP A CG  1 
ATOM   1738  O  OD1 . ASP A  1 226 ? 35.115  -20.048 39.122  1.00 17.88  ? 313  ASP A OD1 1 
ATOM   1739  O  OD2 . ASP A  1 226 ? 36.043  -19.936 41.077  1.00 13.61  ? 313  ASP A OD2 1 
ATOM   1740  N  N   . PRO A  1 227 ? 36.156  -17.676 43.427  1.00 12.94  ? 314  PRO A N   1 
ATOM   1741  C  CA  . PRO A  1 227 ? 37.060  -17.891 44.577  1.00 13.28  ? 314  PRO A CA  1 
ATOM   1742  C  C   . PRO A  1 227 ? 37.747  -19.254 44.611  1.00 13.29  ? 314  PRO A C   1 
ATOM   1743  O  O   . PRO A  1 227 ? 38.649  -19.454 45.439  1.00 13.43  ? 314  PRO A O   1 
ATOM   1744  C  CB  . PRO A  1 227 ? 36.134  -17.767 45.786  1.00 12.67  ? 314  PRO A CB  1 
ATOM   1745  C  CG  . PRO A  1 227 ? 34.797  -18.230 45.265  1.00 12.71  ? 314  PRO A CG  1 
ATOM   1746  C  CD  . PRO A  1 227 ? 34.737  -17.778 43.823  1.00 13.58  ? 314  PRO A CD  1 
ATOM   1747  N  N   . GLU A  1 228 ? 37.307  -20.184 43.758  1.00 13.59  ? 315  GLU A N   1 
ATOM   1748  C  CA  . GLU A  1 228 ? 37.969  -21.501 43.633  1.00 14.00  ? 315  GLU A CA  1 
ATOM   1749  C  C   . GLU A  1 228 ? 39.157  -21.421 42.659  1.00 14.15  ? 315  GLU A C   1 
ATOM   1750  O  O   . GLU A  1 228 ? 40.271  -21.835 42.992  1.00 13.75  ? 315  GLU A O   1 
ATOM   1751  C  CB  . GLU A  1 228 ? 36.980  -22.608 43.206  1.00 13.52  ? 315  GLU A CB  1 
ATOM   1752  C  CG  . GLU A  1 228 ? 35.917  -22.950 44.258  1.00 14.76  ? 315  GLU A CG  1 
ATOM   1753  C  CD  . GLU A  1 228 ? 35.126  -24.226 43.956  1.00 15.14  ? 315  GLU A CD  1 
ATOM   1754  O  OE1 . GLU A  1 228 ? 35.134  -24.705 42.804  1.00 17.78  ? 315  GLU A OE1 1 
ATOM   1755  O  OE2 . GLU A  1 228 ? 34.465  -24.745 44.879  1.00 16.76  ? 315  GLU A OE2 1 
ATOM   1756  N  N   . MET A  1 229 ? 38.913  -20.912 41.456  1.00 14.25  ? 316  MET A N   1 
ATOM   1757  C  CA  . MET A  1 229 ? 39.983  -20.674 40.486  1.00 16.57  ? 316  MET A CA  1 
ATOM   1758  C  C   . MET A  1 229 ? 40.880  -19.463 40.844  1.00 15.69  ? 316  MET A C   1 
ATOM   1759  O  O   . MET A  1 229 ? 42.036  -19.343 40.352  1.00 15.57  ? 316  MET A O   1 
ATOM   1760  C  CB  . MET A  1 229 ? 39.386  -20.482 39.092  1.00 16.33  ? 316  MET A CB  1 
ATOM   1761  C  CG  . MET A  1 229 ? 38.808  -21.737 38.457  1.00 18.87  ? 316  MET A CG  1 
ATOM   1762  S  SD  . MET A  1 229 ? 38.231  -21.404 36.770  1.00 20.68  ? 316  MET A SD  1 
ATOM   1763  C  CE  . MET A  1 229 ? 39.446  -20.190 36.273  1.00 24.55  ? 316  MET A CE  1 
ATOM   1764  N  N   . MET A  1 230 ? 40.354  -18.588 41.711  1.00 14.86  ? 317  MET A N   1 
ATOM   1765  C  CA  . MET A  1 230 ? 40.966  -17.293 42.070  1.00 14.11  ? 317  MET A CA  1 
ATOM   1766  C  C   . MET A  1 230 ? 41.257  -16.408 40.848  1.00 13.12  ? 317  MET A C   1 
ATOM   1767  O  O   . MET A  1 230 ? 42.370  -15.940 40.630  1.00 11.91  ? 317  MET A O   1 
ATOM   1768  C  CB  . MET A  1 230 ? 42.188  -17.472 43.000  1.00 13.56  ? 317  MET A CB  1 
ATOM   1769  C  CG  . MET A  1 230 ? 41.876  -18.294 44.276  1.00 13.93  ? 317  MET A CG  1 
ATOM   1770  S  SD  . MET A  1 230 ? 43.275  -18.494 45.440  1.00 17.46  ? 317  MET A SD  1 
ATOM   1771  C  CE  . MET A  1 230 ? 44.415  -19.495 44.494  1.00 18.52  ? 317  MET A CE  1 
ATOM   1772  N  N   . THR A  1 231 ? 40.221  -16.199 40.042  1.00 13.51  ? 318  THR A N   1 
ATOM   1773  C  CA  . THR A  1 231 ? 40.308  -15.365 38.855  1.00 13.41  ? 318  THR A CA  1 
ATOM   1774  C  C   . THR A  1 231 ? 39.068  -14.465 38.811  1.00 13.89  ? 318  THR A C   1 
ATOM   1775  O  O   . THR A  1 231 ? 38.065  -14.744 39.486  1.00 13.19  ? 318  THR A O   1 
ATOM   1776  C  CB  . THR A  1 231 ? 40.411  -16.233 37.556  1.00 13.59  ? 318  THR A CB  1 
ATOM   1777  O  OG1 . THR A  1 231 ? 39.347  -17.189 37.541  1.00 15.09  ? 318  THR A OG1 1 
ATOM   1778  C  CG2 . THR A  1 231 ? 41.730  -16.998 37.512  1.00 14.73  ? 318  THR A CG2 1 
ATOM   1779  N  N   . HIS A  1 232 ? 39.149  -13.372 38.053  1.00 13.96  ? 319  HIS A N   1 
ATOM   1780  C  CA  . HIS A  1 232 ? 38.037  -12.447 37.949  1.00 14.53  ? 319  HIS A CA  1 
ATOM   1781  C  C   . HIS A  1 232 ? 37.891  -11.883 36.543  1.00 14.73  ? 319  HIS A C   1 
ATOM   1782  O  O   . HIS A  1 232 ? 38.826  -11.919 35.720  1.00 13.73  ? 319  HIS A O   1 
ATOM   1783  C  CB  . HIS A  1 232 ? 38.200  -11.279 38.931  1.00 14.57  ? 319  HIS A CB  1 
ATOM   1784  C  CG  . HIS A  1 232 ? 39.217  -10.275 38.491  1.00 14.39  ? 319  HIS A CG  1 
ATOM   1785  N  ND1 . HIS A  1 232 ? 40.573  -10.501 38.602  1.00 15.59  ? 319  HIS A ND1 1 
ATOM   1786  C  CD2 . HIS A  1 232 ? 39.082  -9.060  37.904  1.00 15.77  ? 319  HIS A CD2 1 
ATOM   1787  C  CE1 . HIS A  1 232 ? 41.229  -9.470  38.102  1.00 15.20  ? 319  HIS A CE1 1 
ATOM   1788  N  NE2 . HIS A  1 232 ? 40.348  -8.582  37.673  1.00 14.39  ? 319  HIS A NE2 1 
ATOM   1789  N  N   . THR A  1 233 ? 36.709  -11.336 36.297  1.00 14.76  ? 320  THR A N   1 
ATOM   1790  C  CA  . THR A  1 233 ? 36.433  -10.510 35.117  1.00 14.91  ? 320  THR A CA  1 
ATOM   1791  C  C   . THR A  1 233 ? 35.801  -9.202  35.610  1.00 15.02  ? 320  THR A C   1 
ATOM   1792  O  O   . THR A  1 233 ? 35.328  -9.134  36.763  1.00 15.14  ? 320  THR A O   1 
ATOM   1793  C  CB  . THR A  1 233 ? 35.478  -11.243 34.128  1.00 15.17  ? 320  THR A CB  1 
ATOM   1794  O  OG1 . THR A  1 233 ? 34.251  -11.585 34.790  1.00 14.57  ? 320  THR A OG1 1 
ATOM   1795  C  CG2 . THR A  1 233 ? 36.114  -12.523 33.623  1.00 15.72  ? 320  THR A CG2 1 
ATOM   1796  N  N   . SER A  1 234 ? 35.783  -8.178  34.756  1.00 14.17  ? 321  SER A N   1 
ATOM   1797  C  CA  . SER A  1 234 ? 35.123  -6.908  35.075  1.00 14.07  ? 321  SER A CA  1 
ATOM   1798  C  C   . SER A  1 234 ? 34.446  -6.243  33.880  1.00 13.75  ? 321  SER A C   1 
ATOM   1799  O  O   . SER A  1 234 ? 34.900  -6.374  32.732  1.00 14.00  ? 321  SER A O   1 
ATOM   1800  C  CB  . SER A  1 234 ? 36.092  -5.914  35.739  1.00 13.46  ? 321  SER A CB  1 
ATOM   1801  O  OG  . SER A  1 234 ? 36.788  -5.099  34.792  1.00 14.15  ? 321  SER A OG  1 
ATOM   1802  N  N   . LYS A  1 235 ? 33.350  -5.550  34.171  1.00 13.18  ? 322  LYS A N   1 
ATOM   1803  C  CA  . LYS A  1 235 ? 32.661  -4.693  33.208  1.00 13.41  ? 322  LYS A CA  1 
ATOM   1804  C  C   . LYS A  1 235 ? 31.811  -3.668  33.979  1.00 13.13  ? 322  LYS A C   1 
ATOM   1805  O  O   . LYS A  1 235 ? 32.127  -3.361  35.132  1.00 12.55  ? 322  LYS A O   1 
ATOM   1806  C  CB  . LYS A  1 235 ? 31.850  -5.546  32.217  1.00 13.49  ? 322  LYS A CB  1 
ATOM   1807  C  CG  . LYS A  1 235 ? 30.772  -6.427  32.876  1.00 13.56  ? 322  LYS A CG  1 
ATOM   1808  C  CD  . LYS A  1 235 ? 30.285  -7.547  31.948  1.00 14.16  ? 322  LYS A CD  1 
ATOM   1809  C  CE  . LYS A  1 235 ? 29.511  -7.020  30.754  1.00 16.08  ? 322  LYS A CE  1 
ATOM   1810  N  NZ  . LYS A  1 235 ? 29.102  -8.144  29.821  1.00 15.28  ? 322  LYS A NZ  1 
ATOM   1811  N  N   . TYR A  1 236 ? 30.763  -3.130  33.346  1.00 12.68  ? 323  TYR A N   1 
ATOM   1812  C  CA  . TYR A  1 236 ? 29.812  -2.221  33.994  1.00 13.16  ? 323  TYR A CA  1 
ATOM   1813  C  C   . TYR A  1 236 ? 28.424  -2.853  34.025  1.00 13.55  ? 323  TYR A C   1 
ATOM   1814  O  O   . TYR A  1 236 ? 28.110  -3.720  33.197  1.00 13.59  ? 323  TYR A O   1 
ATOM   1815  C  CB  . TYR A  1 236 ? 29.742  -0.887  33.243  1.00 13.02  ? 323  TYR A CB  1 
ATOM   1816  C  CG  . TYR A  1 236 ? 30.966  -0.039  33.450  1.00 13.51  ? 323  TYR A CG  1 
ATOM   1817  C  CD1 . TYR A  1 236 ? 32.144  -0.301  32.738  1.00 13.98  ? 323  TYR A CD1 1 
ATOM   1818  C  CD2 . TYR A  1 236 ? 30.956  1.022   34.359  1.00 12.54  ? 323  TYR A CD2 1 
ATOM   1819  C  CE1 . TYR A  1 236 ? 33.282  0.470   32.930  1.00 12.87  ? 323  TYR A CE1 1 
ATOM   1820  C  CE2 . TYR A  1 236 ? 32.094  1.803   34.561  1.00 13.70  ? 323  TYR A CE2 1 
ATOM   1821  C  CZ  . TYR A  1 236 ? 33.252  1.519   33.841  1.00 13.22  ? 323  TYR A CZ  1 
ATOM   1822  O  OH  . TYR A  1 236 ? 34.390  2.283   34.018  1.00 13.26  ? 323  TYR A OH  1 
ATOM   1823  N  N   . LEU A  1 237 ? 27.612  -2.438  34.995  1.00 13.77  ? 324  LEU A N   1 
ATOM   1824  C  CA  . LEU A  1 237 ? 26.187  -2.752  34.991  1.00 14.44  ? 324  LEU A CA  1 
ATOM   1825  C  C   . LEU A  1 237 ? 25.595  -2.289  33.654  1.00 14.33  ? 324  LEU A C   1 
ATOM   1826  O  O   . LEU A  1 237 ? 25.798  -1.136  33.259  1.00 14.85  ? 324  LEU A O   1 
ATOM   1827  C  CB  . LEU A  1 237 ? 25.478  -2.003  36.133  1.00 14.19  ? 324  LEU A CB  1 
ATOM   1828  C  CG  . LEU A  1 237 ? 25.215  -2.665  37.484  1.00 17.24  ? 324  LEU A CG  1 
ATOM   1829  C  CD1 . LEU A  1 237 ? 24.334  -1.758  38.350  1.00 15.76  ? 324  LEU A CD1 1 
ATOM   1830  C  CD2 . LEU A  1 237 ? 24.551  -4.027  37.291  1.00 19.23  ? 324  LEU A CD2 1 
ATOM   1831  N  N   . CYS A  1 238 ? 24.878  -3.182  32.966  1.00 14.37  ? 325  CYS A N   1 
ATOM   1832  C  CA  . CYS A  1 238 ? 24.316  -2.883  31.625  1.00 14.18  ? 325  CYS A CA  1 
ATOM   1833  C  C   . CYS A  1 238 ? 23.140  -1.894  31.652  1.00 13.94  ? 325  CYS A C   1 
ATOM   1834  O  O   . CYS A  1 238 ? 22.967  -1.081  30.715  1.00 13.53  ? 325  CYS A O   1 
ATOM   1835  C  CB  . CYS A  1 238 ? 23.868  -4.178  30.916  1.00 14.01  ? 325  CYS A CB  1 
ATOM   1836  S  SG  . CYS A  1 238 ? 25.183  -5.335  30.386  1.00 14.87  ? 325  CYS A SG  1 
ATOM   1837  N  N   . SER A  1 239 ? 22.330  -1.961  32.714  1.00 13.26  ? 326  SER A N   1 
ATOM   1838  C  CA  . SER A  1 239 ? 21.070  -1.204  32.780  1.00 12.92  ? 326  SER A CA  1 
ATOM   1839  C  C   . SER A  1 239 ? 21.229  0.296   32.509  1.00 12.91  ? 326  SER A C   1 
ATOM   1840  O  O   . SER A  1 239 ? 22.228  0.922   32.903  1.00 12.80  ? 326  SER A O   1 
ATOM   1841  C  CB  . SER A  1 239 ? 20.367  -1.398  34.140  1.00 12.62  ? 326  SER A CB  1 
ATOM   1842  O  OG  . SER A  1 239 ? 19.112  -0.715  34.140  1.00 12.77  ? 326  SER A OG  1 
ATOM   1843  N  N   . LYS A  1 240 ? 20.235  0.856   31.824  1.00 12.32  ? 327  LYS A N   1 
ATOM   1844  C  CA  . LYS A  1 240 ? 20.076  2.307   31.681  1.00 12.94  ? 327  LYS A CA  1 
ATOM   1845  C  C   . LYS A  1 240 ? 19.781  3.018   33.006  1.00 12.72  ? 327  LYS A C   1 
ATOM   1846  O  O   . LYS A  1 240 ? 19.894  4.251   33.100  1.00 12.61  ? 327  LYS A O   1 
ATOM   1847  C  CB  . LYS A  1 240 ? 18.929  2.607   30.706  1.00 13.16  ? 327  LYS A CB  1 
ATOM   1848  C  CG  . LYS A  1 240 ? 17.578  2.106   31.224  1.00 14.09  ? 327  LYS A CG  1 
ATOM   1849  C  CD  . LYS A  1 240 ? 16.518  2.163   30.146  1.00 16.34  ? 327  LYS A CD  1 
ATOM   1850  C  CE  . LYS A  1 240 ? 15.140  1.821   30.710  1.00 18.89  ? 327  LYS A CE  1 
ATOM   1851  N  NZ  . LYS A  1 240 ? 14.142  1.576   29.587  1.00 19.28  ? 327  LYS A NZ  1 
ATOM   1852  N  N   . VAL A  1 241 ? 19.369  2.252   34.015  1.00 12.68  ? 328  VAL A N   1 
ATOM   1853  C  CA  . VAL A  1 241 ? 19.086  2.811   35.347  1.00 12.56  ? 328  VAL A CA  1 
ATOM   1854  C  C   . VAL A  1 241 ? 20.440  3.039   36.050  1.00 12.89  ? 328  VAL A C   1 
ATOM   1855  O  O   . VAL A  1 241 ? 21.054  2.094   36.551  1.00 13.85  ? 328  VAL A O   1 
ATOM   1856  C  CB  . VAL A  1 241 ? 18.156  1.867   36.157  1.00 12.26  ? 328  VAL A CB  1 
ATOM   1857  C  CG1 . VAL A  1 241 ? 17.868  2.406   37.559  1.00 10.70  ? 328  VAL A CG1 1 
ATOM   1858  C  CG2 . VAL A  1 241 ? 16.843  1.624   35.391  1.00 11.87  ? 328  VAL A CG2 1 
ATOM   1859  N  N   . LEU A  1 242 ? 20.896  4.290   36.053  1.00 12.66  ? 329  LEU A N   1 
ATOM   1860  C  CA  . LEU A  1 242 ? 22.231  4.650   36.568  1.00 12.51  ? 329  LEU A CA  1 
ATOM   1861  C  C   . LEU A  1 242 ? 22.180  4.773   38.086  1.00 11.95  ? 329  LEU A C   1 
ATOM   1862  O  O   . LEU A  1 242 ? 21.229  5.328   38.617  1.00 11.59  ? 329  LEU A O   1 
ATOM   1863  C  CB  . LEU A  1 242 ? 22.705  5.966   35.942  1.00 11.72  ? 329  LEU A CB  1 
ATOM   1864  C  CG  . LEU A  1 242 ? 22.782  6.037   34.414  1.00 12.84  ? 329  LEU A CG  1 
ATOM   1865  C  CD1 . LEU A  1 242 ? 23.182  7.455   34.005  1.00 12.79  ? 329  LEU A CD1 1 
ATOM   1866  C  CD2 . LEU A  1 242 ? 23.762  5.009   33.830  1.00 12.67  ? 329  LEU A CD2 1 
ATOM   1867  N  N   . THR A  1 243 ? 23.190  4.253   38.788  1.00 12.22  ? 330  THR A N   1 
ATOM   1868  C  CA  . THR A  1 243 ? 23.068  4.147   40.244  1.00 12.39  ? 330  THR A CA  1 
ATOM   1869  C  C   . THR A  1 243 ? 24.210  4.747   41.070  1.00 12.63  ? 330  THR A C   1 
ATOM   1870  O  O   . THR A  1 243 ? 24.193  4.663   42.303  1.00 12.81  ? 330  THR A O   1 
ATOM   1871  C  CB  . THR A  1 243 ? 22.782  2.684   40.693  1.00 12.79  ? 330  THR A CB  1 
ATOM   1872  O  OG1 . THR A  1 243 ? 23.921  1.862   40.407  1.00 13.71  ? 330  THR A OG1 1 
ATOM   1873  C  CG2 . THR A  1 243 ? 21.522  2.103   40.001  1.00 11.35  ? 330  THR A CG2 1 
ATOM   1874  N  N   . ASP A  1 244 ? 25.166  5.397   40.415  1.00 13.21  ? 331  ASP A N   1 
ATOM   1875  C  CA  . ASP A  1 244 ? 26.133  6.234   41.165  1.00 12.88  ? 331  ASP A CA  1 
ATOM   1876  C  C   . ASP A  1 244 ? 25.536  7.621   41.459  1.00 12.90  ? 331  ASP A C   1 
ATOM   1877  O  O   . ASP A  1 244 ? 24.439  7.945   40.987  1.00 12.49  ? 331  ASP A O   1 
ATOM   1878  C  CB  . ASP A  1 244 ? 27.484  6.338   40.434  1.00 12.64  ? 331  ASP A CB  1 
ATOM   1879  C  CG  . ASP A  1 244 ? 28.685  6.526   41.399  1.00 13.02  ? 331  ASP A CG  1 
ATOM   1880  O  OD1 . ASP A  1 244 ? 28.491  6.746   42.616  1.00 10.21  ? 331  ASP A OD1 1 
ATOM   1881  O  OD2 . ASP A  1 244 ? 29.837  6.447   40.922  1.00 14.00  ? 331  ASP A OD2 1 
ATOM   1882  N  N   . THR A  1 245 ? 26.243  8.412   42.271  1.00 12.55  ? 332  THR A N   1 
ATOM   1883  C  CA  . THR A  1 245 ? 25.867  9.795   42.589  1.00 13.51  ? 332  THR A CA  1 
ATOM   1884  C  C   . THR A  1 245 ? 27.169  10.600  42.611  1.00 13.55  ? 332  THR A C   1 
ATOM   1885  O  O   . THR A  1 245 ? 28.062  10.264  43.380  1.00 12.69  ? 332  THR A O   1 
ATOM   1886  C  CB  . THR A  1 245 ? 25.172  9.904   43.992  1.00 13.62  ? 332  THR A CB  1 
ATOM   1887  O  OG1 . THR A  1 245 ? 24.031  9.039   44.036  1.00 14.35  ? 332  THR A OG1 1 
ATOM   1888  C  CG2 . THR A  1 245 ? 24.744  11.358  44.300  1.00 13.62  ? 332  THR A CG2 1 
ATOM   1889  N  N   . SER A  1 246 ? 27.292  11.670  41.818  1.00 13.87  ? 333  SER A N   1 
ATOM   1890  C  CA  . SER A  1 246 ? 26.228  12.247  40.998  1.00 14.68  ? 333  SER A CA  1 
ATOM   1891  C  C   . SER A  1 246 ? 26.046  11.507  39.666  1.00 15.16  ? 333  SER A C   1 
ATOM   1892  O  O   . SER A  1 246 ? 26.934  10.777  39.197  1.00 15.86  ? 333  SER A O   1 
ATOM   1893  C  CB  . SER A  1 246 ? 26.483  13.750  40.736  1.00 14.55  ? 333  SER A CB  1 
ATOM   1894  O  OG  . SER A  1 246 ? 26.784  14.485  41.920  1.00 14.62  ? 333  SER A OG  1 
ATOM   1895  N  N   . ARG A  1 247 ? 24.883  11.697  39.055  1.00 15.46  ? 334  ARG A N   1 
ATOM   1896  C  CA  . ARG A  1 247 ? 24.596  11.042  37.781  1.00 15.32  ? 334  ARG A CA  1 
ATOM   1897  C  C   . ARG A  1 247 ? 23.699  11.943  36.927  1.00 15.75  ? 334  ARG A C   1 
ATOM   1898  O  O   . ARG A  1 247 ? 22.982  12.805  37.467  1.00 15.71  ? 334  ARG A O   1 
ATOM   1899  C  CB  . ARG A  1 247 ? 23.936  9.675   38.012  1.00 14.80  ? 334  ARG A CB  1 
ATOM   1900  C  CG  . ARG A  1 247 ? 22.603  9.751   38.753  1.00 14.18  ? 334  ARG A CG  1 
ATOM   1901  C  CD  . ARG A  1 247 ? 22.019  8.380   39.048  1.00 14.33  ? 334  ARG A CD  1 
ATOM   1902  N  NE  . ARG A  1 247 ? 20.697  8.527   39.648  1.00 12.54  ? 334  ARG A NE  1 
ATOM   1903  C  CZ  . ARG A  1 247 ? 20.477  8.573   40.958  1.00 11.88  ? 334  ARG A CZ  1 
ATOM   1904  N  NH1 . ARG A  1 247 ? 21.498  8.463   41.813  1.00 9.82   ? 334  ARG A NH1 1 
ATOM   1905  N  NH2 . ARG A  1 247 ? 19.239  8.733   41.402  1.00 11.89  ? 334  ARG A NH2 1 
ATOM   1906  N  N   . PRO A  1 248 ? 23.726  11.754  35.591  1.00 16.36  ? 335  PRO A N   1 
ATOM   1907  C  CA  . PRO A  1 248 ? 22.749  12.500  34.795  1.00 16.68  ? 335  PRO A CA  1 
ATOM   1908  C  C   . PRO A  1 248 ? 21.387  11.790  34.869  1.00 17.38  ? 335  PRO A C   1 
ATOM   1909  O  O   . PRO A  1 248 ? 21.272  10.791  35.570  1.00 17.03  ? 335  PRO A O   1 
ATOM   1910  C  CB  . PRO A  1 248 ? 23.338  12.422  33.383  1.00 16.71  ? 335  PRO A CB  1 
ATOM   1911  C  CG  . PRO A  1 248 ? 23.996  11.073  33.349  1.00 16.40  ? 335  PRO A CG  1 
ATOM   1912  C  CD  . PRO A  1 248 ? 24.586  10.900  34.747  1.00 16.42  ? 335  PRO A CD  1 
ATOM   1913  N  N   . ASN A  1 249 ? 20.370  12.308  34.167  1.00 17.73  ? 336  ASN A N   1 
ATOM   1914  C  CA  . ASN A  1 249 ? 19.112  11.574  33.970  1.00 18.35  ? 336  ASN A CA  1 
ATOM   1915  C  C   . ASN A  1 249 ? 19.413  10.223  33.328  1.00 17.78  ? 336  ASN A C   1 
ATOM   1916  O  O   . ASN A  1 249 ? 20.357  10.115  32.530  1.00 18.02  ? 336  ASN A O   1 
ATOM   1917  C  CB  . ASN A  1 249 ? 18.176  12.356  33.044  1.00 18.73  ? 336  ASN A CB  1 
ATOM   1918  C  CG  . ASN A  1 249 ? 17.588  13.603  33.697  1.00 21.56  ? 336  ASN A CG  1 
ATOM   1919  O  OD1 . ASN A  1 249 ? 17.696  13.811  34.905  1.00 23.98  ? 336  ASN A OD1 1 
ATOM   1920  N  ND2 . ASN A  1 249 ? 16.918  14.420  32.893  1.00 25.44  ? 336  ASN A ND2 1 
ATOM   1921  N  N   . ASP A  1 250 ? 18.635  9.190   33.665  1.00 17.72  ? 337  ASP A N   1 
ATOM   1922  C  CA  . ASP A  1 250 ? 18.813  7.873   33.013  1.00 17.31  ? 337  ASP A CA  1 
ATOM   1923  C  C   . ASP A  1 250 ? 18.641  7.983   31.492  1.00 17.87  ? 337  ASP A C   1 
ATOM   1924  O  O   . ASP A  1 250 ? 17.680  8.611   31.026  1.00 17.84  ? 337  ASP A O   1 
ATOM   1925  C  CB  . ASP A  1 250 ? 17.834  6.834   33.558  1.00 17.13  ? 337  ASP A CB  1 
ATOM   1926  C  CG  . ASP A  1 250 ? 18.140  6.438   34.998  1.00 17.18  ? 337  ASP A CG  1 
ATOM   1927  O  OD1 . ASP A  1 250 ? 17.246  5.835   35.631  1.00 15.99  ? 337  ASP A OD1 1 
ATOM   1928  O  OD2 . ASP A  1 250 ? 19.264  6.724   35.496  1.00 15.02  ? 337  ASP A OD2 1 
ATOM   1929  N  N   . PRO A  1 251 ? 19.574  7.387   30.719  1.00 17.91  ? 338  PRO A N   1 
ATOM   1930  C  CA  . PRO A  1 251 ? 19.484  7.399   29.255  1.00 18.07  ? 338  PRO A CA  1 
ATOM   1931  C  C   . PRO A  1 251 ? 18.527  6.333   28.747  1.00 18.24  ? 338  PRO A C   1 
ATOM   1932  O  O   . PRO A  1 251 ? 17.990  5.550   29.546  1.00 17.38  ? 338  PRO A O   1 
ATOM   1933  C  CB  . PRO A  1 251 ? 20.909  7.070   28.819  1.00 18.16  ? 338  PRO A CB  1 
ATOM   1934  C  CG  . PRO A  1 251 ? 21.447  6.202   29.920  1.00 17.65  ? 338  PRO A CG  1 
ATOM   1935  C  CD  . PRO A  1 251 ? 20.793  6.698   31.191  1.00 18.28  ? 338  PRO A CD  1 
ATOM   1936  N  N   . THR A  1 252 ? 18.306  6.304   27.436  1.00 18.30  ? 339  THR A N   1 
ATOM   1937  C  CA  . THR A  1 252 ? 17.462  5.268   26.846  1.00 18.79  ? 339  THR A CA  1 
ATOM   1938  C  C   . THR A  1 252 ? 18.141  3.895   26.857  1.00 17.83  ? 339  THR A C   1 
ATOM   1939  O  O   . THR A  1 252 ? 17.460  2.893   26.913  1.00 17.62  ? 339  THR A O   1 
ATOM   1940  C  CB  . THR A  1 252 ? 16.971  5.640   25.433  1.00 19.32  ? 339  THR A CB  1 
ATOM   1941  O  OG1 . THR A  1 252 ? 18.062  6.165   24.681  1.00 21.59  ? 339  THR A OG1 1 
ATOM   1942  C  CG2 . THR A  1 252 ? 15.876  6.728   25.521  1.00 20.63  ? 339  THR A CG2 1 
ATOM   1943  N  N   . ASN A  1 253 ? 19.475  3.865   26.802  1.00 17.59  ? 340  ASN A N   1 
ATOM   1944  C  CA  . ASN A  1 253 ? 20.245  2.615   26.904  1.00 17.02  ? 340  ASN A CA  1 
ATOM   1945  C  C   . ASN A  1 253 ? 21.456  2.793   27.817  1.00 15.60  ? 340  ASN A C   1 
ATOM   1946  O  O   . ASN A  1 253 ? 22.132  3.813   27.766  1.00 15.80  ? 340  ASN A O   1 
ATOM   1947  C  CB  . ASN A  1 253 ? 20.781  2.146   25.544  1.00 17.68  ? 340  ASN A CB  1 
ATOM   1948  C  CG  . ASN A  1 253 ? 19.694  1.984   24.495  1.00 20.16  ? 340  ASN A CG  1 
ATOM   1949  O  OD1 . ASN A  1 253 ? 19.449  2.891   23.697  1.00 23.99  ? 340  ASN A OD1 1 
ATOM   1950  N  ND2 . ASN A  1 253 ? 19.044  0.842   24.489  1.00 18.06  ? 340  ASN A ND2 1 
ATOM   1951  N  N   . GLY A  1 254 ? 21.738  1.791   28.632  1.00 14.89  ? 341  GLY A N   1 
ATOM   1952  C  CA  . GLY A  1 254 ? 22.987  1.792   29.382  1.00 14.44  ? 341  GLY A CA  1 
ATOM   1953  C  C   . GLY A  1 254 ? 24.146  1.322   28.511  1.00 14.25  ? 341  GLY A C   1 
ATOM   1954  O  O   . GLY A  1 254 ? 24.023  1.227   27.265  1.00 13.44  ? 341  GLY A O   1 
ATOM   1955  N  N   . ASN A  1 255 ? 25.265  1.023   29.169  1.00 14.00  ? 342  ASN A N   1 
ATOM   1956  C  CA  . ASN A  1 255 ? 26.502  0.589   28.500  1.00 14.62  ? 342  ASN A CA  1 
ATOM   1957  C  C   . ASN A  1 255 ? 27.228  -0.443  29.380  1.00 14.68  ? 342  ASN A C   1 
ATOM   1958  O  O   . ASN A  1 255 ? 27.653  -0.109  30.488  1.00 14.14  ? 342  ASN A O   1 
ATOM   1959  C  CB  . ASN A  1 255 ? 27.403  1.807   28.214  1.00 14.48  ? 342  ASN A CB  1 
ATOM   1960  C  CG  . ASN A  1 255 ? 28.492  1.526   27.162  1.00 15.46  ? 342  ASN A CG  1 
ATOM   1961  O  OD1 . ASN A  1 255 ? 28.824  2.406   26.344  1.00 16.15  ? 342  ASN A OD1 1 
ATOM   1962  N  ND2 . ASN A  1 255 ? 29.045  0.315   27.172  1.00 10.97  ? 342  ASN A ND2 1 
ATOM   1963  N  N   . CYS A  1 256 ? 27.330  -1.691  28.897  1.00 14.72  ? 343  CYS A N   1 
ATOM   1964  C  CA  . CYS A  1 256 ? 27.953  -2.796  29.638  1.00 15.55  ? 343  CYS A CA  1 
ATOM   1965  C  C   . CYS A  1 256 ? 29.480  -2.700  29.742  1.00 15.87  ? 343  CYS A C   1 
ATOM   1966  O  O   . CYS A  1 256 ? 30.083  -3.369  30.579  1.00 16.10  ? 343  CYS A O   1 
ATOM   1967  C  CB  . CYS A  1 256 ? 27.640  -4.156  28.995  1.00 15.02  ? 343  CYS A CB  1 
ATOM   1968  S  SG  . CYS A  1 256 ? 25.895  -4.498  28.654  1.00 17.41  ? 343  CYS A SG  1 
ATOM   1969  N  N   . ASP A  1 257 ? 30.105  -1.924  28.863  1.00 16.08  ? 344  ASP A N   1 
ATOM   1970  C  CA  . ASP A  1 257 ? 31.554  -2.042  28.678  1.00 16.79  ? 344  ASP A CA  1 
ATOM   1971  C  C   . ASP A  1 257 ? 32.318  -0.727  28.651  1.00 17.04  ? 344  ASP A C   1 
ATOM   1972  O  O   . ASP A  1 257 ? 33.491  -0.695  28.247  1.00 17.88  ? 344  ASP A O   1 
ATOM   1973  C  CB  . ASP A  1 257 ? 31.852  -2.843  27.399  1.00 16.67  ? 344  ASP A CB  1 
ATOM   1974  C  CG  . ASP A  1 257 ? 31.473  -4.301  27.528  1.00 17.58  ? 344  ASP A CG  1 
ATOM   1975  O  OD1 . ASP A  1 257 ? 30.426  -4.689  26.954  1.00 18.01  ? 344  ASP A OD1 1 
ATOM   1976  O  OD2 . ASP A  1 257 ? 32.215  -5.053  28.206  1.00 17.81  ? 344  ASP A OD2 1 
ATOM   1977  N  N   . ALA A  1 258 ? 31.656  0.347   29.061  1.00 16.93  ? 345  ALA A N   1 
ATOM   1978  C  CA  . ALA A  1 258 ? 32.262  1.664   29.158  1.00 17.37  ? 345  ALA A CA  1 
ATOM   1979  C  C   . ALA A  1 258 ? 31.459  2.508   30.130  1.00 16.97  ? 345  ALA A C   1 
ATOM   1980  O  O   . ALA A  1 258 ? 30.235  2.312   30.259  1.00 17.50  ? 345  ALA A O   1 
ATOM   1981  C  CB  . ALA A  1 258 ? 32.332  2.354   27.773  1.00 17.60  ? 345  ALA A CB  1 
ATOM   1982  N  N   . PRO A  1 259 ? 32.136  3.457   30.805  1.00 16.78  ? 346  PRO A N   1 
ATOM   1983  C  CA  . PRO A  1 259 ? 31.505  4.443   31.681  1.00 16.75  ? 346  PRO A CA  1 
ATOM   1984  C  C   . PRO A  1 259 ? 30.594  5.405   30.931  1.00 17.35  ? 346  PRO A C   1 
ATOM   1985  O  O   . PRO A  1 259 ? 30.929  5.863   29.826  1.00 16.37  ? 346  PRO A O   1 
ATOM   1986  C  CB  . PRO A  1 259 ? 32.701  5.215   32.271  1.00 16.23  ? 346  PRO A CB  1 
ATOM   1987  C  CG  . PRO A  1 259 ? 33.822  5.010   31.291  1.00 16.28  ? 346  PRO A CG  1 
ATOM   1988  C  CD  . PRO A  1 259 ? 33.608  3.626   30.751  1.00 16.79  ? 346  PRO A CD  1 
ATOM   1989  N  N   . ILE A  1 260 ? 29.436  5.690   31.524  1.00 17.69  ? 347  ILE A N   1 
ATOM   1990  C  CA  . ILE A  1 260 ? 28.520  6.709   31.016  1.00 18.04  ? 347  ILE A CA  1 
ATOM   1991  C  C   . ILE A  1 260 ? 28.797  7.942   31.865  1.00 19.34  ? 347  ILE A C   1 
ATOM   1992  O  O   . ILE A  1 260 ? 28.679  7.903   33.097  1.00 18.89  ? 347  ILE A O   1 
ATOM   1993  C  CB  . ILE A  1 260 ? 27.021  6.265   31.142  1.00 18.16  ? 347  ILE A CB  1 
ATOM   1994  C  CG1 . ILE A  1 260 ? 26.755  5.000   30.312  1.00 17.62  ? 347  ILE A CG1 1 
ATOM   1995  C  CG2 . ILE A  1 260 ? 26.052  7.399   30.775  1.00 17.11  ? 347  ILE A CG2 1 
ATOM   1996  C  CD1 . ILE A  1 260 ? 25.348  4.457   30.443  1.00 17.85  ? 347  ILE A CD1 1 
ATOM   1997  N  N   . THR A  1 261 ? 29.180  9.027   31.197  1.00 19.84  ? 348  THR A N   1 
ATOM   1998  C  CA  . THR A  1 261 ? 29.642  10.239  31.864  1.00 21.16  ? 348  THR A CA  1 
ATOM   1999  C  C   . THR A  1 261 ? 28.474  11.182  32.146  1.00 21.17  ? 348  THR A C   1 
ATOM   2000  O  O   . THR A  1 261 ? 27.351  10.929  31.715  1.00 21.03  ? 348  THR A O   1 
ATOM   2001  C  CB  . THR A  1 261 ? 30.691  10.956  30.988  1.00 21.56  ? 348  THR A CB  1 
ATOM   2002  O  OG1 . THR A  1 261 ? 30.103  11.236  29.710  1.00 22.50  ? 348  THR A OG1 1 
ATOM   2003  C  CG2 . THR A  1 261 ? 31.904  10.076  30.799  1.00 21.69  ? 348  THR A CG2 1 
ATOM   2004  N  N   . GLY A  1 262 ? 28.741  12.265  32.870  1.00 21.66  ? 349  GLY A N   1 
ATOM   2005  C  CA  . GLY A  1 262 ? 27.697  13.196  33.263  1.00 21.75  ? 349  GLY A CA  1 
ATOM   2006  C  C   . GLY A  1 262 ? 27.415  13.198  34.758  1.00 21.93  ? 349  GLY A C   1 
ATOM   2007  O  O   . GLY A  1 262 ? 27.854  12.301  35.497  1.00 22.44  ? 349  GLY A O   1 
ATOM   2008  N  N   . GLY A  1 263 ? 26.662  14.204  35.196  1.00 21.49  ? 350  GLY A N   1 
ATOM   2009  C  CA  . GLY A  1 263 ? 26.312  14.355  36.600  1.00 21.00  ? 350  GLY A CA  1 
ATOM   2010  C  C   . GLY A  1 263 ? 27.186  15.402  37.255  1.00 20.77  ? 350  GLY A C   1 
ATOM   2011  O  O   . GLY A  1 263 ? 28.343  15.599  36.861  1.00 20.35  ? 350  GLY A O   1 
ATOM   2012  N  N   . SER A  1 264 ? 26.641  16.055  38.272  1.00 19.75  ? 351  SER A N   1 
ATOM   2013  C  CA  . SER A  1 264 ? 27.329  17.122  38.978  1.00 19.74  ? 351  SER A CA  1 
ATOM   2014  C  C   . SER A  1 264 ? 26.696  17.287  40.359  1.00 18.69  ? 351  SER A C   1 
ATOM   2015  O  O   . SER A  1 264 ? 25.486  17.156  40.481  1.00 18.43  ? 351  SER A O   1 
ATOM   2016  C  CB  . SER A  1 264 ? 27.180  18.423  38.170  1.00 20.02  ? 351  SER A CB  1 
ATOM   2017  O  OG  . SER A  1 264 ? 27.775  19.524  38.821  1.00 22.42  ? 351  SER A OG  1 
ATOM   2018  N  N   . PRO A  1 265 ? 27.484  17.660  41.387  1.00 18.09  ? 352  PRO A N   1 
ATOM   2019  C  CA  . PRO A  1 265 ? 28.914  17.979  41.406  1.00 18.20  ? 352  PRO A CA  1 
ATOM   2020  C  C   . PRO A  1 265 ? 29.857  16.878  41.922  1.00 18.42  ? 352  PRO A C   1 
ATOM   2021  O  O   . PRO A  1 265 ? 31.072  17.117  41.931  1.00 18.47  ? 352  PRO A O   1 
ATOM   2022  C  CB  . PRO A  1 265 ? 28.965  19.171  42.368  1.00 17.79  ? 352  PRO A CB  1 
ATOM   2023  C  CG  . PRO A  1 265 ? 27.884  18.845  43.399  1.00 17.35  ? 352  PRO A CG  1 
ATOM   2024  C  CD  . PRO A  1 265 ? 26.874  17.923  42.706  1.00 17.65  ? 352  PRO A CD  1 
ATOM   2025  N  N   . ASP A  1 266 ? 29.324  15.711  42.336  1.00 17.88  ? 353  ASP A N   1 
ATOM   2026  C  CA  . ASP A  1 266 ? 30.108  14.638  43.002  1.00 18.19  ? 353  ASP A CA  1 
ATOM   2027  C  C   . ASP A  1 266 ? 30.541  13.558  41.992  1.00 17.23  ? 353  ASP A C   1 
ATOM   2028  O  O   . ASP A  1 266 ? 29.720  13.112  41.189  1.00 16.82  ? 353  ASP A O   1 
ATOM   2029  C  CB  . ASP A  1 266 ? 29.282  13.862  44.083  1.00 18.81  ? 353  ASP A CB  1 
ATOM   2030  C  CG  . ASP A  1 266 ? 28.558  14.743  45.112  1.00 21.40  ? 353  ASP A CG  1 
ATOM   2031  O  OD1 . ASP A  1 266 ? 29.051  15.850  45.435  1.00 20.30  ? 353  ASP A OD1 1 
ATOM   2032  O  OD2 . ASP A  1 266 ? 27.478  14.270  45.645  1.00 22.34  ? 353  ASP A OD2 1 
ATOM   2033  N  N   . PRO A  1 267 ? 31.807  13.081  42.070  1.00 16.47  ? 354  PRO A N   1 
ATOM   2034  C  CA  . PRO A  1 267 ? 32.293  12.004  41.209  1.00 15.70  ? 354  PRO A CA  1 
ATOM   2035  C  C   . PRO A  1 267 ? 31.831  10.585  41.584  1.00 14.54  ? 354  PRO A C   1 
ATOM   2036  O  O   . PRO A  1 267 ? 31.972  9.661   40.775  1.00 13.20  ? 354  PRO A O   1 
ATOM   2037  C  CB  . PRO A  1 267 ? 33.814  12.097  41.373  1.00 16.38  ? 354  PRO A CB  1 
ATOM   2038  C  CG  . PRO A  1 267 ? 33.992  12.607  42.764  1.00 16.19  ? 354  PRO A CG  1 
ATOM   2039  C  CD  . PRO A  1 267 ? 32.881  13.595  42.951  1.00 16.72  ? 354  PRO A CD  1 
ATOM   2040  N  N   . GLY A  1 268 ? 31.308  10.393  42.794  1.00 13.80  ? 355  GLY A N   1 
ATOM   2041  C  CA  . GLY A  1 268 ? 30.872  9.052   43.176  1.00 13.07  ? 355  GLY A CA  1 
ATOM   2042  C  C   . GLY A  1 268 ? 30.428  8.887   44.616  1.00 11.95  ? 355  GLY A C   1 
ATOM   2043  O  O   . GLY A  1 268 ? 30.632  9.778   45.464  1.00 11.06  ? 355  GLY A O   1 
ATOM   2044  N  N   . VAL A  1 269 ? 29.820  7.729   44.859  1.00 11.27  ? 356  VAL A N   1 
ATOM   2045  C  CA  . VAL A  1 269 ? 29.389  7.277   46.202  1.00 9.95   ? 356  VAL A CA  1 
ATOM   2046  C  C   . VAL A  1 269 ? 29.470  5.751   46.202  1.00 9.16   ? 356  VAL A C   1 
ATOM   2047  O  O   . VAL A  1 269 ? 29.227  5.110   45.178  1.00 8.85   ? 356  VAL A O   1 
ATOM   2048  C  CB  . VAL A  1 269 ? 27.960  7.771   46.605  1.00 10.09  ? 356  VAL A CB  1 
ATOM   2049  C  CG1 . VAL A  1 269 ? 26.812  7.060   45.792  1.00 9.03   ? 356  VAL A CG1 1 
ATOM   2050  C  CG2 . VAL A  1 269 ? 27.742  7.595   48.114  1.00 10.11  ? 356  VAL A CG2 1 
ATOM   2051  N  N   . LYS A  1 270 ? 29.866  5.167   47.331  1.00 8.99   ? 357  LYS A N   1 
ATOM   2052  C  CA  . LYS A  1 270 ? 29.784  3.699   47.476  1.00 8.00   ? 357  LYS A CA  1 
ATOM   2053  C  C   . LYS A  1 270 ? 28.314  3.241   47.397  1.00 8.60   ? 357  LYS A C   1 
ATOM   2054  O  O   . LYS A  1 270 ? 27.433  3.865   48.005  1.00 9.04   ? 357  LYS A O   1 
ATOM   2055  C  CB  . LYS A  1 270 ? 30.419  3.256   48.792  1.00 8.35   ? 357  LYS A CB  1 
ATOM   2056  C  CG  . LYS A  1 270 ? 30.271  1.760   49.098  1.00 7.54   ? 357  LYS A CG  1 
ATOM   2057  C  CD  . LYS A  1 270 ? 30.859  1.397   50.446  1.00 7.24   ? 357  LYS A CD  1 
ATOM   2058  C  CE  . LYS A  1 270 ? 30.633  -0.104  50.725  1.00 6.32   ? 357  LYS A CE  1 
ATOM   2059  N  NZ  . LYS A  1 270 ? 31.323  -1.056  49.758  1.00 8.77   ? 357  LYS A NZ  1 
ATOM   2060  N  N   . GLY A  1 271 ? 28.067  2.177   46.636  1.00 8.80   ? 358  GLY A N   1 
ATOM   2061  C  CA  . GLY A  1 271 ? 26.705  1.623   46.489  1.00 8.88   ? 358  GLY A CA  1 
ATOM   2062  C  C   . GLY A  1 271 ? 26.789  0.136   46.233  1.00 9.08   ? 358  GLY A C   1 
ATOM   2063  O  O   . GLY A  1 271 ? 27.851  -0.477  46.420  1.00 8.55   ? 358  GLY A O   1 
ATOM   2064  N  N   . PHE A  1 272 ? 25.673  -0.452  45.802  1.00 9.43   ? 359  PHE A N   1 
ATOM   2065  C  CA  . PHE A  1 272 ? 25.605  -1.915  45.650  1.00 9.89   ? 359  PHE A CA  1 
ATOM   2066  C  C   . PHE A  1 272 ? 24.436  -2.291  44.737  1.00 9.86   ? 359  PHE A C   1 
ATOM   2067  O  O   . PHE A  1 272 ? 23.604  -1.433  44.381  1.00 9.22   ? 359  PHE A O   1 
ATOM   2068  C  CB  . PHE A  1 272 ? 25.389  -2.574  47.034  1.00 9.02   ? 359  PHE A CB  1 
ATOM   2069  C  CG  . PHE A  1 272 ? 23.963  -2.488  47.499  1.00 9.73   ? 359  PHE A CG  1 
ATOM   2070  C  CD1 . PHE A  1 272 ? 23.467  -1.317  48.055  1.00 9.62   ? 359  PHE A CD1 1 
ATOM   2071  C  CD2 . PHE A  1 272 ? 23.098  -3.566  47.311  1.00 8.78   ? 359  PHE A CD2 1 
ATOM   2072  C  CE1 . PHE A  1 272 ? 22.127  -1.213  48.446  1.00 10.43  ? 359  PHE A CE1 1 
ATOM   2073  C  CE2 . PHE A  1 272 ? 21.757  -3.470  47.694  1.00 9.53   ? 359  PHE A CE2 1 
ATOM   2074  C  CZ  . PHE A  1 272 ? 21.285  -2.273  48.255  1.00 9.02   ? 359  PHE A CZ  1 
ATOM   2075  N  N   . ALA A  1 273 ? 24.392  -3.584  44.388  1.00 10.14  ? 360  ALA A N   1 
ATOM   2076  C  CA  . ALA A  1 273 ? 23.276  -4.217  43.698  1.00 10.62  ? 360  ALA A CA  1 
ATOM   2077  C  C   . ALA A  1 273 ? 23.345  -5.735  43.884  1.00 10.87  ? 360  ALA A C   1 
ATOM   2078  O  O   . ALA A  1 273 ? 24.407  -6.286  44.183  1.00 12.13  ? 360  ALA A O   1 
ATOM   2079  C  CB  . ALA A  1 273 ? 23.295  -3.855  42.197  1.00 10.26  ? 360  ALA A CB  1 
ATOM   2080  N  N   . PHE A  1 274 ? 22.197  -6.399  43.743  1.00 10.31  ? 361  PHE A N   1 
ATOM   2081  C  CA  . PHE A  1 274 ? 22.108  -7.849  43.727  1.00 10.87  ? 361  PHE A CA  1 
ATOM   2082  C  C   . PHE A  1 274 ? 21.663  -8.194  42.321  1.00 11.19  ? 361  PHE A C   1 
ATOM   2083  O  O   . PHE A  1 274 ? 20.650  -7.676  41.828  1.00 11.31  ? 361  PHE A O   1 
ATOM   2084  C  CB  . PHE A  1 274 ? 21.135  -8.354  44.797  1.00 10.34  ? 361  PHE A CB  1 
ATOM   2085  C  CG  . PHE A  1 274 ? 21.672  -8.215  46.200  1.00 10.32  ? 361  PHE A CG  1 
ATOM   2086  C  CD1 . PHE A  1 274 ? 22.516  -9.194  46.734  1.00 11.03  ? 361  PHE A CD1 1 
ATOM   2087  C  CD2 . PHE A  1 274 ? 21.366  -7.097  46.975  1.00 11.49  ? 361  PHE A CD2 1 
ATOM   2088  C  CE1 . PHE A  1 274 ? 23.049  -9.069  48.036  1.00 11.19  ? 361  PHE A CE1 1 
ATOM   2089  C  CE2 . PHE A  1 274 ? 21.879  -6.977  48.295  1.00 9.60   ? 361  PHE A CE2 1 
ATOM   2090  C  CZ  . PHE A  1 274 ? 22.705  -7.957  48.821  1.00 9.68   ? 361  PHE A CZ  1 
ATOM   2091  N  N   . LEU A  1 275 ? 22.480  -9.001  41.656  1.00 11.53  ? 362  LEU A N   1 
ATOM   2092  C  CA  . LEU A  1 275 ? 22.280  -9.293  40.238  1.00 11.60  ? 362  LEU A CA  1 
ATOM   2093  C  C   . LEU A  1 275 ? 22.035  -10.777 40.055  1.00 12.00  ? 362  LEU A C   1 
ATOM   2094  O  O   . LEU A  1 275 ? 22.918  -11.611 40.286  1.00 12.30  ? 362  LEU A O   1 
ATOM   2095  C  CB  . LEU A  1 275 ? 23.489  -8.832  39.417  1.00 11.17  ? 362  LEU A CB  1 
ATOM   2096  C  CG  . LEU A  1 275 ? 23.967  -7.388  39.616  1.00 10.15  ? 362  LEU A CG  1 
ATOM   2097  C  CD1 . LEU A  1 275 ? 25.343  -7.217  38.981  1.00 9.57   ? 362  LEU A CD1 1 
ATOM   2098  C  CD2 . LEU A  1 275 ? 22.937  -6.396  39.035  1.00 10.19  ? 362  LEU A CD2 1 
ATOM   2099  N  N   . ASP A  1 276 ? 20.813  -11.107 39.652  1.00 12.56  ? 363  ASP A N   1 
ATOM   2100  C  CA  . ASP A  1 276 ? 20.379  -12.500 39.613  1.00 12.74  ? 363  ASP A CA  1 
ATOM   2101  C  C   . ASP A  1 276 ? 19.253  -12.666 38.591  1.00 13.01  ? 363  ASP A C   1 
ATOM   2102  O  O   . ASP A  1 276 ? 18.134  -13.017 38.944  1.00 11.48  ? 363  ASP A O   1 
ATOM   2103  C  CB  . ASP A  1 276 ? 19.922  -12.925 41.025  1.00 12.95  ? 363  ASP A CB  1 
ATOM   2104  C  CG  . ASP A  1 276 ? 19.557  -14.392 41.115  1.00 15.28  ? 363  ASP A CG  1 
ATOM   2105  O  OD1 . ASP A  1 276 ? 18.663  -14.725 41.927  1.00 14.48  ? 363  ASP A OD1 1 
ATOM   2106  O  OD2 . ASP A  1 276 ? 20.145  -15.211 40.366  1.00 16.89  ? 363  ASP A OD2 1 
ATOM   2107  N  N   . GLY A  1 277 ? 19.550  -12.363 37.328  1.00 12.93  ? 364  GLY A N   1 
ATOM   2108  C  CA  . GLY A  1 277 ? 18.556  -12.463 36.252  1.00 13.36  ? 364  GLY A CA  1 
ATOM   2109  C  C   . GLY A  1 277 ? 17.316  -11.619 36.531  1.00 13.42  ? 364  GLY A C   1 
ATOM   2110  O  O   . GLY A  1 277 ? 17.415  -10.410 36.799  1.00 12.98  ? 364  GLY A O   1 
ATOM   2111  N  N   . GLU A  1 278 ? 16.142  -12.250 36.486  1.00 13.85  ? 365  GLU A N   1 
ATOM   2112  C  CA  . GLU A  1 278 ? 14.893  -11.532 36.780  1.00 15.38  ? 365  GLU A CA  1 
ATOM   2113  C  C   . GLU A  1 278 ? 14.853  -11.030 38.230  1.00 14.83  ? 365  GLU A C   1 
ATOM   2114  O  O   . GLU A  1 278 ? 14.221  -10.011 38.514  1.00 14.69  ? 365  GLU A O   1 
ATOM   2115  C  CB  . GLU A  1 278 ? 13.661  -12.409 36.519  1.00 16.35  ? 365  GLU A CB  1 
ATOM   2116  C  CG  . GLU A  1 278 ? 13.626  -13.079 35.150  1.00 21.43  ? 365  GLU A CG  1 
ATOM   2117  C  CD  . GLU A  1 278 ? 13.330  -12.114 34.023  1.00 28.21  ? 365  GLU A CD  1 
ATOM   2118  O  OE1 . GLU A  1 278 ? 13.831  -12.361 32.894  1.00 32.28  ? 365  GLU A OE1 1 
ATOM   2119  O  OE2 . GLU A  1 278 ? 12.594  -11.121 34.252  1.00 30.52  ? 365  GLU A OE2 1 
ATOM   2120  N  N   . ASN A  1 279 ? 15.554  -11.751 39.113  1.00 14.15  ? 366  ASN A N   1 
ATOM   2121  C  CA  . ASN A  1 279 ? 15.648  -11.437 40.544  1.00 13.85  ? 366  ASN A CA  1 
ATOM   2122  C  C   . ASN A  1 279 ? 16.749  -10.403 40.862  1.00 13.69  ? 366  ASN A C   1 
ATOM   2123  O  O   . ASN A  1 279 ? 17.592  -10.634 41.722  1.00 14.01  ? 366  ASN A O   1 
ATOM   2124  C  CB  . ASN A  1 279 ? 15.874  -12.748 41.319  1.00 13.87  ? 366  ASN A CB  1 
ATOM   2125  C  CG  . ASN A  1 279 ? 15.716  -12.595 42.824  1.00 13.90  ? 366  ASN A CG  1 
ATOM   2126  O  OD1 . ASN A  1 279 ? 14.778  -11.940 43.315  1.00 14.47  ? 366  ASN A OD1 1 
ATOM   2127  N  ND2 . ASN A  1 279 ? 16.618  -13.243 43.572  1.00 10.87  ? 366  ASN A ND2 1 
ATOM   2128  N  N   . SER A  1 280 ? 16.741  -9.262  40.172  1.00 12.82  ? 367  SER A N   1 
ATOM   2129  C  CA  . SER A  1 280 ? 17.828  -8.280  40.317  1.00 11.97  ? 367  SER A CA  1 
ATOM   2130  C  C   . SER A  1 280 ? 17.325  -6.987  40.936  1.00 11.51  ? 367  SER A C   1 
ATOM   2131  O  O   . SER A  1 280 ? 16.295  -6.458  40.521  1.00 10.93  ? 367  SER A O   1 
ATOM   2132  C  CB  . SER A  1 280 ? 18.505  -7.983  38.963  1.00 11.23  ? 367  SER A CB  1 
ATOM   2133  O  OG  . SER A  1 280 ? 19.140  -9.143  38.410  1.00 12.11  ? 367  SER A OG  1 
ATOM   2134  N  N   . TRP A  1 281 ? 18.070  -6.471  41.914  1.00 11.30  ? 368  TRP A N   1 
ATOM   2135  C  CA  . TRP A  1 281 ? 17.722  -5.210  42.577  1.00 11.14  ? 368  TRP A CA  1 
ATOM   2136  C  C   . TRP A  1 281 ? 18.900  -4.250  42.606  1.00 11.27  ? 368  TRP A C   1 
ATOM   2137  O  O   . TRP A  1 281 ? 20.007  -4.658  42.980  1.00 12.25  ? 368  TRP A O   1 
ATOM   2138  C  CB  . TRP A  1 281 ? 17.301  -5.481  44.027  1.00 10.47  ? 368  TRP A CB  1 
ATOM   2139  C  CG  . TRP A  1 281 ? 15.962  -6.082  44.200  1.00 10.08  ? 368  TRP A CG  1 
ATOM   2140  C  CD1 . TRP A  1 281 ? 15.646  -7.420  44.177  1.00 9.88   ? 368  TRP A CD1 1 
ATOM   2141  C  CD2 . TRP A  1 281 ? 14.745  -5.385  44.495  1.00 11.30  ? 368  TRP A CD2 1 
ATOM   2142  N  NE1 . TRP A  1 281 ? 14.297  -7.587  44.400  1.00 9.51   ? 368  TRP A NE1 1 
ATOM   2143  C  CE2 . TRP A  1 281 ? 13.725  -6.364  44.628  1.00 10.24  ? 368  TRP A CE2 1 
ATOM   2144  C  CE3 . TRP A  1 281 ? 14.416  -4.031  44.652  1.00 8.62   ? 368  TRP A CE3 1 
ATOM   2145  C  CZ2 . TRP A  1 281 ? 12.391  -6.037  44.920  1.00 8.29   ? 368  TRP A CZ2 1 
ATOM   2146  C  CZ3 . TRP A  1 281 ? 13.080  -3.699  44.954  1.00 9.72   ? 368  TRP A CZ3 1 
ATOM   2147  C  CH2 . TRP A  1 281 ? 12.088  -4.701  45.074  1.00 10.00  ? 368  TRP A CH2 1 
ATOM   2148  N  N   . LEU A  1 282 ? 18.639  -2.986  42.255  1.00 10.49  ? 369  LEU A N   1 
ATOM   2149  C  CA  . LEU A  1 282 ? 19.608  -1.879  42.306  1.00 11.32  ? 369  LEU A CA  1 
ATOM   2150  C  C   . LEU A  1 282 ? 19.210  -0.858  43.367  1.00 10.64  ? 369  LEU A C   1 
ATOM   2151  O  O   . LEU A  1 282 ? 18.067  -0.362  43.377  1.00 11.17  ? 369  LEU A O   1 
ATOM   2152  C  CB  . LEU A  1 282 ? 19.669  -1.119  40.968  1.00 10.26  ? 369  LEU A CB  1 
ATOM   2153  C  CG  . LEU A  1 282 ? 19.714  -1.886  39.645  1.00 13.91  ? 369  LEU A CG  1 
ATOM   2154  C  CD1 . LEU A  1 282 ? 19.860  -0.940  38.442  1.00 12.79  ? 369  LEU A CD1 1 
ATOM   2155  C  CD2 . LEU A  1 282 ? 20.772  -2.964  39.641  1.00 13.83  ? 369  LEU A CD2 1 
ATOM   2156  N  N   . GLY A  1 283 ? 20.147  -0.523  44.240  1.00 10.24  ? 370  GLY A N   1 
ATOM   2157  C  CA  . GLY A  1 283 ? 19.953  0.623   45.137  1.00 9.79   ? 370  GLY A CA  1 
ATOM   2158  C  C   . GLY A  1 283 ? 20.548  1.905   44.549  1.00 9.72   ? 370  GLY A C   1 
ATOM   2159  O  O   . GLY A  1 283 ? 21.528  1.875   43.795  1.00 10.07  ? 370  GLY A O   1 
ATOM   2160  N  N   . ARG A  1 284 ? 19.962  3.043   44.888  1.00 9.84   ? 371  ARG A N   1 
ATOM   2161  C  CA  . ARG A  1 284 ? 20.624  4.317   44.599  1.00 10.74  ? 371  ARG A CA  1 
ATOM   2162  C  C   . ARG A  1 284 ? 20.033  5.411   45.469  1.00 10.89  ? 371  ARG A C   1 
ATOM   2163  O  O   . ARG A  1 284 ? 18.928  5.246   46.023  1.00 11.21  ? 371  ARG A O   1 
ATOM   2164  C  CB  . ARG A  1 284 ? 20.498  4.662   43.102  1.00 10.13  ? 371  ARG A CB  1 
ATOM   2165  C  CG  . ARG A  1 284 ? 19.064  4.905   42.614  1.00 11.41  ? 371  ARG A CG  1 
ATOM   2166  C  CD  . ARG A  1 284 ? 19.065  5.391   41.150  1.00 11.40  ? 371  ARG A CD  1 
ATOM   2167  N  NE  . ARG A  1 284 ? 17.714  5.719   40.699  1.00 11.97  ? 371  ARG A NE  1 
ATOM   2168  C  CZ  . ARG A  1 284 ? 17.377  5.983   39.441  1.00 12.74  ? 371  ARG A CZ  1 
ATOM   2169  N  NH1 . ARG A  1 284 ? 18.296  5.969   38.472  1.00 10.21  ? 371  ARG A NH1 1 
ATOM   2170  N  NH2 . ARG A  1 284 ? 16.109  6.256   39.154  1.00 12.98  ? 371  ARG A NH2 1 
ATOM   2171  N  N   . THR A  1 285 ? 20.754  6.524   45.603  1.00 10.67  ? 372  THR A N   1 
ATOM   2172  C  CA  . THR A  1 285 ? 20.183  7.720   46.208  1.00 10.60  ? 372  THR A CA  1 
ATOM   2173  C  C   . THR A  1 285 ? 19.010  8.186   45.331  1.00 11.01  ? 372  THR A C   1 
ATOM   2174  O  O   . THR A  1 285 ? 19.012  7.969   44.120  1.00 10.39  ? 372  THR A O   1 
ATOM   2175  C  CB  . THR A  1 285 ? 21.209  8.858   46.349  1.00 10.10  ? 372  THR A CB  1 
ATOM   2176  O  OG1 . THR A  1 285 ? 21.646  9.274   45.044  1.00 10.54  ? 372  THR A OG1 1 
ATOM   2177  C  CG2 . THR A  1 285 ? 22.448  8.397   47.186  1.00 10.45  ? 372  THR A CG2 1 
ATOM   2178  N  N   . ILE A  1 286 ? 18.012  8.826   45.935  1.00 11.84  ? 373  ILE A N   1 
ATOM   2179  C  CA  . ILE A  1 286 ? 16.885  9.345   45.136  1.00 12.03  ? 373  ILE A CA  1 
ATOM   2180  C  C   . ILE A  1 286 ? 17.311  10.568  44.309  1.00 12.94  ? 373  ILE A C   1 
ATOM   2181  O  O   . ILE A  1 286 ? 17.028  10.641  43.100  1.00 12.25  ? 373  ILE A O   1 
ATOM   2182  C  CB  . ILE A  1 286 ? 15.633  9.605   45.995  1.00 12.23  ? 373  ILE A CB  1 
ATOM   2183  C  CG1 . ILE A  1 286 ? 15.100  8.260   46.524  1.00 12.12  ? 373  ILE A CG1 1 
ATOM   2184  C  CG2 . ILE A  1 286 ? 14.552  10.339  45.150  1.00 11.71  ? 373  ILE A CG2 1 
ATOM   2185  C  CD1 . ILE A  1 286 ? 14.008  8.364   47.574  1.00 12.37  ? 373  ILE A CD1 1 
ATOM   2186  N  N   . SER A  1 287 ? 18.033  11.503  44.940  1.00 13.28  ? 374  SER A N   1 
ATOM   2187  C  CA  . SER A  1 287 ? 18.604  12.614  44.211  1.00 13.90  ? 374  SER A CA  1 
ATOM   2188  C  C   . SER A  1 287 ? 19.706  12.115  43.268  1.00 14.47  ? 374  SER A C   1 
ATOM   2189  O  O   . SER A  1 287 ? 20.534  11.253  43.638  1.00 14.66  ? 374  SER A O   1 
ATOM   2190  C  CB  . SER A  1 287 ? 19.146  13.672  45.177  1.00 13.73  ? 374  SER A CB  1 
ATOM   2191  O  OG  . SER A  1 287 ? 20.018  14.569  44.517  1.00 12.70  ? 374  SER A OG  1 
ATOM   2192  N  N   . LYS A  1 288 ? 19.686  12.642  42.039  1.00 15.11  ? 375  LYS A N   1 
ATOM   2193  C  CA  . LYS A  1 288 ? 20.754  12.437  41.044  1.00 16.44  ? 375  LYS A CA  1 
ATOM   2194  C  C   . LYS A  1 288 ? 22.031  13.225  41.355  1.00 16.10  ? 375  LYS A C   1 
ATOM   2195  O  O   . LYS A  1 288 ? 23.115  12.891  40.850  1.00 16.42  ? 375  LYS A O   1 
ATOM   2196  C  CB  . LYS A  1 288 ? 20.269  12.871  39.643  1.00 16.35  ? 375  LYS A CB  1 
ATOM   2197  C  CG  . LYS A  1 288 ? 19.009  12.151  39.198  1.00 17.74  ? 375  LYS A CG  1 
ATOM   2198  C  CD  . LYS A  1 288 ? 18.326  12.844  38.000  1.00 20.02  ? 375  LYS A CD  1 
ATOM   2199  C  CE  . LYS A  1 288 ? 16.829  12.497  37.941  1.00 24.46  ? 375  LYS A CE  1 
ATOM   2200  N  NZ  . LYS A  1 288 ? 16.247  12.687  36.559  1.00 27.75  ? 375  LYS A NZ  1 
ATOM   2201  N  N   . ASP A  1 289 ? 21.901  14.279  42.153  1.00 16.23  ? 376  ASP A N   1 
ATOM   2202  C  CA  . ASP A  1 289 ? 23.022  15.197  42.431  1.00 16.44  ? 376  ASP A CA  1 
ATOM   2203  C  C   . ASP A  1 289 ? 23.719  14.892  43.744  1.00 16.51  ? 376  ASP A C   1 
ATOM   2204  O  O   . ASP A  1 289 ? 24.955  14.880  43.820  1.00 17.10  ? 376  ASP A O   1 
ATOM   2205  C  CB  . ASP A  1 289 ? 22.490  16.622  42.542  1.00 16.36  ? 376  ASP A CB  1 
ATOM   2206  C  CG  . ASP A  1 289 ? 21.762  17.079  41.289  1.00 18.03  ? 376  ASP A CG  1 
ATOM   2207  O  OD1 . ASP A  1 289 ? 21.978  16.494  40.203  1.00 16.74  ? 376  ASP A OD1 1 
ATOM   2208  O  OD2 . ASP A  1 289 ? 20.986  18.053  41.411  1.00 18.24  ? 376  ASP A OD2 1 
ATOM   2209  N  N   . SER A  1 290 ? 22.906  14.653  44.772  1.00 16.27  ? 377  SER A N   1 
ATOM   2210  C  CA  . SER A  1 290 ? 23.352  14.637  46.173  1.00 15.73  ? 377  SER A CA  1 
ATOM   2211  C  C   . SER A  1 290 ? 23.068  13.313  46.875  1.00 14.90  ? 377  SER A C   1 
ATOM   2212  O  O   . SER A  1 290 ? 22.230  12.508  46.428  1.00 13.70  ? 377  SER A O   1 
ATOM   2213  C  CB  . SER A  1 290 ? 22.634  15.748  46.934  1.00 16.14  ? 377  SER A CB  1 
ATOM   2214  O  OG  . SER A  1 290 ? 22.994  17.008  46.394  1.00 19.65  ? 377  SER A OG  1 
ATOM   2215  N  N   . ARG A  1 291 ? 23.763  13.114  47.994  1.00 13.43  ? 378  ARG A N   1 
ATOM   2216  C  CA  . ARG A  1 291 ? 23.559  11.955  48.852  1.00 12.69  ? 378  ARG A CA  1 
ATOM   2217  C  C   . ARG A  1 291 ? 22.325  12.157  49.723  1.00 12.78  ? 378  ARG A C   1 
ATOM   2218  O  O   . ARG A  1 291 ? 22.394  12.276  50.955  1.00 12.20  ? 378  ARG A O   1 
ATOM   2219  C  CB  . ARG A  1 291 ? 24.805  11.691  49.703  1.00 12.20  ? 378  ARG A CB  1 
ATOM   2220  C  CG  . ARG A  1 291 ? 25.977  11.160  48.900  1.00 10.42  ? 378  ARG A CG  1 
ATOM   2221  C  CD  . ARG A  1 291 ? 27.299  11.302  49.694  1.00 9.82   ? 378  ARG A CD  1 
ATOM   2222  N  NE  . ARG A  1 291 ? 28.429  10.945  48.833  1.00 8.76   ? 378  ARG A NE  1 
ATOM   2223  C  CZ  . ARG A  1 291 ? 29.686  10.748  49.248  1.00 11.24  ? 378  ARG A CZ  1 
ATOM   2224  N  NH1 . ARG A  1 291 ? 30.019  10.915  50.525  1.00 10.67  ? 378  ARG A NH1 1 
ATOM   2225  N  NH2 . ARG A  1 291 ? 30.627  10.387  48.365  1.00 11.95  ? 378  ARG A NH2 1 
ATOM   2226  N  N   . SER A  1 292 ? 21.175  12.226  49.072  1.00 12.65  ? 379  SER A N   1 
ATOM   2227  C  CA  . SER A  1 292 ? 19.938  12.276  49.821  1.00 13.43  ? 379  SER A CA  1 
ATOM   2228  C  C   . SER A  1 292 ? 18.941  11.253  49.290  1.00 13.04  ? 379  SER A C   1 
ATOM   2229  O  O   . SER A  1 292 ? 18.910  10.926  48.072  1.00 12.25  ? 379  SER A O   1 
ATOM   2230  C  CB  . SER A  1 292 ? 19.343  13.681  49.834  1.00 14.32  ? 379  SER A CB  1 
ATOM   2231  O  OG  . SER A  1 292 ? 19.025  14.083  48.532  1.00 16.90  ? 379  SER A OG  1 
ATOM   2232  N  N   . GLY A  1 293 ? 18.166  10.722  50.226  1.00 11.99  ? 380  GLY A N   1 
ATOM   2233  C  CA  . GLY A  1 293 ? 17.160  9.726   49.905  1.00 12.28  ? 380  GLY A CA  1 
ATOM   2234  C  C   . GLY A  1 293 ? 17.820  8.415   49.550  1.00 11.67  ? 380  GLY A C   1 
ATOM   2235  O  O   . GLY A  1 293 ? 19.037  8.352   49.321  1.00 11.32  ? 380  GLY A O   1 
ATOM   2236  N  N   . TYR A  1 294 ? 17.017  7.358   49.526  1.00 11.71  ? 381  TYR A N   1 
ATOM   2237  C  CA  . TYR A  1 294 ? 17.500  6.061   49.078  1.00 10.80  ? 381  TYR A CA  1 
ATOM   2238  C  C   . TYR A  1 294 ? 16.319  5.248   48.585  1.00 10.51  ? 381  TYR A C   1 
ATOM   2239  O  O   . TYR A  1 294 ? 15.266  5.206   49.243  1.00 9.20   ? 381  TYR A O   1 
ATOM   2240  C  CB  . TYR A  1 294 ? 18.281  5.300   50.177  1.00 10.39  ? 381  TYR A CB  1 
ATOM   2241  C  CG  . TYR A  1 294 ? 19.258  4.348   49.529  1.00 11.16  ? 381  TYR A CG  1 
ATOM   2242  C  CD1 . TYR A  1 294 ? 18.877  3.033   49.195  1.00 10.42  ? 381  TYR A CD1 1 
ATOM   2243  C  CD2 . TYR A  1 294 ? 20.538  4.784   49.166  1.00 10.55  ? 381  TYR A CD2 1 
ATOM   2244  C  CE1 . TYR A  1 294 ? 19.777  2.155   48.547  1.00 9.92   ? 381  TYR A CE1 1 
ATOM   2245  C  CE2 . TYR A  1 294 ? 21.430  3.921   48.519  1.00 10.30  ? 381  TYR A CE2 1 
ATOM   2246  C  CZ  . TYR A  1 294 ? 21.045  2.623   48.210  1.00 12.03  ? 381  TYR A CZ  1 
ATOM   2247  O  OH  . TYR A  1 294 ? 21.939  1.796   47.569  1.00 11.55  ? 381  TYR A OH  1 
ATOM   2248  N  N   . GLU A  1 295 ? 16.501  4.593   47.437  1.00 10.10  ? 382  GLU A N   1 
ATOM   2249  C  CA  . GLU A  1 295 ? 15.440  3.776   46.845  1.00 10.42  ? 382  GLU A CA  1 
ATOM   2250  C  C   . GLU A  1 295 ? 15.994  2.438   46.372  1.00 9.61   ? 382  GLU A C   1 
ATOM   2251  O  O   . GLU A  1 295 ? 17.155  2.355   45.936  1.00 9.86   ? 382  GLU A O   1 
ATOM   2252  C  CB  . GLU A  1 295 ? 14.775  4.525   45.673  1.00 9.72   ? 382  GLU A CB  1 
ATOM   2253  C  CG  . GLU A  1 295 ? 15.728  4.817   44.500  1.00 10.48  ? 382  GLU A CG  1 
ATOM   2254  C  CD  . GLU A  1 295 ? 15.098  5.669   43.397  1.00 11.95  ? 382  GLU A CD  1 
ATOM   2255  O  OE1 . GLU A  1 295 ? 13.844  5.761   43.331  1.00 14.00  ? 382  GLU A OE1 1 
ATOM   2256  O  OE2 . GLU A  1 295 ? 15.875  6.263   42.621  1.00 12.33  ? 382  GLU A OE2 1 
ATOM   2257  N  N   . MET A  1 296 ? 15.178  1.392   46.484  1.00 9.98   ? 383  MET A N   1 
ATOM   2258  C  CA  . MET A  1 296 ? 15.494  0.081   45.919  1.00 10.33  ? 383  MET A CA  1 
ATOM   2259  C  C   . MET A  1 296 ? 14.622  -0.103  44.675  1.00 11.56  ? 383  MET A C   1 
ATOM   2260  O  O   . MET A  1 296 ? 13.403  0.091   44.730  1.00 11.26  ? 383  MET A O   1 
ATOM   2261  C  CB  . MET A  1 296 ? 15.196  -1.064  46.911  1.00 10.45  ? 383  MET A CB  1 
ATOM   2262  C  CG  . MET A  1 296 ? 16.165  -1.204  48.076  1.00 10.29  ? 383  MET A CG  1 
ATOM   2263  S  SD  . MET A  1 296 ? 17.899  -1.241  47.562  1.00 10.53  ? 383  MET A SD  1 
ATOM   2264  C  CE  . MET A  1 296 ? 18.018  -2.854  46.768  1.00 9.61   ? 383  MET A CE  1 
ATOM   2265  N  N   . LEU A  1 297 ? 15.254  -0.463  43.559  1.00 11.63  ? 384  LEU A N   1 
ATOM   2266  C  CA  . LEU A  1 297 ? 14.548  -0.663  42.288  1.00 11.75  ? 384  LEU A CA  1 
ATOM   2267  C  C   . LEU A  1 297 ? 14.760  -2.077  41.774  1.00 11.34  ? 384  LEU A C   1 
ATOM   2268  O  O   . LEU A  1 297 ? 15.903  -2.532  41.640  1.00 10.58  ? 384  LEU A O   1 
ATOM   2269  C  CB  . LEU A  1 297 ? 15.064  0.335   41.237  1.00 12.06  ? 384  LEU A CB  1 
ATOM   2270  C  CG  . LEU A  1 297 ? 14.980  1.822   41.594  1.00 13.29  ? 384  LEU A CG  1 
ATOM   2271  C  CD1 . LEU A  1 297 ? 15.709  2.644   40.566  1.00 16.20  ? 384  LEU A CD1 1 
ATOM   2272  C  CD2 . LEU A  1 297 ? 13.536  2.276   41.719  1.00 16.09  ? 384  LEU A CD2 1 
ATOM   2273  N  N   . LYS A  1 298 ? 13.666  -2.773  41.480  1.00 11.36  ? 385  LYS A N   1 
ATOM   2274  C  CA  . LYS A  1 298 ? 13.784  -4.118  40.923  1.00 11.44  ? 385  LYS A CA  1 
ATOM   2275  C  C   . LYS A  1 298 ? 13.902  -3.986  39.404  1.00 11.40  ? 385  LYS A C   1 
ATOM   2276  O  O   . LYS A  1 298 ? 12.963  -3.542  38.728  1.00 10.92  ? 385  LYS A O   1 
ATOM   2277  C  CB  . LYS A  1 298 ? 12.612  -5.004  41.318  1.00 11.49  ? 385  LYS A CB  1 
ATOM   2278  C  CG  . LYS A  1 298 ? 12.756  -6.455  40.862  1.00 11.77  ? 385  LYS A CG  1 
ATOM   2279  C  CD  . LYS A  1 298 ? 11.707  -7.356  41.496  1.00 11.91  ? 385  LYS A CD  1 
ATOM   2280  C  CE  . LYS A  1 298 ? 12.095  -8.846  41.349  1.00 12.98  ? 385  LYS A CE  1 
ATOM   2281  N  NZ  . LYS A  1 298 ? 11.079  -9.789  41.901  1.00 13.28  ? 385  LYS A NZ  1 
ATOM   2282  N  N   . VAL A  1 299 ? 15.066  -4.374  38.891  1.00 10.78  ? 386  VAL A N   1 
ATOM   2283  C  CA  . VAL A  1 299 ? 15.418  -4.149  37.497  1.00 11.84  ? 386  VAL A CA  1 
ATOM   2284  C  C   . VAL A  1 299 ? 15.835  -5.488  36.882  1.00 12.23  ? 386  VAL A C   1 
ATOM   2285  O  O   . VAL A  1 299 ? 17.022  -5.851  36.905  1.00 12.20  ? 386  VAL A O   1 
ATOM   2286  C  CB  . VAL A  1 299 ? 16.526  -3.050  37.340  1.00 11.14  ? 386  VAL A CB  1 
ATOM   2287  C  CG1 . VAL A  1 299 ? 16.852  -2.806  35.859  1.00 12.24  ? 386  VAL A CG1 1 
ATOM   2288  C  CG2 . VAL A  1 299 ? 16.101  -1.720  38.027  1.00 11.62  ? 386  VAL A CG2 1 
ATOM   2289  N  N   . PRO A  1 300 ? 14.846  -6.256  36.379  1.00 13.01  ? 387  PRO A N   1 
ATOM   2290  C  CA  . PRO A  1 300 ? 15.132  -7.571  35.807  1.00 13.06  ? 387  PRO A CA  1 
ATOM   2291  C  C   . PRO A  1 300 ? 16.230  -7.486  34.723  1.00 13.40  ? 387  PRO A C   1 
ATOM   2292  O  O   . PRO A  1 300 ? 16.186  -6.603  33.864  1.00 12.41  ? 387  PRO A O   1 
ATOM   2293  C  CB  . PRO A  1 300 ? 13.781  -7.998  35.213  1.00 13.99  ? 387  PRO A CB  1 
ATOM   2294  C  CG  . PRO A  1 300 ? 12.758  -7.258  36.053  1.00 14.97  ? 387  PRO A CG  1 
ATOM   2295  C  CD  . PRO A  1 300 ? 13.401  -5.926  36.332  1.00 13.36  ? 387  PRO A CD  1 
ATOM   2296  N  N   . ASN A  1 301 ? 17.226  -8.375  34.818  1.00 13.37  ? 388  ASN A N   1 
ATOM   2297  C  CA  . ASN A  1 301 ? 18.323  -8.464  33.834  1.00 13.79  ? 388  ASN A CA  1 
ATOM   2298  C  C   . ASN A  1 301 ? 19.187  -7.186  33.734  1.00 13.75  ? 388  ASN A C   1 
ATOM   2299  O  O   . ASN A  1 301 ? 19.774  -6.884  32.682  1.00 14.20  ? 388  ASN A O   1 
ATOM   2300  C  CB  . ASN A  1 301 ? 17.774  -8.920  32.462  1.00 13.66  ? 388  ASN A CB  1 
ATOM   2301  C  CG  . ASN A  1 301 ? 16.976  -10.220 32.554  1.00 14.72  ? 388  ASN A CG  1 
ATOM   2302  O  OD1 . ASN A  1 301 ? 17.454  -11.226 33.077  1.00 14.61  ? 388  ASN A OD1 1 
ATOM   2303  N  ND2 . ASN A  1 301 ? 15.764  -10.206 32.029  1.00 16.25  ? 388  ASN A ND2 1 
ATOM   2304  N  N   . ALA A  1 302 ? 19.286  -6.455  34.853  1.00 12.73  ? 389  ALA A N   1 
ATOM   2305  C  CA  . ALA A  1 302 ? 20.133  -5.257  34.941  1.00 12.73  ? 389  ALA A CA  1 
ATOM   2306  C  C   . ALA A  1 302 ? 21.581  -5.564  34.526  1.00 12.12  ? 389  ALA A C   1 
ATOM   2307  O  O   . ALA A  1 302 ? 22.253  -4.721  33.963  1.00 11.78  ? 389  ALA A O   1 
ATOM   2308  C  CB  . ALA A  1 302 ? 20.099  -4.673  36.353  1.00 11.86  ? 389  ALA A CB  1 
ATOM   2309  N  N   . GLU A  1 303 ? 22.030  -6.793  34.778  1.00 11.88  ? 390  GLU A N   1 
ATOM   2310  C  CA  . GLU A  1 303 ? 23.422  -7.171  34.510  1.00 12.69  ? 390  GLU A CA  1 
ATOM   2311  C  C   . GLU A  1 303 ? 23.719  -7.386  33.022  1.00 12.92  ? 390  GLU A C   1 
ATOM   2312  O  O   . GLU A  1 303 ? 24.876  -7.360  32.606  1.00 12.80  ? 390  GLU A O   1 
ATOM   2313  C  CB  . GLU A  1 303 ? 23.789  -8.437  35.284  1.00 12.00  ? 390  GLU A CB  1 
ATOM   2314  C  CG  . GLU A  1 303 ? 25.311  -8.712  35.330  1.00 12.98  ? 390  GLU A CG  1 
ATOM   2315  C  CD  . GLU A  1 303 ? 25.684  -9.844  36.291  1.00 13.35  ? 390  GLU A CD  1 
ATOM   2316  O  OE1 . GLU A  1 303 ? 26.891  -10.035 36.550  1.00 14.88  ? 390  GLU A OE1 1 
ATOM   2317  O  OE2 . GLU A  1 303 ? 24.787  -10.538 36.793  1.00 12.09  ? 390  GLU A OE2 1 
ATOM   2318  N  N   . THR A  1 304 ? 22.678  -7.570  32.216  1.00 13.43  ? 391  THR A N   1 
ATOM   2319  C  CA  . THR A  1 304 ? 22.888  -8.039  30.846  1.00 13.79  ? 391  THR A CA  1 
ATOM   2320  C  C   . THR A  1 304 ? 22.113  -7.250  29.787  1.00 14.01  ? 391  THR A C   1 
ATOM   2321  O  O   . THR A  1 304 ? 22.459  -7.311  28.598  1.00 14.56  ? 391  THR A O   1 
ATOM   2322  C  CB  . THR A  1 304 ? 22.506  -9.526  30.714  1.00 13.72  ? 391  THR A CB  1 
ATOM   2323  O  OG1 . THR A  1 304 ? 21.096  -9.671  30.905  1.00 14.01  ? 391  THR A OG1 1 
ATOM   2324  C  CG2 . THR A  1 304 ? 23.252  -10.404 31.736  1.00 13.43  ? 391  THR A CG2 1 
ATOM   2325  N  N   . ASP A  1 305 ? 21.070  -6.537  30.200  1.00 13.76  ? 392  ASP A N   1 
ATOM   2326  C  CA  . ASP A  1 305 ? 20.195  -5.837  29.251  1.00 13.82  ? 392  ASP A CA  1 
ATOM   2327  C  C   . ASP A  1 305 ? 20.331  -4.312  29.368  1.00 13.91  ? 392  ASP A C   1 
ATOM   2328  O  O   . ASP A  1 305 ? 19.957  -3.708  30.385  1.00 13.64  ? 392  ASP A O   1 
ATOM   2329  C  CB  . ASP A  1 305 ? 18.739  -6.315  29.459  1.00 13.92  ? 392  ASP A CB  1 
ATOM   2330  C  CG  . ASP A  1 305 ? 17.763  -5.751  28.433  1.00 16.43  ? 392  ASP A CG  1 
ATOM   2331  O  OD1 . ASP A  1 305 ? 18.103  -4.816  27.660  1.00 16.07  ? 392  ASP A OD1 1 
ATOM   2332  O  OD2 . ASP A  1 305 ? 16.610  -6.234  28.435  1.00 19.64  ? 392  ASP A OD2 1 
ATOM   2333  N  N   . ILE A  1 306 ? 20.859  -3.679  28.320  1.00 14.16  ? 393  ILE A N   1 
ATOM   2334  C  CA  . ILE A  1 306 ? 21.044  -2.209  28.333  1.00 14.02  ? 393  ILE A CA  1 
ATOM   2335  C  C   . ILE A  1 306 ? 19.728  -1.425  28.429  1.00 14.38  ? 393  ILE A C   1 
ATOM   2336  O  O   . ILE A  1 306 ? 19.721  -0.284  28.874  1.00 14.44  ? 393  ILE A O   1 
ATOM   2337  C  CB  . ILE A  1 306 ? 21.888  -1.707  27.131  1.00 14.39  ? 393  ILE A CB  1 
ATOM   2338  C  CG1 . ILE A  1 306 ? 21.127  -1.881  25.803  1.00 13.95  ? 393  ILE A CG1 1 
ATOM   2339  C  CG2 . ILE A  1 306 ? 23.259  -2.416  27.123  1.00 14.08  ? 393  ILE A CG2 1 
ATOM   2340  C  CD1 . ILE A  1 306 ? 21.964  -1.540  24.578  1.00 14.74  ? 393  ILE A CD1 1 
ATOM   2341  N  N   . GLN A  1 307 ? 18.629  -2.053  28.014  1.00 14.95  ? 394  GLN A N   1 
ATOM   2342  C  CA  . GLN A  1 307 ? 17.313  -1.412  27.991  1.00 16.61  ? 394  GLN A CA  1 
ATOM   2343  C  C   . GLN A  1 307 ? 16.508  -1.687  29.269  1.00 15.73  ? 394  GLN A C   1 
ATOM   2344  O  O   . GLN A  1 307 ? 15.369  -1.208  29.407  1.00 15.71  ? 394  GLN A O   1 
ATOM   2345  C  CB  . GLN A  1 307 ? 16.511  -1.941  26.800  1.00 16.89  ? 394  GLN A CB  1 
ATOM   2346  C  CG  . GLN A  1 307 ? 17.028  -1.524  25.422  1.00 19.08  ? 394  GLN A CG  1 
ATOM   2347  C  CD  . GLN A  1 307 ? 15.990  -1.824  24.336  1.00 19.87  ? 394  GLN A CD  1 
ATOM   2348  O  OE1 . GLN A  1 307 ? 15.755  -2.981  23.979  1.00 25.63  ? 394  GLN A OE1 1 
ATOM   2349  N  NE2 . GLN A  1 307 ? 15.352  -0.780  23.832  1.00 24.45  ? 394  GLN A NE2 1 
ATOM   2350  N  N   . SER A  1 308 ? 17.083  -2.476  30.178  1.00 15.79  ? 395  SER A N   1 
ATOM   2351  C  CA  . SER A  1 308 ? 16.401  -2.871  31.426  1.00 15.10  ? 395  SER A CA  1 
ATOM   2352  C  C   . SER A  1 308 ? 15.997  -1.694  32.318  1.00 14.80  ? 395  SER A C   1 
ATOM   2353  O  O   . SER A  1 308 ? 16.816  -0.817  32.656  1.00 14.76  ? 395  SER A O   1 
ATOM   2354  C  CB  . SER A  1 308 ? 17.237  -3.886  32.205  1.00 15.70  ? 395  SER A CB  1 
ATOM   2355  O  OG  . SER A  1 308 ? 18.481  -3.331  32.612  1.00 15.41  ? 395  SER A OG  1 
ATOM   2356  N  N   . GLY A  1 309 ? 14.716  -1.668  32.682  1.00 14.62  ? 396  GLY A N   1 
ATOM   2357  C  CA  . GLY A  1 309 ? 14.183  -0.666  33.609  1.00 13.50  ? 396  GLY A CA  1 
ATOM   2358  C  C   . GLY A  1 309 ? 13.453  -1.293  34.801  1.00 13.29  ? 396  GLY A C   1 
ATOM   2359  O  O   . GLY A  1 309 ? 13.296  -2.510  34.872  1.00 12.55  ? 396  GLY A O   1 
ATOM   2360  N  N   . PRO A  1 310 ? 13.030  -0.456  35.762  1.00 13.34  ? 397  PRO A N   1 
ATOM   2361  C  CA  . PRO A  1 310 ? 12.413  -0.949  36.987  1.00 13.67  ? 397  PRO A CA  1 
ATOM   2362  C  C   . PRO A  1 310 ? 10.995  -1.454  36.784  1.00 14.28  ? 397  PRO A C   1 
ATOM   2363  O  O   . PRO A  1 310 ? 10.236  -0.878  35.984  1.00 14.64  ? 397  PRO A O   1 
ATOM   2364  C  CB  . PRO A  1 310 ? 12.405  0.284   37.906  1.00 13.52  ? 397  PRO A CB  1 
ATOM   2365  C  CG  . PRO A  1 310 ? 13.329  1.271   37.270  1.00 13.72  ? 397  PRO A CG  1 
ATOM   2366  C  CD  . PRO A  1 310 ? 13.178  1.006   35.789  1.00 12.60  ? 397  PRO A CD  1 
ATOM   2367  N  N   . ILE A  1 311 ? 10.652  -2.513  37.516  1.00 14.54  ? 398  ILE A N   1 
ATOM   2368  C  CA  . ILE A  1 311 ? 9.292   -3.047  37.550  1.00 14.49  ? 398  ILE A CA  1 
ATOM   2369  C  C   . ILE A  1 311 ? 8.657   -2.915  38.929  1.00 15.01  ? 398  ILE A C   1 
ATOM   2370  O  O   . ILE A  1 311 ? 7.474   -3.242  39.110  1.00 14.30  ? 398  ILE A O   1 
ATOM   2371  C  CB  . ILE A  1 311 ? 9.252   -4.529  37.098  1.00 14.20  ? 398  ILE A CB  1 
ATOM   2372  C  CG1 . ILE A  1 311 ? 10.020  -5.433  38.087  1.00 14.27  ? 398  ILE A CG1 1 
ATOM   2373  C  CG2 . ILE A  1 311 ? 9.774   -4.655  35.642  1.00 14.93  ? 398  ILE A CG2 1 
ATOM   2374  C  CD1 . ILE A  1 311 ? 9.739   -6.923  37.915  1.00 15.41  ? 398  ILE A CD1 1 
ATOM   2375  N  N   . SER A  1 312 ? 9.453   -2.475  39.901  1.00 14.61  ? 399  SER A N   1 
ATOM   2376  C  CA  . SER A  1 312 ? 8.954   -2.168  41.246  1.00 15.67  ? 399  SER A CA  1 
ATOM   2377  C  C   . SER A  1 312 ? 9.951   -1.293  41.987  1.00 14.86  ? 399  SER A C   1 
ATOM   2378  O  O   . SER A  1 312 ? 11.118  -1.165  41.590  1.00 13.94  ? 399  SER A O   1 
ATOM   2379  C  CB  . SER A  1 312 ? 8.628   -3.443  42.039  1.00 15.72  ? 399  SER A CB  1 
ATOM   2380  O  OG  . SER A  1 312 ? 9.791   -4.032  42.557  1.00 21.48  ? 399  SER A OG  1 
ATOM   2381  N  N   . ASN A  1 313 ? 9.486   -0.679  43.065  1.00 14.26  ? 400  ASN A N   1 
ATOM   2382  C  CA  . ASN A  1 313 ? 10.314  0.234   43.825  1.00 15.16  ? 400  ASN A CA  1 
ATOM   2383  C  C   . ASN A  1 313 ? 9.990   0.115   45.313  1.00 14.35  ? 400  ASN A C   1 
ATOM   2384  O  O   . ASN A  1 313 ? 8.876   -0.280  45.692  1.00 14.54  ? 400  ASN A O   1 
ATOM   2385  C  CB  . ASN A  1 313 ? 10.105  1.679   43.350  1.00 15.03  ? 400  ASN A CB  1 
ATOM   2386  C  CG  . ASN A  1 313 ? 8.726   2.242   43.740  1.00 18.35  ? 400  ASN A CG  1 
ATOM   2387  O  OD1 . ASN A  1 313 ? 7.719   2.049   43.031  1.00 22.95  ? 400  ASN A OD1 1 
ATOM   2388  N  ND2 . ASN A  1 313 ? 8.679   2.951   44.872  1.00 21.64  ? 400  ASN A ND2 1 
ATOM   2389  N  N   . GLN A  1 314 ? 10.964  0.464   46.145  1.00 13.24  ? 401  GLN A N   1 
ATOM   2390  C  CA  . GLN A  1 314 ? 10.699  0.674   47.559  1.00 12.41  ? 401  GLN A CA  1 
ATOM   2391  C  C   . GLN A  1 314 ? 11.533  1.859   48.035  1.00 12.09  ? 401  GLN A C   1 
ATOM   2392  O  O   . GLN A  1 314 ? 12.770  1.811   47.959  1.00 12.35  ? 401  GLN A O   1 
ATOM   2393  C  CB  . GLN A  1 314 ? 11.040  -0.586  48.363  1.00 12.04  ? 401  GLN A CB  1 
ATOM   2394  C  CG  . GLN A  1 314 ? 10.597  -0.452  49.839  1.00 11.18  ? 401  GLN A CG  1 
ATOM   2395  C  CD  . GLN A  1 314 ? 10.682  -1.763  50.590  1.00 8.53   ? 401  GLN A CD  1 
ATOM   2396  O  OE1 . GLN A  1 314 ? 10.534  -2.836  50.011  1.00 9.26   ? 401  GLN A OE1 1 
ATOM   2397  N  NE2 . GLN A  1 314 ? 10.937  -1.674  51.881  1.00 9.15   ? 401  GLN A NE2 1 
ATOM   2398  N  N   . VAL A  1 315 ? 10.876  2.921   48.513  1.00 11.70  ? 402  VAL A N   1 
ATOM   2399  C  CA  . VAL A  1 315 ? 11.615  4.008   49.157  1.00 11.42  ? 402  VAL A CA  1 
ATOM   2400  C  C   . VAL A  1 315 ? 12.125  3.559   50.544  1.00 11.45  ? 402  VAL A C   1 
ATOM   2401  O  O   . VAL A  1 315 ? 11.336  3.169   51.414  1.00 11.98  ? 402  VAL A O   1 
ATOM   2402  C  CB  . VAL A  1 315 ? 10.788  5.299   49.280  1.00 11.32  ? 402  VAL A CB  1 
ATOM   2403  C  CG1 . VAL A  1 315 ? 11.533  6.356   50.080  1.00 10.59  ? 402  VAL A CG1 1 
ATOM   2404  C  CG2 . VAL A  1 315 ? 10.414  5.842   47.897  1.00 12.08  ? 402  VAL A CG2 1 
ATOM   2405  N  N   . ILE A  1 316 ? 13.447  3.621   50.725  1.00 10.24  ? 403  ILE A N   1 
ATOM   2406  C  CA  . ILE A  1 316 ? 14.096  3.235   51.990  1.00 9.90   ? 403  ILE A CA  1 
ATOM   2407  C  C   . ILE A  1 316 ? 14.319  4.448   52.913  1.00 10.76  ? 403  ILE A C   1 
ATOM   2408  O  O   . ILE A  1 316 ? 14.186  4.342   54.139  1.00 10.56  ? 403  ILE A O   1 
ATOM   2409  C  CB  . ILE A  1 316 ? 15.448  2.518   51.729  1.00 11.06  ? 403  ILE A CB  1 
ATOM   2410  C  CG1 . ILE A  1 316 ? 15.278  1.348   50.721  1.00 10.39  ? 403  ILE A CG1 1 
ATOM   2411  C  CG2 . ILE A  1 316 ? 16.093  2.050   53.049  1.00 8.58   ? 403  ILE A CG2 1 
ATOM   2412  C  CD1 . ILE A  1 316 ? 14.178  0.302   51.088  1.00 9.56   ? 403  ILE A CD1 1 
ATOM   2413  N  N   . VAL A  1 317 ? 14.678  5.584   52.312  1.00 10.33  ? 404  VAL A N   1 
ATOM   2414  C  CA  . VAL A  1 317 ? 14.892  6.841   53.029  1.00 10.89  ? 404  VAL A CA  1 
ATOM   2415  C  C   . VAL A  1 317 ? 14.285  7.910   52.117  1.00 11.51  ? 404  VAL A C   1 
ATOM   2416  O  O   . VAL A  1 317 ? 14.647  7.987   50.942  1.00 10.38  ? 404  VAL A O   1 
ATOM   2417  C  CB  . VAL A  1 317 ? 16.396  7.161   53.196  1.00 10.62  ? 404  VAL A CB  1 
ATOM   2418  C  CG1 . VAL A  1 317 ? 16.606  8.535   53.862  1.00 10.70  ? 404  VAL A CG1 1 
ATOM   2419  C  CG2 . VAL A  1 317 ? 17.139  6.029   53.918  1.00 12.02  ? 404  VAL A CG2 1 
ATOM   2420  N  N   . ASN A  1 318 ? 13.356  8.711   52.631  1.00 13.04  ? 405  ASN A N   1 
ATOM   2421  C  CA  . ASN A  1 318 ? 12.710  9.706   51.751  1.00 14.80  ? 405  ASN A CA  1 
ATOM   2422  C  C   . ASN A  1 318 ? 13.688  10.789  51.256  1.00 15.08  ? 405  ASN A C   1 
ATOM   2423  O  O   . ASN A  1 318 ? 14.752  11.000  51.859  1.00 15.16  ? 405  ASN A O   1 
ATOM   2424  C  CB  . ASN A  1 318 ? 11.424  10.257  52.370  1.00 15.73  ? 405  ASN A CB  1 
ATOM   2425  C  CG  . ASN A  1 318 ? 11.665  11.104  53.592  1.00 16.70  ? 405  ASN A CG  1 
ATOM   2426  O  OD1 . ASN A  1 318 ? 12.626  11.874  53.668  1.00 19.28  ? 405  ASN A OD1 1 
ATOM   2427  N  ND2 . ASN A  1 318 ? 10.761  10.984  54.565  1.00 21.43  ? 405  ASN A ND2 1 
ATOM   2428  N  N   . ASN A  1 319 ? 13.369  11.448  50.145  1.00 16.35  ? 406  ASN A N   1 
ATOM   2429  C  CA  . ASN A  1 319 ? 14.325  12.408  49.564  1.00 17.28  ? 406  ASN A CA  1 
ATOM   2430  C  C   . ASN A  1 319 ? 14.447  13.737  50.337  1.00 17.02  ? 406  ASN A C   1 
ATOM   2431  O  O   . ASN A  1 319 ? 15.171  14.630  49.912  1.00 17.77  ? 406  ASN A O   1 
ATOM   2432  C  CB  . ASN A  1 319 ? 14.075  12.647  48.051  1.00 17.36  ? 406  ASN A CB  1 
ATOM   2433  C  CG  . ASN A  1 319 ? 15.295  13.295  47.318  1.00 19.60  ? 406  ASN A CG  1 
ATOM   2434  O  OD1 . ASN A  1 319 ? 15.123  14.036  46.333  1.00 22.80  ? 406  ASN A OD1 1 
ATOM   2435  N  ND2 . ASN A  1 319 ? 16.510  13.025  47.793  1.00 15.77  ? 406  ASN A ND2 1 
ATOM   2436  N  N   . GLN A  1 320 ? 13.747  13.876  51.462  1.00 16.99  ? 407  GLN A N   1 
ATOM   2437  C  CA  . GLN A  1 320 ? 13.957  15.047  52.338  1.00 16.65  ? 407  GLN A CA  1 
ATOM   2438  C  C   . GLN A  1 320 ? 14.994  14.727  53.421  1.00 15.93  ? 407  GLN A C   1 
ATOM   2439  O  O   . GLN A  1 320 ? 15.269  15.552  54.304  1.00 16.13  ? 407  GLN A O   1 
ATOM   2440  C  CB  . GLN A  1 320 ? 12.640  15.541  52.970  1.00 17.44  ? 407  GLN A CB  1 
ATOM   2441  C  CG  . GLN A  1 320 ? 11.558  15.950  51.944  1.00 20.79  ? 407  GLN A CG  1 
ATOM   2442  C  CD  . GLN A  1 320 ? 10.948  14.731  51.238  1.00 25.33  ? 407  GLN A CD  1 
ATOM   2443  O  OE1 . GLN A  1 320 ? 10.375  13.848  51.881  1.00 27.91  ? 407  GLN A OE1 1 
ATOM   2444  N  NE2 . GLN A  1 320 ? 11.092  14.671  49.914  1.00 26.42  ? 407  GLN A NE2 1 
ATOM   2445  N  N   . ASN A  1 321 ? 15.568  13.527  53.341  1.00 14.31  ? 408  ASN A N   1 
ATOM   2446  C  CA  . ASN A  1 321 ? 16.556  13.086  54.320  1.00 13.45  ? 408  ASN A CA  1 
ATOM   2447  C  C   . ASN A  1 321 ? 17.877  12.628  53.703  1.00 12.75  ? 408  ASN A C   1 
ATOM   2448  O  O   . ASN A  1 321 ? 17.901  12.092  52.593  1.00 11.47  ? 408  ASN A O   1 
ATOM   2449  C  CB  . ASN A  1 321 ? 15.958  11.978  55.188  1.00 13.39  ? 408  ASN A CB  1 
ATOM   2450  C  CG  . ASN A  1 321 ? 14.897  12.497  56.127  1.00 14.15  ? 408  ASN A CG  1 
ATOM   2451  O  OD1 . ASN A  1 321 ? 13.683  12.386  55.865  1.00 14.55  ? 408  ASN A OD1 1 
ATOM   2452  N  ND2 . ASN A  1 321 ? 15.340  13.084  57.221  1.00 13.52  ? 408  ASN A ND2 1 
ATOM   2453  N  N   . TRP A  1 322 ? 18.963  12.843  54.452  1.00 12.41  ? 409  TRP A N   1 
ATOM   2454  C  CA  . TRP A  1 322 ? 20.296  12.477  54.039  1.00 12.57  ? 409  TRP A CA  1 
ATOM   2455  C  C   . TRP A  1 322 ? 20.555  10.973  54.094  1.00 12.25  ? 409  TRP A C   1 
ATOM   2456  O  O   . TRP A  1 322 ? 20.185  10.282  55.057  1.00 12.34  ? 409  TRP A O   1 
ATOM   2457  C  CB  . TRP A  1 322 ? 21.340  13.221  54.894  1.00 12.83  ? 409  TRP A CB  1 
ATOM   2458  C  CG  . TRP A  1 322 ? 21.131  14.716  54.824  1.00 13.75  ? 409  TRP A CG  1 
ATOM   2459  C  CD1 . TRP A  1 322 ? 20.758  15.543  55.839  1.00 12.66  ? 409  TRP A CD1 1 
ATOM   2460  C  CD2 . TRP A  1 322 ? 21.232  15.524  53.650  1.00 14.49  ? 409  TRP A CD2 1 
ATOM   2461  N  NE1 . TRP A  1 322 ? 20.645  16.845  55.367  1.00 14.60  ? 409  TRP A NE1 1 
ATOM   2462  C  CE2 . TRP A  1 322 ? 20.932  16.853  54.027  1.00 15.61  ? 409  TRP A CE2 1 
ATOM   2463  C  CE3 . TRP A  1 322 ? 21.568  15.257  52.310  1.00 14.99  ? 409  TRP A CE3 1 
ATOM   2464  C  CZ2 . TRP A  1 322 ? 20.951  17.916  53.112  1.00 15.84  ? 409  TRP A CZ2 1 
ATOM   2465  C  CZ3 . TRP A  1 322 ? 21.573  16.324  51.387  1.00 14.24  ? 409  TRP A CZ3 1 
ATOM   2466  C  CH2 . TRP A  1 322 ? 21.264  17.631  51.803  1.00 14.59  ? 409  TRP A CH2 1 
ATOM   2467  N  N   . SER A  1 323 ? 21.217  10.481  53.056  1.00 11.70  ? 410  SER A N   1 
ATOM   2468  C  CA  . SER A  1 323 ? 21.698  9.124   53.043  1.00 11.93  ? 410  SER A CA  1 
ATOM   2469  C  C   . SER A  1 323 ? 23.242  9.168   53.070  1.00 11.60  ? 410  SER A C   1 
ATOM   2470  O  O   . SER A  1 323 ? 23.843  9.940   53.845  1.00 10.72  ? 410  SER A O   1 
ATOM   2471  C  CB  . SER A  1 323 ? 21.081  8.329   51.863  1.00 11.84  ? 410  SER A CB  1 
ATOM   2472  O  OG  . SER A  1 323 ? 21.368  8.938   50.596  1.00 13.16  ? 410  SER A OG  1 
ATOM   2473  N  N   . GLY A  1 324 ? 23.884  8.390   52.214  1.00 11.04  ? 411  GLY A N   1 
ATOM   2474  C  CA  . GLY A  1 324 ? 25.346  8.217   52.292  1.00 10.75  ? 411  GLY A CA  1 
ATOM   2475  C  C   . GLY A  1 324 ? 25.736  6.945   51.571  1.00 10.75  ? 411  GLY A C   1 
ATOM   2476  O  O   . GLY A  1 324 ? 25.080  6.548   50.592  1.00 11.44  ? 411  GLY A O   1 
ATOM   2477  N  N   . TYR A  1 325 ? 26.821  6.314   52.027  1.00 9.94   ? 412  TYR A N   1 
ATOM   2478  C  CA  . TYR A  1 325 ? 27.255  5.018   51.481  1.00 10.27  ? 412  TYR A CA  1 
ATOM   2479  C  C   . TYR A  1 325 ? 26.201  3.951   51.686  1.00 9.86   ? 412  TYR A C   1 
ATOM   2480  O  O   . TYR A  1 325 ? 25.368  4.049   52.607  1.00 10.65  ? 412  TYR A O   1 
ATOM   2481  C  CB  . TYR A  1 325 ? 28.560  4.576   52.163  1.00 9.98   ? 412  TYR A CB  1 
ATOM   2482  C  CG  . TYR A  1 325 ? 29.796  5.272   51.666  1.00 10.46  ? 412  TYR A CG  1 
ATOM   2483  C  CD1 . TYR A  1 325 ? 29.709  6.434   50.874  1.00 9.26   ? 412  TYR A CD1 1 
ATOM   2484  C  CD2 . TYR A  1 325 ? 31.064  4.757   51.967  1.00 10.46  ? 412  TYR A CD2 1 
ATOM   2485  C  CE1 . TYR A  1 325 ? 30.874  7.084   50.395  1.00 11.61  ? 412  TYR A CE1 1 
ATOM   2486  C  CE2 . TYR A  1 325 ? 32.225  5.382   51.495  1.00 11.26  ? 412  TYR A CE2 1 
ATOM   2487  C  CZ  . TYR A  1 325 ? 32.118  6.538   50.709  1.00 11.41  ? 412  TYR A CZ  1 
ATOM   2488  O  OH  . TYR A  1 325 ? 33.265  7.137   50.261  1.00 11.83  ? 412  TYR A OH  1 
ATOM   2489  N  N   . SER A  1 326 ? 26.230  2.929   50.837  1.00 9.16   ? 413  SER A N   1 
ATOM   2490  C  CA  . SER A  1 326 ? 25.386  1.737   51.006  1.00 9.50   ? 413  SER A CA  1 
ATOM   2491  C  C   . SER A  1 326 ? 26.166  0.511   50.545  1.00 9.47   ? 413  SER A C   1 
ATOM   2492  O  O   . SER A  1 326 ? 27.077  0.609   49.704  1.00 10.14  ? 413  SER A O   1 
ATOM   2493  C  CB  . SER A  1 326 ? 24.057  1.842   50.223  1.00 8.80   ? 413  SER A CB  1 
ATOM   2494  O  OG  . SER A  1 326 ? 24.260  2.077   48.829  1.00 9.39   ? 413  SER A OG  1 
ATOM   2495  N  N   . GLY A  1 327 ? 25.836  -0.645  51.097  1.00 9.52   ? 414  GLY A N   1 
ATOM   2496  C  CA  . GLY A  1 327 ? 26.574  -1.857  50.719  1.00 9.34   ? 414  GLY A CA  1 
ATOM   2497  C  C   . GLY A  1 327 ? 25.810  -3.119  51.006  1.00 10.02  ? 414  GLY A C   1 
ATOM   2498  O  O   . GLY A  1 327 ? 24.766  -3.099  51.682  1.00 10.35  ? 414  GLY A O   1 
ATOM   2499  N  N   . ALA A  1 328 ? 26.357  -4.219  50.497  1.00 9.71   ? 415  ALA A N   1 
ATOM   2500  C  CA  . ALA A  1 328 ? 25.733  -5.523  50.562  1.00 10.27  ? 415  ALA A CA  1 
ATOM   2501  C  C   . ALA A  1 328 ? 26.281  -6.338  51.732  1.00 10.11  ? 415  ALA A C   1 
ATOM   2502  O  O   . ALA A  1 328 ? 27.473  -6.267  52.043  1.00 10.49  ? 415  ALA A O   1 
ATOM   2503  C  CB  . ALA A  1 328 ? 25.972  -6.276  49.248  1.00 9.79   ? 415  ALA A CB  1 
ATOM   2504  N  N   . PHE A  1 329 ? 25.412  -7.146  52.329  1.00 9.23   ? 416  PHE A N   1 
ATOM   2505  C  CA  . PHE A  1 329 ? 25.845  -8.277  53.161  1.00 9.12   ? 416  PHE A CA  1 
ATOM   2506  C  C   . PHE A  1 329 ? 24.772  -9.356  53.145  1.00 9.24   ? 416  PHE A C   1 
ATOM   2507  O  O   . PHE A  1 329 ? 23.631  -9.103  52.749  1.00 9.06   ? 416  PHE A O   1 
ATOM   2508  C  CB  . PHE A  1 329 ? 26.150  -7.830  54.609  1.00 8.64   ? 416  PHE A CB  1 
ATOM   2509  C  CG  . PHE A  1 329 ? 24.930  -7.363  55.384  1.00 8.06   ? 416  PHE A CG  1 
ATOM   2510  C  CD1 . PHE A  1 329 ? 24.357  -6.123  55.135  1.00 7.40   ? 416  PHE A CD1 1 
ATOM   2511  C  CD2 . PHE A  1 329 ? 24.383  -8.161  56.391  1.00 8.58   ? 416  PHE A CD2 1 
ATOM   2512  C  CE1 . PHE A  1 329 ? 23.228  -5.689  55.856  1.00 6.11   ? 416  PHE A CE1 1 
ATOM   2513  C  CE2 . PHE A  1 329 ? 23.256  -7.735  57.103  1.00 7.76   ? 416  PHE A CE2 1 
ATOM   2514  C  CZ  . PHE A  1 329 ? 22.696  -6.496  56.845  1.00 7.88   ? 416  PHE A CZ  1 
ATOM   2515  N  N   . ILE A  1 330 ? 25.144  -10.561 53.558  1.00 9.64   ? 417  ILE A N   1 
ATOM   2516  C  CA  . ILE A  1 330 ? 24.196  -11.666 53.695  1.00 9.82   ? 417  ILE A CA  1 
ATOM   2517  C  C   . ILE A  1 330 ? 24.523  -12.439 54.969  1.00 9.54   ? 417  ILE A C   1 
ATOM   2518  O  O   . ILE A  1 330 ? 25.689  -12.608 55.338  1.00 9.33   ? 417  ILE A O   1 
ATOM   2519  C  CB  . ILE A  1 330 ? 24.210  -12.645 52.461  1.00 10.40  ? 417  ILE A CB  1 
ATOM   2520  C  CG1 . ILE A  1 330 ? 23.796  -11.916 51.176  1.00 10.22  ? 417  ILE A CG1 1 
ATOM   2521  C  CG2 . ILE A  1 330 ? 23.312  -13.909 52.708  1.00 9.65   ? 417  ILE A CG2 1 
ATOM   2522  C  CD1 . ILE A  1 330 ? 23.953  -12.755 49.894  1.00 8.75   ? 417  ILE A CD1 1 
ATOM   2523  N  N   . ASP A  1 331 ? 23.481  -12.899 55.649  1.00 10.88  ? 418  ASP A N   1 
ATOM   2524  C  CA  . ASP A  1 331 ? 23.673  -13.892 56.699  1.00 10.39  ? 418  ASP A CA  1 
ATOM   2525  C  C   . ASP A  1 331 ? 23.801  -15.293 56.056  1.00 10.88  ? 418  ASP A C   1 
ATOM   2526  O  O   . ASP A  1 331 ? 22.812  -16.038 55.946  1.00 9.78   ? 418  ASP A O   1 
ATOM   2527  C  CB  . ASP A  1 331 ? 22.527  -13.838 57.705  1.00 10.98  ? 418  ASP A CB  1 
ATOM   2528  C  CG  . ASP A  1 331 ? 22.687  -14.859 58.823  1.00 11.62  ? 418  ASP A CG  1 
ATOM   2529  O  OD1 . ASP A  1 331 ? 23.779  -15.495 58.931  1.00 11.47  ? 418  ASP A OD1 1 
ATOM   2530  O  OD2 . ASP A  1 331 ? 21.722  -15.010 59.597  1.00 10.96  ? 418  ASP A OD2 1 
ATOM   2531  N  N   . TYR A  1 332 ? 25.030  -15.638 55.654  1.00 10.36  ? 419  TYR A N   1 
ATOM   2532  C  CA  . TYR A  1 332 ? 25.336  -16.922 54.982  1.00 10.89  ? 419  TYR A CA  1 
ATOM   2533  C  C   . TYR A  1 332 ? 25.067  -18.139 55.853  1.00 10.78  ? 419  TYR A C   1 
ATOM   2534  O  O   . TYR A  1 332 ? 25.075  -19.275 55.377  1.00 12.00  ? 419  TYR A O   1 
ATOM   2535  C  CB  . TYR A  1 332 ? 26.795  -16.910 54.482  1.00 10.53  ? 419  TYR A CB  1 
ATOM   2536  C  CG  . TYR A  1 332 ? 27.038  -15.842 53.429  1.00 10.76  ? 419  TYR A CG  1 
ATOM   2537  C  CD1 . TYR A  1 332 ? 26.638  -16.043 52.116  1.00 10.81  ? 419  TYR A CD1 1 
ATOM   2538  C  CD2 . TYR A  1 332 ? 27.655  -14.624 53.756  1.00 9.98   ? 419  TYR A CD2 1 
ATOM   2539  C  CE1 . TYR A  1 332 ? 26.820  -15.067 51.143  1.00 11.30  ? 419  TYR A CE1 1 
ATOM   2540  C  CE2 . TYR A  1 332 ? 27.846  -13.628 52.797  1.00 11.55  ? 419  TYR A CE2 1 
ATOM   2541  C  CZ  . TYR A  1 332 ? 27.415  -13.867 51.473  1.00 10.83  ? 419  TYR A CZ  1 
ATOM   2542  O  OH  . TYR A  1 332 ? 27.582  -12.932 50.480  1.00 11.02  ? 419  TYR A OH  1 
ATOM   2543  N  N   . TRP A  1 333 ? 24.801  -17.905 57.133  1.00 10.76  ? 420  TRP A N   1 
ATOM   2544  C  CA  . TRP A  1 333 ? 24.616  -18.995 58.098  1.00 11.25  ? 420  TRP A CA  1 
ATOM   2545  C  C   . TRP A  1 333 ? 23.145  -19.137 58.526  1.00 12.41  ? 420  TRP A C   1 
ATOM   2546  O  O   . TRP A  1 333 ? 22.822  -19.900 59.454  1.00 12.18  ? 420  TRP A O   1 
ATOM   2547  C  CB  . TRP A  1 333 ? 25.542  -18.778 59.293  1.00 11.46  ? 420  TRP A CB  1 
ATOM   2548  C  CG  . TRP A  1 333 ? 27.007  -18.790 58.870  1.00 12.37  ? 420  TRP A CG  1 
ATOM   2549  C  CD1 . TRP A  1 333 ? 27.839  -19.879 58.812  1.00 12.27  ? 420  TRP A CD1 1 
ATOM   2550  C  CD2 . TRP A  1 333 ? 27.783  -17.665 58.415  1.00 11.33  ? 420  TRP A CD2 1 
ATOM   2551  N  NE1 . TRP A  1 333 ? 29.083  -19.500 58.359  1.00 10.74  ? 420  TRP A NE1 1 
ATOM   2552  C  CE2 . TRP A  1 333 ? 29.077  -18.147 58.109  1.00 12.17  ? 420  TRP A CE2 1 
ATOM   2553  C  CE3 . TRP A  1 333 ? 27.505  -16.299 58.237  1.00 11.49  ? 420  TRP A CE3 1 
ATOM   2554  C  CZ2 . TRP A  1 333 ? 30.101  -17.310 57.633  1.00 13.03  ? 420  TRP A CZ2 1 
ATOM   2555  C  CZ3 . TRP A  1 333 ? 28.525  -15.455 57.769  1.00 10.73  ? 420  TRP A CZ3 1 
ATOM   2556  C  CH2 . TRP A  1 333 ? 29.812  -15.969 57.479  1.00 12.61  ? 420  TRP A CH2 1 
ATOM   2557  N  N   . ALA A  1 334 ? 22.250  -18.415 57.846  1.00 12.55  ? 421  ALA A N   1 
ATOM   2558  C  CA  . ALA A  1 334 ? 20.809  -18.575 58.120  1.00 13.64  ? 421  ALA A CA  1 
ATOM   2559  C  C   . ALA A  1 334 ? 20.341  -20.015 57.829  1.00 14.40  ? 421  ALA A C   1 
ATOM   2560  O  O   . ALA A  1 334 ? 20.959  -20.760 57.057  1.00 14.04  ? 421  ALA A O   1 
ATOM   2561  C  CB  . ALA A  1 334 ? 19.979  -17.566 57.340  1.00 13.09  ? 421  ALA A CB  1 
ATOM   2562  N  N   . ASN A  1 335 ? 19.256  -20.402 58.481  1.00 15.93  ? 422  ASN A N   1 
ATOM   2563  C  CA  . ASN A  1 335 ? 18.656  -21.699 58.272  1.00 18.02  ? 422  ASN A CA  1 
ATOM   2564  C  C   . ASN A  1 335 ? 17.662  -21.583 57.105  1.00 18.82  ? 422  ASN A C   1 
ATOM   2565  O  O   . ASN A  1 335 ? 16.435  -21.510 57.307  1.00 18.97  ? 422  ASN A O   1 
ATOM   2566  C  CB  . ASN A  1 335 ? 17.985  -22.125 59.579  1.00 18.43  ? 422  ASN A CB  1 
ATOM   2567  C  CG  . ASN A  1 335 ? 17.355  -23.498 59.507  1.00 20.59  ? 422  ASN A CG  1 
ATOM   2568  O  OD1 . ASN A  1 335 ? 16.485  -23.824 60.320  1.00 23.84  ? 422  ASN A OD1 1 
ATOM   2569  N  ND2 . ASN A  1 335 ? 17.779  -24.307 58.542  1.00 21.42  ? 422  ASN A ND2 1 
ATOM   2570  N  N   . LYS A  1 336 ? 18.225  -21.530 55.897  1.00 19.40  ? 423  LYS A N   1 
ATOM   2571  C  CA  . LYS A  1 336 ? 17.489  -21.365 54.645  1.00 19.70  ? 423  LYS A CA  1 
ATOM   2572  C  C   . LYS A  1 336 ? 18.211  -22.094 53.526  1.00 19.62  ? 423  LYS A C   1 
ATOM   2573  O  O   . LYS A  1 336 ? 19.425  -22.282 53.578  1.00 20.03  ? 423  LYS A O   1 
ATOM   2574  C  CB  . LYS A  1 336 ? 17.426  -19.888 54.236  1.00 19.99  ? 423  LYS A CB  1 
ATOM   2575  C  CG  . LYS A  1 336 ? 16.562  -19.001 55.079  1.00 21.04  ? 423  LYS A CG  1 
ATOM   2576  C  CD  . LYS A  1 336 ? 16.455  -17.625 54.460  1.00 25.45  ? 423  LYS A CD  1 
ATOM   2577  C  CE  . LYS A  1 336 ? 15.721  -16.689 55.397  1.00 27.19  ? 423  LYS A CE  1 
ATOM   2578  N  NZ  . LYS A  1 336 ? 14.991  -15.653 54.623  1.00 30.80  ? 423  LYS A NZ  1 
ATOM   2579  N  N   . GLU A  1 337 ? 17.467  -22.449 52.486  1.00 18.90  ? 424  GLU A N   1 
ATOM   2580  C  CA  . GLU A  1 337 ? 18.015  -23.158 51.332  1.00 18.92  ? 424  GLU A CA  1 
ATOM   2581  C  C   . GLU A  1 337 ? 18.666  -22.215 50.323  1.00 17.41  ? 424  GLU A C   1 
ATOM   2582  O  O   . GLU A  1 337 ? 19.319  -22.655 49.380  1.00 17.15  ? 424  GLU A O   1 
ATOM   2583  C  CB  . GLU A  1 337 ? 16.914  -23.991 50.660  1.00 19.25  ? 424  GLU A CB  1 
ATOM   2584  C  CG  . GLU A  1 337 ? 16.344  -25.067 51.579  1.00 24.38  ? 424  GLU A CG  1 
ATOM   2585  C  CD  . GLU A  1 337 ? 16.096  -26.410 50.882  1.00 30.15  ? 424  GLU A CD  1 
ATOM   2586  O  OE1 . GLU A  1 337 ? 15.768  -26.435 49.672  1.00 33.12  ? 424  GLU A OE1 1 
ATOM   2587  O  OE2 . GLU A  1 337 ? 16.226  -27.452 51.562  1.00 34.22  ? 424  GLU A OE2 1 
ATOM   2588  N  N   . CYS A  1 338 ? 18.465  -20.917 50.530  1.00 16.02  ? 425  CYS A N   1 
ATOM   2589  C  CA  . CYS A  1 338 ? 18.992  -19.866 49.661  1.00 15.56  ? 425  CYS A CA  1 
ATOM   2590  C  C   . CYS A  1 338 ? 19.618  -18.783 50.536  1.00 14.54  ? 425  CYS A C   1 
ATOM   2591  O  O   . CYS A  1 338 ? 19.305  -18.704 51.724  1.00 14.67  ? 425  CYS A O   1 
ATOM   2592  C  CB  . CYS A  1 338 ? 17.868  -19.264 48.792  1.00 15.60  ? 425  CYS A CB  1 
ATOM   2593  S  SG  . CYS A  1 338 ? 16.413  -18.670 49.725  1.00 17.04  ? 425  CYS A SG  1 
ATOM   2594  N  N   . PHE A  1 339 ? 20.503  -17.982 49.945  1.00 13.18  ? 426  PHE A N   1 
ATOM   2595  C  CA  . PHE A  1 339 ? 21.118  -16.814 50.594  1.00 12.48  ? 426  PHE A CA  1 
ATOM   2596  C  C   . PHE A  1 339 ? 20.232  -15.593 50.390  1.00 11.62  ? 426  PHE A C   1 
ATOM   2597  O  O   . PHE A  1 339 ? 19.988  -15.181 49.260  1.00 11.17  ? 426  PHE A O   1 
ATOM   2598  C  CB  . PHE A  1 339 ? 22.489  -16.500 49.968  1.00 11.76  ? 426  PHE A CB  1 
ATOM   2599  C  CG  . PHE A  1 339 ? 23.542  -17.542 50.219  1.00 11.75  ? 426  PHE A CG  1 
ATOM   2600  C  CD1 . PHE A  1 339 ? 23.594  -18.236 51.430  1.00 10.79  ? 426  PHE A CD1 1 
ATOM   2601  C  CD2 . PHE A  1 339 ? 24.513  -17.806 49.241  1.00 10.34  ? 426  PHE A CD2 1 
ATOM   2602  C  CE1 . PHE A  1 339 ? 24.584  -19.193 51.671  1.00 11.86  ? 426  PHE A CE1 1 
ATOM   2603  C  CE2 . PHE A  1 339 ? 25.513  -18.776 49.466  1.00 12.12  ? 426  PHE A CE2 1 
ATOM   2604  C  CZ  . PHE A  1 339 ? 25.554  -19.468 50.685  1.00 11.03  ? 426  PHE A CZ  1 
ATOM   2605  N  N   . ASN A  1 340 ? 19.757  -15.006 51.478  1.00 10.92  ? 427  ASN A N   1 
ATOM   2606  C  CA  . ASN A  1 340 ? 18.863  -13.867 51.370  1.00 10.37  ? 427  ASN A CA  1 
ATOM   2607  C  C   . ASN A  1 340 ? 19.633  -12.539 51.331  1.00 9.71   ? 427  ASN A C   1 
ATOM   2608  O  O   . ASN A  1 340 ? 20.366  -12.227 52.274  1.00 10.30  ? 427  ASN A O   1 
ATOM   2609  C  CB  . ASN A  1 340 ? 17.865  -13.869 52.536  1.00 9.74   ? 427  ASN A CB  1 
ATOM   2610  C  CG  . ASN A  1 340 ? 16.718  -12.886 52.330  1.00 10.22  ? 427  ASN A CG  1 
ATOM   2611  O  OD1 . ASN A  1 340 ? 16.237  -12.263 53.288  1.00 12.44  ? 427  ASN A OD1 1 
ATOM   2612  N  ND2 . ASN A  1 340 ? 16.257  -12.762 51.102  1.00 7.57   ? 427  ASN A ND2 1 
ATOM   2613  N  N   . PRO A  1 341 ? 19.500  -11.775 50.222  1.00 9.71   ? 428  PRO A N   1 
ATOM   2614  C  CA  . PRO A  1 341 ? 20.159  -10.453 50.170  1.00 9.38   ? 428  PRO A CA  1 
ATOM   2615  C  C   . PRO A  1 341 ? 19.821  -9.532  51.354  1.00 9.62   ? 428  PRO A C   1 
ATOM   2616  O  O   . PRO A  1 341 ? 18.640  -9.394  51.733  1.00 10.39  ? 428  PRO A O   1 
ATOM   2617  C  CB  . PRO A  1 341 ? 19.594  -9.825  48.880  1.00 9.04   ? 428  PRO A CB  1 
ATOM   2618  C  CG  . PRO A  1 341 ? 19.346  -11.034 47.947  1.00 9.49   ? 428  PRO A CG  1 
ATOM   2619  C  CD  . PRO A  1 341 ? 18.793  -12.099 48.961  1.00 9.12   ? 428  PRO A CD  1 
ATOM   2620  N  N   . CYS A  1 342 ? 20.838  -8.876  51.906  1.00 9.78   ? 429  CYS A N   1 
ATOM   2621  C  CA  . CYS A  1 342 ? 20.625  -7.763  52.831  1.00 9.54   ? 429  CYS A CA  1 
ATOM   2622  C  C   . CYS A  1 342 ? 21.464  -6.569  52.382  1.00 9.89   ? 429  CYS A C   1 
ATOM   2623  O  O   . CYS A  1 342 ? 22.440  -6.725  51.643  1.00 9.00   ? 429  CYS A O   1 
ATOM   2624  C  CB  . CYS A  1 342 ? 21.020  -8.103  54.279  1.00 9.72   ? 429  CYS A CB  1 
ATOM   2625  S  SG  . CYS A  1 342 ? 20.249  -9.532  55.001  1.00 10.88  ? 429  CYS A SG  1 
ATOM   2626  N  N   . PHE A  1 343 ? 21.092  -5.386  52.853  1.00 8.93   ? 430  PHE A N   1 
ATOM   2627  C  CA  . PHE A  1 343 ? 21.906  -4.194  52.616  1.00 9.43   ? 430  PHE A CA  1 
ATOM   2628  C  C   . PHE A  1 343 ? 21.803  -3.199  53.787  1.00 9.96   ? 430  PHE A C   1 
ATOM   2629  O  O   . PHE A  1 343 ? 20.919  -3.308  54.635  1.00 10.64  ? 430  PHE A O   1 
ATOM   2630  C  CB  . PHE A  1 343 ? 21.519  -3.538  51.285  1.00 8.48   ? 430  PHE A CB  1 
ATOM   2631  C  CG  . PHE A  1 343 ? 20.156  -2.874  51.294  1.00 9.86   ? 430  PHE A CG  1 
ATOM   2632  C  CD1 . PHE A  1 343 ? 20.033  -1.511  51.602  1.00 8.02   ? 430  PHE A CD1 1 
ATOM   2633  C  CD2 . PHE A  1 343 ? 19.001  -3.612  51.023  1.00 9.92   ? 430  PHE A CD2 1 
ATOM   2634  C  CE1 . PHE A  1 343 ? 18.788  -0.889  51.640  1.00 9.47   ? 430  PHE A CE1 1 
ATOM   2635  C  CE2 . PHE A  1 343 ? 17.741  -2.992  51.027  1.00 9.40   ? 430  PHE A CE2 1 
ATOM   2636  C  CZ  . PHE A  1 343 ? 17.637  -1.624  51.338  1.00 8.24   ? 430  PHE A CZ  1 
ATOM   2637  N  N   . TYR A  1 344 ? 22.711  -2.231  53.822  1.00 9.87   ? 431  TYR A N   1 
ATOM   2638  C  CA  . TYR A  1 344 ? 22.592  -1.126  54.775  1.00 9.49   ? 431  TYR A CA  1 
ATOM   2639  C  C   . TYR A  1 344 ? 22.679  0.182   54.002  1.00 9.82   ? 431  TYR A C   1 
ATOM   2640  O  O   . TYR A  1 344 ? 23.179  0.203   52.854  1.00 9.66   ? 431  TYR A O   1 
ATOM   2641  C  CB  . TYR A  1 344 ? 23.724  -1.190  55.821  1.00 9.28   ? 431  TYR A CB  1 
ATOM   2642  C  CG  . TYR A  1 344 ? 25.070  -0.952  55.174  1.00 10.49  ? 431  TYR A CG  1 
ATOM   2643  C  CD1 . TYR A  1 344 ? 25.794  -2.014  54.638  1.00 8.58   ? 431  TYR A CD1 1 
ATOM   2644  C  CD2 . TYR A  1 344 ? 25.577  0.342   55.030  1.00 9.23   ? 431  TYR A CD2 1 
ATOM   2645  C  CE1 . TYR A  1 344 ? 27.036  -1.802  54.009  1.00 9.52   ? 431  TYR A CE1 1 
ATOM   2646  C  CE2 . TYR A  1 344 ? 26.797  0.575   54.370  1.00 9.90   ? 431  TYR A CE2 1 
ATOM   2647  C  CZ  . TYR A  1 344 ? 27.515  -0.499  53.880  1.00 9.90   ? 431  TYR A CZ  1 
ATOM   2648  O  OH  . TYR A  1 344 ? 28.702  -0.254  53.242  1.00 11.33  ? 431  TYR A OH  1 
ATOM   2649  N  N   . VAL A  1 345 ? 22.199  1.258   54.635  1.00 8.49   ? 432  VAL A N   1 
ATOM   2650  C  CA  . VAL A  1 345 ? 22.406  2.617   54.187  1.00 9.11   ? 432  VAL A CA  1 
ATOM   2651  C  C   . VAL A  1 345 ? 23.029  3.395   55.351  1.00 8.78   ? 432  VAL A C   1 
ATOM   2652  O  O   . VAL A  1 345 ? 22.528  3.351   56.486  1.00 9.75   ? 432  VAL A O   1 
ATOM   2653  C  CB  . VAL A  1 345 ? 21.074  3.330   53.780  1.00 8.63   ? 432  VAL A CB  1 
ATOM   2654  C  CG1 . VAL A  1 345 ? 21.351  4.746   53.168  1.00 7.15   ? 432  VAL A CG1 1 
ATOM   2655  C  CG2 . VAL A  1 345 ? 20.264  2.456   52.823  1.00 8.76   ? 432  VAL A CG2 1 
ATOM   2656  N  N   . GLU A  1 346 ? 24.122  4.079   55.061  1.00 8.71   ? 433  GLU A N   1 
ATOM   2657  C  CA  . GLU A  1 346 ? 24.740  5.019   55.995  1.00 8.60   ? 433  GLU A CA  1 
ATOM   2658  C  C   . GLU A  1 346 ? 23.945  6.323   55.962  1.00 8.65   ? 433  GLU A C   1 
ATOM   2659  O  O   . GLU A  1 346 ? 23.699  6.873   54.894  1.00 8.07   ? 433  GLU A O   1 
ATOM   2660  C  CB  . GLU A  1 346 ? 26.194  5.271   55.564  1.00 9.04   ? 433  GLU A CB  1 
ATOM   2661  C  CG  . GLU A  1 346 ? 26.881  6.382   56.360  1.00 8.90   ? 433  GLU A CG  1 
ATOM   2662  C  CD  . GLU A  1 346 ? 28.204  6.773   55.763  1.00 9.84   ? 433  GLU A CD  1 
ATOM   2663  O  OE1 . GLU A  1 346 ? 29.136  7.037   56.570  1.00 8.26   ? 433  GLU A OE1 1 
ATOM   2664  O  OE2 . GLU A  1 346 ? 28.321  6.760   54.515  1.00 9.22   ? 433  GLU A OE2 1 
ATOM   2665  N  N   . LEU A  1 347 ? 23.531  6.814   57.132  1.00 8.77   ? 434  LEU A N   1 
ATOM   2666  C  CA  . LEU A  1 347 ? 22.702  8.004   57.207  1.00 9.37   ? 434  LEU A CA  1 
ATOM   2667  C  C   . LEU A  1 347 ? 23.599  9.122   57.738  1.00 9.50   ? 434  LEU A C   1 
ATOM   2668  O  O   . LEU A  1 347 ? 23.759  9.279   58.942  1.00 10.51  ? 434  LEU A O   1 
ATOM   2669  C  CB  . LEU A  1 347 ? 21.464  7.744   58.099  1.00 9.41   ? 434  LEU A CB  1 
ATOM   2670  C  CG  . LEU A  1 347 ? 20.619  6.513   57.675  1.00 9.86   ? 434  LEU A CG  1 
ATOM   2671  C  CD1 . LEU A  1 347 ? 19.484  6.243   58.663  1.00 7.94   ? 434  LEU A CD1 1 
ATOM   2672  C  CD2 . LEU A  1 347 ? 20.041  6.689   56.271  1.00 9.66   ? 434  LEU A CD2 1 
ATOM   2673  N  N   . ILE A  1 348 ? 24.212  9.881   56.830  1.00 8.99   ? 435  ILE A N   1 
ATOM   2674  C  CA  . ILE A  1 348 ? 25.202  10.895  57.224  1.00 9.49   ? 435  ILE A CA  1 
ATOM   2675  C  C   . ILE A  1 348 ? 24.526  12.164  57.787  1.00 10.06  ? 435  ILE A C   1 
ATOM   2676  O  O   . ILE A  1 348 ? 23.603  12.736  57.176  1.00 10.33  ? 435  ILE A O   1 
ATOM   2677  C  CB  . ILE A  1 348 ? 26.154  11.279  56.048  1.00 9.12   ? 435  ILE A CB  1 
ATOM   2678  C  CG1 . ILE A  1 348 ? 26.874  10.033  55.524  1.00 7.77   ? 435  ILE A CG1 1 
ATOM   2679  C  CG2 . ILE A  1 348 ? 27.152  12.405  56.467  1.00 9.23   ? 435  ILE A CG2 1 
ATOM   2680  C  CD1 . ILE A  1 348 ? 27.607  10.241  54.171  1.00 10.13  ? 435  ILE A CD1 1 
ATOM   2681  N  N   . ARG A  1 349 ? 24.985  12.579  58.964  1.00 10.41  ? 436  ARG A N   1 
ATOM   2682  C  CA  . ARG A  1 349 ? 24.594  13.874  59.532  1.00 11.13  ? 436  ARG A CA  1 
ATOM   2683  C  C   . ARG A  1 349 ? 25.796  14.803  59.705  1.00 11.56  ? 436  ARG A C   1 
ATOM   2684  O  O   . ARG A  1 349 ? 26.937  14.338  59.846  1.00 11.19  ? 436  ARG A O   1 
ATOM   2685  C  CB  . ARG A  1 349 ? 23.859  13.659  60.865  1.00 11.29  ? 436  ARG A CB  1 
ATOM   2686  C  CG  . ARG A  1 349 ? 22.644  12.714  60.738  1.00 10.36  ? 436  ARG A CG  1 
ATOM   2687  C  CD  . ARG A  1 349 ? 21.583  13.195  59.715  1.00 12.06  ? 436  ARG A CD  1 
ATOM   2688  N  NE  . ARG A  1 349 ? 21.098  14.571  59.956  1.00 11.64  ? 436  ARG A NE  1 
ATOM   2689  C  CZ  . ARG A  1 349 ? 20.012  14.877  60.662  1.00 11.86  ? 436  ARG A CZ  1 
ATOM   2690  N  NH1 . ARG A  1 349 ? 19.302  13.918  61.257  1.00 10.36  ? 436  ARG A NH1 1 
ATOM   2691  N  NH2 . ARG A  1 349 ? 19.643  16.162  60.802  1.00 12.51  ? 436  ARG A NH2 1 
ATOM   2692  N  N   . GLY A  1 350 ? 25.527  16.115  59.702  1.00 9.80   ? 437  GLY A N   1 
ATOM   2693  C  CA  . GLY A  1 350 ? 26.571  17.106  59.907  1.00 11.00  ? 437  GLY A CA  1 
ATOM   2694  C  C   . GLY A  1 350 ? 27.170  17.507  58.579  1.00 10.96  ? 437  GLY A C   1 
ATOM   2695  O  O   . GLY A  1 350 ? 26.485  17.489  57.544  1.00 10.52  ? 437  GLY A O   1 
ATOM   2696  N  N   . ARG A  1 351 ? 28.466  17.821  58.598  1.00 11.79  ? 438  ARG A N   1 
ATOM   2697  C  CA  . ARG A  1 351 ? 29.163  18.368  57.421  1.00 12.28  ? 438  ARG A CA  1 
ATOM   2698  C  C   . ARG A  1 351 ? 29.372  17.377  56.262  1.00 12.51  ? 438  ARG A C   1 
ATOM   2699  O  O   . ARG A  1 351 ? 29.514  16.171  56.500  1.00 13.20  ? 438  ARG A O   1 
ATOM   2700  C  CB  . ARG A  1 351 ? 30.507  18.952  57.864  1.00 12.39  ? 438  ARG A CB  1 
ATOM   2701  C  CG  . ARG A  1 351 ? 30.300  20.173  58.726  1.00 16.58  ? 438  ARG A CG  1 
ATOM   2702  C  CD  . ARG A  1 351 ? 31.589  20.776  59.204  1.00 20.19  ? 438  ARG A CD  1 
ATOM   2703  N  NE  . ARG A  1 351 ? 31.286  22.008  59.920  1.00 26.58  ? 438  ARG A NE  1 
ATOM   2704  C  CZ  . ARG A  1 351 ? 31.246  23.210  59.358  1.00 28.80  ? 438  ARG A CZ  1 
ATOM   2705  N  NH1 . ARG A  1 351 ? 31.528  23.356  58.068  1.00 32.04  ? 438  ARG A NH1 1 
ATOM   2706  N  NH2 . ARG A  1 351 ? 30.944  24.272  60.091  1.00 29.40  ? 438  ARG A NH2 1 
ATOM   2707  N  N   . PRO A  1 352 ? 29.408  17.872  55.005  1.00 13.00  ? 439  PRO A N   1 
ATOM   2708  C  CA  . PRO A  1 352 ? 29.247  19.277  54.571  1.00 13.13  ? 439  PRO A CA  1 
ATOM   2709  C  C   . PRO A  1 352 ? 27.800  19.781  54.397  1.00 13.84  ? 439  PRO A C   1 
ATOM   2710  O  O   . PRO A  1 352 ? 27.590  21.010  54.286  1.00 13.74  ? 439  PRO A O   1 
ATOM   2711  C  CB  . PRO A  1 352 ? 29.927  19.276  53.198  1.00 13.58  ? 439  PRO A CB  1 
ATOM   2712  C  CG  . PRO A  1 352 ? 29.662  17.894  52.651  1.00 13.26  ? 439  PRO A CG  1 
ATOM   2713  C  CD  . PRO A  1 352 ? 29.685  16.974  53.860  1.00 12.62  ? 439  PRO A CD  1 
ATOM   2714  N  N   . LYS A  1 353 ? 26.825  18.877  54.338  1.00 13.42  ? 440  LYS A N   1 
ATOM   2715  C  CA  . LYS A  1 353 ? 25.446  19.284  54.014  1.00 13.95  ? 440  LYS A CA  1 
ATOM   2716  C  C   . LYS A  1 353 ? 24.756  20.055  55.156  1.00 14.25  ? 440  LYS A C   1 
ATOM   2717  O  O   . LYS A  1 353 ? 23.887  20.896  54.911  1.00 13.91  ? 440  LYS A O   1 
ATOM   2718  C  CB  . LYS A  1 353 ? 24.583  18.100  53.539  1.00 14.40  ? 440  LYS A CB  1 
ATOM   2719  C  CG  . LYS A  1 353 ? 25.016  17.477  52.193  1.00 16.62  ? 440  LYS A CG  1 
ATOM   2720  C  CD  . LYS A  1 353 ? 24.699  18.388  50.994  1.00 18.38  ? 440  LYS A CD  1 
ATOM   2721  C  CE  . LYS A  1 353 ? 25.084  17.753  49.664  1.00 18.33  ? 440  LYS A CE  1 
ATOM   2722  N  NZ  . LYS A  1 353 ? 26.550  17.772  49.428  1.00 19.71  ? 440  LYS A NZ  1 
ATOM   2723  N  N   . GLU A  1 354 ? 25.154  19.760  56.393  1.00 13.43  ? 441  GLU A N   1 
ATOM   2724  C  CA  . GLU A  1 354 ? 24.603  20.422  57.565  1.00 13.68  ? 441  GLU A CA  1 
ATOM   2725  C  C   . GLU A  1 354 ? 25.739  21.155  58.269  1.00 14.78  ? 441  GLU A C   1 
ATOM   2726  O  O   . GLU A  1 354 ? 26.403  20.603  59.161  1.00 14.59  ? 441  GLU A O   1 
ATOM   2727  C  CB  . GLU A  1 354 ? 23.903  19.396  58.474  1.00 13.32  ? 441  GLU A CB  1 
ATOM   2728  C  CG  . GLU A  1 354 ? 22.722  18.722  57.756  1.00 13.17  ? 441  GLU A CG  1 
ATOM   2729  C  CD  . GLU A  1 354 ? 22.060  17.641  58.572  1.00 14.19  ? 441  GLU A CD  1 
ATOM   2730  O  OE1 . GLU A  1 354 ? 20.864  17.779  58.889  1.00 14.34  ? 441  GLU A OE1 1 
ATOM   2731  O  OE2 . GLU A  1 354 ? 22.740  16.644  58.883  1.00 14.68  ? 441  GLU A OE2 1 
ATOM   2732  N  N   . SER A  1 355 ? 25.983  22.391  57.825  1.00 14.82  ? 442  SER A N   1 
ATOM   2733  C  CA  . SER A  1 355 ? 27.161  23.154  58.244  1.00 15.99  ? 442  SER A CA  1 
ATOM   2734  C  C   . SER A  1 355 ? 27.003  23.869  59.597  1.00 15.35  ? 442  SER A C   1 
ATOM   2735  O  O   . SER A  1 355 ? 27.947  24.509  60.065  1.00 16.18  ? 442  SER A O   1 
ATOM   2736  C  CB  . SER A  1 355 ? 27.533  24.176  57.146  1.00 16.52  ? 442  SER A CB  1 
ATOM   2737  O  OG  . SER A  1 355 ? 26.548  25.206  57.068  1.00 19.38  ? 442  SER A OG  1 
ATOM   2738  N  N   . SER A  1 356 ? 25.833  23.757  60.226  1.00 14.86  ? 443  SER A N   1 
ATOM   2739  C  CA  . SER A  1 356 ? 25.555  24.438  61.494  1.00 14.83  ? 443  SER A CA  1 
ATOM   2740  C  C   . SER A  1 356 ? 26.196  23.704  62.667  1.00 14.57  ? 443  SER A C   1 
ATOM   2741  O  O   . SER A  1 356 ? 26.165  24.172  63.805  1.00 15.02  ? 443  SER A O   1 
ATOM   2742  C  CB  . SER A  1 356 ? 24.049  24.544  61.728  1.00 14.65  ? 443  SER A CB  1 
ATOM   2743  O  OG  . SER A  1 356 ? 23.475  23.273  61.961  1.00 16.26  ? 443  SER A OG  1 
ATOM   2744  N  N   . VAL A  1 357 ? 26.750  22.531  62.389  1.00 14.19  ? 444  VAL A N   1 
ATOM   2745  C  CA  . VAL A  1 357 ? 27.554  21.806  63.392  1.00 13.73  ? 444  VAL A CA  1 
ATOM   2746  C  C   . VAL A  1 357 ? 28.995  21.671  62.881  1.00 13.57  ? 444  VAL A C   1 
ATOM   2747  O  O   . VAL A  1 357 ? 29.256  21.894  61.688  1.00 14.01  ? 444  VAL A O   1 
ATOM   2748  C  CB  . VAL A  1 357 ? 26.925  20.424  63.768  1.00 13.37  ? 444  VAL A CB  1 
ATOM   2749  C  CG1 . VAL A  1 357 ? 25.555  20.610  64.378  1.00 13.19  ? 444  VAL A CG1 1 
ATOM   2750  C  CG2 . VAL A  1 357 ? 26.812  19.488  62.553  1.00 13.90  ? 444  VAL A CG2 1 
ATOM   2751  N  N   . LEU A  1 358 ? 29.914  21.292  63.772  1.00 12.51  ? 445  LEU A N   1 
ATOM   2752  C  CA  . LEU A  1 358 ? 31.340  21.229  63.471  1.00 12.49  ? 445  LEU A CA  1 
ATOM   2753  C  C   . LEU A  1 358 ? 31.815  19.824  63.052  1.00 12.32  ? 445  LEU A C   1 
ATOM   2754  O  O   . LEU A  1 358 ? 32.993  19.636  62.672  1.00 11.58  ? 445  LEU A O   1 
ATOM   2755  C  CB  . LEU A  1 358 ? 32.127  21.669  64.708  1.00 12.42  ? 445  LEU A CB  1 
ATOM   2756  C  CG  . LEU A  1 358 ? 32.644  23.109  64.897  1.00 15.87  ? 445  LEU A CG  1 
ATOM   2757  C  CD1 . LEU A  1 358 ? 31.960  24.125  64.038  1.00 16.66  ? 445  LEU A CD1 1 
ATOM   2758  C  CD2 . LEU A  1 358 ? 32.649  23.500  66.365  1.00 13.66  ? 445  LEU A CD2 1 
ATOM   2759  N  N   . TRP A  1 359 ? 30.900  18.851  63.144  1.00 11.93  ? 446  TRP A N   1 
ATOM   2760  C  CA  . TRP A  1 359 ? 31.245  17.429  63.000  1.00 10.68  ? 446  TRP A CA  1 
ATOM   2761  C  C   . TRP A  1 359 ? 30.590  16.773  61.788  1.00 10.58  ? 446  TRP A C   1 
ATOM   2762  O  O   . TRP A  1 359 ? 29.709  17.352  61.163  1.00 9.97   ? 446  TRP A O   1 
ATOM   2763  C  CB  . TRP A  1 359 ? 30.870  16.635  64.281  1.00 10.47  ? 446  TRP A CB  1 
ATOM   2764  C  CG  . TRP A  1 359 ? 29.464  16.878  64.807  1.00 9.49   ? 446  TRP A CG  1 
ATOM   2765  C  CD1 . TRP A  1 359 ? 29.106  17.727  65.829  1.00 10.47  ? 446  TRP A CD1 1 
ATOM   2766  C  CD2 . TRP A  1 359 ? 28.248  16.263  64.354  1.00 9.62   ? 446  TRP A CD2 1 
ATOM   2767  N  NE1 . TRP A  1 359 ? 27.728  17.685  66.026  1.00 9.73   ? 446  TRP A NE1 1 
ATOM   2768  C  CE2 . TRP A  1 359 ? 27.187  16.790  65.141  1.00 10.82  ? 446  TRP A CE2 1 
ATOM   2769  C  CE3 . TRP A  1 359 ? 27.948  15.306  63.364  1.00 9.31   ? 446  TRP A CE3 1 
ATOM   2770  C  CZ2 . TRP A  1 359 ? 25.847  16.398  64.961  1.00 10.20  ? 446  TRP A CZ2 1 
ATOM   2771  C  CZ3 . TRP A  1 359 ? 26.614  14.914  63.193  1.00 10.04  ? 446  TRP A CZ3 1 
ATOM   2772  C  CH2 . TRP A  1 359 ? 25.587  15.461  63.984  1.00 10.87  ? 446  TRP A CH2 1 
ATOM   2773  N  N   . THR A  1 360 ? 31.034  15.545  61.486  1.00 10.37  ? 447  THR A N   1 
ATOM   2774  C  CA  . THR A  1 360 ? 30.398  14.664  60.524  1.00 10.41  ? 447  THR A CA  1 
ATOM   2775  C  C   . THR A  1 360 ? 30.308  13.291  61.182  1.00 10.22  ? 447  THR A C   1 
ATOM   2776  O  O   . THR A  1 360 ? 31.292  12.777  61.720  1.00 9.59   ? 447  THR A O   1 
ATOM   2777  C  CB  . THR A  1 360 ? 31.208  14.548  59.212  1.00 11.08  ? 447  THR A CB  1 
ATOM   2778  O  OG1 . THR A  1 360 ? 31.291  15.834  58.579  1.00 9.94   ? 447  THR A OG1 1 
ATOM   2779  C  CG2 . THR A  1 360 ? 30.572  13.509  58.241  1.00 10.43  ? 447  THR A CG2 1 
ATOM   2780  N  N   . SER A  1 361 ? 29.119  12.713  61.161  1.00 10.12  ? 448  SER A N   1 
ATOM   2781  C  CA  . SER A  1 361 ? 28.949  11.342  61.641  1.00 9.54   ? 448  SER A CA  1 
ATOM   2782  C  C   . SER A  1 361 ? 27.821  10.656  60.860  1.00 9.10   ? 448  SER A C   1 
ATOM   2783  O  O   . SER A  1 361 ? 27.403  11.134  59.808  1.00 8.91   ? 448  SER A O   1 
ATOM   2784  C  CB  . SER A  1 361 ? 28.667  11.359  63.159  1.00 9.72   ? 448  SER A CB  1 
ATOM   2785  O  OG  . SER A  1 361 ? 28.950  10.082  63.730  1.00 10.50  ? 448  SER A OG  1 
ATOM   2786  N  N   . ASN A  1 362 ? 27.334  9.529   61.368  1.00 8.56   ? 449  ASN A N   1 
ATOM   2787  C  CA  . ASN A  1 362 ? 26.220  8.823   60.747  1.00 8.47   ? 449  ASN A CA  1 
ATOM   2788  C  C   . ASN A  1 362 ? 25.491  7.921   61.736  1.00 8.58   ? 449  ASN A C   1 
ATOM   2789  O  O   . ASN A  1 362 ? 25.999  7.636   62.842  1.00 9.04   ? 449  ASN A O   1 
ATOM   2790  C  CB  . ASN A  1 362 ? 26.738  7.943   59.609  1.00 8.47   ? 449  ASN A CB  1 
ATOM   2791  C  CG  . ASN A  1 362 ? 27.479  6.719   60.122  1.00 8.82   ? 449  ASN A CG  1 
ATOM   2792  O  OD1 . ASN A  1 362 ? 26.919  5.621   60.189  1.00 11.24  ? 449  ASN A OD1 1 
ATOM   2793  N  ND2 . ASN A  1 362 ? 28.724  6.913   60.516  1.00 7.22   ? 449  ASN A ND2 1 
ATOM   2794  N  N   . SER A  1 363 ? 24.313  7.463   61.324  1.00 7.86   ? 450  SER A N   1 
ATOM   2795  C  CA  . SER A  1 363 ? 23.711  6.279   61.923  1.00 8.04   ? 450  SER A CA  1 
ATOM   2796  C  C   . SER A  1 363 ? 23.518  5.241   60.808  1.00 8.42   ? 450  SER A C   1 
ATOM   2797  O  O   . SER A  1 363 ? 23.931  5.469   59.663  1.00 8.17   ? 450  SER A O   1 
ATOM   2798  C  CB  . SER A  1 363 ? 22.403  6.608   62.638  1.00 7.77   ? 450  SER A CB  1 
ATOM   2799  O  OG  . SER A  1 363 ? 21.406  6.942   61.703  1.00 8.31   ? 450  SER A OG  1 
ATOM   2800  N  N   . ILE A  1 364 ? 22.900  4.116   61.154  1.00 7.80   ? 451  ILE A N   1 
ATOM   2801  C  CA  . ILE A  1 364 ? 22.778  2.957   60.257  1.00 8.48   ? 451  ILE A CA  1 
ATOM   2802  C  C   . ILE A  1 364 ? 21.322  2.468   60.195  1.00 8.96   ? 451  ILE A C   1 
ATOM   2803  O  O   . ILE A  1 364 ? 20.611  2.470   61.217  1.00 8.69   ? 451  ILE A O   1 
ATOM   2804  C  CB  . ILE A  1 364 ? 23.682  1.764   60.760  1.00 7.41   ? 451  ILE A CB  1 
ATOM   2805  C  CG1 . ILE A  1 364 ? 25.162  2.180   60.855  1.00 7.72   ? 451  ILE A CG1 1 
ATOM   2806  C  CG2 . ILE A  1 364 ? 23.487  0.482   59.880  1.00 7.07   ? 451  ILE A CG2 1 
ATOM   2807  C  CD1 . ILE A  1 364 ? 26.032  1.194   61.659  1.00 9.47   ? 451  ILE A CD1 1 
ATOM   2808  N  N   . VAL A  1 365 ? 20.889  2.057   59.000  1.00 9.02   ? 452  VAL A N   1 
ATOM   2809  C  CA  . VAL A  1 365 ? 19.704  1.227   58.847  1.00 9.32   ? 452  VAL A CA  1 
ATOM   2810  C  C   . VAL A  1 365 ? 20.072  0.045   57.941  1.00 9.22   ? 452  VAL A C   1 
ATOM   2811  O  O   . VAL A  1 365 ? 20.883  0.192   57.033  1.00 9.42   ? 452  VAL A O   1 
ATOM   2812  C  CB  . VAL A  1 365 ? 18.466  2.017   58.294  1.00 8.53   ? 452  VAL A CB  1 
ATOM   2813  C  CG1 . VAL A  1 365 ? 18.735  2.579   56.883  1.00 8.77   ? 452  VAL A CG1 1 
ATOM   2814  C  CG2 . VAL A  1 365 ? 17.204  1.121   58.308  1.00 9.94   ? 452  VAL A CG2 1 
ATOM   2815  N  N   . ALA A  1 366 ? 19.483  -1.117  58.212  1.00 9.38   ? 453  ALA A N   1 
ATOM   2816  C  CA  . ALA A  1 366 ? 19.739  -2.328  57.456  1.00 9.27   ? 453  ALA A CA  1 
ATOM   2817  C  C   . ALA A  1 366 ? 18.419  -3.069  57.215  1.00 9.16   ? 453  ALA A C   1 
ATOM   2818  O  O   . ALA A  1 366 ? 17.534  -3.091  58.082  1.00 7.99   ? 453  ALA A O   1 
ATOM   2819  C  CB  . ALA A  1 366 ? 20.760  -3.211  58.180  1.00 9.33   ? 453  ALA A CB  1 
ATOM   2820  N  N   . LEU A  1 367 ? 18.292  -3.627  56.014  1.00 9.05   ? 454  LEU A N   1 
ATOM   2821  C  CA  . LEU A  1 367 ? 17.096  -4.360  55.579  1.00 9.82   ? 454  LEU A CA  1 
ATOM   2822  C  C   . LEU A  1 367 ? 17.514  -5.627  54.845  1.00 10.36  ? 454  LEU A C   1 
ATOM   2823  O  O   . LEU A  1 367 ? 18.643  -5.706  54.327  1.00 10.13  ? 454  LEU A O   1 
ATOM   2824  C  CB  . LEU A  1 367 ? 16.235  -3.477  54.660  1.00 9.61   ? 454  LEU A CB  1 
ATOM   2825  C  CG  . LEU A  1 367 ? 15.578  -2.228  55.279  1.00 10.01  ? 454  LEU A CG  1 
ATOM   2826  C  CD1 . LEU A  1 367 ? 16.471  -0.993  55.210  1.00 9.14   ? 454  LEU A CD1 1 
ATOM   2827  C  CD2 . LEU A  1 367 ? 14.241  -1.926  54.584  1.00 10.14  ? 454  LEU A CD2 1 
ATOM   2828  N  N   . CYS A  1 368 ? 16.629  -6.624  54.828  1.00 9.73   ? 455  CYS A N   1 
ATOM   2829  C  CA  . CYS A  1 368 ? 16.871  -7.870  54.071  1.00 10.74  ? 455  CYS A CA  1 
ATOM   2830  C  C   . CYS A  1 368 ? 15.670  -8.169  53.194  1.00 10.46  ? 455  CYS A C   1 
ATOM   2831  O  O   . CYS A  1 368 ? 14.594  -7.585  53.393  1.00 10.62  ? 455  CYS A O   1 
ATOM   2832  C  CB  . CYS A  1 368 ? 17.169  -9.053  54.993  1.00 10.98  ? 455  CYS A CB  1 
ATOM   2833  S  SG  . CYS A  1 368 ? 18.644  -8.805  56.058  1.00 12.42  ? 455  CYS A SG  1 
ATOM   2834  N  N   . GLY A  1 369 ? 15.855  -9.062  52.225  1.00 10.18  ? 456  GLY A N   1 
ATOM   2835  C  CA  . GLY A  1 369 ? 14.783  -9.435  51.313  1.00 10.89  ? 456  GLY A CA  1 
ATOM   2836  C  C   . GLY A  1 369 ? 13.588  -10.153 51.942  1.00 10.45  ? 456  GLY A C   1 
ATOM   2837  O  O   . GLY A  1 369 ? 13.709  -10.859 52.951  1.00 9.59   ? 456  GLY A O   1 
ATOM   2838  N  N   . SER A  1 370 ? 12.432  -9.943  51.320  1.00 10.57  ? 457  SER A N   1 
ATOM   2839  C  CA  . SER A  1 370 ? 11.250  -10.745 51.583  1.00 11.62  ? 457  SER A CA  1 
ATOM   2840  C  C   . SER A  1 370 ? 10.655  -11.206 50.253  1.00 11.64  ? 457  SER A C   1 
ATOM   2841  O  O   . SER A  1 370 ? 10.725  -10.495 49.261  1.00 11.14  ? 457  SER A O   1 
ATOM   2842  C  CB  . SER A  1 370 ? 10.205  -9.937  52.361  1.00 11.51  ? 457  SER A CB  1 
ATOM   2843  O  OG  . SER A  1 370 ? 9.049   -10.733 52.637  1.00 12.24  ? 457  SER A OG  1 
ATOM   2844  N  N   . LYS A  1 371 ? 10.093  -12.409 50.251  1.00 13.52  ? 458  LYS A N   1 
ATOM   2845  C  CA  . LYS A  1 371 ? 9.284   -12.898 49.134  1.00 15.29  ? 458  LYS A CA  1 
ATOM   2846  C  C   . LYS A  1 371 ? 7.867   -12.319 49.206  1.00 15.35  ? 458  LYS A C   1 
ATOM   2847  O  O   . LYS A  1 371 ? 7.152   -12.301 48.202  1.00 14.99  ? 458  LYS A O   1 
ATOM   2848  C  CB  . LYS A  1 371 ? 9.210   -14.432 49.135  1.00 15.66  ? 458  LYS A CB  1 
ATOM   2849  C  CG  . LYS A  1 371 ? 10.495  -15.164 48.781  1.00 20.14  ? 458  LYS A CG  1 
ATOM   2850  C  CD  . LYS A  1 371 ? 10.159  -16.476 48.035  1.00 25.40  ? 458  LYS A CD  1 
ATOM   2851  C  CE  . LYS A  1 371 ? 10.348  -17.746 48.877  1.00 28.65  ? 458  LYS A CE  1 
ATOM   2852  N  NZ  . LYS A  1 371 ? 9.942   -17.592 50.313  1.00 32.60  ? 458  LYS A NZ  1 
ATOM   2853  N  N   . LYS A  1 372 ? 7.466   -11.856 50.395  1.00 15.73  ? 459  LYS A N   1 
ATOM   2854  C  CA  . LYS A  1 372 ? 6.181   -11.186 50.571  1.00 16.34  ? 459  LYS A CA  1 
ATOM   2855  C  C   . LYS A  1 372 ? 6.191   -9.771  49.961  1.00 16.96  ? 459  LYS A C   1 
ATOM   2856  O  O   . LYS A  1 372 ? 7.243   -9.220  49.607  1.00 16.59  ? 459  LYS A O   1 
ATOM   2857  C  CB  . LYS A  1 372 ? 5.766   -11.134 52.062  1.00 17.01  ? 459  LYS A CB  1 
ATOM   2858  C  CG  . LYS A  1 372 ? 5.910   -12.450 52.853  1.00 18.66  ? 459  LYS A CG  1 
ATOM   2859  C  CD  . LYS A  1 372 ? 4.809   -13.431 52.540  1.00 21.56  ? 459  LYS A CD  1 
ATOM   2860  C  CE  . LYS A  1 372 ? 5.017   -14.781 53.243  1.00 21.60  ? 459  LYS A CE  1 
ATOM   2861  N  NZ  . LYS A  1 372 ? 4.887   -14.728 54.729  1.00 22.53  ? 459  LYS A NZ  1 
ATOM   2862  N  N   . ARG A  1 373 ? 5.000   -9.195  49.834  1.00 17.47  ? 460  ARG A N   1 
ATOM   2863  C  CA  . ARG A  1 373 ? 4.835   -7.809  49.424  1.00 18.17  ? 460  ARG A CA  1 
ATOM   2864  C  C   . ARG A  1 373 ? 4.560   -6.995  50.680  1.00 17.65  ? 460  ARG A C   1 
ATOM   2865  O  O   . ARG A  1 373 ? 3.407   -6.898  51.147  1.00 17.94  ? 460  ARG A O   1 
ATOM   2866  C  CB  . ARG A  1 373 ? 3.672   -7.669  48.435  1.00 19.33  ? 460  ARG A CB  1 
ATOM   2867  C  CG  . ARG A  1 373 ? 4.103   -7.603  46.965  1.00 24.78  ? 460  ARG A CG  1 
ATOM   2868  C  CD  . ARG A  1 373 ? 4.665   -8.929  46.484  1.00 29.29  ? 460  ARG A CD  1 
ATOM   2869  N  NE  . ARG A  1 373 ? 4.987   -8.895  45.060  1.00 35.02  ? 460  ARG A NE  1 
ATOM   2870  C  CZ  . ARG A  1 373 ? 5.304   -9.959  44.320  1.00 36.98  ? 460  ARG A CZ  1 
ATOM   2871  N  NH1 . ARG A  1 373 ? 5.341   -11.178 44.861  1.00 39.43  ? 460  ARG A NH1 1 
ATOM   2872  N  NH2 . ARG A  1 373 ? 5.582   -9.802  43.025  1.00 38.05  ? 460  ARG A NH2 1 
ATOM   2873  N  N   . LEU A  1 374 ? 5.621   -6.440  51.253  1.00 15.53  ? 461  LEU A N   1 
ATOM   2874  C  CA  . LEU A  1 374 ? 5.504   -5.728  52.516  1.00 14.74  ? 461  LEU A CA  1 
ATOM   2875  C  C   . LEU A  1 374 ? 5.361   -4.249  52.257  1.00 14.06  ? 461  LEU A C   1 
ATOM   2876  O  O   . LEU A  1 374 ? 5.975   -3.710  51.333  1.00 14.25  ? 461  LEU A O   1 
ATOM   2877  C  CB  . LEU A  1 374 ? 6.736   -5.969  53.389  1.00 14.01  ? 461  LEU A CB  1 
ATOM   2878  C  CG  . LEU A  1 374 ? 7.054   -7.435  53.676  1.00 13.60  ? 461  LEU A CG  1 
ATOM   2879  C  CD1 . LEU A  1 374 ? 8.336   -7.510  54.481  1.00 14.10  ? 461  LEU A CD1 1 
ATOM   2880  C  CD2 . LEU A  1 374 ? 5.910   -8.146  54.389  1.00 12.74  ? 461  LEU A CD2 1 
ATOM   2881  N  N   . GLY A  1 375 ? 4.542   -3.597  53.070  1.00 14.09  ? 462  GLY A N   1 
ATOM   2882  C  CA  . GLY A  1 375 ? 4.446   -2.147  53.060  1.00 12.96  ? 462  GLY A CA  1 
ATOM   2883  C  C   . GLY A  1 375 ? 5.762   -1.549  53.511  1.00 13.27  ? 462  GLY A C   1 
ATOM   2884  O  O   . GLY A  1 375 ? 6.616   -2.245  54.062  1.00 12.55  ? 462  GLY A O   1 
ATOM   2885  N  N   . SER A  1 376 ? 5.933   -0.252  53.283  1.00 13.33  ? 463  SER A N   1 
ATOM   2886  C  CA  . SER A  1 376 ? 7.200   0.392   53.644  1.00 13.44  ? 463  SER A CA  1 
ATOM   2887  C  C   . SER A  1 376 ? 7.023   1.825   54.129  1.00 12.98  ? 463  SER A C   1 
ATOM   2888  O  O   . SER A  1 376 ? 6.044   2.489   53.790  1.00 12.56  ? 463  SER A O   1 
ATOM   2889  C  CB  . SER A  1 376 ? 8.139   0.379   52.442  1.00 13.53  ? 463  SER A CB  1 
ATOM   2890  O  OG  . SER A  1 376 ? 7.615   1.172   51.388  1.00 15.77  ? 463  SER A OG  1 
ATOM   2891  N  N   . TRP A  1 377 ? 7.974   2.292   54.937  1.00 11.97  ? 464  TRP A N   1 
ATOM   2892  C  CA  . TRP A  1 377 ? 8.120   3.724   55.197  1.00 11.89  ? 464  TRP A CA  1 
ATOM   2893  C  C   . TRP A  1 377 ? 9.598   4.096   55.249  1.00 11.31  ? 464  TRP A C   1 
ATOM   2894  O  O   . TRP A  1 377 ? 10.482  3.223   55.159  1.00 11.74  ? 464  TRP A O   1 
ATOM   2895  C  CB  . TRP A  1 377 ? 7.340   4.181   56.454  1.00 12.35  ? 464  TRP A CB  1 
ATOM   2896  C  CG  . TRP A  1 377 ? 7.813   3.637   57.785  1.00 11.91  ? 464  TRP A CG  1 
ATOM   2897  C  CD1 . TRP A  1 377 ? 8.788   2.690   58.007  1.00 11.94  ? 464  TRP A CD1 1 
ATOM   2898  C  CD2 . TRP A  1 377 ? 7.294   3.991   59.076  1.00 11.85  ? 464  TRP A CD2 1 
ATOM   2899  N  NE1 . TRP A  1 377 ? 8.913   2.456   59.366  1.00 13.00  ? 464  TRP A NE1 1 
ATOM   2900  C  CE2 . TRP A  1 377 ? 8.014   3.237   60.042  1.00 12.49  ? 464  TRP A CE2 1 
ATOM   2901  C  CE3 . TRP A  1 377 ? 6.298   4.882   59.510  1.00 10.87  ? 464  TRP A CE3 1 
ATOM   2902  C  CZ2 . TRP A  1 377 ? 7.750   3.325   61.430  1.00 11.20  ? 464  TRP A CZ2 1 
ATOM   2903  C  CZ3 . TRP A  1 377 ? 6.035   4.977   60.897  1.00 11.91  ? 464  TRP A CZ3 1 
ATOM   2904  C  CH2 . TRP A  1 377 ? 6.772   4.201   61.835  1.00 11.83  ? 464  TRP A CH2 1 
ATOM   2905  N  N   . SER A  1 378 ? 9.849   5.388   55.388  1.00 10.71  ? 465  SER A N   1 
ATOM   2906  C  CA  . SER A  1 378 ? 11.194  5.948   55.387  1.00 11.23  ? 465  SER A CA  1 
ATOM   2907  C  C   . SER A  1 378 ? 11.892  5.700   56.733  1.00 10.38  ? 465  SER A C   1 
ATOM   2908  O  O   . SER A  1 378 ? 11.340  6.000   57.812  1.00 10.45  ? 465  SER A O   1 
ATOM   2909  C  CB  . SER A  1 378 ? 11.111  7.454   55.107  1.00 10.60  ? 465  SER A CB  1 
ATOM   2910  O  OG  . SER A  1 378 ? 12.393  8.062   55.155  1.00 12.39  ? 465  SER A OG  1 
ATOM   2911  N  N   . TRP A  1 379 ? 13.103  5.154   56.645  1.00 10.24  ? 466  TRP A N   1 
ATOM   2912  C  CA  . TRP A  1 379 ? 13.946  4.849   57.819  1.00 9.88   ? 466  TRP A CA  1 
ATOM   2913  C  C   . TRP A  1 379 ? 15.091  5.875   57.927  1.00 9.61   ? 466  TRP A C   1 
ATOM   2914  O  O   . TRP A  1 379 ? 16.263  5.514   58.025  1.00 9.31   ? 466  TRP A O   1 
ATOM   2915  C  CB  . TRP A  1 379 ? 14.508  3.422   57.706  1.00 8.96   ? 466  TRP A CB  1 
ATOM   2916  C  CG  . TRP A  1 379 ? 13.454  2.328   57.722  1.00 9.04   ? 466  TRP A CG  1 
ATOM   2917  C  CD1 . TRP A  1 379 ? 12.944  1.640   56.640  1.00 10.08  ? 466  TRP A CD1 1 
ATOM   2918  C  CD2 . TRP A  1 379 ? 12.798  1.811   58.877  1.00 7.43   ? 466  TRP A CD2 1 
ATOM   2919  N  NE1 . TRP A  1 379 ? 11.996  0.718   57.073  1.00 9.40   ? 466  TRP A NE1 1 
ATOM   2920  C  CE2 . TRP A  1 379 ? 11.893  0.802   58.439  1.00 9.77   ? 466  TRP A CE2 1 
ATOM   2921  C  CE3 . TRP A  1 379 ? 12.883  2.098   60.250  1.00 8.65   ? 466  TRP A CE3 1 
ATOM   2922  C  CZ2 . TRP A  1 379 ? 11.085  0.077   59.333  1.00 8.66   ? 466  TRP A CZ2 1 
ATOM   2923  C  CZ3 . TRP A  1 379 ? 12.081  1.364   61.146  1.00 9.91   ? 466  TRP A CZ3 1 
ATOM   2924  C  CH2 . TRP A  1 379 ? 11.196  0.367   60.679  1.00 9.00   ? 466  TRP A CH2 1 
ATOM   2925  N  N   . HIS A  1 380 ? 14.739  7.159   57.906  1.00 9.10   ? 467  HIS A N   1 
ATOM   2926  C  CA  . HIS A  1 380 ? 15.744  8.221   57.989  1.00 10.06  ? 467  HIS A CA  1 
ATOM   2927  C  C   . HIS A  1 380 ? 16.394  8.266   59.381  1.00 9.71   ? 467  HIS A C   1 
ATOM   2928  O  O   . HIS A  1 380 ? 15.924  7.625   60.335  1.00 9.24   ? 467  HIS A O   1 
ATOM   2929  C  CB  . HIS A  1 380 ? 15.125  9.596   57.656  1.00 9.85   ? 467  HIS A CB  1 
ATOM   2930  C  CG  . HIS A  1 380 ? 13.724  9.759   58.151  1.00 9.59   ? 467  HIS A CG  1 
ATOM   2931  N  ND1 . HIS A  1 380 ? 13.406  10.495  59.275  1.00 13.46  ? 467  HIS A ND1 1 
ATOM   2932  C  CD2 . HIS A  1 380 ? 12.557  9.247   57.696  1.00 10.28  ? 467  HIS A CD2 1 
ATOM   2933  C  CE1 . HIS A  1 380 ? 12.101  10.442  59.479  1.00 11.05  ? 467  HIS A CE1 1 
ATOM   2934  N  NE2 . HIS A  1 380 ? 11.563  9.690   58.535  1.00 14.84  ? 467  HIS A NE2 1 
ATOM   2935  N  N   . ASP A  1 381 ? 17.441  9.064   59.502  1.00 10.22  ? 468  ASP A N   1 
ATOM   2936  C  CA  . ASP A  1 381 ? 18.202  9.127   60.743  1.00 10.56  ? 468  ASP A CA  1 
ATOM   2937  C  C   . ASP A  1 381 ? 17.345  9.491   61.976  1.00 10.68  ? 468  ASP A C   1 
ATOM   2938  O  O   . ASP A  1 381 ? 17.373  8.795   62.995  1.00 10.51  ? 468  ASP A O   1 
ATOM   2939  C  CB  . ASP A  1 381 ? 19.395  10.073  60.597  1.00 10.60  ? 468  ASP A CB  1 
ATOM   2940  C  CG  . ASP A  1 381 ? 20.090  10.297  61.907  1.00 10.46  ? 468  ASP A CG  1 
ATOM   2941  O  OD1 . ASP A  1 381 ? 20.766  9.352   62.410  1.00 9.80   ? 468  ASP A OD1 1 
ATOM   2942  O  OD2 . ASP A  1 381 ? 19.895  11.391  62.470  1.00 10.28  ? 468  ASP A OD2 1 
ATOM   2943  N  N   . GLY A  1 382 ? 16.568  10.561  61.875  1.00 10.63  ? 469  GLY A N   1 
ATOM   2944  C  CA  . GLY A  1 382 ? 15.676  10.915  62.971  1.00 10.84  ? 469  GLY A CA  1 
ATOM   2945  C  C   . GLY A  1 382 ? 16.147  11.955  63.980  1.00 11.15  ? 469  GLY A C   1 
ATOM   2946  O  O   . GLY A  1 382 ? 15.349  12.358  64.826  1.00 10.77  ? 469  GLY A O   1 
ATOM   2947  N  N   . ALA A  1 383 ? 17.413  12.400  63.903  1.00 10.12  ? 470  ALA A N   1 
ATOM   2948  C  CA  . ALA A  1 383 ? 17.900  13.439  64.820  1.00 11.10  ? 470  ALA A CA  1 
ATOM   2949  C  C   . ALA A  1 383 ? 17.507  14.829  64.329  1.00 11.33  ? 470  ALA A C   1 
ATOM   2950  O  O   . ALA A  1 383 ? 17.347  15.038  63.122  1.00 11.37  ? 470  ALA A O   1 
ATOM   2951  C  CB  . ALA A  1 383 ? 19.423  13.351  65.025  1.00 10.38  ? 470  ALA A CB  1 
ATOM   2952  N  N   . GLU A  1 384 ? 17.350  15.760  65.267  1.00 11.34  ? 471  GLU A N   1 
ATOM   2953  C  CA  . GLU A  1 384 ? 17.091  17.166  64.954  1.00 12.62  ? 471  GLU A CA  1 
ATOM   2954  C  C   . GLU A  1 384 ? 18.390  17.945  65.053  1.00 11.88  ? 471  GLU A C   1 
ATOM   2955  O  O   . GLU A  1 384 ? 18.934  18.138  66.141  1.00 11.66  ? 471  GLU A O   1 
ATOM   2956  C  CB  . GLU A  1 384 ? 16.055  17.756  65.918  1.00 12.73  ? 471  GLU A CB  1 
ATOM   2957  C  CG  . GLU A  1 384 ? 14.721  17.076  65.884  1.00 17.79  ? 471  GLU A CG  1 
ATOM   2958  C  CD  . GLU A  1 384 ? 14.056  17.187  64.531  1.00 24.14  ? 471  GLU A CD  1 
ATOM   2959  O  OE1 . GLU A  1 384 ? 13.502  16.158  64.072  1.00 27.97  ? 471  GLU A OE1 1 
ATOM   2960  O  OE2 . GLU A  1 384 ? 14.103  18.291  63.927  1.00 24.66  ? 471  GLU A OE2 1 
ATOM   2961  N  N   . ILE A  1 385 ? 18.899  18.400  63.919  1.00 11.86  ? 472  ILE A N   1 
ATOM   2962  C  CA  . ILE A  1 385 ? 20.194  19.076  63.934  1.00 12.57  ? 472  ILE A CA  1 
ATOM   2963  C  C   . ILE A  1 385 ? 20.173  20.316  64.855  1.00 12.51  ? 472  ILE A C   1 
ATOM   2964  O  O   . ILE A  1 385 ? 21.201  20.693  65.410  1.00 12.31  ? 472  ILE A O   1 
ATOM   2965  C  CB  . ILE A  1 385 ? 20.686  19.423  62.498  1.00 12.74  ? 472  ILE A CB  1 
ATOM   2966  C  CG1 . ILE A  1 385 ? 22.217  19.609  62.469  1.00 13.65  ? 472  ILE A CG1 1 
ATOM   2967  C  CG2 . ILE A  1 385 ? 19.929  20.623  61.913  1.00 13.64  ? 472  ILE A CG2 1 
ATOM   2968  C  CD1 . ILE A  1 385 ? 23.006  18.284  62.552  1.00 13.15  ? 472  ILE A CD1 1 
ATOM   2969  N  N   . ILE A  1 386 ? 18.995  20.922  65.030  1.00 12.81  ? 473  ILE A N   1 
ATOM   2970  C  CA  . ILE A  1 386 ? 18.871  22.130  65.879  1.00 14.07  ? 473  ILE A CA  1 
ATOM   2971  C  C   . ILE A  1 386 ? 19.307  21.833  67.305  1.00 13.12  ? 473  ILE A C   1 
ATOM   2972  O  O   . ILE A  1 386 ? 19.835  22.705  67.995  1.00 12.70  ? 473  ILE A O   1 
ATOM   2973  C  CB  . ILE A  1 386 ? 17.409  22.698  65.911  1.00 14.17  ? 473  ILE A CB  1 
ATOM   2974  C  CG1 . ILE A  1 386 ? 16.910  23.044  64.502  1.00 18.21  ? 473  ILE A CG1 1 
ATOM   2975  C  CG2 . ILE A  1 386 ? 17.319  23.946  66.805  1.00 16.33  ? 473  ILE A CG2 1 
ATOM   2976  C  CD1 . ILE A  1 386 ? 17.467  24.305  63.899  1.00 23.63  ? 473  ILE A CD1 1 
ATOM   2977  N  N   . TYR A  1 387 ? 19.066  20.601  67.746  1.00 12.63  ? 474  TYR A N   1 
ATOM   2978  C  CA  . TYR A  1 387 ? 19.413  20.191  69.099  1.00 12.83  ? 474  TYR A CA  1 
ATOM   2979  C  C   . TYR A  1 387 ? 20.916  20.213  69.345  1.00 12.54  ? 474  TYR A C   1 
ATOM   2980  O  O   . TYR A  1 387 ? 21.335  20.265  70.504  1.00 13.29  ? 474  TYR A O   1 
ATOM   2981  C  CB  . TYR A  1 387 ? 18.851  18.791  69.431  1.00 12.87  ? 474  TYR A CB  1 
ATOM   2982  C  CG  . TYR A  1 387 ? 17.338  18.705  69.569  1.00 12.17  ? 474  TYR A CG  1 
ATOM   2983  C  CD1 . TYR A  1 387 ? 16.708  17.481  69.451  1.00 12.64  ? 474  TYR A CD1 1 
ATOM   2984  C  CD2 . TYR A  1 387 ? 16.543  19.846  69.832  1.00 13.48  ? 474  TYR A CD2 1 
ATOM   2985  C  CE1 . TYR A  1 387 ? 15.328  17.359  69.578  1.00 13.05  ? 474  TYR A CE1 1 
ATOM   2986  C  CE2 . TYR A  1 387 ? 15.137  19.736  69.965  1.00 12.27  ? 474  TYR A CE2 1 
ATOM   2987  C  CZ  . TYR A  1 387 ? 14.549  18.468  69.834  1.00 12.94  ? 474  TYR A CZ  1 
ATOM   2988  O  OH  . TYR A  1 387 ? 13.187  18.287  69.967  1.00 13.53  ? 474  TYR A OH  1 
ATOM   2989  N  N   . PHE A  1 388 ? 21.704  20.178  68.267  1.00 12.15  ? 475  PHE A N   1 
ATOM   2990  C  CA  . PHE A  1 388 ? 23.171  20.142  68.330  1.00 12.71  ? 475  PHE A CA  1 
ATOM   2991  C  C   . PHE A  1 388 ? 23.799  21.531  68.107  1.00 13.68  ? 475  PHE A C   1 
ATOM   2992  O  O   . PHE A  1 388 ? 25.032  21.677  68.104  1.00 13.28  ? 475  PHE A O   1 
ATOM   2993  C  CB  . PHE A  1 388 ? 23.738  19.194  67.268  1.00 11.51  ? 475  PHE A CB  1 
ATOM   2994  C  CG  . PHE A  1 388 ? 23.554  17.745  67.567  1.00 11.55  ? 475  PHE A CG  1 
ATOM   2995  C  CD1 . PHE A  1 388 ? 22.438  17.061  67.079  1.00 10.70  ? 475  PHE A CD1 1 
ATOM   2996  C  CD2 . PHE A  1 388 ? 24.517  17.037  68.291  1.00 11.21  ? 475  PHE A CD2 1 
ATOM   2997  C  CE1 . PHE A  1 388 ? 22.269  15.703  67.321  1.00 10.30  ? 475  PHE A CE1 1 
ATOM   2998  C  CE2 . PHE A  1 388 ? 24.357  15.659  68.524  1.00 12.15  ? 475  PHE A CE2 1 
ATOM   2999  C  CZ  . PHE A  1 388 ? 23.235  15.003  68.037  1.00 10.83  ? 475  PHE A CZ  1 
ATOM   3000  N  N   . GLU A  1 389 ? 22.941  22.535  67.949  1.00 14.65  ? 476  GLU A N   1 
ATOM   3001  C  CA  . GLU A  1 389 ? 23.378  23.899  67.693  1.00 16.28  ? 476  GLU A CA  1 
ATOM   3002  C  C   . GLU A  1 389 ? 23.487  24.647  69.016  1.00 17.27  ? 476  GLU A C   1 
ATOM   3003  O  O   . GLU A  1 389 ? 23.900  25.814  69.073  1.00 18.74  ? 476  GLU A O   1 
ATOM   3004  C  CB  . GLU A  1 389 ? 22.413  24.591  66.721  1.00 16.01  ? 476  GLU A CB  1 
ATOM   3005  C  CG  . GLU A  1 389 ? 22.464  24.007  65.299  1.00 15.50  ? 476  GLU A CG  1 
ATOM   3006  C  CD  . GLU A  1 389 ? 21.383  24.555  64.372  1.00 16.45  ? 476  GLU A CD  1 
ATOM   3007  O  OE1 . GLU A  1 389 ? 20.656  25.493  64.777  1.00 17.82  ? 476  GLU A OE1 1 
ATOM   3008  O  OE2 . GLU A  1 389 ? 21.264  24.051  63.238  1.00 15.18  ? 476  GLU A OE2 1 
ATOM   3009  O  OXT . GLU A  1 389 ? 23.174  24.088  70.077  1.00 17.71  ? 476  GLU A OXT 1 
ATOM   3010  N  N   . ARG B  1 1   ? 17.587  -27.190 76.772  1.00 30.93  ? 88   ARG B N   1 
ATOM   3011  C  CA  . ARG B  1 1   ? 17.829  -28.489 76.089  1.00 30.34  ? 88   ARG B CA  1 
ATOM   3012  C  C   . ARG B  1 1   ? 16.570  -29.121 75.459  1.00 29.25  ? 88   ARG B C   1 
ATOM   3013  O  O   . ARG B  1 1   ? 16.702  -29.968 74.572  1.00 29.77  ? 88   ARG B O   1 
ATOM   3014  C  CB  . ARG B  1 1   ? 18.556  -29.486 77.021  1.00 31.00  ? 88   ARG B CB  1 
ATOM   3015  C  CG  . ARG B  1 1   ? 17.670  -30.210 78.041  1.00 33.16  ? 88   ARG B CG  1 
ATOM   3016  C  CD  . ARG B  1 1   ? 17.631  -29.478 79.378  1.00 38.61  ? 88   ARG B CD  1 
ATOM   3017  N  NE  . ARG B  1 1   ? 16.260  -29.202 79.826  1.00 42.47  ? 88   ARG B NE  1 
ATOM   3018  C  CZ  . ARG B  1 1   ? 15.453  -30.078 80.428  1.00 44.99  ? 88   ARG B CZ  1 
ATOM   3019  N  NH1 . ARG B  1 1   ? 15.853  -31.327 80.672  1.00 45.68  ? 88   ARG B NH1 1 
ATOM   3020  N  NH2 . ARG B  1 1   ? 14.228  -29.700 80.786  1.00 46.04  ? 88   ARG B NH2 1 
ATOM   3021  N  N   . THR B  1 2   ? 15.374  -28.708 75.895  1.00 27.04  ? 89   THR B N   1 
ATOM   3022  C  CA  . THR B  1 2   ? 14.106  -29.325 75.462  1.00 24.87  ? 89   THR B CA  1 
ATOM   3023  C  C   . THR B  1 2   ? 12.972  -28.291 75.272  1.00 22.97  ? 89   THR B C   1 
ATOM   3024  O  O   . THR B  1 2   ? 12.969  -27.253 75.938  1.00 21.80  ? 89   THR B O   1 
ATOM   3025  C  CB  . THR B  1 2   ? 13.650  -30.399 76.497  1.00 25.78  ? 89   THR B CB  1 
ATOM   3026  O  OG1 . THR B  1 2   ? 12.709  -31.298 75.903  1.00 28.21  ? 89   THR B OG1 1 
ATOM   3027  C  CG2 . THR B  1 2   ? 13.023  -29.770 77.747  1.00 24.76  ? 89   THR B CG2 1 
ATOM   3028  N  N   . PHE B  1 3   ? 12.018  -28.569 74.382  1.00 20.61  ? 90   PHE B N   1 
ATOM   3029  C  CA  . PHE B  1 3   ? 10.819  -27.711 74.281  1.00 19.53  ? 90   PHE B CA  1 
ATOM   3030  C  C   . PHE B  1 3   ? 10.034  -27.720 75.591  1.00 18.64  ? 90   PHE B C   1 
ATOM   3031  O  O   . PHE B  1 3   ? 9.742   -28.778 76.145  1.00 18.25  ? 90   PHE B O   1 
ATOM   3032  C  CB  . PHE B  1 3   ? 9.873   -28.147 73.153  1.00 19.85  ? 90   PHE B CB  1 
ATOM   3033  C  CG  . PHE B  1 3   ? 10.348  -27.804 71.776  1.00 19.96  ? 90   PHE B CG  1 
ATOM   3034  C  CD1 . PHE B  1 3   ? 10.300  -28.762 70.759  1.00 20.96  ? 90   PHE B CD1 1 
ATOM   3035  C  CD2 . PHE B  1 3   ? 10.840  -26.533 71.477  1.00 19.23  ? 90   PHE B CD2 1 
ATOM   3036  C  CE1 . PHE B  1 3   ? 10.732  -28.445 69.462  1.00 21.88  ? 90   PHE B CE1 1 
ATOM   3037  C  CE2 . PHE B  1 3   ? 11.276  -26.217 70.201  1.00 19.75  ? 90   PHE B CE2 1 
ATOM   3038  C  CZ  . PHE B  1 3   ? 11.220  -27.166 69.185  1.00 20.17  ? 90   PHE B CZ  1 
ATOM   3039  N  N   . LEU B  1 4   ? 9.691   -26.531 76.079  1.00 17.22  ? 91   LEU B N   1 
ATOM   3040  C  CA  . LEU B  1 4   ? 8.793   -26.388 77.210  1.00 16.44  ? 91   LEU B CA  1 
ATOM   3041  C  C   . LEU B  1 4   ? 7.419   -27.035 76.973  1.00 17.05  ? 91   LEU B C   1 
ATOM   3042  O  O   . LEU B  1 4   ? 6.781   -26.806 75.933  1.00 16.96  ? 91   LEU B O   1 
ATOM   3043  C  CB  . LEU B  1 4   ? 8.601   -24.894 77.514  1.00 15.92  ? 91   LEU B CB  1 
ATOM   3044  C  CG  . LEU B  1 4   ? 7.547   -24.542 78.578  1.00 15.70  ? 91   LEU B CG  1 
ATOM   3045  C  CD1 . LEU B  1 4   ? 7.964   -25.085 79.948  1.00 14.22  ? 91   LEU B CD1 1 
ATOM   3046  C  CD2 . LEU B  1 4   ? 7.347   -23.017 78.591  1.00 14.92  ? 91   LEU B CD2 1 
ATOM   3047  N  N   . ASN B  1 5   ? 6.959   -27.813 77.951  1.00 17.27  ? 92   ASN B N   1 
ATOM   3048  C  CA  . ASN B  1 5   ? 5.593   -28.342 77.945  1.00 18.03  ? 92   ASN B CA  1 
ATOM   3049  C  C   . ASN B  1 5   ? 4.814   -27.732 79.104  1.00 18.03  ? 92   ASN B C   1 
ATOM   3050  O  O   . ASN B  1 5   ? 5.332   -27.640 80.216  1.00 17.77  ? 92   ASN B O   1 
ATOM   3051  C  CB  . ASN B  1 5   ? 5.572   -29.875 78.087  1.00 18.71  ? 92   ASN B CB  1 
ATOM   3052  C  CG  . ASN B  1 5   ? 6.281   -30.600 76.945  1.00 21.62  ? 92   ASN B CG  1 
ATOM   3053  O  OD1 . ASN B  1 5   ? 6.507   -30.051 75.865  1.00 23.16  ? 92   ASN B OD1 1 
ATOM   3054  N  ND2 . ASN B  1 5   ? 6.631   -31.868 77.188  1.00 25.96  ? 92   ASN B ND2 1 
ATOM   3055  N  N   . LEU B  1 6   ? 3.569   -27.346 78.848  1.00 17.93  ? 93   LEU B N   1 
ATOM   3056  C  CA  . LEU B  1 6   ? 2.751   -26.616 79.841  1.00 19.12  ? 93   LEU B CA  1 
ATOM   3057  C  C   . LEU B  1 6   ? 2.032   -27.557 80.799  1.00 19.93  ? 93   LEU B C   1 
ATOM   3058  O  O   . LEU B  1 6   ? 0.862   -27.377 81.112  1.00 20.86  ? 93   LEU B O   1 
ATOM   3059  C  CB  . LEU B  1 6   ? 1.763   -25.677 79.139  1.00 18.13  ? 93   LEU B CB  1 
ATOM   3060  C  CG  . LEU B  1 6   ? 2.407   -24.574 78.281  1.00 18.19  ? 93   LEU B CG  1 
ATOM   3061  C  CD1 . LEU B  1 6   ? 1.348   -23.737 77.605  1.00 15.92  ? 93   LEU B CD1 1 
ATOM   3062  C  CD2 . LEU B  1 6   ? 3.373   -23.691 79.089  1.00 15.74  ? 93   LEU B CD2 1 
ATOM   3063  N  N   . THR B  1 7   ? 2.758   -28.552 81.281  1.00 21.59  ? 94   THR B N   1 
ATOM   3064  C  CA  . THR B  1 7   ? 2.145   -29.669 81.996  1.00 23.00  ? 94   THR B CA  1 
ATOM   3065  C  C   . THR B  1 7   ? 1.667   -29.316 83.409  1.00 22.34  ? 94   THR B C   1 
ATOM   3066  O  O   . THR B  1 7   ? 0.637   -29.842 83.880  1.00 23.62  ? 94   THR B O   1 
ATOM   3067  C  CB  . THR B  1 7   ? 3.097   -30.881 82.025  1.00 23.51  ? 94   THR B CB  1 
ATOM   3068  O  OG1 . THR B  1 7   ? 4.388   -30.464 82.504  1.00 26.42  ? 94   THR B OG1 1 
ATOM   3069  C  CG2 . THR B  1 7   ? 3.249   -31.464 80.626  1.00 24.90  ? 94   THR B CG2 1 
ATOM   3070  N  N   . LYS B  1 8   ? 2.389   -28.413 84.067  1.00 20.73  ? 95   LYS B N   1 
ATOM   3071  C  CA  . LYS B  1 8   ? 2.184   -28.135 85.492  1.00 18.90  ? 95   LYS B CA  1 
ATOM   3072  C  C   . LYS B  1 8   ? 0.921   -27.292 85.737  1.00 17.83  ? 95   LYS B C   1 
ATOM   3073  O  O   . LYS B  1 8   ? 0.510   -26.526 84.851  1.00 16.73  ? 95   LYS B O   1 
ATOM   3074  C  CB  . LYS B  1 8   ? 3.419   -27.453 86.081  1.00 19.22  ? 95   LYS B CB  1 
ATOM   3075  C  CG  . LYS B  1 8   ? 4.680   -28.294 85.995  1.00 18.48  ? 95   LYS B CG  1 
ATOM   3076  C  CD  . LYS B  1 8   ? 5.864   -27.615 86.646  1.00 16.58  ? 95   LYS B CD  1 
ATOM   3077  C  CE  . LYS B  1 8   ? 7.079   -28.517 86.523  1.00 15.78  ? 95   LYS B CE  1 
ATOM   3078  N  NZ  . LYS B  1 8   ? 8.362   -27.858 86.800  1.00 16.35  ? 95   LYS B NZ  1 
ATOM   3079  N  N   . PRO B  1 9   ? 0.289   -27.449 86.928  1.00 17.28  ? 96   PRO B N   1 
ATOM   3080  C  CA  . PRO B  1 9   ? -0.839  -26.583 87.294  1.00 16.61  ? 96   PRO B CA  1 
ATOM   3081  C  C   . PRO B  1 9   ? -0.342  -25.220 87.817  1.00 16.51  ? 96   PRO B C   1 
ATOM   3082  O  O   . PRO B  1 9   ? 0.839   -25.093 88.159  1.00 15.78  ? 96   PRO B O   1 
ATOM   3083  C  CB  . PRO B  1 9   ? -1.511  -27.357 88.436  1.00 16.30  ? 96   PRO B CB  1 
ATOM   3084  C  CG  . PRO B  1 9   ? -0.368  -28.070 89.105  1.00 17.57  ? 96   PRO B CG  1 
ATOM   3085  C  CD  . PRO B  1 9   ? 0.615   -28.416 88.003  1.00 17.11  ? 96   PRO B CD  1 
ATOM   3086  N  N   . LEU B  1 10  ? -1.226  -24.224 87.908  1.00 16.07  ? 97   LEU B N   1 
ATOM   3087  C  CA  . LEU B  1 10  ? -0.863  -22.961 88.585  1.00 15.89  ? 97   LEU B CA  1 
ATOM   3088  C  C   . LEU B  1 10  ? -0.670  -23.176 90.094  1.00 15.93  ? 97   LEU B C   1 
ATOM   3089  O  O   . LEU B  1 10  ? -1.435  -23.917 90.731  1.00 15.85  ? 97   LEU B O   1 
ATOM   3090  C  CB  . LEU B  1 10  ? -1.925  -21.857 88.382  1.00 15.92  ? 97   LEU B CB  1 
ATOM   3091  C  CG  . LEU B  1 10  ? -2.069  -20.967 87.150  1.00 17.09  ? 97   LEU B CG  1 
ATOM   3092  C  CD1 . LEU B  1 10  ? -3.077  -19.826 87.433  1.00 13.14  ? 97   LEU B CD1 1 
ATOM   3093  C  CD2 . LEU B  1 10  ? -0.733  -20.426 86.632  1.00 12.20  ? 97   LEU B CD2 1 
ATOM   3094  N  N   . CYS B  1 11  ? 0.338   -22.525 90.668  1.00 15.35  ? 98   CYS B N   1 
ATOM   3095  C  CA  . CYS B  1 11  ? 0.521   -22.531 92.124  1.00 14.66  ? 98   CYS B CA  1 
ATOM   3096  C  C   . CYS B  1 11  ? -0.612  -21.806 92.802  1.00 13.97  ? 98   CYS B C   1 
ATOM   3097  O  O   . CYS B  1 11  ? -1.158  -20.861 92.244  1.00 12.89  ? 98   CYS B O   1 
ATOM   3098  C  CB  . CYS B  1 11  ? 1.798   -21.804 92.512  1.00 14.54  ? 98   CYS B CB  1 
ATOM   3099  S  SG  . CYS B  1 11  ? 3.320   -22.486 91.833  1.00 14.96  ? 98   CYS B SG  1 
ATOM   3100  N  N   . GLU B  1 12  ? -0.918  -22.220 94.030  1.00 14.07  ? 99   GLU B N   1 
ATOM   3101  C  CA  . GLU B  1 12  ? -1.822  -21.474 94.906  1.00 14.20  ? 99   GLU B CA  1 
ATOM   3102  C  C   . GLU B  1 12  ? -1.231  -20.082 95.223  1.00 13.15  ? 99   GLU B C   1 
ATOM   3103  O  O   . GLU B  1 12  ? -0.042  -19.950 95.554  1.00 12.91  ? 99   GLU B O   1 
ATOM   3104  C  CB  . GLU B  1 12  ? -2.063  -22.251 96.203  1.00 13.88  ? 99   GLU B CB  1 
ATOM   3105  C  CG  . GLU B  1 12  ? -2.857  -21.474 97.276  1.00 15.43  ? 99   GLU B CG  1 
ATOM   3106  C  CD  . GLU B  1 12  ? -3.071  -22.274 98.557  1.00 16.70  ? 99   GLU B CD  1 
ATOM   3107  O  OE1 . GLU B  1 12  ? -3.328  -21.658 99.612  1.00 17.37  ? 99   GLU B OE1 1 
ATOM   3108  O  OE2 . GLU B  1 12  ? -2.989  -23.525 98.503  1.00 22.59  ? 99   GLU B OE2 1 
ATOM   3109  N  N   . VAL B  1 13  ? -2.073  -19.056 95.123  1.00 12.20  ? 100  VAL B N   1 
ATOM   3110  C  CA  . VAL B  1 13  ? -1.654  -17.672 95.398  1.00 11.61  ? 100  VAL B CA  1 
ATOM   3111  C  C   . VAL B  1 13  ? -2.560  -16.999 96.436  1.00 12.08  ? 100  VAL B C   1 
ATOM   3112  O  O   . VAL B  1 13  ? -3.775  -16.851 96.227  1.00 11.66  ? 100  VAL B O   1 
ATOM   3113  C  CB  . VAL B  1 13  ? -1.577  -16.807 94.102  1.00 12.09  ? 100  VAL B CB  1 
ATOM   3114  C  CG1 . VAL B  1 13  ? -1.190  -15.366 94.439  1.00 10.81  ? 100  VAL B CG1 1 
ATOM   3115  C  CG2 . VAL B  1 13  ? -0.579  -17.421 93.074  1.00 11.06  ? 100  VAL B CG2 1 
ATOM   3116  N  N   . ASN B  1 14  ? -1.944  -16.561 97.537  1.00 11.49  ? 101  ASN B N   1 
ATOM   3117  C  CA  . ASN B  1 14  ? -2.634  -15.859 98.608  1.00 11.36  ? 101  ASN B CA  1 
ATOM   3118  C  C   . ASN B  1 14  ? -2.208  -14.395 98.806  1.00 11.11  ? 101  ASN B C   1 
ATOM   3119  O  O   . ASN B  1 14  ? -2.959  -13.606 99.372  1.00 10.00  ? 101  ASN B O   1 
ATOM   3120  C  CB  . ASN B  1 14  ? -2.521  -16.682 99.903  1.00 11.37  ? 101  ASN B CB  1 
ATOM   3121  C  CG  . ASN B  1 14  ? -3.213  -18.023 99.771  1.00 12.57  ? 101  ASN B CG  1 
ATOM   3122  O  OD1 . ASN B  1 14  ? -4.337  -18.088 99.277  1.00 15.28  ? 101  ASN B OD1 1 
ATOM   3123  N  ND2 . ASN B  1 14  ? -2.543  -19.085 100.158 1.00 13.92  ? 101  ASN B ND2 1 
ATOM   3124  N  N   . SER B  1 15  ? -1.011  -14.041 98.329  1.00 10.35  ? 102  SER B N   1 
ATOM   3125  C  CA  . SER B  1 15  ? -0.511  -12.648 98.336  1.00 10.84  ? 102  SER B CA  1 
ATOM   3126  C  C   . SER B  1 15  ? 0.599   -12.556 97.279  1.00 10.48  ? 102  SER B C   1 
ATOM   3127  O  O   . SER B  1 15  ? 0.900   -13.551 96.615  1.00 10.13  ? 102  SER B O   1 
ATOM   3128  C  CB  . SER B  1 15  ? -0.009  -12.191 99.718  1.00 10.70  ? 102  SER B CB  1 
ATOM   3129  O  OG  . SER B  1 15  ? 1.128   -12.951 100.130 1.00 13.62  ? 102  SER B OG  1 
ATOM   3130  N  N   . TRP B  1 16  ? 1.176   -11.370 97.101  1.00 9.45   ? 103  TRP B N   1 
ATOM   3131  C  CA  . TRP B  1 16  ? 2.157   -11.157 96.024  1.00 9.66   ? 103  TRP B CA  1 
ATOM   3132  C  C   . TRP B  1 16  ? 3.466   -10.654 96.628  1.00 10.01  ? 103  TRP B C   1 
ATOM   3133  O  O   . TRP B  1 16  ? 3.454   -9.714  97.429  1.00 9.64   ? 103  TRP B O   1 
ATOM   3134  C  CB  . TRP B  1 16  ? 1.608   -10.161 94.986  1.00 9.54   ? 103  TRP B CB  1 
ATOM   3135  C  CG  . TRP B  1 16  ? 0.343   -10.684 94.358  1.00 10.05  ? 103  TRP B CG  1 
ATOM   3136  C  CD1 . TRP B  1 16  ? -0.931  -10.498 94.799  1.00 10.03  ? 103  TRP B CD1 1 
ATOM   3137  C  CD2 . TRP B  1 16  ? 0.256   -11.554 93.213  1.00 9.93   ? 103  TRP B CD2 1 
ATOM   3138  N  NE1 . TRP B  1 16  ? -1.829  -11.193 93.977  1.00 10.47  ? 103  TRP B NE1 1 
ATOM   3139  C  CE2 . TRP B  1 16  ? -1.118  -11.841 93.000  1.00 9.22   ? 103  TRP B CE2 1 
ATOM   3140  C  CE3 . TRP B  1 16  ? 1.208   -12.107 92.338  1.00 9.54   ? 103  TRP B CE3 1 
ATOM   3141  C  CZ2 . TRP B  1 16  ? -1.567  -12.656 91.941  1.00 8.72   ? 103  TRP B CZ2 1 
ATOM   3142  C  CZ3 . TRP B  1 16  ? 0.763   -12.907 91.275  1.00 10.71  ? 103  TRP B CZ3 1 
ATOM   3143  C  CH2 . TRP B  1 16  ? -0.617  -13.164 91.080  1.00 10.58  ? 103  TRP B CH2 1 
ATOM   3144  N  N   . HIS B  1 17  ? 4.587   -11.281 96.260  1.00 9.50   ? 104  HIS B N   1 
ATOM   3145  C  CA  . HIS B  1 17  ? 5.896   -10.807 96.742  1.00 9.04   ? 104  HIS B CA  1 
ATOM   3146  C  C   . HIS B  1 17  ? 6.644   -10.019 95.657  1.00 9.46   ? 104  HIS B C   1 
ATOM   3147  O  O   . HIS B  1 17  ? 6.471   -10.290 94.470  1.00 8.92   ? 104  HIS B O   1 
ATOM   3148  C  CB  . HIS B  1 17  ? 6.768   -11.976 97.230  1.00 9.26   ? 104  HIS B CB  1 
ATOM   3149  C  CG  . HIS B  1 17  ? 7.370   -12.799 96.129  1.00 9.68   ? 104  HIS B CG  1 
ATOM   3150  N  ND1 . HIS B  1 17  ? 8.506   -12.409 95.447  1.00 9.17   ? 104  HIS B ND1 1 
ATOM   3151  C  CD2 . HIS B  1 17  ? 7.020   -14.006 95.621  1.00 10.72  ? 104  HIS B CD2 1 
ATOM   3152  C  CE1 . HIS B  1 17  ? 8.813   -13.334 94.550  1.00 11.69  ? 104  HIS B CE1 1 
ATOM   3153  N  NE2 . HIS B  1 17  ? 7.935   -14.318 94.645  1.00 11.63  ? 104  HIS B NE2 1 
ATOM   3154  N  N   . ILE B  1 18  ? 7.471   -9.055  96.063  1.00 9.38   ? 105  ILE B N   1 
ATOM   3155  C  CA  . ILE B  1 18  ? 8.268   -8.264  95.108  1.00 9.70   ? 105  ILE B CA  1 
ATOM   3156  C  C   . ILE B  1 18  ? 9.294   -9.170  94.373  1.00 9.88   ? 105  ILE B C   1 
ATOM   3157  O  O   . ILE B  1 18  ? 10.002  -9.971  95.015  1.00 9.97   ? 105  ILE B O   1 
ATOM   3158  C  CB  . ILE B  1 18  ? 8.963   -7.048  95.805  1.00 9.24   ? 105  ILE B CB  1 
ATOM   3159  C  CG1 . ILE B  1 18  ? 9.599   -6.076  94.786  1.00 9.47   ? 105  ILE B CG1 1 
ATOM   3160  C  CG2 . ILE B  1 18  ? 9.986   -7.518  96.844  1.00 9.01   ? 105  ILE B CG2 1 
ATOM   3161  C  CD1 . ILE B  1 18  ? 8.607   -5.448  93.785  1.00 7.01   ? 105  ILE B CD1 1 
ATOM   3162  N  N   . LEU B  1 19  ? 9.340   -9.062  93.039  1.00 9.28   ? 106  LEU B N   1 
ATOM   3163  C  CA  . LEU B  1 19  ? 10.327  -9.795  92.212  1.00 9.24   ? 106  LEU B CA  1 
ATOM   3164  C  C   . LEU B  1 19  ? 11.429  -8.857  91.720  1.00 9.45   ? 106  LEU B C   1 
ATOM   3165  O  O   . LEU B  1 19  ? 12.624  -9.131  91.897  1.00 9.34   ? 106  LEU B O   1 
ATOM   3166  C  CB  . LEU B  1 19  ? 9.661   -10.476 90.999  1.00 8.76   ? 106  LEU B CB  1 
ATOM   3167  C  CG  . LEU B  1 19  ? 10.589  -11.300 90.086  1.00 8.62   ? 106  LEU B CG  1 
ATOM   3168  C  CD1 . LEU B  1 19  ? 10.922  -12.632 90.760  1.00 6.04   ? 106  LEU B CD1 1 
ATOM   3169  C  CD2 . LEU B  1 19  ? 9.954   -11.549 88.721  1.00 9.41   ? 106  LEU B CD2 1 
ATOM   3170  N  N   . SER B  1 20  ? 11.028  -7.752  91.098  1.00 9.16   ? 107  SER B N   1 
ATOM   3171  C  CA  . SER B  1 20  ? 11.999  -6.811  90.558  1.00 9.25   ? 107  SER B CA  1 
ATOM   3172  C  C   . SER B  1 20  ? 11.410  -5.396  90.441  1.00 8.75   ? 107  SER B C   1 
ATOM   3173  O  O   . SER B  1 20  ? 10.187  -5.208  90.400  1.00 8.63   ? 107  SER B O   1 
ATOM   3174  C  CB  . SER B  1 20  ? 12.514  -7.279  89.187  1.00 8.87   ? 107  SER B CB  1 
ATOM   3175  O  OG  . SER B  1 20  ? 13.665  -6.541  88.828  1.00 10.01  ? 107  SER B OG  1 
ATOM   3176  N  N   . LYS B  1 21  ? 12.301  -4.418  90.408  1.00 8.29   ? 108  LYS B N   1 
ATOM   3177  C  CA  . LYS B  1 21  ? 11.928  -3.007  90.179  1.00 8.58   ? 108  LYS B CA  1 
ATOM   3178  C  C   . LYS B  1 21  ? 13.148  -2.322  89.634  1.00 8.46   ? 108  LYS B C   1 
ATOM   3179  O  O   . LYS B  1 21  ? 14.230  -2.459  90.219  1.00 10.05  ? 108  LYS B O   1 
ATOM   3180  C  CB  . LYS B  1 21  ? 11.544  -2.317  91.489  1.00 8.34   ? 108  LYS B CB  1 
ATOM   3181  C  CG  . LYS B  1 21  ? 10.862  -0.955  91.283  1.00 8.46   ? 108  LYS B CG  1 
ATOM   3182  C  CD  . LYS B  1 21  ? 10.579  -0.298  92.644  1.00 8.96   ? 108  LYS B CD  1 
ATOM   3183  C  CE  . LYS B  1 21  ? 9.646   0.917   92.577  1.00 8.85   ? 108  LYS B CE  1 
ATOM   3184  N  NZ  . LYS B  1 21  ? 10.205  2.056   91.805  1.00 9.29   ? 108  LYS B NZ  1 
ATOM   3185  N  N   . ASP B  1 22  ? 13.000  -1.600  88.532  1.00 8.17   ? 109  ASP B N   1 
ATOM   3186  C  CA  . ASP B  1 22  ? 14.191  -1.038  87.876  1.00 8.63   ? 109  ASP B CA  1 
ATOM   3187  C  C   . ASP B  1 22  ? 14.460  0.433   88.196  1.00 8.70   ? 109  ASP B C   1 
ATOM   3188  O  O   . ASP B  1 22  ? 15.578  0.909   87.968  1.00 8.97   ? 109  ASP B O   1 
ATOM   3189  C  CB  . ASP B  1 22  ? 14.214  -1.305  86.364  1.00 8.68   ? 109  ASP B CB  1 
ATOM   3190  C  CG  . ASP B  1 22  ? 13.191  -0.477  85.578  1.00 9.62   ? 109  ASP B CG  1 
ATOM   3191  O  OD1 . ASP B  1 22  ? 12.304  0.194   86.171  1.00 8.48   ? 109  ASP B OD1 1 
ATOM   3192  O  OD2 . ASP B  1 22  ? 13.299  -0.510  84.327  1.00 9.72   ? 109  ASP B OD2 1 
ATOM   3193  N  N   . ASN B  1 23  ? 13.455  1.136   88.724  1.00 8.48   ? 110  ASN B N   1 
ATOM   3194  C  CA  . ASN B  1 23  ? 13.646  2.542   89.136  1.00 8.36   ? 110  ASN B CA  1 
ATOM   3195  C  C   . ASN B  1 23  ? 14.243  3.382   87.991  1.00 8.28   ? 110  ASN B C   1 
ATOM   3196  O  O   . ASN B  1 23  ? 15.097  4.260   88.205  1.00 8.18   ? 110  ASN B O   1 
ATOM   3197  C  CB  . ASN B  1 23  ? 14.541  2.611   90.402  1.00 8.38   ? 110  ASN B CB  1 
ATOM   3198  C  CG  . ASN B  1 23  ? 13.904  1.941   91.596  1.00 9.14   ? 110  ASN B CG  1 
ATOM   3199  O  OD1 . ASN B  1 23  ? 12.877  2.399   92.086  1.00 10.80  ? 110  ASN B OD1 1 
ATOM   3200  N  ND2 . ASN B  1 23  ? 14.489  0.816   92.043  1.00 8.42   ? 110  ASN B ND2 1 
ATOM   3201  N  N   . ALA B  1 24  ? 13.782  3.110   86.768  1.00 8.26   ? 111  ALA B N   1 
ATOM   3202  C  CA  . ALA B  1 24  ? 14.427  3.679   85.577  1.00 8.42   ? 111  ALA B CA  1 
ATOM   3203  C  C   . ALA B  1 24  ? 14.396  5.218   85.514  1.00 8.11   ? 111  ALA B C   1 
ATOM   3204  O  O   . ALA B  1 24  ? 15.365  5.835   85.054  1.00 8.29   ? 111  ALA B O   1 
ATOM   3205  C  CB  . ALA B  1 24  ? 13.854  3.074   84.276  1.00 7.86   ? 111  ALA B CB  1 
ATOM   3206  N  N   . ILE B  1 25  ? 13.283  5.814   85.951  1.00 8.02   ? 112  ILE B N   1 
ATOM   3207  C  CA  . ILE B  1 25  ? 13.095  7.281   85.856  1.00 8.03   ? 112  ILE B CA  1 
ATOM   3208  C  C   . ILE B  1 25  ? 13.971  7.992   86.881  1.00 7.74   ? 112  ILE B C   1 
ATOM   3209  O  O   . ILE B  1 25  ? 14.635  8.963   86.552  1.00 7.77   ? 112  ILE B O   1 
ATOM   3210  C  CB  . ILE B  1 25  ? 11.625  7.700   86.026  1.00 7.58   ? 112  ILE B CB  1 
ATOM   3211  C  CG1 . ILE B  1 25  ? 10.725  6.917   85.042  1.00 8.60   ? 112  ILE B CG1 1 
ATOM   3212  C  CG2 . ILE B  1 25  ? 11.452  9.229   85.852  1.00 8.07   ? 112  ILE B CG2 1 
ATOM   3213  C  CD1 . ILE B  1 25  ? 11.097  7.093   83.557  1.00 9.74   ? 112  ILE B CD1 1 
ATOM   3214  N  N   . ARG B  1 26  ? 13.975  7.495   88.115  1.00 7.64   ? 113  ARG B N   1 
ATOM   3215  C  CA  . ARG B  1 26  ? 14.884  8.014   89.153  1.00 7.80   ? 113  ARG B CA  1 
ATOM   3216  C  C   . ARG B  1 26  ? 16.351  8.009   88.669  1.00 7.78   ? 113  ARG B C   1 
ATOM   3217  O  O   . ARG B  1 26  ? 17.056  9.048   88.716  1.00 8.22   ? 113  ARG B O   1 
ATOM   3218  C  CB  . ARG B  1 26  ? 14.771  7.155   90.412  1.00 7.02   ? 113  ARG B CB  1 
ATOM   3219  C  CG  . ARG B  1 26  ? 13.500  7.381   91.222  1.00 8.04   ? 113  ARG B CG  1 
ATOM   3220  C  CD  . ARG B  1 26  ? 13.419  6.388   92.429  1.00 8.58   ? 113  ARG B CD  1 
ATOM   3221  N  NE  . ARG B  1 26  ? 14.611  6.432   93.289  1.00 10.13  ? 113  ARG B NE  1 
ATOM   3222  C  CZ  . ARG B  1 26  ? 14.804  7.275   94.304  1.00 10.69  ? 113  ARG B CZ  1 
ATOM   3223  N  NH1 . ARG B  1 26  ? 13.890  8.205   94.618  1.00 9.94   ? 113  ARG B NH1 1 
ATOM   3224  N  NH2 . ARG B  1 26  ? 15.943  7.206   94.993  1.00 9.02   ? 113  ARG B NH2 1 
ATOM   3225  N  N   . ILE B  1 27  ? 16.793  6.841   88.186  1.00 7.55   ? 114  ILE B N   1 
ATOM   3226  C  CA  . ILE B  1 27  ? 18.174  6.646   87.722  1.00 7.33   ? 114  ILE B CA  1 
ATOM   3227  C  C   . ILE B  1 27  ? 18.462  7.521   86.482  1.00 7.20   ? 114  ILE B C   1 
ATOM   3228  O  O   . ILE B  1 27  ? 19.492  8.195   86.419  1.00 7.61   ? 114  ILE B O   1 
ATOM   3229  C  CB  . ILE B  1 27  ? 18.490  5.121   87.475  1.00 7.20   ? 114  ILE B CB  1 
ATOM   3230  C  CG1 . ILE B  1 27  ? 18.536  4.363   88.820  1.00 7.65   ? 114  ILE B CG1 1 
ATOM   3231  C  CG2 . ILE B  1 27  ? 19.829  4.931   86.749  1.00 7.68   ? 114  ILE B CG2 1 
ATOM   3232  C  CD1 . ILE B  1 27  ? 18.441  2.815   88.696  1.00 7.68   ? 114  ILE B CD1 1 
ATOM   3233  N  N   . GLY B  1 28  ? 17.529  7.513   85.526  1.00 7.17   ? 115  GLY B N   1 
ATOM   3234  C  CA  . GLY B  1 28  ? 17.662  8.221   84.243  1.00 7.45   ? 115  GLY B CA  1 
ATOM   3235  C  C   . GLY B  1 28  ? 17.577  9.734   84.305  1.00 7.78   ? 115  GLY B C   1 
ATOM   3236  O  O   . GLY B  1 28  ? 17.815  10.413  83.292  1.00 8.02   ? 115  GLY B O   1 
ATOM   3237  N  N   . GLU B  1 29  ? 17.215  10.269  85.473  1.00 7.96   ? 116  GLU B N   1 
ATOM   3238  C  CA  . GLU B  1 29  ? 17.340  11.699  85.724  1.00 9.00   ? 116  GLU B CA  1 
ATOM   3239  C  C   . GLU B  1 29  ? 18.799  12.158  85.524  1.00 9.82   ? 116  GLU B C   1 
ATOM   3240  O  O   . GLU B  1 29  ? 19.059  13.313  85.185  1.00 9.82   ? 116  GLU B O   1 
ATOM   3241  C  CB  . GLU B  1 29  ? 16.843  12.039  87.146  1.00 8.93   ? 116  GLU B CB  1 
ATOM   3242  C  CG  . GLU B  1 29  ? 16.792  13.548  87.470  1.00 9.35   ? 116  GLU B CG  1 
ATOM   3243  C  CD  . GLU B  1 29  ? 18.158  14.147  87.865  1.00 11.54  ? 116  GLU B CD  1 
ATOM   3244  O  OE1 . GLU B  1 29  ? 18.365  15.340  87.577  1.00 10.31  ? 116  GLU B OE1 1 
ATOM   3245  O  OE2 . GLU B  1 29  ? 19.027  13.450  88.448  1.00 10.99  ? 116  GLU B OE2 1 
ATOM   3246  N  N   . ASP B  1 30  ? 19.757  11.259  85.750  1.00 10.47  ? 117  ASP B N   1 
ATOM   3247  C  CA  . ASP B  1 30  ? 21.165  11.625  85.603  1.00 12.01  ? 117  ASP B CA  1 
ATOM   3248  C  C   . ASP B  1 30  ? 21.983  10.673  84.707  1.00 12.11  ? 117  ASP B C   1 
ATOM   3249  O  O   . ASP B  1 30  ? 22.835  11.118  83.924  1.00 14.75  ? 117  ASP B O   1 
ATOM   3250  C  CB  . ASP B  1 30  ? 21.818  11.831  86.992  1.00 11.99  ? 117  ASP B CB  1 
ATOM   3251  C  CG  . ASP B  1 30  ? 23.319  12.105  86.907  1.00 16.93  ? 117  ASP B CG  1 
ATOM   3252  O  OD1 . ASP B  1 30  ? 24.123  11.334  87.518  1.00 20.05  ? 117  ASP B OD1 1 
ATOM   3253  O  OD2 . ASP B  1 30  ? 23.692  13.101  86.225  1.00 20.50  ? 117  ASP B OD2 1 
ATOM   3254  N  N   . ALA B  1 31  ? 21.688  9.384   84.767  1.00 12.41  ? 118  ALA B N   1 
ATOM   3255  C  CA  . ALA B  1 31  ? 22.399  8.398   83.972  1.00 10.48  ? 118  ALA B CA  1 
ATOM   3256  C  C   . ALA B  1 31  ? 21.787  8.293   82.566  1.00 9.90   ? 118  ALA B C   1 
ATOM   3257  O  O   . ALA B  1 31  ? 20.681  8.807   82.311  1.00 9.93   ? 118  ALA B O   1 
ATOM   3258  C  CB  . ALA B  1 31  ? 22.384  7.047   84.690  1.00 10.77  ? 118  ALA B CB  1 
ATOM   3259  N  N   . HIS B  1 32  ? 22.488  7.616   81.661  1.00 8.70   ? 119  HIS B N   1 
ATOM   3260  C  CA  . HIS B  1 32  ? 22.027  7.500   80.269  1.00 8.31   ? 119  HIS B CA  1 
ATOM   3261  C  C   . HIS B  1 32  ? 21.004  6.354   80.176  1.00 8.44   ? 119  HIS B C   1 
ATOM   3262  O  O   . HIS B  1 32  ? 21.387  5.211   80.002  1.00 8.29   ? 119  HIS B O   1 
ATOM   3263  C  CB  . HIS B  1 32  ? 23.197  7.253   79.287  1.00 8.19   ? 119  HIS B CB  1 
ATOM   3264  C  CG  . HIS B  1 32  ? 24.210  8.363   79.249  1.00 8.70   ? 119  HIS B CG  1 
ATOM   3265  N  ND1 . HIS B  1 32  ? 25.521  8.165   78.866  1.00 8.77   ? 119  HIS B ND1 1 
ATOM   3266  C  CD2 . HIS B  1 32  ? 24.100  9.681   79.558  1.00 9.69   ? 119  HIS B CD2 1 
ATOM   3267  C  CE1 . HIS B  1 32  ? 26.178  9.311   78.943  1.00 11.52  ? 119  HIS B CE1 1 
ATOM   3268  N  NE2 . HIS B  1 32  ? 25.345  10.247  79.364  1.00 10.67  ? 119  HIS B NE2 1 
ATOM   3269  N  N   . ILE B  1 33  ? 19.715  6.679   80.295  1.00 8.21   ? 120  ILE B N   1 
ATOM   3270  C  CA  . ILE B  1 33  ? 18.643  5.676   80.340  1.00 7.48   ? 120  ILE B CA  1 
ATOM   3271  C  C   . ILE B  1 33  ? 17.719  5.972   79.172  1.00 7.49   ? 120  ILE B C   1 
ATOM   3272  O  O   . ILE B  1 33  ? 17.346  7.137   78.938  1.00 7.19   ? 120  ILE B O   1 
ATOM   3273  C  CB  . ILE B  1 33  ? 17.890  5.706   81.698  1.00 7.65   ? 120  ILE B CB  1 
ATOM   3274  C  CG1 . ILE B  1 33  ? 18.875  5.373   82.852  1.00 8.63   ? 120  ILE B CG1 1 
ATOM   3275  C  CG2 . ILE B  1 33  ? 16.639  4.794   81.689  1.00 6.87   ? 120  ILE B CG2 1 
ATOM   3276  C  CD1 . ILE B  1 33  ? 19.533  3.932   82.783  1.00 7.99   ? 120  ILE B CD1 1 
ATOM   3277  N  N   . LEU B  1 34  ? 17.398  4.932   78.410  1.00 7.21   ? 121  LEU B N   1 
ATOM   3278  C  CA  . LEU B  1 34  ? 16.560  5.081   77.214  1.00 7.75   ? 121  LEU B CA  1 
ATOM   3279  C  C   . LEU B  1 34  ? 15.111  5.404   77.605  1.00 7.87   ? 121  LEU B C   1 
ATOM   3280  O  O   . LEU B  1 34  ? 14.629  4.882   78.594  1.00 7.44   ? 121  LEU B O   1 
ATOM   3281  C  CB  . LEU B  1 34  ? 16.560  3.799   76.391  1.00 7.73   ? 121  LEU B CB  1 
ATOM   3282  C  CG  . LEU B  1 34  ? 17.894  3.459   75.708  1.00 9.21   ? 121  LEU B CG  1 
ATOM   3283  C  CD1 . LEU B  1 34  ? 17.904  1.987   75.305  1.00 6.96   ? 121  LEU B CD1 1 
ATOM   3284  C  CD2 . LEU B  1 34  ? 18.154  4.328   74.486  1.00 9.52   ? 121  LEU B CD2 1 
ATOM   3285  N  N   . VAL B  1 35  ? 14.453  6.264   76.816  1.00 7.81   ? 122  VAL B N   1 
ATOM   3286  C  CA  . VAL B  1 35  ? 12.997  6.418   76.895  1.00 7.46   ? 122  VAL B CA  1 
ATOM   3287  C  C   . VAL B  1 35  ? 12.314  5.149   76.366  1.00 7.28   ? 122  VAL B C   1 
ATOM   3288  O  O   . VAL B  1 35  ? 12.674  4.637   75.299  1.00 7.00   ? 122  VAL B O   1 
ATOM   3289  C  CB  . VAL B  1 35  ? 12.498  7.640   76.087  1.00 7.54   ? 122  VAL B CB  1 
ATOM   3290  C  CG1 . VAL B  1 35  ? 10.946  7.714   76.134  1.00 7.70   ? 122  VAL B CG1 1 
ATOM   3291  C  CG2 . VAL B  1 35  ? 13.132  8.944   76.607  1.00 7.07   ? 122  VAL B CG2 1 
ATOM   3292  N  N   . THR B  1 36  ? 11.345  4.641   77.123  1.00 7.29   ? 123  THR B N   1 
ATOM   3293  C  CA  . THR B  1 36  ? 10.611  3.434   76.756  1.00 6.77   ? 123  THR B CA  1 
ATOM   3294  C  C   . THR B  1 36  ? 9.108   3.643   76.978  1.00 6.60   ? 123  THR B C   1 
ATOM   3295  O  O   . THR B  1 36  ? 8.690   4.706   77.453  1.00 5.58   ? 123  THR B O   1 
ATOM   3296  C  CB  . THR B  1 36  ? 11.083  2.211   77.605  1.00 6.58   ? 123  THR B CB  1 
ATOM   3297  O  OG1 . THR B  1 36  ? 10.871  2.490   78.991  1.00 8.97   ? 123  THR B OG1 1 
ATOM   3298  C  CG2 . THR B  1 36  ? 12.562  1.901   77.394  1.00 6.03   ? 123  THR B CG2 1 
ATOM   3299  N  N   . ARG B  1 37  ? 8.320   2.617   76.640  1.00 6.76   ? 124  ARG B N   1 
ATOM   3300  C  CA  . ARG B  1 37  ? 6.914   2.402   77.104  1.00 6.60   ? 124  ARG B CA  1 
ATOM   3301  C  C   . ARG B  1 37  ? 6.561   0.976   76.674  1.00 6.97   ? 124  ARG B C   1 
ATOM   3302  O  O   . ARG B  1 37  ? 7.382   0.326   76.005  1.00 8.13   ? 124  ARG B O   1 
ATOM   3303  C  CB  . ARG B  1 37  ? 5.897   3.447   76.568  1.00 5.84   ? 124  ARG B CB  1 
ATOM   3304  C  CG  . ARG B  1 37  ? 5.513   4.543   77.596  1.00 6.97   ? 124  ARG B CG  1 
ATOM   3305  C  CD  . ARG B  1 37  ? 4.006   4.914   77.509  1.00 6.99   ? 124  ARG B CD  1 
ATOM   3306  N  NE  . ARG B  1 37  ? 3.168   3.764   77.827  1.00 9.81   ? 124  ARG B NE  1 
ATOM   3307  C  CZ  . ARG B  1 37  ? 1.959   3.546   77.324  1.00 9.80   ? 124  ARG B CZ  1 
ATOM   3308  N  NH1 . ARG B  1 37  ? 1.307   2.450   77.653  1.00 8.15   ? 124  ARG B NH1 1 
ATOM   3309  N  NH2 . ARG B  1 37  ? 1.411   4.422   76.487  1.00 10.59  ? 124  ARG B NH2 1 
ATOM   3310  N  N   . GLU B  1 38  ? 5.387   0.472   77.056  1.00 6.76   ? 125  GLU B N   1 
ATOM   3311  C  CA  . GLU B  1 38  ? 4.955   -0.898  76.702  1.00 7.74   ? 125  GLU B CA  1 
ATOM   3312  C  C   . GLU B  1 38  ? 5.977   -1.981  77.141  1.00 7.82   ? 125  GLU B C   1 
ATOM   3313  O  O   . GLU B  1 38  ? 6.420   -2.798  76.327  1.00 7.77   ? 125  GLU B O   1 
ATOM   3314  C  CB  . GLU B  1 38  ? 4.611   -1.012  75.199  1.00 7.48   ? 125  GLU B CB  1 
ATOM   3315  C  CG  . GLU B  1 38  ? 3.490   -0.082  74.742  1.00 8.32   ? 125  GLU B CG  1 
ATOM   3316  C  CD  . GLU B  1 38  ? 3.962   1.321   74.381  1.00 8.68   ? 125  GLU B CD  1 
ATOM   3317  O  OE1 . GLU B  1 38  ? 3.111   2.256   74.456  1.00 11.36  ? 125  GLU B OE1 1 
ATOM   3318  O  OE2 . GLU B  1 38  ? 5.154   1.508   74.035  1.00 7.58   ? 125  GLU B OE2 1 
ATOM   3319  N  N   . PRO B  1 39  ? 6.345   -1.988  78.439  1.00 8.55   ? 126  PRO B N   1 
ATOM   3320  C  CA  . PRO B  1 39  ? 7.329   -2.950  78.963  1.00 8.30   ? 126  PRO B CA  1 
ATOM   3321  C  C   . PRO B  1 39  ? 6.670   -4.270  79.303  1.00 9.10   ? 126  PRO B C   1 
ATOM   3322  O  O   . PRO B  1 39  ? 5.435   -4.350  79.402  1.00 8.82   ? 126  PRO B O   1 
ATOM   3323  C  CB  . PRO B  1 39  ? 7.777   -2.288  80.269  1.00 7.79   ? 126  PRO B CB  1 
ATOM   3324  C  CG  . PRO B  1 39  ? 6.460   -1.692  80.777  1.00 8.33   ? 126  PRO B CG  1 
ATOM   3325  C  CD  . PRO B  1 39  ? 5.840   -1.109  79.515  1.00 8.11   ? 126  PRO B CD  1 
ATOM   3326  N  N   . TYR B  1 40  ? 7.498   -5.300  79.477  1.00 9.03   ? 127  TYR B N   1 
ATOM   3327  C  CA  . TYR B  1 40  ? 7.063   -6.560  80.036  1.00 9.01   ? 127  TYR B CA  1 
ATOM   3328  C  C   . TYR B  1 40  ? 8.266   -7.349  80.518  1.00 8.75   ? 127  TYR B C   1 
ATOM   3329  O  O   . TYR B  1 40  ? 9.370   -6.822  80.536  1.00 9.57   ? 127  TYR B O   1 
ATOM   3330  C  CB  . TYR B  1 40  ? 6.215   -7.355  79.036  1.00 8.77   ? 127  TYR B CB  1 
ATOM   3331  C  CG  . TYR B  1 40  ? 6.776   -7.566  77.639  1.00 7.71   ? 127  TYR B CG  1 
ATOM   3332  C  CD1 . TYR B  1 40  ? 6.673   -6.577  76.657  1.00 6.50   ? 127  TYR B CD1 1 
ATOM   3333  C  CD2 . TYR B  1 40  ? 7.310   -8.803  77.275  1.00 7.59   ? 127  TYR B CD2 1 
ATOM   3334  C  CE1 . TYR B  1 40  ? 7.136   -6.797  75.337  1.00 4.92   ? 127  TYR B CE1 1 
ATOM   3335  C  CE2 . TYR B  1 40  ? 7.765   -9.048  75.958  1.00 7.81   ? 127  TYR B CE2 1 
ATOM   3336  C  CZ  . TYR B  1 40  ? 7.686   -8.039  75.010  1.00 8.01   ? 127  TYR B CZ  1 
ATOM   3337  O  OH  . TYR B  1 40  ? 8.123   -8.311  73.737  1.00 9.28   ? 127  TYR B OH  1 
ATOM   3338  N  N   . LEU B  1 41  ? 8.038   -8.583  80.969  1.00 9.20   ? 128  LEU B N   1 
ATOM   3339  C  CA  . LEU B  1 41  ? 9.134   -9.481  81.336  1.00 9.45   ? 128  LEU B CA  1 
ATOM   3340  C  C   . LEU B  1 41  ? 8.855   -10.808 80.665  1.00 9.27   ? 128  LEU B C   1 
ATOM   3341  O  O   . LEU B  1 41  ? 7.693   -11.147 80.436  1.00 8.46   ? 128  LEU B O   1 
ATOM   3342  C  CB  . LEU B  1 41  ? 9.188   -9.745  82.842  1.00 8.60   ? 128  LEU B CB  1 
ATOM   3343  C  CG  . LEU B  1 41  ? 9.411   -8.769  84.009  1.00 11.96  ? 128  LEU B CG  1 
ATOM   3344  C  CD1 . LEU B  1 41  ? 10.797  -8.823  84.598  1.00 13.77  ? 128  LEU B CD1 1 
ATOM   3345  C  CD2 . LEU B  1 41  ? 8.836   -7.404  83.858  1.00 10.31  ? 128  LEU B CD2 1 
ATOM   3346  N  N   . SER B  1 42  ? 9.921   -11.551 80.370  1.00 9.17   ? 129  SER B N   1 
ATOM   3347  C  CA  . SER B  1 42  ? 9.822   -12.904 79.821  1.00 9.55   ? 129  SER B CA  1 
ATOM   3348  C  C   . SER B  1 42  ? 11.043  -13.673 80.304  1.00 10.16  ? 129  SER B C   1 
ATOM   3349  O  O   . SER B  1 42  ? 12.150  -13.123 80.375  1.00 8.77   ? 129  SER B O   1 
ATOM   3350  C  CB  . SER B  1 42  ? 9.801   -12.856 78.294  1.00 9.56   ? 129  SER B CB  1 
ATOM   3351  O  OG  . SER B  1 42  ? 9.565   -14.127 77.730  1.00 10.30  ? 129  SER B OG  1 
ATOM   3352  N  N   . CYS B  1 43  ? 10.839  -14.945 80.613  1.00 10.96  ? 130  CYS B N   1 
ATOM   3353  C  CA  . CYS B  1 43  ? 11.918  -15.787 81.134  1.00 12.99  ? 130  CYS B CA  1 
ATOM   3354  C  C   . CYS B  1 43  ? 12.350  -16.868 80.143  1.00 13.19  ? 130  CYS B C   1 
ATOM   3355  O  O   . CYS B  1 43  ? 11.701  -17.100 79.124  1.00 13.15  ? 130  CYS B O   1 
ATOM   3356  C  CB  . CYS B  1 43  ? 11.483  -16.423 82.457  1.00 13.51  ? 130  CYS B CB  1 
ATOM   3357  S  SG  . CYS B  1 43  ? 10.842  -15.221 83.666  1.00 14.38  ? 130  CYS B SG  1 
ATOM   3358  N  N   . ASP B  1 44  ? 13.470  -17.508 80.459  1.00 14.39  ? 131  ASP B N   1 
ATOM   3359  C  CA  . ASP B  1 44  ? 14.032  -18.600 79.673  1.00 14.90  ? 131  ASP B CA  1 
ATOM   3360  C  C   . ASP B  1 44  ? 14.708  -19.555 80.680  1.00 15.31  ? 131  ASP B C   1 
ATOM   3361  O  O   . ASP B  1 44  ? 14.676  -19.277 81.889  1.00 15.24  ? 131  ASP B O   1 
ATOM   3362  C  CB  . ASP B  1 44  ? 14.961  -18.052 78.558  1.00 15.41  ? 131  ASP B CB  1 
ATOM   3363  C  CG  . ASP B  1 44  ? 16.173  -17.290 79.084  1.00 16.51  ? 131  ASP B CG  1 
ATOM   3364  O  OD1 . ASP B  1 44  ? 16.467  -16.186 78.563  1.00 22.43  ? 131  ASP B OD1 1 
ATOM   3365  O  OD2 . ASP B  1 44  ? 16.851  -17.780 80.000  1.00 20.08  ? 131  ASP B OD2 1 
ATOM   3366  N  N   . PRO B  1 45  ? 15.257  -20.700 80.217  1.00 15.20  ? 132  PRO B N   1 
ATOM   3367  C  CA  . PRO B  1 45  ? 15.861  -21.675 81.135  1.00 15.51  ? 132  PRO B CA  1 
ATOM   3368  C  C   . PRO B  1 45  ? 16.916  -21.103 82.080  1.00 16.12  ? 132  PRO B C   1 
ATOM   3369  O  O   . PRO B  1 45  ? 17.118  -21.654 83.166  1.00 15.76  ? 132  PRO B O   1 
ATOM   3370  C  CB  . PRO B  1 45  ? 16.484  -22.704 80.180  1.00 15.43  ? 132  PRO B CB  1 
ATOM   3371  C  CG  . PRO B  1 45  ? 15.547  -22.662 78.992  1.00 15.37  ? 132  PRO B CG  1 
ATOM   3372  C  CD  . PRO B  1 45  ? 15.309  -21.180 78.825  1.00 14.91  ? 132  PRO B CD  1 
ATOM   3373  N  N   . GLN B  1 46  ? 17.538  -19.993 81.683  1.00 17.06  ? 133  GLN B N   1 
ATOM   3374  C  CA  . GLN B  1 46  ? 18.628  -19.370 82.454  1.00 19.17  ? 133  GLN B CA  1 
ATOM   3375  C  C   . GLN B  1 46  ? 18.174  -18.284 83.426  1.00 19.34  ? 133  GLN B C   1 
ATOM   3376  O  O   . GLN B  1 46  ? 18.739  -18.136 84.511  1.00 20.26  ? 133  GLN B O   1 
ATOM   3377  C  CB  . GLN B  1 46  ? 19.706  -18.821 81.517  1.00 19.83  ? 133  GLN B CB  1 
ATOM   3378  C  CG  . GLN B  1 46  ? 20.835  -19.817 81.238  1.00 23.97  ? 133  GLN B CG  1 
ATOM   3379  C  CD  . GLN B  1 46  ? 20.345  -21.097 80.590  1.00 29.30  ? 133  GLN B CD  1 
ATOM   3380  O  OE1 . GLN B  1 46  ? 19.774  -21.070 79.490  1.00 32.68  ? 133  GLN B OE1 1 
ATOM   3381  N  NE2 . GLN B  1 46  ? 20.574  -22.234 81.259  1.00 31.00  ? 133  GLN B NE2 1 
ATOM   3382  N  N   . GLY B  1 47  ? 17.138  -17.545 83.062  1.00 18.46  ? 134  GLY B N   1 
ATOM   3383  C  CA  . GLY B  1 47  ? 16.677  -16.460 83.940  1.00 18.57  ? 134  GLY B CA  1 
ATOM   3384  C  C   . GLY B  1 47  ? 15.614  -15.615 83.271  1.00 17.17  ? 134  GLY B C   1 
ATOM   3385  O  O   . GLY B  1 47  ? 15.087  -15.994 82.220  1.00 17.03  ? 134  GLY B O   1 
ATOM   3386  N  N   . CYS B  1 48  ? 15.310  -14.472 83.885  1.00 15.36  ? 135  CYS B N   1 
ATOM   3387  C  CA  . CYS B  1 48  ? 14.234  -13.607 83.391  1.00 13.95  ? 135  CYS B CA  1 
ATOM   3388  C  C   . CYS B  1 48  ? 14.828  -12.282 82.930  1.00 12.01  ? 135  CYS B C   1 
ATOM   3389  O  O   . CYS B  1 48  ? 15.855  -11.833 83.474  1.00 11.01  ? 135  CYS B O   1 
ATOM   3390  C  CB  . CYS B  1 48  ? 13.175  -13.388 84.469  1.00 13.90  ? 135  CYS B CB  1 
ATOM   3391  S  SG  . CYS B  1 48  ? 12.352  -14.943 84.990  1.00 17.80  ? 135  CYS B SG  1 
ATOM   3392  N  N   . ARG B  1 49  ? 14.198  -11.681 81.919  1.00 9.81   ? 136  ARG B N   1 
ATOM   3393  C  CA  . ARG B  1 49  ? 14.675  -10.422 81.365  1.00 9.42   ? 136  ARG B CA  1 
ATOM   3394  C  C   . ARG B  1 49  ? 13.532  -9.420  81.273  1.00 8.79   ? 136  ARG B C   1 
ATOM   3395  O  O   . ARG B  1 49  ? 12.364  -9.798  81.174  1.00 8.26   ? 136  ARG B O   1 
ATOM   3396  C  CB  . ARG B  1 49  ? 15.299  -10.639 79.981  1.00 9.49   ? 136  ARG B CB  1 
ATOM   3397  C  CG  . ARG B  1 49  ? 16.651  -11.385 80.034  1.00 9.83   ? 136  ARG B CG  1 
ATOM   3398  C  CD  . ARG B  1 49  ? 17.122  -11.814 78.649  1.00 10.68  ? 136  ARG B CD  1 
ATOM   3399  N  NE  . ARG B  1 49  ? 17.552  -10.707 77.791  1.00 10.35  ? 136  ARG B NE  1 
ATOM   3400  C  CZ  . ARG B  1 49  ? 18.675  -9.997  77.940  1.00 12.85  ? 136  ARG B CZ  1 
ATOM   3401  N  NH1 . ARG B  1 49  ? 19.509  -10.237 78.953  1.00 11.56  ? 136  ARG B NH1 1 
ATOM   3402  N  NH2 . ARG B  1 49  ? 18.963  -9.022  77.078  1.00 10.27  ? 136  ARG B NH2 1 
ATOM   3403  N  N   . MET B  1 50  ? 13.879  -8.144  81.338  1.00 8.50   ? 137  MET B N   1 
ATOM   3404  C  CA  . MET B  1 50  ? 12.918  -7.081  81.096  1.00 8.18   ? 137  MET B CA  1 
ATOM   3405  C  C   . MET B  1 50  ? 12.937  -6.724  79.620  1.00 8.22   ? 137  MET B C   1 
ATOM   3406  O  O   . MET B  1 50  ? 13.988  -6.818  78.965  1.00 8.42   ? 137  MET B O   1 
ATOM   3407  C  CB  . MET B  1 50  ? 13.246  -5.871  81.964  1.00 8.01   ? 137  MET B CB  1 
ATOM   3408  C  CG  . MET B  1 50  ? 12.847  -6.099  83.417  1.00 8.29   ? 137  MET B CG  1 
ATOM   3409  S  SD  . MET B  1 50  ? 13.489  -4.798  84.490  1.00 9.28   ? 137  MET B SD  1 
ATOM   3410  C  CE  . MET B  1 50  ? 12.404  -5.010  85.939  1.00 7.52   ? 137  MET B CE  1 
ATOM   3411  N  N   . PHE B  1 51  ? 11.765  -6.363  79.098  1.00 8.13   ? 138  PHE B N   1 
ATOM   3412  C  CA  . PHE B  1 51  ? 11.568  -5.979  77.687  1.00 7.95   ? 138  PHE B CA  1 
ATOM   3413  C  C   . PHE B  1 51  ? 10.794  -4.654  77.625  1.00 7.76   ? 138  PHE B C   1 
ATOM   3414  O  O   . PHE B  1 51  ? 9.980   -4.367  78.508  1.00 7.81   ? 138  PHE B O   1 
ATOM   3415  C  CB  . PHE B  1 51  ? 10.735  -7.068  76.956  1.00 7.72   ? 138  PHE B CB  1 
ATOM   3416  C  CG  . PHE B  1 51  ? 11.467  -8.350  76.727  1.00 8.69   ? 138  PHE B CG  1 
ATOM   3417  C  CD1 . PHE B  1 51  ? 11.718  -9.228  77.791  1.00 9.38   ? 138  PHE B CD1 1 
ATOM   3418  C  CD2 . PHE B  1 51  ? 11.863  -8.716  75.435  1.00 9.39   ? 138  PHE B CD2 1 
ATOM   3419  C  CE1 . PHE B  1 51  ? 12.403  -10.444 77.594  1.00 9.54   ? 138  PHE B CE1 1 
ATOM   3420  C  CE2 . PHE B  1 51  ? 12.560  -9.937  75.217  1.00 10.82  ? 138  PHE B CE2 1 
ATOM   3421  C  CZ  . PHE B  1 51  ? 12.831  -10.795 76.295  1.00 8.15   ? 138  PHE B CZ  1 
ATOM   3422  N  N   . ALA B  1 52  ? 11.018  -3.847  76.589  1.00 7.58   ? 139  ALA B N   1 
ATOM   3423  C  CA  . ALA B  1 52  ? 10.171  -2.659  76.352  1.00 7.84   ? 139  ALA B CA  1 
ATOM   3424  C  C   . ALA B  1 52  ? 10.403  -2.117  74.945  1.00 8.10   ? 139  ALA B C   1 
ATOM   3425  O  O   . ALA B  1 52  ? 11.360  -2.495  74.279  1.00 7.62   ? 139  ALA B O   1 
ATOM   3426  C  CB  . ALA B  1 52  ? 10.436  -1.554  77.409  1.00 8.43   ? 139  ALA B CB  1 
ATOM   3427  N  N   . LEU B  1 53  ? 9.510   -1.251  74.489  1.00 7.36   ? 140  LEU B N   1 
ATOM   3428  C  CA  . LEU B  1 53  ? 9.746   -0.556  73.234  1.00 7.02   ? 140  LEU B CA  1 
ATOM   3429  C  C   . LEU B  1 53  ? 10.538  0.728   73.506  1.00 7.37   ? 140  LEU B C   1 
ATOM   3430  O  O   . LEU B  1 53  ? 10.009  1.696   74.046  1.00 7.75   ? 140  LEU B O   1 
ATOM   3431  C  CB  . LEU B  1 53  ? 8.408   -0.260  72.562  1.00 8.07   ? 140  LEU B CB  1 
ATOM   3432  C  CG  . LEU B  1 53  ? 7.625   -1.504  72.144  1.00 7.37   ? 140  LEU B CG  1 
ATOM   3433  C  CD1 . LEU B  1 53  ? 6.195   -1.137  71.684  1.00 9.49   ? 140  LEU B CD1 1 
ATOM   3434  C  CD2 . LEU B  1 53  ? 8.380   -2.197  71.023  1.00 7.73   ? 140  LEU B CD2 1 
ATOM   3435  N  N   . SER B  1 54  ? 11.812  0.740   73.134  1.00 7.34   ? 141  SER B N   1 
ATOM   3436  C  CA  . SER B  1 54  ? 12.589  1.986   73.159  1.00 7.54   ? 141  SER B CA  1 
ATOM   3437  C  C   . SER B  1 54  ? 11.970  3.036   72.231  1.00 8.05   ? 141  SER B C   1 
ATOM   3438  O  O   . SER B  1 54  ? 11.294  2.680   71.258  1.00 8.02   ? 141  SER B O   1 
ATOM   3439  C  CB  . SER B  1 54  ? 14.026  1.751   72.692  1.00 7.76   ? 141  SER B CB  1 
ATOM   3440  O  OG  . SER B  1 54  ? 14.747  2.983   72.764  1.00 6.98   ? 141  SER B OG  1 
ATOM   3441  N  N   . GLN B  1 55  ? 12.201  4.309   72.562  1.00 7.91   ? 142  GLN B N   1 
ATOM   3442  C  CA  . GLN B  1 55  ? 11.927  5.448   71.672  1.00 8.46   ? 142  GLN B CA  1 
ATOM   3443  C  C   . GLN B  1 55  ? 13.178  5.969   70.933  1.00 8.37   ? 142  GLN B C   1 
ATOM   3444  O  O   . GLN B  1 55  ? 13.114  6.975   70.220  1.00 9.25   ? 142  GLN B O   1 
ATOM   3445  C  CB  . GLN B  1 55  ? 11.236  6.572   72.453  1.00 7.79   ? 142  GLN B CB  1 
ATOM   3446  C  CG  . GLN B  1 55  ? 9.826   6.201   72.916  1.00 7.19   ? 142  GLN B CG  1 
ATOM   3447  C  CD  . GLN B  1 55  ? 8.709   6.545   71.905  1.00 9.35   ? 142  GLN B CD  1 
ATOM   3448  O  OE1 . GLN B  1 55  ? 7.540   6.678   72.298  1.00 10.57  ? 142  GLN B OE1 1 
ATOM   3449  N  NE2 . GLN B  1 55  ? 9.054   6.677   70.629  1.00 5.17   ? 142  GLN B NE2 1 
ATOM   3450  N  N   . GLY B  1 56  ? 14.318  5.289   71.087  1.00 8.78   ? 143  GLY B N   1 
ATOM   3451  C  CA  . GLY B  1 56  ? 15.526  5.658   70.345  1.00 8.21   ? 143  GLY B CA  1 
ATOM   3452  C  C   . GLY B  1 56  ? 16.111  7.004   70.755  1.00 8.37   ? 143  GLY B C   1 
ATOM   3453  O  O   . GLY B  1 56  ? 16.533  7.789   69.905  1.00 8.60   ? 143  GLY B O   1 
ATOM   3454  N  N   . THR B  1 57  ? 16.137  7.243   72.063  1.00 8.12   ? 144  THR B N   1 
ATOM   3455  C  CA  . THR B  1 57  ? 16.664  8.460   72.689  1.00 8.64   ? 144  THR B CA  1 
ATOM   3456  C  C   . THR B  1 57  ? 16.789  8.184   74.168  1.00 8.53   ? 144  THR B C   1 
ATOM   3457  O  O   . THR B  1 57  ? 16.073  7.330   74.678  1.00 7.84   ? 144  THR B O   1 
ATOM   3458  C  CB  . THR B  1 57  ? 15.737  9.705   72.455  1.00 8.65   ? 144  THR B CB  1 
ATOM   3459  O  OG1 . THR B  1 57  ? 16.266  10.861  73.130  1.00 11.10  ? 144  THR B OG1 1 
ATOM   3460  C  CG2 . THR B  1 57  ? 14.286  9.455   72.931  1.00 8.04   ? 144  THR B CG2 1 
ATOM   3461  N  N   . THR B  1 58  ? 17.698  8.886   74.850  1.00 8.04   ? 145  THR B N   1 
ATOM   3462  C  CA  . THR B  1 58  ? 17.729  8.865   76.316  1.00 7.59   ? 145  THR B CA  1 
ATOM   3463  C  C   . THR B  1 58  ? 16.693  9.831   76.904  1.00 7.79   ? 145  THR B C   1 
ATOM   3464  O  O   . THR B  1 58  ? 16.163  10.718  76.211  1.00 7.76   ? 145  THR B O   1 
ATOM   3465  C  CB  . THR B  1 58  ? 19.119  9.239   76.892  1.00 7.69   ? 145  THR B CB  1 
ATOM   3466  O  OG1 . THR B  1 58  ? 19.445  10.599  76.518  1.00 6.87   ? 145  THR B OG1 1 
ATOM   3467  C  CG2 . THR B  1 58  ? 20.198  8.243   76.396  1.00 8.59   ? 145  THR B CG2 1 
ATOM   3468  N  N   . LEU B  1 59  ? 16.417  9.655   78.194  1.00 7.79   ? 146  LEU B N   1 
ATOM   3469  C  CA  . LEU B  1 59  ? 15.376  10.400  78.894  1.00 8.56   ? 146  LEU B CA  1 
ATOM   3470  C  C   . LEU B  1 59  ? 15.726  11.893  79.072  1.00 8.95   ? 146  LEU B C   1 
ATOM   3471  O  O   . LEU B  1 59  ? 14.837  12.758  78.998  1.00 9.67   ? 146  LEU B O   1 
ATOM   3472  C  CB  . LEU B  1 59  ? 15.119  9.710   80.240  1.00 8.24   ? 146  LEU B CB  1 
ATOM   3473  C  CG  . LEU B  1 59  ? 14.046  10.318  81.164  1.00 10.24  ? 146  LEU B CG  1 
ATOM   3474  C  CD1 . LEU B  1 59  ? 12.619  10.217  80.577  1.00 8.73   ? 146  LEU B CD1 1 
ATOM   3475  C  CD2 . LEU B  1 59  ? 14.122  9.664   82.539  1.00 7.62   ? 146  LEU B CD2 1 
ATOM   3476  N  N   . ARG B  1 60  ? 17.005  12.171  79.356  1.00 8.50   ? 147  ARG B N   1 
ATOM   3477  C  CA  . ARG B  1 60  ? 17.511  13.548  79.517  1.00 9.81   ? 147  ARG B CA  1 
ATOM   3478  C  C   . ARG B  1 60  ? 17.907  14.178  78.183  1.00 10.01  ? 147  ARG B C   1 
ATOM   3479  O  O   . ARG B  1 60  ? 18.214  15.372  78.116  1.00 10.46  ? 147  ARG B O   1 
ATOM   3480  C  CB  . ARG B  1 60  ? 18.688  13.587  80.505  1.00 9.13   ? 147  ARG B CB  1 
ATOM   3481  C  CG  . ARG B  1 60  ? 18.245  13.611  81.966  1.00 10.22  ? 147  ARG B CG  1 
ATOM   3482  C  CD  . ARG B  1 60  ? 17.442  14.889  82.246  1.00 10.55  ? 147  ARG B CD  1 
ATOM   3483  N  NE  . ARG B  1 60  ? 17.410  15.255  83.666  1.00 10.14  ? 147  ARG B NE  1 
ATOM   3484  C  CZ  . ARG B  1 60  ? 16.787  16.338  84.139  1.00 12.00  ? 147  ARG B CZ  1 
ATOM   3485  N  NH1 . ARG B  1 60  ? 16.077  17.120  83.318  1.00 9.58   ? 147  ARG B NH1 1 
ATOM   3486  N  NH2 . ARG B  1 60  ? 16.855  16.624  85.435  1.00 11.24  ? 147  ARG B NH2 1 
ATOM   3487  N  N   . GLY B  1 61  ? 17.885  13.371  77.127  1.00 9.40   ? 148  GLY B N   1 
ATOM   3488  C  CA  . GLY B  1 61  ? 18.223  13.845  75.769  1.00 9.92   ? 148  GLY B CA  1 
ATOM   3489  C  C   . GLY B  1 61  ? 17.152  14.778  75.223  1.00 9.79   ? 148  GLY B C   1 
ATOM   3490  O  O   . GLY B  1 61  ? 15.973  14.646  75.567  1.00 10.94  ? 148  GLY B O   1 
ATOM   3491  N  N   . ARG B  1 62  ? 17.551  15.712  74.364  1.00 9.52   ? 149  ARG B N   1 
ATOM   3492  C  CA  . ARG B  1 62  ? 16.604  16.621  73.718  1.00 10.04  ? 149  ARG B CA  1 
ATOM   3493  C  C   . ARG B  1 62  ? 15.604  15.875  72.836  1.00 10.01  ? 149  ARG B C   1 
ATOM   3494  O  O   . ARG B  1 62  ? 14.460  16.338  72.670  1.00 9.35   ? 149  ARG B O   1 
ATOM   3495  C  CB  . ARG B  1 62  ? 17.343  17.724  72.923  1.00 9.43   ? 149  ARG B CB  1 
ATOM   3496  C  CG  . ARG B  1 62  ? 18.149  18.623  73.835  1.00 11.49  ? 149  ARG B CG  1 
ATOM   3497  C  CD  . ARG B  1 62  ? 18.865  19.748  73.117  1.00 12.43  ? 149  ARG B CD  1 
ATOM   3498  N  NE  . ARG B  1 62  ? 19.318  20.724  74.113  1.00 19.16  ? 149  ARG B NE  1 
ATOM   3499  C  CZ  . ARG B  1 62  ? 20.406  21.486  74.010  1.00 22.42  ? 149  ARG B CZ  1 
ATOM   3500  N  NH1 . ARG B  1 62  ? 21.197  21.419  72.937  1.00 22.04  ? 149  ARG B NH1 1 
ATOM   3501  N  NH2 . ARG B  1 62  ? 20.711  22.316  75.003  1.00 22.82  ? 149  ARG B NH2 1 
ATOM   3502  N  N   . HIS B  1 63  ? 15.990  14.703  72.319  1.00 9.55   ? 150  HIS B N   1 
ATOM   3503  C  CA  . HIS B  1 63  ? 15.039  13.895  71.534  1.00 9.90   ? 150  HIS B CA  1 
ATOM   3504  C  C   . HIS B  1 63  ? 13.936  13.226  72.371  1.00 8.92   ? 150  HIS B C   1 
ATOM   3505  O  O   . HIS B  1 63  ? 13.017  12.626  71.813  1.00 9.88   ? 150  HIS B O   1 
ATOM   3506  C  CB  . HIS B  1 63  ? 15.734  12.885  70.606  1.00 10.35  ? 150  HIS B CB  1 
ATOM   3507  C  CG  . HIS B  1 63  ? 16.662  13.520  69.606  1.00 10.68  ? 150  HIS B CG  1 
ATOM   3508  N  ND1 . HIS B  1 63  ? 18.014  13.649  69.833  1.00 10.28  ? 150  HIS B ND1 1 
ATOM   3509  C  CD2 . HIS B  1 63  ? 16.427  14.083  68.392  1.00 10.81  ? 150  HIS B CD2 1 
ATOM   3510  C  CE1 . HIS B  1 63  ? 18.579  14.246  68.797  1.00 10.36  ? 150  HIS B CE1 1 
ATOM   3511  N  NE2 . HIS B  1 63  ? 17.637  14.528  67.913  1.00 9.78   ? 150  HIS B NE2 1 
ATOM   3512  N  N   . ALA B  1 64  ? 14.009  13.320  73.692  1.00 9.07   ? 151  ALA B N   1 
ATOM   3513  C  CA  . ALA B  1 64  ? 12.901  12.786  74.516  1.00 9.52   ? 151  ALA B CA  1 
ATOM   3514  C  C   . ALA B  1 64  ? 11.645  13.650  74.296  1.00 9.40   ? 151  ALA B C   1 
ATOM   3515  O  O   . ALA B  1 64  ? 10.510  13.224  74.529  1.00 10.11  ? 151  ALA B O   1 
ATOM   3516  C  CB  . ALA B  1 64  ? 13.280  12.692  76.010  1.00 8.91   ? 151  ALA B CB  1 
ATOM   3517  N  N   . ASN B  1 65  ? 11.854  14.864  73.796  1.00 10.12  ? 152  ASN B N   1 
ATOM   3518  C  CA  . ASN B  1 65  ? 10.733  15.737  73.445  1.00 10.68  ? 152  ASN B CA  1 
ATOM   3519  C  C   . ASN B  1 65  ? 9.866   15.135  72.318  1.00 10.53  ? 152  ASN B C   1 
ATOM   3520  O  O   . ASN B  1 65  ? 10.354  14.841  71.226  1.00 11.15  ? 152  ASN B O   1 
ATOM   3521  C  CB  . ASN B  1 65  ? 11.266  17.126  73.141  1.00 10.50  ? 152  ASN B CB  1 
ATOM   3522  C  CG  . ASN B  1 65  ? 10.221  18.062  72.578  1.00 11.74  ? 152  ASN B CG  1 
ATOM   3523  O  OD1 . ASN B  1 65  ? 8.998   17.949  72.806  1.00 10.56  ? 152  ASN B OD1 1 
ATOM   3524  N  ND2 . ASN B  1 65  ? 10.715  19.017  71.835  1.00 11.88  ? 152  ASN B ND2 1 
ATOM   3525  N  N   . GLY B  1 66  ? 8.586   14.919  72.630  1.00 10.58  ? 153  GLY B N   1 
ATOM   3526  C  CA  . GLY B  1 66  ? 7.596   14.397  71.674  1.00 10.21  ? 153  GLY B CA  1 
ATOM   3527  C  C   . GLY B  1 66  ? 7.361   12.894  71.780  1.00 10.23  ? 153  GLY B C   1 
ATOM   3528  O  O   . GLY B  1 66  ? 6.660   12.321  70.944  1.00 10.05  ? 153  GLY B O   1 
ATOM   3529  N  N   . THR B  1 67  ? 7.936   12.267  72.813  1.00 10.59  ? 154  THR B N   1 
ATOM   3530  C  CA  . THR B  1 67  ? 7.845   10.817  72.996  1.00 11.05  ? 154  THR B CA  1 
ATOM   3531  C  C   . THR B  1 67  ? 6.490   10.311  73.533  1.00 11.56  ? 154  THR B C   1 
ATOM   3532  O  O   . THR B  1 67  ? 6.329   9.105   73.779  1.00 12.67  ? 154  THR B O   1 
ATOM   3533  C  CB  . THR B  1 67  ? 9.032   10.212  73.824  1.00 11.16  ? 154  THR B CB  1 
ATOM   3534  O  OG1 . THR B  1 67  ? 9.208   10.950  75.038  1.00 9.46   ? 154  THR B OG1 1 
ATOM   3535  C  CG2 . THR B  1 67  ? 10.338  10.214  72.998  1.00 10.17  ? 154  THR B CG2 1 
ATOM   3536  N  N   . ILE B  1 68  ? 5.505   11.199  73.663  1.00 11.74  ? 155  ILE B N   1 
ATOM   3537  C  CA  . ILE B  1 68  ? 4.120   10.724  73.817  1.00 12.71  ? 155  ILE B CA  1 
ATOM   3538  C  C   . ILE B  1 68  ? 3.666   9.910   72.570  1.00 12.67  ? 155  ILE B C   1 
ATOM   3539  O  O   . ILE B  1 68  ? 2.842   9.001   72.676  1.00 13.95  ? 155  ILE B O   1 
ATOM   3540  C  CB  . ILE B  1 68  ? 3.108   11.878  74.156  1.00 11.83  ? 155  ILE B CB  1 
ATOM   3541  C  CG1 . ILE B  1 68  ? 1.804   11.263  74.719  1.00 12.59  ? 155  ILE B CG1 1 
ATOM   3542  C  CG2 . ILE B  1 68  ? 2.912   12.811  72.925  1.00 12.57  ? 155  ILE B CG2 1 
ATOM   3543  C  CD1 . ILE B  1 68  ? 0.801   12.257  75.274  1.00 13.97  ? 155  ILE B CD1 1 
ATOM   3544  N  N   . HIS B  1 69  ? 4.248   10.230  71.414  1.00 12.46  ? 156  HIS B N   1 
ATOM   3545  C  CA  . HIS B  1 69  ? 3.893   9.637   70.134  1.00 12.73  ? 156  HIS B CA  1 
ATOM   3546  C  C   . HIS B  1 69  ? 4.218   8.131   70.149  1.00 12.31  ? 156  HIS B C   1 
ATOM   3547  O  O   . HIS B  1 69  ? 5.327   7.735   70.510  1.00 12.27  ? 156  HIS B O   1 
ATOM   3548  C  CB  . HIS B  1 69  ? 4.665   10.373  69.026  1.00 13.17  ? 156  HIS B CB  1 
ATOM   3549  C  CG  . HIS B  1 69  ? 4.219   10.044  67.640  1.00 16.02  ? 156  HIS B CG  1 
ATOM   3550  N  ND1 . HIS B  1 69  ? 3.021   10.483  67.115  1.00 18.63  ? 156  HIS B ND1 1 
ATOM   3551  C  CD2 . HIS B  1 69  ? 4.834   9.353   66.650  1.00 16.89  ? 156  HIS B CD2 1 
ATOM   3552  C  CE1 . HIS B  1 69  ? 2.903   10.048  65.869  1.00 18.63  ? 156  HIS B CE1 1 
ATOM   3553  N  NE2 . HIS B  1 69  ? 3.993   9.364   65.561  1.00 17.86  ? 156  HIS B NE2 1 
ATOM   3554  N  N   . ASP B  1 70  ? 3.241   7.313   69.762  1.00 11.55  ? 157  ASP B N   1 
ATOM   3555  C  CA  . ASP B  1 70  ? 3.353   5.845   69.838  1.00 12.18  ? 157  ASP B CA  1 
ATOM   3556  C  C   . ASP B  1 70  ? 4.173   5.162   68.732  1.00 11.77  ? 157  ASP B C   1 
ATOM   3557  O  O   . ASP B  1 70  ? 4.817   4.119   68.973  1.00 11.52  ? 157  ASP B O   1 
ATOM   3558  C  CB  . ASP B  1 70  ? 1.965   5.199   69.845  1.00 12.77  ? 157  ASP B CB  1 
ATOM   3559  C  CG  . ASP B  1 70  ? 1.137   5.589   71.047  1.00 15.30  ? 157  ASP B CG  1 
ATOM   3560  O  OD1 . ASP B  1 70  ? 1.594   5.388   72.190  1.00 17.03  ? 157  ASP B OD1 1 
ATOM   3561  O  OD2 . ASP B  1 70  ? 0.005   6.076   70.843  1.00 18.78  ? 157  ASP B OD2 1 
ATOM   3562  N  N   . ARG B  1 71  ? 4.114   5.691   67.518  1.00 11.35  ? 158  ARG B N   1 
ATOM   3563  C  CA  . ARG B  1 71  ? 4.718   4.958   66.392  1.00 11.48  ? 158  ARG B CA  1 
ATOM   3564  C  C   . ARG B  1 71  ? 5.700   5.830   65.609  1.00 11.19  ? 158  ARG B C   1 
ATOM   3565  O  O   . ARG B  1 71  ? 5.355   6.938   65.166  1.00 11.76  ? 158  ARG B O   1 
ATOM   3566  C  CB  . ARG B  1 71  ? 3.631   4.316   65.487  1.00 10.91  ? 158  ARG B CB  1 
ATOM   3567  C  CG  . ARG B  1 71  ? 2.690   3.319   66.206  1.00 11.98  ? 158  ARG B CG  1 
ATOM   3568  C  CD  . ARG B  1 71  ? 1.512   2.861   65.311  1.00 11.48  ? 158  ARG B CD  1 
ATOM   3569  N  NE  . ARG B  1 71  ? 0.608   3.984   65.023  1.00 12.34  ? 158  ARG B NE  1 
ATOM   3570  C  CZ  . ARG B  1 71  ? -0.327  4.440   65.864  1.00 14.01  ? 158  ARG B CZ  1 
ATOM   3571  N  NH1 . ARG B  1 71  ? -0.512  3.887   67.053  1.00 12.15  ? 158  ARG B NH1 1 
ATOM   3572  N  NH2 . ARG B  1 71  ? -1.077  5.475   65.523  1.00 14.02  ? 158  ARG B NH2 1 
ATOM   3573  N  N   . SER B  1 72  ? 6.939   5.342   65.476  1.00 10.62  ? 159  SER B N   1 
ATOM   3574  C  CA  . SER B  1 72  ? 7.978   6.029   64.699  1.00 9.71   ? 159  SER B CA  1 
ATOM   3575  C  C   . SER B  1 72  ? 8.981   5.010   64.161  1.00 9.65   ? 159  SER B C   1 
ATOM   3576  O  O   . SER B  1 72  ? 9.028   3.861   64.635  1.00 8.66   ? 159  SER B O   1 
ATOM   3577  C  CB  . SER B  1 72  ? 8.716   7.075   65.553  1.00 9.91   ? 159  SER B CB  1 
ATOM   3578  O  OG  . SER B  1 72  ? 9.721   6.444   66.350  1.00 8.99   ? 159  SER B OG  1 
ATOM   3579  N  N   . PRO B  1 73  ? 9.794   5.419   63.173  1.00 10.18  ? 160  PRO B N   1 
ATOM   3580  C  CA  . PRO B  1 73  ? 10.874  4.553   62.686  1.00 10.04  ? 160  PRO B CA  1 
ATOM   3581  C  C   . PRO B  1 73  ? 12.023  4.407   63.679  1.00 10.40  ? 160  PRO B C   1 
ATOM   3582  O  O   . PRO B  1 73  ? 12.962  3.660   63.382  1.00 10.41  ? 160  PRO B O   1 
ATOM   3583  C  CB  . PRO B  1 73  ? 11.379  5.269   61.416  1.00 9.43   ? 160  PRO B CB  1 
ATOM   3584  C  CG  . PRO B  1 73  ? 10.296  6.308   61.077  1.00 10.95  ? 160  PRO B CG  1 
ATOM   3585  C  CD  . PRO B  1 73  ? 9.737   6.697   62.433  1.00 10.20  ? 160  PRO B CD  1 
ATOM   3586  N  N   . PHE B  1 74  ? 11.941  5.077   64.836  1.00 9.91   ? 161  PHE B N   1 
ATOM   3587  C  CA  . PHE B  1 74  ? 13.058  5.114   65.824  1.00 9.68   ? 161  PHE B CA  1 
ATOM   3588  C  C   . PHE B  1 74  ? 12.841  4.204   67.034  1.00 9.56   ? 161  PHE B C   1 
ATOM   3589  O  O   . PHE B  1 74  ? 13.670  4.158   67.955  1.00 9.50   ? 161  PHE B O   1 
ATOM   3590  C  CB  . PHE B  1 74  ? 13.327  6.553   66.268  1.00 9.80   ? 161  PHE B CB  1 
ATOM   3591  C  CG  . PHE B  1 74  ? 13.127  7.547   65.172  1.00 10.17  ? 161  PHE B CG  1 
ATOM   3592  C  CD1 . PHE B  1 74  ? 12.240  8.612   65.335  1.00 10.64  ? 161  PHE B CD1 1 
ATOM   3593  C  CD2 . PHE B  1 74  ? 13.764  7.373   63.930  1.00 11.31  ? 161  PHE B CD2 1 
ATOM   3594  C  CE1 . PHE B  1 74  ? 12.019  9.525   64.284  1.00 10.90  ? 161  PHE B CE1 1 
ATOM   3595  C  CE2 . PHE B  1 74  ? 13.543  8.270   62.871  1.00 12.27  ? 161  PHE B CE2 1 
ATOM   3596  C  CZ  . PHE B  1 74  ? 12.668  9.351   63.048  1.00 9.31   ? 161  PHE B CZ  1 
ATOM   3597  N  N   . ARG B  1 75  ? 11.738  3.466   67.011  1.00 8.88   ? 162  ARG B N   1 
ATOM   3598  C  CA  . ARG B  1 75  ? 11.408  2.529   68.079  1.00 7.78   ? 162  ARG B CA  1 
ATOM   3599  C  C   . ARG B  1 75  ? 11.916  1.120   67.779  1.00 7.92   ? 162  ARG B C   1 
ATOM   3600  O  O   . ARG B  1 75  ? 12.054  0.727   66.606  1.00 7.56   ? 162  ARG B O   1 
ATOM   3601  C  CB  . ARG B  1 75  ? 9.888   2.537   68.339  1.00 8.74   ? 162  ARG B CB  1 
ATOM   3602  C  CG  . ARG B  1 75  ? 9.321   3.895   68.740  1.00 7.54   ? 162  ARG B CG  1 
ATOM   3603  C  CD  . ARG B  1 75  ? 7.993   3.733   69.533  1.00 7.62   ? 162  ARG B CD  1 
ATOM   3604  N  NE  . ARG B  1 75  ? 8.228   3.365   70.936  1.00 7.81   ? 162  ARG B NE  1 
ATOM   3605  C  CZ  . ARG B  1 75  ? 7.271   3.276   71.859  1.00 7.77   ? 162  ARG B CZ  1 
ATOM   3606  N  NH1 . ARG B  1 75  ? 6.001   3.518   71.545  1.00 8.98   ? 162  ARG B NH1 1 
ATOM   3607  N  NH2 . ARG B  1 75  ? 7.581   2.944   73.098  1.00 6.06   ? 162  ARG B NH2 1 
ATOM   3608  N  N   . ALA B  1 76  ? 12.200  0.366   68.841  1.00 7.72   ? 163  ALA B N   1 
ATOM   3609  C  CA  . ALA B  1 76  ? 12.696  -1.014  68.736  1.00 7.93   ? 163  ALA B CA  1 
ATOM   3610  C  C   . ALA B  1 76  ? 12.349  -1.797  70.003  1.00 7.76   ? 163  ALA B C   1 
ATOM   3611  O  O   . ALA B  1 76  ? 12.286  -1.220  71.093  1.00 8.83   ? 163  ALA B O   1 
ATOM   3612  C  CB  . ALA B  1 76  ? 14.232  -0.997  68.541  1.00 8.23   ? 163  ALA B CB  1 
ATOM   3613  N  N   . LEU B  1 77  ? 12.153  -3.106  69.889  1.00 8.48   ? 164  LEU B N   1 
ATOM   3614  C  CA  . LEU B  1 77  ? 12.009  -3.913  71.101  1.00 7.99   ? 164  LEU B CA  1 
ATOM   3615  C  C   . LEU B  1 77  ? 13.404  -4.134  71.610  1.00 8.79   ? 164  LEU B C   1 
ATOM   3616  O  O   . LEU B  1 77  ? 14.263  -4.614  70.866  1.00 8.89   ? 164  LEU B O   1 
ATOM   3617  C  CB  . LEU B  1 77  ? 11.333  -5.262  70.839  1.00 7.91   ? 164  LEU B CB  1 
ATOM   3618  C  CG  . LEU B  1 77  ? 11.243  -6.267  72.009  1.00 7.99   ? 164  LEU B CG  1 
ATOM   3619  C  CD1 . LEU B  1 77  ? 10.424  -5.746  73.223  1.00 5.49   ? 164  LEU B CD1 1 
ATOM   3620  C  CD2 . LEU B  1 77  ? 10.653  -7.617  71.532  1.00 7.06   ? 164  LEU B CD2 1 
ATOM   3621  N  N   . ILE B  1 78  ? 13.615  -3.780  72.875  1.00 9.13   ? 165  ILE B N   1 
ATOM   3622  C  CA  . ILE B  1 78  ? 14.884  -4.054  73.567  1.00 9.06   ? 165  ILE B CA  1 
ATOM   3623  C  C   . ILE B  1 78  ? 14.642  -4.955  74.782  1.00 8.70   ? 165  ILE B C   1 
ATOM   3624  O  O   . ILE B  1 78  ? 13.530  -4.974  75.368  1.00 8.77   ? 165  ILE B O   1 
ATOM   3625  C  CB  . ILE B  1 78  ? 15.580  -2.739  74.021  1.00 9.19   ? 165  ILE B CB  1 
ATOM   3626  C  CG1 . ILE B  1 78  ? 14.609  -1.835  74.817  1.00 9.61   ? 165  ILE B CG1 1 
ATOM   3627  C  CG2 . ILE B  1 78  ? 16.178  -1.972  72.813  1.00 8.70   ? 165  ILE B CG2 1 
ATOM   3628  C  CD1 . ILE B  1 78  ? 15.313  -0.723  75.649  1.00 10.03  ? 165  ILE B CD1 1 
ATOM   3629  N  N   . SER B  1 79  ? 15.677  -5.695  75.175  1.00 7.87   ? 166  SER B N   1 
ATOM   3630  C  CA  . SER B  1 79  ? 15.612  -6.549  76.355  1.00 7.14   ? 166  SER B CA  1 
ATOM   3631  C  C   . SER B  1 79  ? 16.887  -6.332  77.145  1.00 7.72   ? 166  SER B C   1 
ATOM   3632  O  O   . SER B  1 79  ? 17.924  -5.911  76.600  1.00 8.08   ? 166  SER B O   1 
ATOM   3633  C  CB  . SER B  1 79  ? 15.432  -8.037  75.979  1.00 7.01   ? 166  SER B CB  1 
ATOM   3634  O  OG  . SER B  1 79  ? 16.606  -8.520  75.307  1.00 9.03   ? 166  SER B OG  1 
ATOM   3635  N  N   . TRP B  1 80  ? 16.806  -6.596  78.439  1.00 8.13   ? 167  TRP B N   1 
ATOM   3636  C  CA  . TRP B  1 80  ? 17.941  -6.402  79.343  1.00 8.28   ? 167  TRP B CA  1 
ATOM   3637  C  C   . TRP B  1 80  ? 17.766  -7.242  80.602  1.00 8.43   ? 167  TRP B C   1 
ATOM   3638  O  O   . TRP B  1 80  ? 16.670  -7.737  80.886  1.00 8.01   ? 167  TRP B O   1 
ATOM   3639  C  CB  . TRP B  1 80  ? 18.137  -4.906  79.682  1.00 7.44   ? 167  TRP B CB  1 
ATOM   3640  C  CG  . TRP B  1 80  ? 17.006  -4.218  80.470  1.00 8.39   ? 167  TRP B CG  1 
ATOM   3641  C  CD1 . TRP B  1 80  ? 16.970  -3.993  81.828  1.00 7.46   ? 167  TRP B CD1 1 
ATOM   3642  C  CD2 . TRP B  1 80  ? 15.805  -3.626  79.932  1.00 6.70   ? 167  TRP B CD2 1 
ATOM   3643  N  NE1 . TRP B  1 80  ? 15.807  -3.319  82.169  1.00 6.72   ? 167  TRP B NE1 1 
ATOM   3644  C  CE2 . TRP B  1 80  ? 15.084  -3.072  81.025  1.00 7.50   ? 167  TRP B CE2 1 
ATOM   3645  C  CE3 . TRP B  1 80  ? 15.261  -3.514  78.623  1.00 7.10   ? 167  TRP B CE3 1 
ATOM   3646  C  CZ2 . TRP B  1 80  ? 13.851  -2.408  80.861  1.00 6.06   ? 167  TRP B CZ2 1 
ATOM   3647  C  CZ3 . TRP B  1 80  ? 14.017  -2.878  78.458  1.00 7.86   ? 167  TRP B CZ3 1 
ATOM   3648  C  CH2 . TRP B  1 80  ? 13.324  -2.335  79.582  1.00 8.06   ? 167  TRP B CH2 1 
ATOM   3649  N  N   . GLU B  1 81  ? 18.862  -7.411  81.346  1.00 9.11   ? 168  GLU B N   1 
ATOM   3650  C  CA  . GLU B  1 81  ? 18.862  -8.258  82.536  1.00 11.11  ? 168  GLU B CA  1 
ATOM   3651  C  C   . GLU B  1 81  ? 17.897  -7.703  83.583  1.00 10.43  ? 168  GLU B C   1 
ATOM   3652  O  O   . GLU B  1 81  ? 17.933  -6.507  83.907  1.00 10.01  ? 168  GLU B O   1 
ATOM   3653  C  CB  . GLU B  1 81  ? 20.284  -8.353  83.102  1.00 10.62  ? 168  GLU B CB  1 
ATOM   3654  C  CG  . GLU B  1 81  ? 20.419  -9.122  84.415  1.00 14.05  ? 168  GLU B CG  1 
ATOM   3655  C  CD  . GLU B  1 81  ? 21.884  -9.114  84.891  1.00 15.32  ? 168  GLU B CD  1 
ATOM   3656  O  OE1 . GLU B  1 81  ? 22.747  -9.685  84.169  1.00 19.21  ? 168  GLU B OE1 1 
ATOM   3657  O  OE2 . GLU B  1 81  ? 22.175  -8.497  85.938  1.00 21.31  ? 168  GLU B OE2 1 
ATOM   3658  N  N   . MET B  1 82  ? 17.032  -8.572  84.100  1.00 11.04  ? 169  MET B N   1 
ATOM   3659  C  CA  . MET B  1 82  ? 15.967  -8.142  85.013  1.00 11.10  ? 169  MET B CA  1 
ATOM   3660  C  C   . MET B  1 82  ? 16.535  -7.369  86.197  1.00 10.32  ? 169  MET B C   1 
ATOM   3661  O  O   . MET B  1 82  ? 17.471  -7.840  86.868  1.00 9.15   ? 169  MET B O   1 
ATOM   3662  C  CB  . MET B  1 82  ? 15.199  -9.361  85.520  1.00 11.46  ? 169  MET B CB  1 
ATOM   3663  C  CG  . MET B  1 82  ? 14.061  -9.045  86.487  1.00 10.58  ? 169  MET B CG  1 
ATOM   3664  S  SD  . MET B  1 82  ? 13.171  -10.532 86.993  1.00 12.51  ? 169  MET B SD  1 
ATOM   3665  C  CE  . MET B  1 82  ? 14.342  -11.363 88.080  1.00 11.87  ? 169  MET B CE  1 
ATOM   3666  N  N   . GLY B  1 83  ? 15.970  -6.182  86.445  1.00 8.93   ? 170  GLY B N   1 
ATOM   3667  C  CA  . GLY B  1 83  ? 16.376  -5.373  87.590  1.00 9.41   ? 170  GLY B CA  1 
ATOM   3668  C  C   . GLY B  1 83  ? 17.199  -4.152  87.223  1.00 9.66   ? 170  GLY B C   1 
ATOM   3669  O  O   . GLY B  1 83  ? 17.107  -3.117  87.887  1.00 9.63   ? 170  GLY B O   1 
ATOM   3670  N  N   . GLN B  1 84  ? 18.065  -4.271  86.210  1.00 9.90   ? 171  GLN B N   1 
ATOM   3671  C  CA  . GLN B  1 84  ? 18.768  -3.090  85.698  1.00 10.42  ? 171  GLN B CA  1 
ATOM   3672  C  C   . GLN B  1 84  ? 17.781  -2.159  84.992  1.00 9.40   ? 171  GLN B C   1 
ATOM   3673  O  O   . GLN B  1 84  ? 16.687  -2.574  84.585  1.00 10.22  ? 171  GLN B O   1 
ATOM   3674  C  CB  . GLN B  1 84  ? 19.905  -3.474  84.734  1.00 9.97   ? 171  GLN B CB  1 
ATOM   3675  C  CG  . GLN B  1 84  ? 21.085  -4.196  85.382  1.00 12.16  ? 171  GLN B CG  1 
ATOM   3676  C  CD  . GLN B  1 84  ? 22.135  -4.622  84.362  1.00 13.88  ? 171  GLN B CD  1 
ATOM   3677  O  OE1 . GLN B  1 84  ? 21.840  -4.743  83.166  1.00 15.31  ? 171  GLN B OE1 1 
ATOM   3678  N  NE2 . GLN B  1 84  ? 23.382  -4.815  84.828  1.00 17.65  ? 171  GLN B NE2 1 
ATOM   3679  N  N   . ALA B  1 85  ? 18.151  -0.891  84.880  1.00 9.77   ? 172  ALA B N   1 
ATOM   3680  C  CA  . ALA B  1 85  ? 17.412  0.077   84.067  1.00 8.78   ? 172  ALA B CA  1 
ATOM   3681  C  C   . ALA B  1 85  ? 17.940  -0.011  82.623  1.00 9.08   ? 172  ALA B C   1 
ATOM   3682  O  O   . ALA B  1 85  ? 19.092  -0.409  82.417  1.00 9.46   ? 172  ALA B O   1 
ATOM   3683  C  CB  . ALA B  1 85  ? 17.595  1.471   84.639  1.00 8.64   ? 172  ALA B CB  1 
ATOM   3684  N  N   . PRO B  1 86  ? 17.096  0.312   81.619  1.00 9.35   ? 173  PRO B N   1 
ATOM   3685  C  CA  . PRO B  1 86  ? 17.526  0.169   80.223  1.00 8.89   ? 173  PRO B CA  1 
ATOM   3686  C  C   . PRO B  1 86  ? 18.395  1.333   79.722  1.00 10.15  ? 173  PRO B C   1 
ATOM   3687  O  O   . PRO B  1 86  ? 17.909  2.478   79.568  1.00 10.03  ? 173  PRO B O   1 
ATOM   3688  C  CB  . PRO B  1 86  ? 16.195  0.070   79.473  1.00 8.61   ? 173  PRO B CB  1 
ATOM   3689  C  CG  . PRO B  1 86  ? 15.252  0.945   80.287  1.00 8.37   ? 173  PRO B CG  1 
ATOM   3690  C  CD  . PRO B  1 86  ? 15.681  0.750   81.721  1.00 8.32   ? 173  PRO B CD  1 
ATOM   3691  N  N   . SER B  1 87  ? 19.684  1.050   79.483  1.00 10.50  ? 174  SER B N   1 
ATOM   3692  C  CA  . SER B  1 87  ? 20.596  2.055   78.918  1.00 10.34  ? 174  SER B CA  1 
ATOM   3693  C  C   . SER B  1 87  ? 20.995  1.654   77.488  1.00 9.92   ? 174  SER B C   1 
ATOM   3694  O  O   . SER B  1 87  ? 20.743  0.521   77.061  1.00 8.73   ? 174  SER B O   1 
ATOM   3695  C  CB  . SER B  1 87  ? 21.862  2.177   79.781  1.00 11.17  ? 174  SER B CB  1 
ATOM   3696  O  OG  . SER B  1 87  ? 22.679  1.013   79.623  1.00 12.29  ? 174  SER B OG  1 
ATOM   3697  N  N   . PRO B  1 88  ? 21.626  2.584   76.740  1.00 10.14  ? 175  PRO B N   1 
ATOM   3698  C  CA  . PRO B  1 88  ? 22.208  2.217   75.442  1.00 10.49  ? 175  PRO B CA  1 
ATOM   3699  C  C   . PRO B  1 88  ? 23.334  1.180   75.545  1.00 10.73  ? 175  PRO B C   1 
ATOM   3700  O  O   . PRO B  1 88  ? 23.754  0.639   74.510  1.00 10.92  ? 175  PRO B O   1 
ATOM   3701  C  CB  . PRO B  1 88  ? 22.823  3.533   74.935  1.00 10.26  ? 175  PRO B CB  1 
ATOM   3702  C  CG  . PRO B  1 88  ? 22.165  4.627   75.694  1.00 11.76  ? 175  PRO B CG  1 
ATOM   3703  C  CD  . PRO B  1 88  ? 21.837  4.012   77.053  1.00 10.41  ? 175  PRO B CD  1 
ATOM   3704  N  N   . TYR B  1 89  ? 23.829  0.945   76.758  1.00 9.78   ? 176  TYR B N   1 
ATOM   3705  C  CA  . TYR B  1 89  ? 24.996  0.075   76.996  1.00 10.49  ? 176  TYR B CA  1 
ATOM   3706  C  C   . TYR B  1 89  ? 24.686  -1.365  77.462  1.00 10.12  ? 176  TYR B C   1 
ATOM   3707  O  O   . TYR B  1 89  ? 25.567  -2.239  77.408  1.00 10.68  ? 176  TYR B O   1 
ATOM   3708  C  CB  . TYR B  1 89  ? 25.953  0.738   78.011  1.00 9.85   ? 176  TYR B CB  1 
ATOM   3709  C  CG  . TYR B  1 89  ? 26.116  2.226   77.820  1.00 9.95   ? 176  TYR B CG  1 
ATOM   3710  C  CD1 . TYR B  1 89  ? 25.892  3.105   78.876  1.00 8.66   ? 176  TYR B CD1 1 
ATOM   3711  C  CD2 . TYR B  1 89  ? 26.463  2.760   76.570  1.00 10.03  ? 176  TYR B CD2 1 
ATOM   3712  C  CE1 . TYR B  1 89  ? 26.034  4.504   78.705  1.00 9.95   ? 176  TYR B CE1 1 
ATOM   3713  C  CE2 . TYR B  1 89  ? 26.607  4.152   76.391  1.00 10.15  ? 176  TYR B CE2 1 
ATOM   3714  C  CZ  . TYR B  1 89  ? 26.386  5.004   77.453  1.00 9.72   ? 176  TYR B CZ  1 
ATOM   3715  O  OH  . TYR B  1 89  ? 26.520  6.366   77.271  1.00 11.20  ? 176  TYR B OH  1 
ATOM   3716  N  N   . ASN B  1 90  ? 23.481  -1.607  77.966  1.00 9.63   ? 177  ASN B N   1 
ATOM   3717  C  CA  . ASN B  1 90  ? 23.148  -2.928  78.526  1.00 9.80   ? 177  ASN B CA  1 
ATOM   3718  C  C   . ASN B  1 90  ? 21.930  -3.570  77.875  1.00 9.83   ? 177  ASN B C   1 
ATOM   3719  O  O   . ASN B  1 90  ? 21.366  -4.517  78.425  1.00 10.44  ? 177  ASN B O   1 
ATOM   3720  C  CB  . ASN B  1 90  ? 22.897  -2.816  80.050  1.00 9.83   ? 177  ASN B CB  1 
ATOM   3721  C  CG  . ASN B  1 90  ? 21.553  -2.134  80.372  1.00 10.35  ? 177  ASN B CG  1 
ATOM   3722  O  OD1 . ASN B  1 90  ? 21.096  -1.245  79.618  1.00 11.64  ? 177  ASN B OD1 1 
ATOM   3723  N  ND2 . ASN B  1 90  ? 20.889  -2.584  81.454  1.00 9.93   ? 177  ASN B ND2 1 
ATOM   3724  N  N   . THR B  1 91  ? 21.513  -3.068  76.710  1.00 9.70   ? 178  THR B N   1 
ATOM   3725  C  CA  . THR B  1 91  ? 20.241  -3.520  76.114  1.00 10.18  ? 178  THR B CA  1 
ATOM   3726  C  C   . THR B  1 91  ? 20.493  -4.276  74.797  1.00 10.87  ? 178  THR B C   1 
ATOM   3727  O  O   . THR B  1 91  ? 21.354  -3.871  73.983  1.00 10.91  ? 178  THR B O   1 
ATOM   3728  C  CB  . THR B  1 91  ? 19.266  -2.350  75.838  1.00 10.11  ? 178  THR B CB  1 
ATOM   3729  O  OG1 . THR B  1 91  ? 19.992  -1.280  75.232  1.00 10.02  ? 178  THR B OG1 1 
ATOM   3730  C  CG2 . THR B  1 91  ? 18.563  -1.850  77.136  1.00 9.87   ? 178  THR B CG2 1 
ATOM   3731  N  N   . ARG B  1 92  ? 19.749  -5.357  74.589  1.00 11.32  ? 179  ARG B N   1 
ATOM   3732  C  CA  . ARG B  1 92  ? 19.792  -6.106  73.334  1.00 12.08  ? 179  ARG B CA  1 
ATOM   3733  C  C   . ARG B  1 92  ? 18.599  -5.705  72.449  1.00 10.96  ? 179  ARG B C   1 
ATOM   3734  O  O   . ARG B  1 92  ? 17.461  -5.722  72.913  1.00 10.52  ? 179  ARG B O   1 
ATOM   3735  C  CB  . ARG B  1 92  ? 19.754  -7.621  73.622  1.00 11.88  ? 179  ARG B CB  1 
ATOM   3736  C  CG  . ARG B  1 92  ? 19.764  -8.515  72.355  1.00 13.86  ? 179  ARG B CG  1 
ATOM   3737  C  CD  . ARG B  1 92  ? 19.925  -10.046 72.683  1.00 16.30  ? 179  ARG B CD  1 
ATOM   3738  N  NE  . ARG B  1 92  ? 20.435  -10.268 74.043  1.00 25.69  ? 179  ARG B NE  1 
ATOM   3739  C  CZ  . ARG B  1 92  ? 21.182  -11.296 74.450  1.00 30.08  ? 179  ARG B CZ  1 
ATOM   3740  N  NH1 . ARG B  1 92  ? 21.559  -12.250 73.605  1.00 33.59  ? 179  ARG B NH1 1 
ATOM   3741  N  NH2 . ARG B  1 92  ? 21.579  -11.361 75.720  1.00 32.19  ? 179  ARG B NH2 1 
ATOM   3742  N  N   . VAL B  1 93  ? 18.860  -5.323  71.193  1.00 9.75   ? 180  VAL B N   1 
ATOM   3743  C  CA  . VAL B  1 93  ? 17.772  -5.055  70.249  1.00 9.20   ? 180  VAL B CA  1 
ATOM   3744  C  C   . VAL B  1 93  ? 17.236  -6.397  69.687  1.00 10.11  ? 180  VAL B C   1 
ATOM   3745  O  O   . VAL B  1 93  ? 17.946  -7.159  69.002  1.00 9.24   ? 180  VAL B O   1 
ATOM   3746  C  CB  . VAL B  1 93  ? 18.164  -4.106  69.111  1.00 9.68   ? 180  VAL B CB  1 
ATOM   3747  C  CG1 . VAL B  1 93  ? 16.962  -3.875  68.191  1.00 8.89   ? 180  VAL B CG1 1 
ATOM   3748  C  CG2 . VAL B  1 93  ? 18.727  -2.778  69.651  1.00 9.25   ? 180  VAL B CG2 1 
ATOM   3749  N  N   . GLU B  1 94  ? 15.984  -6.666  70.022  1.00 9.61   ? 181  GLU B N   1 
ATOM   3750  C  CA  . GLU B  1 94  ? 15.297  -7.910  69.687  1.00 9.90   ? 181  GLU B CA  1 
ATOM   3751  C  C   . GLU B  1 94  ? 14.724  -7.833  68.264  1.00 10.09  ? 181  GLU B C   1 
ATOM   3752  O  O   . GLU B  1 94  ? 14.671  -8.832  67.566  1.00 10.63  ? 181  GLU B O   1 
ATOM   3753  C  CB  . GLU B  1 94  ? 14.157  -8.165  70.696  1.00 9.60   ? 181  GLU B CB  1 
ATOM   3754  C  CG  . GLU B  1 94  ? 14.650  -8.468  72.128  1.00 11.55  ? 181  GLU B CG  1 
ATOM   3755  C  CD  . GLU B  1 94  ? 15.140  -9.903  72.313  1.00 13.80  ? 181  GLU B CD  1 
ATOM   3756  O  OE1 . GLU B  1 94  ? 14.691  -10.800 71.562  1.00 12.31  ? 181  GLU B OE1 1 
ATOM   3757  O  OE2 . GLU B  1 94  ? 15.968  -10.144 73.226  1.00 14.17  ? 181  GLU B OE2 1 
ATOM   3758  N  N   . CYS B  1 95  ? 14.246  -6.645  67.881  1.00 10.09  ? 182  CYS B N   1 
ATOM   3759  C  CA  . CYS B  1 95  ? 13.658  -6.386  66.566  1.00 9.84   ? 182  CYS B CA  1 
ATOM   3760  C  C   . CYS B  1 95  ? 13.281  -4.908  66.486  1.00 9.57   ? 182  CYS B C   1 
ATOM   3761  O  O   . CYS B  1 95  ? 13.268  -4.201  67.500  1.00 9.08   ? 182  CYS B O   1 
ATOM   3762  C  CB  . CYS B  1 95  ? 12.452  -7.297  66.247  1.00 10.19  ? 182  CYS B CB  1 
ATOM   3763  S  SG  . CYS B  1 95  ? 11.199  -7.547  67.582  1.00 13.43  ? 182  CYS B SG  1 
ATOM   3764  N  N   . ILE B  1 96  ? 12.970  -4.452  65.278  1.00 8.94   ? 183  ILE B N   1 
ATOM   3765  C  CA  . ILE B  1 96  ? 12.688  -3.042  65.053  1.00 8.00   ? 183  ILE B CA  1 
ATOM   3766  C  C   . ILE B  1 96  ? 11.170  -2.844  64.868  1.00 9.25   ? 183  ILE B C   1 
ATOM   3767  O  O   . ILE B  1 96  ? 10.545  -3.541  64.052  1.00 8.90   ? 183  ILE B O   1 
ATOM   3768  C  CB  . ILE B  1 96  ? 13.458  -2.513  63.814  1.00 8.38   ? 183  ILE B CB  1 
ATOM   3769  C  CG1 . ILE B  1 96  ? 14.967  -2.823  63.920  1.00 7.75   ? 183  ILE B CG1 1 
ATOM   3770  C  CG2 . ILE B  1 96  ? 13.188  -1.005  63.603  1.00 6.17   ? 183  ILE B CG2 1 
ATOM   3771  C  CD1 . ILE B  1 96  ? 15.668  -2.257  65.193  1.00 8.15   ? 183  ILE B CD1 1 
ATOM   3772  N  N   . GLY B  1 97  ? 10.603  -1.886  65.606  1.00 8.40   ? 184  GLY B N   1 
ATOM   3773  C  CA  . GLY B  1 97  ? 9.173   -1.576  65.488  1.00 8.61   ? 184  GLY B CA  1 
ATOM   3774  C  C   . GLY B  1 97  ? 8.540   -1.015  66.738  1.00 9.19   ? 184  GLY B C   1 
ATOM   3775  O  O   . GLY B  1 97  ? 9.248   -0.627  67.685  1.00 9.45   ? 184  GLY B O   1 
ATOM   3776  N  N   . TRP B  1 98  ? 7.202   -0.972  66.725  1.00 8.66   ? 185  TRP B N   1 
ATOM   3777  C  CA  . TRP B  1 98  ? 6.426   -0.183  67.699  1.00 8.82   ? 185  TRP B CA  1 
ATOM   3778  C  C   . TRP B  1 98  ? 5.255   -0.974  68.314  1.00 8.08   ? 185  TRP B C   1 
ATOM   3779  O  O   . TRP B  1 98  ? 4.402   -0.404  68.982  1.00 7.87   ? 185  TRP B O   1 
ATOM   3780  C  CB  . TRP B  1 98  ? 5.949   1.159   67.093  1.00 8.51   ? 185  TRP B CB  1 
ATOM   3781  C  CG  . TRP B  1 98  ? 5.467   1.098   65.655  1.00 8.59   ? 185  TRP B CG  1 
ATOM   3782  C  CD1 . TRP B  1 98  ? 6.042   1.724   64.576  1.00 9.40   ? 185  TRP B CD1 1 
ATOM   3783  C  CD2 . TRP B  1 98  ? 4.316   0.386   65.137  1.00 8.79   ? 185  TRP B CD2 1 
ATOM   3784  N  NE1 . TRP B  1 98  ? 5.335   1.438   63.429  1.00 9.54   ? 185  TRP B NE1 1 
ATOM   3785  C  CE2 . TRP B  1 98  ? 4.265   0.635   63.746  1.00 9.32   ? 185  TRP B CE2 1 
ATOM   3786  C  CE3 . TRP B  1 98  ? 3.317   -0.417  65.718  1.00 8.64   ? 185  TRP B CE3 1 
ATOM   3787  C  CZ2 . TRP B  1 98  ? 3.268   0.089   62.917  1.00 9.48   ? 185  TRP B CZ2 1 
ATOM   3788  C  CZ3 . TRP B  1 98  ? 2.333   -0.973  64.892  1.00 10.22  ? 185  TRP B CZ3 1 
ATOM   3789  C  CH2 . TRP B  1 98  ? 2.311   -0.710  63.511  1.00 8.76   ? 185  TRP B CH2 1 
ATOM   3790  N  N   . SER B  1 99  ? 5.249   -2.294  68.090  1.00 8.09   ? 186  SER B N   1 
ATOM   3791  C  CA  . SER B  1 99  ? 4.371   -3.238  68.801  1.00 8.89   ? 186  SER B CA  1 
ATOM   3792  C  C   . SER B  1 99  ? 5.120   -4.541  68.810  1.00 8.97   ? 186  SER B C   1 
ATOM   3793  O  O   . SER B  1 99  ? 5.829   -4.861  67.815  1.00 9.53   ? 186  SER B O   1 
ATOM   3794  C  CB  . SER B  1 99  ? 3.012   -3.431  68.115  1.00 8.54   ? 186  SER B CB  1 
ATOM   3795  O  OG  . SER B  1 99  ? 2.211   -4.339  68.871  1.00 8.89   ? 186  SER B OG  1 
ATOM   3796  N  N   . SER B  1 100 ? 5.006   -5.291  69.906  1.00 8.75   ? 187  SER B N   1 
ATOM   3797  C  CA  . SER B  1 100 ? 5.826   -6.494  70.050  1.00 8.47   ? 187  SER B CA  1 
ATOM   3798  C  C   . SER B  1 100 ? 5.250   -7.569  70.950  1.00 9.02   ? 187  SER B C   1 
ATOM   3799  O  O   . SER B  1 100 ? 4.352   -7.330  71.753  1.00 9.73   ? 187  SER B O   1 
ATOM   3800  C  CB  . SER B  1 100 ? 7.260   -6.154  70.536  1.00 7.52   ? 187  SER B CB  1 
ATOM   3801  O  OG  . SER B  1 100 ? 7.302   -6.036  71.956  1.00 10.53  ? 187  SER B OG  1 
ATOM   3802  N  N   . THR B  1 101 ? 5.792   -8.763  70.775  1.00 8.88   ? 188  THR B N   1 
ATOM   3803  C  CA  . THR B  1 101 ? 5.690   -9.837  71.752  1.00 8.43   ? 188  THR B CA  1 
ATOM   3804  C  C   . THR B  1 101 ? 6.990   -10.642 71.717  1.00 8.79   ? 188  THR B C   1 
ATOM   3805  O  O   . THR B  1 101 ? 7.782   -10.521 70.771  1.00 8.41   ? 188  THR B O   1 
ATOM   3806  C  CB  . THR B  1 101 ? 4.460   -10.753 71.491  1.00 8.34   ? 188  THR B CB  1 
ATOM   3807  O  OG1 . THR B  1 101 ? 4.298   -11.650 72.599  1.00 8.24   ? 188  THR B OG1 1 
ATOM   3808  C  CG2 . THR B  1 101 ? 4.621   -11.549 70.177  1.00 8.70   ? 188  THR B CG2 1 
ATOM   3809  N  N   . SER B  1 102 ? 7.205   -11.448 72.752  1.00 9.27   ? 189  SER B N   1 
ATOM   3810  C  CA  . SER B  1 102 ? 8.376   -12.316 72.824  1.00 9.55   ? 189  SER B CA  1 
ATOM   3811  C  C   . SER B  1 102 ? 8.087   -13.500 73.730  1.00 9.87   ? 189  SER B C   1 
ATOM   3812  O  O   . SER B  1 102 ? 7.371   -13.355 74.721  1.00 9.34   ? 189  SER B O   1 
ATOM   3813  C  CB  . SER B  1 102 ? 9.577   -11.559 73.375  1.00 9.72   ? 189  SER B CB  1 
ATOM   3814  O  OG  . SER B  1 102 ? 10.779  -12.285 73.105  1.00 9.94   ? 189  SER B OG  1 
ATOM   3815  N  N   . CYS B  1 103 ? 8.658   -14.662 73.407  1.00 9.25   ? 190  CYS B N   1 
ATOM   3816  C  CA  . CYS B  1 103 ? 8.631   -15.813 74.318  1.00 9.88   ? 190  CYS B CA  1 
ATOM   3817  C  C   . CYS B  1 103 ? 9.720   -16.841 73.975  1.00 10.29  ? 190  CYS B C   1 
ATOM   3818  O  O   . CYS B  1 103 ? 10.210  -16.907 72.845  1.00 10.33  ? 190  CYS B O   1 
ATOM   3819  C  CB  . CYS B  1 103 ? 7.251   -16.492 74.339  1.00 9.37   ? 190  CYS B CB  1 
ATOM   3820  S  SG  . CYS B  1 103 ? 6.520   -16.808 72.695  1.00 12.28  ? 190  CYS B SG  1 
ATOM   3821  N  N   . HIS B  1 104 ? 10.069  -17.651 74.967  1.00 10.99  ? 191  HIS B N   1 
ATOM   3822  C  CA  . HIS B  1 104 ? 11.075  -18.689 74.792  1.00 10.96  ? 191  HIS B CA  1 
ATOM   3823  C  C   . HIS B  1 104 ? 10.385  -20.055 74.785  1.00 11.59  ? 191  HIS B C   1 
ATOM   3824  O  O   . HIS B  1 104 ? 9.522   -20.347 75.634  1.00 11.47  ? 191  HIS B O   1 
ATOM   3825  C  CB  . HIS B  1 104 ? 12.093  -18.587 75.932  1.00 11.10  ? 191  HIS B CB  1 
ATOM   3826  C  CG  . HIS B  1 104 ? 13.425  -19.194 75.614  1.00 11.06  ? 191  HIS B CG  1 
ATOM   3827  N  ND1 . HIS B  1 104 ? 13.662  -20.546 75.676  1.00 11.21  ? 191  HIS B ND1 1 
ATOM   3828  C  CD2 . HIS B  1 104 ? 14.603  -18.619 75.262  1.00 11.69  ? 191  HIS B CD2 1 
ATOM   3829  C  CE1 . HIS B  1 104 ? 14.926  -20.784 75.364  1.00 11.18  ? 191  HIS B CE1 1 
ATOM   3830  N  NE2 . HIS B  1 104 ? 15.522  -19.629 75.121  1.00 10.90  ? 191  HIS B NE2 1 
ATOM   3831  N  N   . ASP B  1 105 ? 10.717  -20.886 73.802  1.00 12.06  ? 192  ASP B N   1 
ATOM   3832  C  CA  . ASP B  1 105 ? 10.064  -22.202 73.729  1.00 12.31  ? 192  ASP B CA  1 
ATOM   3833  C  C   . ASP B  1 105 ? 10.802  -23.304 74.479  1.00 12.47  ? 192  ASP B C   1 
ATOM   3834  O  O   . ASP B  1 105 ? 10.398  -24.468 74.423  1.00 12.58  ? 192  ASP B O   1 
ATOM   3835  C  CB  . ASP B  1 105 ? 9.788   -22.607 72.271  1.00 12.70  ? 192  ASP B CB  1 
ATOM   3836  C  CG  . ASP B  1 105 ? 11.051  -22.774 71.450  1.00 12.78  ? 192  ASP B CG  1 
ATOM   3837  O  OD1 . ASP B  1 105 ? 12.160  -22.866 72.031  1.00 10.72  ? 192  ASP B OD1 1 
ATOM   3838  O  OD2 . ASP B  1 105 ? 10.922  -22.809 70.199  1.00 13.71  ? 192  ASP B OD2 1 
ATOM   3839  N  N   . GLY B  1 106 ? 11.869  -22.933 75.180  1.00 12.83  ? 193  GLY B N   1 
ATOM   3840  C  CA  . GLY B  1 106 ? 12.704  -23.911 75.901  1.00 13.03  ? 193  GLY B CA  1 
ATOM   3841  C  C   . GLY B  1 106 ? 14.033  -24.133 75.204  1.00 13.53  ? 193  GLY B C   1 
ATOM   3842  O  O   . GLY B  1 106 ? 15.047  -24.457 75.843  1.00 13.73  ? 193  GLY B O   1 
ATOM   3843  N  N   . MET B  1 107 ? 14.009  -23.967 73.886  1.00 13.77  ? 194  MET B N   1 
ATOM   3844  C  CA  . MET B  1 107 ? 15.201  -24.028 73.039  1.00 14.03  ? 194  MET B CA  1 
ATOM   3845  C  C   . MET B  1 107 ? 15.759  -22.640 72.699  1.00 13.50  ? 194  MET B C   1 
ATOM   3846  O  O   . MET B  1 107 ? 16.954  -22.346 72.953  1.00 12.85  ? 194  MET B O   1 
ATOM   3847  C  CB  . MET B  1 107 ? 14.883  -24.776 71.739  1.00 13.96  ? 194  MET B CB  1 
ATOM   3848  C  CG  . MET B  1 107 ? 14.419  -26.211 71.949  1.00 17.75  ? 194  MET B CG  1 
ATOM   3849  S  SD  . MET B  1 107 ? 15.702  -27.260 72.663  1.00 24.73  ? 194  MET B SD  1 
ATOM   3850  C  CE  . MET B  1 107 ? 16.858  -27.322 71.295  1.00 24.23  ? 194  MET B CE  1 
ATOM   3851  N  N   . SER B  1 108 ? 14.912  -21.803 72.097  1.00 12.99  ? 195  SER B N   1 
ATOM   3852  C  CA  . SER B  1 108 ? 15.311  -20.458 71.698  1.00 12.85  ? 195  SER B CA  1 
ATOM   3853  C  C   . SER B  1 108 ? 14.173  -19.456 71.883  1.00 12.20  ? 195  SER B C   1 
ATOM   3854  O  O   . SER B  1 108 ? 13.017  -19.855 72.075  1.00 11.48  ? 195  SER B O   1 
ATOM   3855  C  CB  . SER B  1 108 ? 15.734  -20.428 70.219  1.00 13.16  ? 195  SER B CB  1 
ATOM   3856  O  OG  . SER B  1 108 ? 16.874  -21.231 69.969  1.00 15.45  ? 195  SER B OG  1 
ATOM   3857  N  N   . ARG B  1 109 ? 14.520  -18.166 71.775  1.00 11.58  ? 196  ARG B N   1 
ATOM   3858  C  CA  . ARG B  1 109 ? 13.566  -17.057 71.927  1.00 11.62  ? 196  ARG B CA  1 
ATOM   3859  C  C   . ARG B  1 109 ? 12.994  -16.608 70.591  1.00 11.38  ? 196  ARG B C   1 
ATOM   3860  O  O   . ARG B  1 109 ? 13.742  -16.346 69.638  1.00 11.70  ? 196  ARG B O   1 
ATOM   3861  C  CB  . ARG B  1 109 ? 14.198  -15.851 72.647  1.00 11.37  ? 196  ARG B CB  1 
ATOM   3862  C  CG  . ARG B  1 109 ? 13.250  -14.612 72.769  1.00 11.37  ? 196  ARG B CG  1 
ATOM   3863  C  CD  . ARG B  1 109 ? 13.697  -13.627 73.874  1.00 11.71  ? 196  ARG B CD  1 
ATOM   3864  N  NE  . ARG B  1 109 ? 13.593  -14.227 75.213  1.00 10.38  ? 196  ARG B NE  1 
ATOM   3865  C  CZ  . ARG B  1 109 ? 12.447  -14.410 75.875  1.00 10.77  ? 196  ARG B CZ  1 
ATOM   3866  N  NH1 . ARG B  1 109 ? 12.468  -14.970 77.078  1.00 9.18   ? 196  ARG B NH1 1 
ATOM   3867  N  NH2 . ARG B  1 109 ? 11.280  -14.045 75.340  1.00 7.78   ? 196  ARG B NH2 1 
ATOM   3868  N  N   . MET B  1 110 ? 11.668  -16.497 70.539  1.00 10.11  ? 197  MET B N   1 
ATOM   3869  C  CA  . MET B  1 110 ? 11.003  -15.879 69.408  1.00 10.03  ? 197  MET B CA  1 
ATOM   3870  C  C   . MET B  1 110 ? 10.665  -14.447 69.802  1.00 9.62   ? 197  MET B C   1 
ATOM   3871  O  O   . MET B  1 110 ? 10.155  -14.222 70.902  1.00 8.80   ? 197  MET B O   1 
ATOM   3872  C  CB  . MET B  1 110 ? 9.714   -16.621 69.052  1.00 10.03  ? 197  MET B CB  1 
ATOM   3873  C  CG  . MET B  1 110 ? 8.946   -15.968 67.878  1.00 10.11  ? 197  MET B CG  1 
ATOM   3874  S  SD  . MET B  1 110 ? 7.412   -16.820 67.436  1.00 10.66  ? 197  MET B SD  1 
ATOM   3875  C  CE  . MET B  1 110 ? 6.384   -16.527 68.895  1.00 10.88  ? 197  MET B CE  1 
ATOM   3876  N  N   . SER B  1 111 ? 10.952  -13.501 68.913  1.00 8.65   ? 198  SER B N   1 
ATOM   3877  C  CA  . SER B  1 111 ? 10.545  -12.102 69.114  1.00 9.49   ? 198  SER B CA  1 
ATOM   3878  C  C   . SER B  1 111 ? 9.886   -11.576 67.864  1.00 9.18   ? 198  SER B C   1 
ATOM   3879  O  O   . SER B  1 111 ? 10.349  -11.855 66.744  1.00 9.57   ? 198  SER B O   1 
ATOM   3880  C  CB  . SER B  1 111 ? 11.747  -11.244 69.504  1.00 9.04   ? 198  SER B CB  1 
ATOM   3881  O  OG  . SER B  1 111 ? 12.211  -11.635 70.790  1.00 9.73   ? 198  SER B OG  1 
ATOM   3882  N  N   . ILE B  1 112 ? 8.793   -10.830 68.047  1.00 9.08   ? 199  ILE B N   1 
ATOM   3883  C  CA  . ILE B  1 112 ? 8.052   -10.283 66.923  1.00 8.90   ? 199  ILE B CA  1 
ATOM   3884  C  C   . ILE B  1 112 ? 7.865   -8.783  67.111  1.00 9.47   ? 199  ILE B C   1 
ATOM   3885  O  O   . ILE B  1 112 ? 7.464   -8.353  68.195  1.00 8.58   ? 199  ILE B O   1 
ATOM   3886  C  CB  . ILE B  1 112 ? 6.642   -10.941 66.785  1.00 10.03  ? 199  ILE B CB  1 
ATOM   3887  C  CG1 . ILE B  1 112 ? 6.758   -12.481 66.712  1.00 10.81  ? 199  ILE B CG1 1 
ATOM   3888  C  CG2 . ILE B  1 112 ? 5.848   -10.304 65.603  1.00 8.63   ? 199  ILE B CG2 1 
ATOM   3889  C  CD1 . ILE B  1 112 ? 5.424   -13.215 66.696  1.00 9.14   ? 199  ILE B CD1 1 
ATOM   3890  N  N   . CYS B  1 113 ? 8.156   -8.002  66.058  1.00 9.04   ? 200  CYS B N   1 
ATOM   3891  C  CA  . CYS B  1 113 ? 7.916   -6.550  66.042  1.00 9.78   ? 200  CYS B CA  1 
ATOM   3892  C  C   . CYS B  1 113 ? 7.143   -6.171  64.801  1.00 9.81   ? 200  CYS B C   1 
ATOM   3893  O  O   . CYS B  1 113 ? 7.442   -6.690  63.702  1.00 10.59  ? 200  CYS B O   1 
ATOM   3894  C  CB  . CYS B  1 113 ? 9.238   -5.782  66.018  1.00 9.34   ? 200  CYS B CB  1 
ATOM   3895  S  SG  . CYS B  1 113 ? 10.146  -5.791  67.561  1.00 13.92  ? 200  CYS B SG  1 
ATOM   3896  N  N   . MET B  1 114 ? 6.147   -5.303  64.969  1.00 9.54   ? 201  MET B N   1 
ATOM   3897  C  CA  . MET B  1 114 ? 5.446   -4.681  63.841  1.00 9.48   ? 201  MET B CA  1 
ATOM   3898  C  C   . MET B  1 114 ? 6.060   -3.316  63.597  1.00 9.69   ? 201  MET B C   1 
ATOM   3899  O  O   . MET B  1 114 ? 6.380   -2.615  64.535  1.00 9.08   ? 201  MET B O   1 
ATOM   3900  C  CB  . MET B  1 114 ? 3.972   -4.489  64.145  1.00 9.87   ? 201  MET B CB  1 
ATOM   3901  C  CG  . MET B  1 114 ? 3.155   -5.745  63.931  1.00 10.08  ? 201  MET B CG  1 
ATOM   3902  S  SD  . MET B  1 114 ? 3.516   -7.021  65.140  1.00 12.29  ? 201  MET B SD  1 
ATOM   3903  C  CE  . MET B  1 114 ? 2.059   -8.032  64.842  1.00 10.69  ? 201  MET B CE  1 
ATOM   3904  N  N   . SER B  1 115 ? 6.218   -2.941  62.335  1.00 10.08  ? 202  SER B N   1 
ATOM   3905  C  CA  . SER B  1 115 ? 6.665   -1.586  62.041  1.00 10.94  ? 202  SER B CA  1 
ATOM   3906  C  C   . SER B  1 115 ? 6.052   -1.108  60.732  1.00 11.01  ? 202  SER B C   1 
ATOM   3907  O  O   . SER B  1 115 ? 5.387   -1.880  60.035  1.00 11.34  ? 202  SER B O   1 
ATOM   3908  C  CB  . SER B  1 115 ? 8.206   -1.539  61.963  1.00 11.61  ? 202  SER B CB  1 
ATOM   3909  O  OG  . SER B  1 115 ? 8.654   -2.008  60.710  1.00 14.60  ? 202  SER B OG  1 
ATOM   3910  N  N   . GLY B  1 116 ? 6.305   0.149   60.382  1.00 9.62   ? 203  GLY B N   1 
ATOM   3911  C  CA  . GLY B  1 116 ? 5.808   0.689   59.114  1.00 10.20  ? 203  GLY B CA  1 
ATOM   3912  C  C   . GLY B  1 116 ? 4.699   1.711   59.316  1.00 9.83   ? 203  GLY B C   1 
ATOM   3913  O  O   . GLY B  1 116 ? 4.379   2.066   60.459  1.00 10.15  ? 203  GLY B O   1 
ATOM   3914  N  N   . PRO B  1 117 ? 4.087   2.176   58.207  1.00 10.06  ? 204  PRO B N   1 
ATOM   3915  C  CA  . PRO B  1 117 ? 3.039   3.186   58.314  1.00 10.19  ? 204  PRO B CA  1 
ATOM   3916  C  C   . PRO B  1 117 ? 1.712   2.543   58.761  1.00 10.98  ? 204  PRO B C   1 
ATOM   3917  O  O   . PRO B  1 117 ? 1.543   1.315   58.617  1.00 10.20  ? 204  PRO B O   1 
ATOM   3918  C  CB  . PRO B  1 117 ? 2.929   3.736   56.885  1.00 10.14  ? 204  PRO B CB  1 
ATOM   3919  C  CG  . PRO B  1 117 ? 3.332   2.566   55.989  1.00 9.59   ? 204  PRO B CG  1 
ATOM   3920  C  CD  . PRO B  1 117 ? 4.343   1.750   56.809  1.00 9.85   ? 204  PRO B CD  1 
ATOM   3921  N  N   . ASN B  1 118 ? 0.785   3.361   59.249  1.00 10.92  ? 205  ASN B N   1 
ATOM   3922  C  CA  . ASN B  1 118 ? -0.526  2.859   59.744  1.00 11.98  ? 205  ASN B CA  1 
ATOM   3923  C  C   . ASN B  1 118 ? -1.265  2.006   58.725  1.00 12.09  ? 205  ASN B C   1 
ATOM   3924  O  O   . ASN B  1 118 ? -1.811  0.928   59.066  1.00 12.34  ? 205  ASN B O   1 
ATOM   3925  C  CB  . ASN B  1 118 ? -1.434  4.005   60.202  1.00 12.68  ? 205  ASN B CB  1 
ATOM   3926  C  CG  . ASN B  1 118 ? -0.897  4.749   61.420  1.00 13.52  ? 205  ASN B CG  1 
ATOM   3927  O  OD1 . ASN B  1 118 ? 0.084   4.350   62.036  1.00 14.33  ? 205  ASN B OD1 1 
ATOM   3928  N  ND2 . ASN B  1 118 ? -1.561  5.842   61.770  1.00 14.18  ? 205  ASN B ND2 1 
ATOM   3929  N  N   . ASN B  1 119 ? -1.242  2.450   57.469  1.00 12.02  ? 206  ASN B N   1 
ATOM   3930  C  CA  . ASN B  1 119 ? -1.988  1.772   56.418  1.00 13.24  ? 206  ASN B CA  1 
ATOM   3931  C  C   . ASN B  1 119 ? -1.262  0.580   55.787  1.00 13.11  ? 206  ASN B C   1 
ATOM   3932  O  O   . ASN B  1 119 ? -1.783  -0.048  54.864  1.00 13.02  ? 206  ASN B O   1 
ATOM   3933  C  CB  . ASN B  1 119 ? -2.431  2.782   55.338  1.00 13.73  ? 206  ASN B CB  1 
ATOM   3934  C  CG  . ASN B  1 119 ? -1.259  3.316   54.486  1.00 15.98  ? 206  ASN B CG  1 
ATOM   3935  O  OD1 . ASN B  1 119 ? -0.086  3.021   54.742  1.00 16.96  ? 206  ASN B OD1 1 
ATOM   3936  N  ND2 . ASN B  1 119 ? -1.591  4.109   53.461  1.00 18.79  ? 206  ASN B ND2 1 
ATOM   3937  N  N   . ASN B  1 120 ? -0.053  0.267   56.267  1.00 12.61  ? 207  ASN B N   1 
ATOM   3938  C  CA  . ASN B  1 120 ? 0.784   -0.721  55.585  1.00 12.77  ? 207  ASN B CA  1 
ATOM   3939  C  C   . ASN B  1 120 ? 1.903   -1.295  56.472  1.00 12.06  ? 207  ASN B C   1 
ATOM   3940  O  O   . ASN B  1 120 ? 3.040   -1.457  56.024  1.00 10.71  ? 207  ASN B O   1 
ATOM   3941  C  CB  . ASN B  1 120 ? 1.421   -0.037  54.366  1.00 12.43  ? 207  ASN B CB  1 
ATOM   3942  C  CG  . ASN B  1 120 ? 1.387   -0.874  53.120  1.00 17.34  ? 207  ASN B CG  1 
ATOM   3943  O  OD1 . ASN B  1 120 ? 1.023   -2.053  53.124  1.00 20.55  ? 207  ASN B OD1 1 
ATOM   3944  N  ND2 . ASN B  1 120 ? 1.775   -0.253  52.017  1.00 19.19  ? 207  ASN B ND2 1 
ATOM   3945  N  N   . ALA B  1 121 ? 1.565   -1.627  57.713  1.00 11.95  ? 208  ALA B N   1 
ATOM   3946  C  CA  . ALA B  1 121 ? 2.540   -2.157  58.643  1.00 11.57  ? 208  ALA B CA  1 
ATOM   3947  C  C   . ALA B  1 121 ? 2.846   -3.619  58.341  1.00 11.44  ? 208  ALA B C   1 
ATOM   3948  O  O   . ALA B  1 121 ? 2.129   -4.281  57.596  1.00 11.19  ? 208  ALA B O   1 
ATOM   3949  C  CB  . ALA B  1 121 ? 2.046   -1.993  60.072  1.00 11.93  ? 208  ALA B CB  1 
ATOM   3950  N  N   . SER B  1 122 ? 3.920   -4.123  58.925  1.00 11.65  ? 209  SER B N   1 
ATOM   3951  C  CA  . SER B  1 122 ? 4.305   -5.507  58.729  1.00 10.81  ? 209  SER B CA  1 
ATOM   3952  C  C   . SER B  1 122 ? 5.007   -6.039  59.974  1.00 10.51  ? 209  SER B C   1 
ATOM   3953  O  O   . SER B  1 122 ? 5.698   -5.297  60.656  1.00 10.16  ? 209  SER B O   1 
ATOM   3954  C  CB  . SER B  1 122 ? 5.211   -5.644  57.485  1.00 12.01  ? 209  SER B CB  1 
ATOM   3955  O  OG  . SER B  1 122 ? 6.470   -5.057  57.713  1.00 14.03  ? 209  SER B OG  1 
ATOM   3956  N  N   . ALA B  1 123 ? 4.810   -7.318  60.266  1.00 10.33  ? 210  ALA B N   1 
ATOM   3957  C  CA  . ALA B  1 123 ? 5.538   -7.982  61.351  1.00 10.80  ? 210  ALA B CA  1 
ATOM   3958  C  C   . ALA B  1 123 ? 6.743   -8.700  60.791  1.00 10.61  ? 210  ALA B C   1 
ATOM   3959  O  O   . ALA B  1 123 ? 6.705   -9.201  59.661  1.00 10.67  ? 210  ALA B O   1 
ATOM   3960  C  CB  . ALA B  1 123 ? 4.649   -8.957  62.095  1.00 9.86   ? 210  ALA B CB  1 
ATOM   3961  N  N   . VAL B  1 124 ? 7.828   -8.704  61.565  1.00 10.20  ? 211  VAL B N   1 
ATOM   3962  C  CA  . VAL B  1 124 ? 8.971   -9.567  61.285  1.00 10.25  ? 211  VAL B CA  1 
ATOM   3963  C  C   . VAL B  1 124 ? 9.106   -10.463 62.513  1.00 10.25  ? 211  VAL B C   1 
ATOM   3964  O  O   . VAL B  1 124 ? 9.136   -9.969  63.651  1.00 10.18  ? 211  VAL B O   1 
ATOM   3965  C  CB  . VAL B  1 124 ? 10.293  -8.788  61.026  1.00 10.98  ? 211  VAL B CB  1 
ATOM   3966  C  CG1 . VAL B  1 124 ? 11.436  -9.790  60.727  1.00 10.48  ? 211  VAL B CG1 1 
ATOM   3967  C  CG2 . VAL B  1 124 ? 10.116  -7.753  59.860  1.00 10.59  ? 211  VAL B CG2 1 
ATOM   3968  N  N   . VAL B  1 125 ? 9.157   -11.769 62.264  1.00 10.29  ? 212  VAL B N   1 
ATOM   3969  C  CA  . VAL B  1 125 ? 9.216   -12.803 63.311  1.00 10.36  ? 212  VAL B CA  1 
ATOM   3970  C  C   . VAL B  1 125 ? 10.657  -13.319 63.392  1.00 10.82  ? 212  VAL B C   1 
ATOM   3971  O  O   . VAL B  1 125 ? 11.193  -13.847 62.416  1.00 11.18  ? 212  VAL B O   1 
ATOM   3972  C  CB  . VAL B  1 125 ? 8.260   -13.986 63.002  1.00 10.21  ? 212  VAL B CB  1 
ATOM   3973  C  CG1 . VAL B  1 125 ? 8.298   -15.031 64.135  1.00 10.74  ? 212  VAL B CG1 1 
ATOM   3974  C  CG2 . VAL B  1 125 ? 6.833   -13.466 62.760  1.00 9.40   ? 212  VAL B CG2 1 
ATOM   3975  N  N   . TRP B  1 126 ? 11.277  -13.135 64.551  1.00 10.80  ? 213  TRP B N   1 
ATOM   3976  C  CA  . TRP B  1 126 ? 12.670  -13.544 64.779  1.00 10.61  ? 213  TRP B CA  1 
ATOM   3977  C  C   . TRP B  1 126 ? 12.702  -14.786 65.662  1.00 10.51  ? 213  TRP B C   1 
ATOM   3978  O  O   . TRP B  1 126 ? 11.854  -14.951 66.550  1.00 9.82   ? 213  TRP B O   1 
ATOM   3979  C  CB  . TRP B  1 126 ? 13.452  -12.436 65.486  1.00 10.45  ? 213  TRP B CB  1 
ATOM   3980  C  CG  . TRP B  1 126 ? 13.604  -11.156 64.701  1.00 10.45  ? 213  TRP B CG  1 
ATOM   3981  C  CD1 . TRP B  1 126 ? 12.613  -10.312 64.297  1.00 10.44  ? 213  TRP B CD1 1 
ATOM   3982  C  CD2 . TRP B  1 126 ? 14.834  -10.580 64.257  1.00 10.68  ? 213  TRP B CD2 1 
ATOM   3983  N  NE1 . TRP B  1 126 ? 13.150  -9.232  63.615  1.00 11.29  ? 213  TRP B NE1 1 
ATOM   3984  C  CE2 . TRP B  1 126 ? 14.516  -9.383  63.575  1.00 11.47  ? 213  TRP B CE2 1 
ATOM   3985  C  CE3 . TRP B  1 126 ? 16.189  -10.964 64.363  1.00 12.69  ? 213  TRP B CE3 1 
ATOM   3986  C  CZ2 . TRP B  1 126 ? 15.499  -8.556  63.016  1.00 11.50  ? 213  TRP B CZ2 1 
ATOM   3987  C  CZ3 . TRP B  1 126 ? 17.177  -10.120 63.789  1.00 10.94  ? 213  TRP B CZ3 1 
ATOM   3988  C  CH2 . TRP B  1 126 ? 16.819  -8.958  63.120  1.00 10.62  ? 213  TRP B CH2 1 
ATOM   3989  N  N   . TYR B  1 127 ? 13.685  -15.652 65.429  1.00 10.50  ? 214  TYR B N   1 
ATOM   3990  C  CA  . TYR B  1 127 ? 13.868  -16.859 66.246  1.00 11.47  ? 214  TYR B CA  1 
ATOM   3991  C  C   . TYR B  1 127 ? 15.362  -17.084 66.443  1.00 12.06  ? 214  TYR B C   1 
ATOM   3992  O  O   . TYR B  1 127 ? 16.146  -17.106 65.468  1.00 11.76  ? 214  TYR B O   1 
ATOM   3993  C  CB  . TYR B  1 127 ? 13.180  -18.083 65.612  1.00 10.79  ? 214  TYR B CB  1 
ATOM   3994  C  CG  . TYR B  1 127 ? 13.207  -19.340 66.467  1.00 11.39  ? 214  TYR B CG  1 
ATOM   3995  C  CD1 . TYR B  1 127 ? 14.018  -20.430 66.125  1.00 12.21  ? 214  TYR B CD1 1 
ATOM   3996  C  CD2 . TYR B  1 127 ? 12.397  -19.455 67.611  1.00 10.19  ? 214  TYR B CD2 1 
ATOM   3997  C  CE1 . TYR B  1 127 ? 14.030  -21.593 66.915  1.00 10.64  ? 214  TYR B CE1 1 
ATOM   3998  C  CE2 . TYR B  1 127 ? 12.411  -20.597 68.392  1.00 11.84  ? 214  TYR B CE2 1 
ATOM   3999  C  CZ  . TYR B  1 127 ? 13.221  -21.660 68.042  1.00 10.26  ? 214  TYR B CZ  1 
ATOM   4000  O  OH  . TYR B  1 127 ? 13.203  -22.792 68.834  1.00 12.90  ? 214  TYR B OH  1 
ATOM   4001  N  N   . GLY B  1 128 ? 15.756  -17.198 67.710  1.00 12.68  ? 215  GLY B N   1 
ATOM   4002  C  CA  . GLY B  1 128 ? 17.168  -17.344 68.074  1.00 13.26  ? 215  GLY B CA  1 
ATOM   4003  C  C   . GLY B  1 128 ? 18.056  -16.260 67.508  1.00 13.61  ? 215  GLY B C   1 
ATOM   4004  O  O   . GLY B  1 128 ? 19.204  -16.529 67.149  1.00 14.11  ? 215  GLY B O   1 
ATOM   4005  N  N   . GLY B  1 129 ? 17.524  -15.038 67.414  1.00 13.30  ? 216  GLY B N   1 
ATOM   4006  C  CA  . GLY B  1 129 ? 18.294  -13.879 66.966  1.00 13.52  ? 216  GLY B CA  1 
ATOM   4007  C  C   . GLY B  1 129 ? 18.370  -13.634 65.462  1.00 13.12  ? 216  GLY B C   1 
ATOM   4008  O  O   . GLY B  1 129 ? 19.052  -12.714 65.031  1.00 13.21  ? 216  GLY B O   1 
ATOM   4009  N  N   . ARG B  1 130 ? 17.658  -14.438 64.664  1.00 12.78  ? 217  ARG B N   1 
ATOM   4010  C  CA  . ARG B  1 130 ? 17.636  -14.296 63.198  1.00 12.99  ? 217  ARG B CA  1 
ATOM   4011  C  C   . ARG B  1 130 ? 16.191  -14.100 62.705  1.00 12.38  ? 217  ARG B C   1 
ATOM   4012  O  O   . ARG B  1 130 ? 15.267  -14.688 63.291  1.00 12.31  ? 217  ARG B O   1 
ATOM   4013  C  CB  . ARG B  1 130 ? 18.231  -15.558 62.547  1.00 12.30  ? 217  ARG B CB  1 
ATOM   4014  C  CG  . ARG B  1 130 ? 19.760  -15.660 62.692  1.00 14.72  ? 217  ARG B CG  1 
ATOM   4015  C  CD  . ARG B  1 130 ? 20.363  -16.895 62.017  1.00 14.52  ? 217  ARG B CD  1 
ATOM   4016  N  NE  . ARG B  1 130 ? 21.732  -16.623 61.570  1.00 15.04  ? 217  ARG B NE  1 
ATOM   4017  C  CZ  . ARG B  1 130 ? 22.864  -16.990 62.186  1.00 17.12  ? 217  ARG B CZ  1 
ATOM   4018  N  NH1 . ARG B  1 130 ? 22.851  -17.684 63.323  1.00 14.98  ? 217  ARG B NH1 1 
ATOM   4019  N  NH2 . ARG B  1 130 ? 24.040  -16.649 61.648  1.00 16.05  ? 217  ARG B NH2 1 
ATOM   4020  N  N   . PRO B  1 131 ? 15.989  -13.281 61.647  1.00 12.63  ? 218  PRO B N   1 
ATOM   4021  C  CA  . PRO B  1 131 ? 14.645  -13.086 61.079  1.00 13.07  ? 218  PRO B CA  1 
ATOM   4022  C  C   . PRO B  1 131 ? 14.181  -14.309 60.287  1.00 13.66  ? 218  PRO B C   1 
ATOM   4023  O  O   . PRO B  1 131 ? 14.938  -14.850 59.459  1.00 13.73  ? 218  PRO B O   1 
ATOM   4024  C  CB  . PRO B  1 131 ? 14.818  -11.854 60.176  1.00 13.13  ? 218  PRO B CB  1 
ATOM   4025  C  CG  . PRO B  1 131 ? 16.275  -11.904 59.755  1.00 11.73  ? 218  PRO B CG  1 
ATOM   4026  C  CD  . PRO B  1 131 ? 17.006  -12.459 60.949  1.00 12.90  ? 218  PRO B CD  1 
ATOM   4027  N  N   . ILE B  1 132 ? 12.961  -14.771 60.561  1.00 13.03  ? 219  ILE B N   1 
ATOM   4028  C  CA  . ILE B  1 132 ? 12.484  -16.026 59.962  1.00 12.25  ? 219  ILE B CA  1 
ATOM   4029  C  C   . ILE B  1 132 ? 11.344  -15.835 58.958  1.00 12.59  ? 219  ILE B C   1 
ATOM   4030  O  O   . ILE B  1 132 ? 11.313  -16.474 57.889  1.00 12.72  ? 219  ILE B O   1 
ATOM   4031  C  CB  . ILE B  1 132 ? 12.031  -17.058 61.054  1.00 12.05  ? 219  ILE B CB  1 
ATOM   4032  C  CG1 . ILE B  1 132 ? 13.146  -17.311 62.101  1.00 10.11  ? 219  ILE B CG1 1 
ATOM   4033  C  CG2 . ILE B  1 132 ? 11.558  -18.372 60.411  1.00 12.70  ? 219  ILE B CG2 1 
ATOM   4034  C  CD1 . ILE B  1 132 ? 14.506  -17.749 61.515  1.00 9.32   ? 219  ILE B CD1 1 
ATOM   4035  N  N   . THR B  1 133 ? 10.407  -14.970 59.321  1.00 11.65  ? 220  THR B N   1 
ATOM   4036  C  CA  . THR B  1 133 ? 9.122   -14.831 58.615  1.00 12.61  ? 220  THR B CA  1 
ATOM   4037  C  C   . THR B  1 133 ? 8.701   -13.363 58.665  1.00 11.77  ? 220  THR B C   1 
ATOM   4038  O  O   . THR B  1 133 ? 8.998   -12.670 59.637  1.00 12.14  ? 220  THR B O   1 
ATOM   4039  C  CB  . THR B  1 133 ? 8.010   -15.677 59.315  1.00 11.68  ? 220  THR B CB  1 
ATOM   4040  O  OG1 . THR B  1 133 ? 8.407   -17.053 59.390  1.00 13.22  ? 220  THR B OG1 1 
ATOM   4041  C  CG2 . THR B  1 133 ? 6.656   -15.567 58.607  1.00 14.21  ? 220  THR B CG2 1 
ATOM   4042  N  N   . GLU B  1 134 ? 8.003   -12.906 57.625  1.00 11.36  ? 221  GLU B N   1 
ATOM   4043  C  CA  . GLU B  1 134 ? 7.410   -11.576 57.593  1.00 12.21  ? 221  GLU B CA  1 
ATOM   4044  C  C   . GLU B  1 134 ? 5.894   -11.703 57.319  1.00 12.30  ? 221  GLU B C   1 
ATOM   4045  O  O   . GLU B  1 134 ? 5.467   -12.559 56.528  1.00 12.70  ? 221  GLU B O   1 
ATOM   4046  C  CB  . GLU B  1 134 ? 8.099   -10.699 56.533  1.00 11.87  ? 221  GLU B CB  1 
ATOM   4047  C  CG  . GLU B  1 134 ? 9.656   -10.760 56.531  1.00 13.38  ? 221  GLU B CG  1 
ATOM   4048  C  CD  . GLU B  1 134 ? 10.195  -11.991 55.798  1.00 15.65  ? 221  GLU B CD  1 
ATOM   4049  O  OE1 . GLU B  1 134 ? 11.077  -12.682 56.341  1.00 16.80  ? 221  GLU B OE1 1 
ATOM   4050  O  OE2 . GLU B  1 134 ? 9.723   -12.279 54.678  1.00 19.22  ? 221  GLU B OE2 1 
ATOM   4051  N  N   . ILE B  1 135 ? 5.099   -10.870 57.977  1.00 12.31  ? 222  ILE B N   1 
ATOM   4052  C  CA  . ILE B  1 135 ? 3.639   -10.884 57.801  1.00 11.83  ? 222  ILE B CA  1 
ATOM   4053  C  C   . ILE B  1 135 ? 3.133   -9.478  57.435  1.00 11.99  ? 222  ILE B C   1 
ATOM   4054  O  O   . ILE B  1 135 ? 3.192   -8.577  58.269  1.00 11.75  ? 222  ILE B O   1 
ATOM   4055  C  CB  . ILE B  1 135 ? 2.913   -11.399 59.078  1.00 11.60  ? 222  ILE B CB  1 
ATOM   4056  C  CG1 . ILE B  1 135 ? 3.515   -12.725 59.591  1.00 11.24  ? 222  ILE B CG1 1 
ATOM   4057  C  CG2 . ILE B  1 135 ? 1.396   -11.538 58.829  1.00 11.14  ? 222  ILE B CG2 1 
ATOM   4058  C  CD1 . ILE B  1 135 ? 3.080   -13.088 61.024  1.00 11.79  ? 222  ILE B CD1 1 
ATOM   4059  N  N   . PRO B  1 136 ? 2.599   -9.294  56.203  1.00 11.96  ? 223  PRO B N   1 
ATOM   4060  C  CA  . PRO B  1 136 ? 2.030   -7.991  55.881  1.00 12.20  ? 223  PRO B CA  1 
ATOM   4061  C  C   . PRO B  1 136 ? 0.666   -7.788  56.552  1.00 12.07  ? 223  PRO B C   1 
ATOM   4062  O  O   . PRO B  1 136 ? -0.042  -8.766  56.855  1.00 12.54  ? 223  PRO B O   1 
ATOM   4063  C  CB  . PRO B  1 136 ? 1.878   -8.023  54.354  1.00 12.04  ? 223  PRO B CB  1 
ATOM   4064  C  CG  . PRO B  1 136 ? 1.809   -9.458  54.001  1.00 12.44  ? 223  PRO B CG  1 
ATOM   4065  C  CD  . PRO B  1 136 ? 2.467   -10.251 55.088  1.00 12.10  ? 223  PRO B CD  1 
ATOM   4066  N  N   . SER B  1 137 ? 0.347   -6.524  56.820  1.00 12.19  ? 224  SER B N   1 
ATOM   4067  C  CA  . SER B  1 137 ? -0.966  -6.103  57.309  1.00 11.82  ? 224  SER B CA  1 
ATOM   4068  C  C   . SER B  1 137 ? -2.077  -6.736  56.442  1.00 12.81  ? 224  SER B C   1 
ATOM   4069  O  O   . SER B  1 137 ? -1.968  -6.766  55.202  1.00 11.61  ? 224  SER B O   1 
ATOM   4070  C  CB  . SER B  1 137 ? -1.050  -4.563  57.293  1.00 12.21  ? 224  SER B CB  1 
ATOM   4071  O  OG  . SER B  1 137 ? -2.359  -4.061  57.588  1.00 10.62  ? 224  SER B OG  1 
ATOM   4072  N  N   . TRP B  1 138 ? -3.115  -7.256  57.092  1.00 12.86  ? 225  TRP B N   1 
ATOM   4073  C  CA  . TRP B  1 138 ? -4.279  -7.807  56.380  1.00 13.27  ? 225  TRP B CA  1 
ATOM   4074  C  C   . TRP B  1 138 ? -5.479  -6.844  56.329  1.00 14.22  ? 225  TRP B C   1 
ATOM   4075  O  O   . TRP B  1 138 ? -6.383  -7.017  55.508  1.00 14.65  ? 225  TRP B O   1 
ATOM   4076  C  CB  . TRP B  1 138 ? -4.683  -9.196  56.922  1.00 13.04  ? 225  TRP B CB  1 
ATOM   4077  C  CG  . TRP B  1 138 ? -4.913  -9.281  58.420  1.00 12.85  ? 225  TRP B CG  1 
ATOM   4078  C  CD1 . TRP B  1 138 ? -6.033  -8.901  59.104  1.00 12.98  ? 225  TRP B CD1 1 
ATOM   4079  C  CD2 . TRP B  1 138 ? -3.997  -9.789  59.401  1.00 12.16  ? 225  TRP B CD2 1 
ATOM   4080  N  NE1 . TRP B  1 138 ? -5.877  -9.153  60.451  1.00 12.52  ? 225  TRP B NE1 1 
ATOM   4081  C  CE2 . TRP B  1 138 ? -4.633  -9.693  60.661  1.00 12.55  ? 225  TRP B CE2 1 
ATOM   4082  C  CE3 . TRP B  1 138 ? -2.705  -10.326 59.335  1.00 13.29  ? 225  TRP B CE3 1 
ATOM   4083  C  CZ2 . TRP B  1 138 ? -4.016  -10.112 61.854  1.00 11.80  ? 225  TRP B CZ2 1 
ATOM   4084  C  CZ3 . TRP B  1 138 ? -2.084  -10.747 60.527  1.00 13.16  ? 225  TRP B CZ3 1 
ATOM   4085  C  CH2 . TRP B  1 138 ? -2.745  -10.637 61.766  1.00 11.33  ? 225  TRP B CH2 1 
ATOM   4086  N  N   . ALA B  1 139 ? -5.486  -5.807  57.165  1.00 13.63  ? 226  ALA B N   1 
ATOM   4087  C  CA  . ALA B  1 139 ? -6.640  -4.899  57.211  1.00 13.83  ? 226  ALA B CA  1 
ATOM   4088  C  C   . ALA B  1 139 ? -6.279  -3.421  56.989  1.00 13.45  ? 226  ALA B C   1 
ATOM   4089  O  O   . ALA B  1 139 ? -7.159  -2.547  57.030  1.00 13.61  ? 226  ALA B O   1 
ATOM   4090  C  CB  . ALA B  1 139 ? -7.434  -5.090  58.519  1.00 13.07  ? 226  ALA B CB  1 
ATOM   4091  N  N   . GLY B  1 140 ? -4.981  -3.159  56.770  1.00 13.18  ? 227  GLY B N   1 
ATOM   4092  C  CA  . GLY B  1 140 ? -4.456  -1.811  56.475  1.00 13.04  ? 227  GLY B CA  1 
ATOM   4093  C  C   . GLY B  1 140 ? -4.688  -0.786  57.560  1.00 12.69  ? 227  GLY B C   1 
ATOM   4094  O  O   . GLY B  1 140 ? -4.885  0.399   57.264  1.00 12.95  ? 227  GLY B O   1 
ATOM   4095  N  N   . ASN B  1 141 ? -4.670  -1.224  58.822  1.00 12.87  ? 228  ASN B N   1 
ATOM   4096  C  CA  . ASN B  1 141 ? -4.891  -0.315  59.971  1.00 12.59  ? 228  ASN B CA  1 
ATOM   4097  C  C   . ASN B  1 141 ? -4.129  -0.774  61.214  1.00 12.86  ? 228  ASN B C   1 
ATOM   4098  O  O   . ASN B  1 141 ? -4.711  -1.412  62.123  1.00 12.59  ? 228  ASN B O   1 
ATOM   4099  C  CB  . ASN B  1 141 ? -6.404  -0.172  60.286  1.00 13.02  ? 228  ASN B CB  1 
ATOM   4100  C  CG  . ASN B  1 141 ? -6.736  1.102   61.088  1.00 14.49  ? 228  ASN B CG  1 
ATOM   4101  O  OD1 . ASN B  1 141 ? -5.865  1.732   61.669  1.00 14.66  ? 228  ASN B OD1 1 
ATOM   4102  N  ND2 . ASN B  1 141 ? -8.031  1.470   61.121  1.00 17.57  ? 228  ASN B ND2 1 
ATOM   4103  N  N   . ILE B  1 142 ? -2.831  -0.455  61.241  1.00 11.95  ? 229  ILE B N   1 
ATOM   4104  C  CA  . ILE B  1 142 ? -1.966  -0.677  62.419  1.00 11.73  ? 229  ILE B CA  1 
ATOM   4105  C  C   . ILE B  1 142 ? -1.975  -2.140  62.904  1.00 11.30  ? 229  ILE B C   1 
ATOM   4106  O  O   . ILE B  1 142 ? -2.439  -2.449  64.019  1.00 10.89  ? 229  ILE B O   1 
ATOM   4107  C  CB  . ILE B  1 142 ? -2.255  0.358   63.576  1.00 11.60  ? 229  ILE B CB  1 
ATOM   4108  C  CG1 . ILE B  1 142 ? -2.449  1.768   62.986  1.00 11.89  ? 229  ILE B CG1 1 
ATOM   4109  C  CG2 . ILE B  1 142 ? -1.103  0.356   64.649  1.00 11.35  ? 229  ILE B CG2 1 
ATOM   4110  C  CD1 . ILE B  1 142 ? -2.887  2.877   64.001  1.00 13.13  ? 229  ILE B CD1 1 
ATOM   4111  N  N   . LEU B  1 143 ? -1.478  -3.044  62.055  1.00 10.60  ? 230  LEU B N   1 
ATOM   4112  C  CA  . LEU B  1 143 ? -1.164  -4.403  62.509  1.00 10.71  ? 230  LEU B CA  1 
ATOM   4113  C  C   . LEU B  1 143 ? -0.341  -4.313  63.788  1.00 10.72  ? 230  LEU B C   1 
ATOM   4114  O  O   . LEU B  1 143 ? 0.613   -3.533  63.866  1.00 9.53   ? 230  LEU B O   1 
ATOM   4115  C  CB  . LEU B  1 143 ? -0.430  -5.214  61.436  1.00 10.85  ? 230  LEU B CB  1 
ATOM   4116  C  CG  . LEU B  1 143 ? -0.014  -6.656  61.735  1.00 10.92  ? 230  LEU B CG  1 
ATOM   4117  C  CD1 . LEU B  1 143 ? -1.231  -7.546  61.827  1.00 11.50  ? 230  LEU B CD1 1 
ATOM   4118  C  CD2 . LEU B  1 143 ? 0.979   -7.179  60.668  1.00 11.18  ? 230  LEU B CD2 1 
ATOM   4119  N  N   . ARG B  1 144 ? -0.731  -5.103  64.790  1.00 10.22  ? 231  ARG B N   1 
ATOM   4120  C  CA  . ARG B  1 144 ? -0.253  -4.907  66.165  1.00 9.79   ? 231  ARG B CA  1 
ATOM   4121  C  C   . ARG B  1 144 ? -0.459  -6.170  66.993  1.00 10.11  ? 231  ARG B C   1 
ATOM   4122  O  O   . ARG B  1 144 ? -1.207  -7.050  66.587  1.00 10.76  ? 231  ARG B O   1 
ATOM   4123  C  CB  . ARG B  1 144 ? -0.960  -3.714  66.828  1.00 9.93   ? 231  ARG B CB  1 
ATOM   4124  C  CG  . ARG B  1 144 ? -2.508  -3.820  66.956  1.00 8.79   ? 231  ARG B CG  1 
ATOM   4125  C  CD  . ARG B  1 144 ? -3.100  -2.426  67.158  1.00 9.41   ? 231  ARG B CD  1 
ATOM   4126  N  NE  . ARG B  1 144 ? -4.570  -2.426  67.302  1.00 9.75   ? 231  ARG B NE  1 
ATOM   4127  C  CZ  . ARG B  1 144 ? -5.435  -2.218  66.311  1.00 10.83  ? 231  ARG B CZ  1 
ATOM   4128  N  NH1 . ARG B  1 144 ? -5.004  -2.027  65.063  1.00 8.69   ? 231  ARG B NH1 1 
ATOM   4129  N  NH2 . ARG B  1 144 ? -6.747  -2.228  66.568  1.00 10.88  ? 231  ARG B NH2 1 
ATOM   4130  N  N   . THR B  1 145 ? 0.166   -6.237  68.168  1.00 9.51   ? 232  THR B N   1 
ATOM   4131  C  CA  . THR B  1 145 ? 0.114   -7.445  68.963  1.00 9.48   ? 232  THR B CA  1 
ATOM   4132  C  C   . THR B  1 145 ? 0.155   -7.185  70.500  1.00 9.72   ? 232  THR B C   1 
ATOM   4133  O  O   . THR B  1 145 ? -0.155  -6.077  70.976  1.00 9.38   ? 232  THR B O   1 
ATOM   4134  C  CB  . THR B  1 145 ? 1.163   -8.516  68.431  1.00 9.69   ? 232  THR B CB  1 
ATOM   4135  O  OG1 . THR B  1 145 ? 0.979   -9.787  69.084  1.00 10.10  ? 232  THR B OG1 1 
ATOM   4136  C  CG2 . THR B  1 145 ? 2.624   -8.042  68.634  1.00 8.29   ? 232  THR B CG2 1 
ATOM   4137  N  N   . GLN B  1 146 ? 0.571   -8.202  71.250  1.00 8.95   ? 233  GLN B N   1 
ATOM   4138  C  CA  . GLN B  1 146 ? 0.318   -8.300  72.680  1.00 8.86   ? 233  GLN B CA  1 
ATOM   4139  C  C   . GLN B  1 146 ? 0.879   -7.229  73.624  1.00 8.67   ? 233  GLN B C   1 
ATOM   4140  O  O   . GLN B  1 146 ? 0.180   -6.809  74.563  1.00 7.54   ? 233  GLN B O   1 
ATOM   4141  C  CB  . GLN B  1 146 ? 0.741   -9.700  73.162  1.00 9.31   ? 233  GLN B CB  1 
ATOM   4142  C  CG  . GLN B  1 146 ? -0.054  -10.826 72.460  1.00 8.94   ? 233  GLN B CG  1 
ATOM   4143  C  CD  . GLN B  1 146 ? 0.316   -12.198 72.964  1.00 10.07  ? 233  GLN B CD  1 
ATOM   4144  O  OE1 . GLN B  1 146 ? 0.965   -12.351 74.015  1.00 11.66  ? 233  GLN B OE1 1 
ATOM   4145  N  NE2 . GLN B  1 146 ? -0.110  -13.206 72.243  1.00 9.05   ? 233  GLN B NE2 1 
ATOM   4146  N  N   . GLU B  1 147 ? 2.129   -6.805  73.385  1.00 8.75   ? 234  GLU B N   1 
ATOM   4147  C  CA  . GLU B  1 147 ? 2.899   -5.941  74.319  1.00 9.29   ? 234  GLU B CA  1 
ATOM   4148  C  C   . GLU B  1 147 ? 3.202   -6.628  75.662  1.00 9.15   ? 234  GLU B C   1 
ATOM   4149  O  O   . GLU B  1 147 ? 3.474   -5.967  76.659  1.00 9.23   ? 234  GLU B O   1 
ATOM   4150  C  CB  . GLU B  1 147 ? 2.297   -4.517  74.539  1.00 8.80   ? 234  GLU B CB  1 
ATOM   4151  C  CG  . GLU B  1 147 ? 1.539   -3.886  73.364  1.00 11.28  ? 234  GLU B CG  1 
ATOM   4152  C  CD  . GLU B  1 147 ? 2.383   -3.638  72.121  1.00 11.07  ? 234  GLU B CD  1 
ATOM   4153  O  OE1 . GLU B  1 147 ? 1.805   -3.114  71.142  1.00 12.76  ? 234  GLU B OE1 1 
ATOM   4154  O  OE2 . GLU B  1 147 ? 3.606   -3.933  72.106  1.00 11.21  ? 234  GLU B OE2 1 
ATOM   4155  N  N   . SER B  1 148 ? 3.157   -7.959  75.666  1.00 8.66   ? 235  SER B N   1 
ATOM   4156  C  CA  . SER B  1 148 ? 3.729   -8.776  76.746  1.00 9.45   ? 235  SER B CA  1 
ATOM   4157  C  C   . SER B  1 148 ? 4.003   -10.179 76.179  1.00 9.09   ? 235  SER B C   1 
ATOM   4158  O  O   . SER B  1 148 ? 3.762   -10.436 74.984  1.00 8.83   ? 235  SER B O   1 
ATOM   4159  C  CB  . SER B  1 148 ? 2.836   -8.824  78.002  1.00 8.44   ? 235  SER B CB  1 
ATOM   4160  O  OG  . SER B  1 148 ? 1.587   -9.458  77.723  1.00 10.19  ? 235  SER B OG  1 
ATOM   4161  N  N   . GLU B  1 149 ? 4.524   -11.074 77.014  1.00 9.55   ? 236  GLU B N   1 
ATOM   4162  C  CA  . GLU B  1 149 ? 5.024   -12.349 76.502  1.00 9.94   ? 236  GLU B CA  1 
ATOM   4163  C  C   . GLU B  1 149 ? 3.958   -13.268 75.910  1.00 10.13  ? 236  GLU B C   1 
ATOM   4164  O  O   . GLU B  1 149 ? 2.793   -13.282 76.358  1.00 10.64  ? 236  GLU B O   1 
ATOM   4165  C  CB  . GLU B  1 149 ? 5.890   -13.090 77.539  1.00 10.25  ? 236  GLU B CB  1 
ATOM   4166  C  CG  . GLU B  1 149 ? 5.134   -13.864 78.622  1.00 10.05  ? 236  GLU B CG  1 
ATOM   4167  C  CD  . GLU B  1 149 ? 6.058   -14.799 79.427  1.00 10.38  ? 236  GLU B CD  1 
ATOM   4168  O  OE1 . GLU B  1 149 ? 7.303   -14.756 79.266  1.00 10.60  ? 236  GLU B OE1 1 
ATOM   4169  O  OE2 . GLU B  1 149 ? 5.528   -15.586 80.219  1.00 9.33   ? 236  GLU B OE2 1 
ATOM   4170  N  N   . CYS B  1 150 ? 4.373   -14.003 74.873  1.00 10.91  ? 237  CYS B N   1 
ATOM   4171  C  CA  . CYS B  1 150 ? 3.626   -15.155 74.367  1.00 11.29  ? 237  CYS B CA  1 
ATOM   4172  C  C   . CYS B  1 150 ? 3.965   -16.406 75.211  1.00 11.67  ? 237  CYS B C   1 
ATOM   4173  O  O   . CYS B  1 150 ? 4.695   -16.309 76.207  1.00 11.89  ? 237  CYS B O   1 
ATOM   4174  C  CB  . CYS B  1 150 ? 3.837   -15.359 72.850  1.00 11.36  ? 237  CYS B CB  1 
ATOM   4175  S  SG  . CYS B  1 150 ? 5.537   -15.091 72.214  1.00 11.46  ? 237  CYS B SG  1 
ATOM   4176  N  N   . VAL B  1 151 ? 3.406   -17.558 74.844  1.00 12.13  ? 238  VAL B N   1 
ATOM   4177  C  CA  . VAL B  1 151 ? 3.584   -18.789 75.623  1.00 12.73  ? 238  VAL B CA  1 
ATOM   4178  C  C   . VAL B  1 151 ? 3.741   -19.930 74.632  1.00 12.75  ? 238  VAL B C   1 
ATOM   4179  O  O   . VAL B  1 151 ? 3.105   -19.915 73.578  1.00 13.40  ? 238  VAL B O   1 
ATOM   4180  C  CB  . VAL B  1 151 ? 2.376   -19.031 76.591  1.00 12.43  ? 238  VAL B CB  1 
ATOM   4181  C  CG1 . VAL B  1 151 ? 2.680   -20.131 77.612  1.00 12.58  ? 238  VAL B CG1 1 
ATOM   4182  C  CG2 . VAL B  1 151 ? 2.020   -17.758 77.314  1.00 13.32  ? 238  VAL B CG2 1 
ATOM   4183  N  N   . CYS B  1 152 ? 4.607   -20.891 74.951  1.00 12.78  ? 239  CYS B N   1 
ATOM   4184  C  CA  . CYS B  1 152 ? 4.924   -21.996 74.039  1.00 13.09  ? 239  CYS B CA  1 
ATOM   4185  C  C   . CYS B  1 152 ? 4.668   -23.347 74.705  1.00 13.82  ? 239  CYS B C   1 
ATOM   4186  O  O   . CYS B  1 152 ? 4.881   -23.506 75.927  1.00 14.33  ? 239  CYS B O   1 
ATOM   4187  C  CB  . CYS B  1 152 ? 6.387   -21.934 73.626  1.00 12.96  ? 239  CYS B CB  1 
ATOM   4188  S  SG  . CYS B  1 152 ? 6.863   -20.353 72.900  1.00 12.42  ? 239  CYS B SG  1 
ATOM   4189  N  N   . HIS B  1 153 ? 4.235   -24.313 73.897  1.00 13.48  ? 240  HIS B N   1 
ATOM   4190  C  CA  . HIS B  1 153 ? 3.992   -25.668 74.359  1.00 14.10  ? 240  HIS B CA  1 
ATOM   4191  C  C   . HIS B  1 153 ? 4.452   -26.627 73.255  1.00 14.53  ? 240  HIS B C   1 
ATOM   4192  O  O   . HIS B  1 153 ? 3.950   -26.546 72.124  1.00 14.63  ? 240  HIS B O   1 
ATOM   4193  C  CB  . HIS B  1 153 ? 2.507   -25.861 74.639  1.00 13.95  ? 240  HIS B CB  1 
ATOM   4194  C  CG  . HIS B  1 153 ? 2.163   -27.230 75.126  1.00 14.51  ? 240  HIS B CG  1 
ATOM   4195  N  ND1 . HIS B  1 153 ? 1.473   -28.144 74.360  1.00 16.46  ? 240  HIS B ND1 1 
ATOM   4196  C  CD2 . HIS B  1 153 ? 2.429   -27.845 76.300  1.00 14.41  ? 240  HIS B CD2 1 
ATOM   4197  C  CE1 . HIS B  1 153 ? 1.305   -29.256 75.053  1.00 14.74  ? 240  HIS B CE1 1 
ATOM   4198  N  NE2 . HIS B  1 153 ? 1.883   -29.104 76.230  1.00 18.02  ? 240  HIS B NE2 1 
ATOM   4199  N  N   . LYS B  1 154 ? 5.406   -27.510 73.570  1.00 14.77  ? 241  LYS B N   1 
ATOM   4200  C  CA  . LYS B  1 154 ? 5.928   -28.483 72.581  1.00 14.97  ? 241  LYS B CA  1 
ATOM   4201  C  C   . LYS B  1 154 ? 6.430   -27.805 71.300  1.00 14.68  ? 241  LYS B C   1 
ATOM   4202  O  O   . LYS B  1 154 ? 6.304   -28.341 70.187  1.00 15.13  ? 241  LYS B O   1 
ATOM   4203  C  CB  . LYS B  1 154 ? 4.866   -29.554 72.265  1.00 14.87  ? 241  LYS B CB  1 
ATOM   4204  C  CG  . LYS B  1 154 ? 4.581   -30.490 73.448  1.00 14.93  ? 241  LYS B CG  1 
ATOM   4205  C  CD  . LYS B  1 154 ? 3.509   -31.524 73.130  1.00 15.92  ? 241  LYS B CD  1 
ATOM   4206  C  CE  . LYS B  1 154 ? 3.223   -32.374 74.371  1.00 19.39  ? 241  LYS B CE  1 
ATOM   4207  N  NZ  . LYS B  1 154 ? 2.200   -33.446 74.107  1.00 21.32  ? 241  LYS B NZ  1 
ATOM   4208  N  N   . GLY B  1 155 ? 6.993   -26.614 71.465  1.00 14.47  ? 242  GLY B N   1 
ATOM   4209  C  CA  . GLY B  1 155 ? 7.497   -25.824 70.340  1.00 14.07  ? 242  GLY B CA  1 
ATOM   4210  C  C   . GLY B  1 155 ? 6.521   -24.929 69.605  1.00 12.87  ? 242  GLY B C   1 
ATOM   4211  O  O   . GLY B  1 155 ? 6.929   -24.143 68.759  1.00 13.48  ? 242  GLY B O   1 
ATOM   4212  N  N   . VAL B  1 156 ? 5.232   -25.051 69.909  1.00 13.22  ? 243  VAL B N   1 
ATOM   4213  C  CA  . VAL B  1 156 ? 4.188   -24.199 69.310  1.00 12.44  ? 243  VAL B CA  1 
ATOM   4214  C  C   . VAL B  1 156 ? 3.871   -23.002 70.214  1.00 12.21  ? 243  VAL B C   1 
ATOM   4215  O  O   . VAL B  1 156 ? 3.490   -23.183 71.375  1.00 12.68  ? 243  VAL B O   1 
ATOM   4216  C  CB  . VAL B  1 156 ? 2.878   -24.995 69.024  1.00 13.18  ? 243  VAL B CB  1 
ATOM   4217  C  CG1 . VAL B  1 156 ? 1.809   -24.086 68.411  1.00 11.84  ? 243  VAL B CG1 1 
ATOM   4218  C  CG2 . VAL B  1 156 ? 3.172   -26.180 68.091  1.00 13.65  ? 243  VAL B CG2 1 
ATOM   4219  N  N   . CYS B  1 157 ? 4.022   -21.800 69.660  1.00 11.66  ? 244  CYS B N   1 
ATOM   4220  C  CA  . CYS B  1 157 ? 3.839   -20.553 70.403  1.00 11.35  ? 244  CYS B CA  1 
ATOM   4221  C  C   . CYS B  1 157 ? 2.733   -19.732 69.731  1.00 11.03  ? 244  CYS B C   1 
ATOM   4222  O  O   . CYS B  1 157 ? 2.985   -19.095 68.692  1.00 11.28  ? 244  CYS B O   1 
ATOM   4223  C  CB  . CYS B  1 157 ? 5.147   -19.753 70.414  1.00 11.60  ? 244  CYS B CB  1 
ATOM   4224  S  SG  . CYS B  1 157 ? 6.663   -20.645 70.892  1.00 13.19  ? 244  CYS B SG  1 
ATOM   4225  N  N   . PRO B  1 158 ? 1.494   -19.790 70.264  1.00 10.00  ? 245  PRO B N   1 
ATOM   4226  C  CA  . PRO B  1 158 ? 0.425   -18.940 69.699  1.00 10.34  ? 245  PRO B CA  1 
ATOM   4227  C  C   . PRO B  1 158 ? 0.640   -17.459 70.034  1.00 9.99   ? 245  PRO B C   1 
ATOM   4228  O  O   . PRO B  1 158 ? 1.130   -17.130 71.123  1.00 9.54   ? 245  PRO B O   1 
ATOM   4229  C  CB  . PRO B  1 158 ? -0.848  -19.443 70.394  1.00 10.51  ? 245  PRO B CB  1 
ATOM   4230  C  CG  . PRO B  1 158 ? -0.468  -20.841 70.976  1.00 11.55  ? 245  PRO B CG  1 
ATOM   4231  C  CD  . PRO B  1 158 ? 0.996   -20.648 71.357  1.00 10.08  ? 245  PRO B CD  1 
ATOM   4232  N  N   . VAL B  1 159 ? 0.249   -16.594 69.103  1.00 9.89   ? 246  VAL B N   1 
ATOM   4233  C  CA  . VAL B  1 159 ? 0.362   -15.138 69.249  1.00 10.03  ? 246  VAL B CA  1 
ATOM   4234  C  C   . VAL B  1 159 ? -0.936  -14.522 68.742  1.00 10.16  ? 246  VAL B C   1 
ATOM   4235  O  O   . VAL B  1 159 ? -1.399  -14.853 67.644  1.00 11.53  ? 246  VAL B O   1 
ATOM   4236  C  CB  . VAL B  1 159 ? 1.558   -14.554 68.452  1.00 9.58   ? 246  VAL B CB  1 
ATOM   4237  C  CG1 . VAL B  1 159 ? 1.544   -13.017 68.465  1.00 8.97   ? 246  VAL B CG1 1 
ATOM   4238  C  CG2 . VAL B  1 159 ? 2.937   -15.111 68.985  1.00 9.52   ? 246  VAL B CG2 1 
ATOM   4239  N  N   . VAL B  1 160 ? -1.510  -13.623 69.537  1.00 10.33  ? 247  VAL B N   1 
ATOM   4240  C  CA  . VAL B  1 160 ? -2.750  -12.946 69.159  1.00 9.61   ? 247  VAL B CA  1 
ATOM   4241  C  C   . VAL B  1 160 ? -2.363  -11.615 68.530  1.00 9.88   ? 247  VAL B C   1 
ATOM   4242  O  O   . VAL B  1 160 ? -1.592  -10.847 69.119  1.00 9.73   ? 247  VAL B O   1 
ATOM   4243  C  CB  . VAL B  1 160 ? -3.703  -12.765 70.366  1.00 9.54   ? 247  VAL B CB  1 
ATOM   4244  C  CG1 . VAL B  1 160 ? -5.032  -12.094 69.931  1.00 8.51   ? 247  VAL B CG1 1 
ATOM   4245  C  CG2 . VAL B  1 160 ? -3.962  -14.123 71.059  1.00 8.52   ? 247  VAL B CG2 1 
ATOM   4246  N  N   . MET B  1 161 ? -2.868  -11.372 67.321  1.00 9.96   ? 248  MET B N   1 
ATOM   4247  C  CA  . MET B  1 161 ? -2.621  -10.108 66.604  1.00 9.81   ? 248  MET B CA  1 
ATOM   4248  C  C   . MET B  1 161 ? -3.920  -9.463  66.136  1.00 10.48  ? 248  MET B C   1 
ATOM   4249  O  O   . MET B  1 161 ? -4.882  -10.157 65.836  1.00 10.41  ? 248  MET B O   1 
ATOM   4250  C  CB  . MET B  1 161 ? -1.744  -10.356 65.375  1.00 9.71   ? 248  MET B CB  1 
ATOM   4251  C  CG  . MET B  1 161 ? -0.353  -10.952 65.674  1.00 8.82   ? 248  MET B CG  1 
ATOM   4252  S  SD  . MET B  1 161 ? 0.523   -11.251 64.121  1.00 10.58  ? 248  MET B SD  1 
ATOM   4253  C  CE  . MET B  1 161 ? 1.957   -12.149 64.730  1.00 8.89   ? 248  MET B CE  1 
ATOM   4254  N  N   . THR B  1 162 ? -3.926  -8.135  66.062  1.00 10.37  ? 249  THR B N   1 
ATOM   4255  C  CA  . THR B  1 162 ? -5.091  -7.377  65.576  1.00 11.19  ? 249  THR B CA  1 
ATOM   4256  C  C   . THR B  1 162 ? -4.694  -6.409  64.475  1.00 11.02  ? 249  THR B C   1 
ATOM   4257  O  O   . THR B  1 162 ? -3.596  -5.867  64.497  1.00 10.47  ? 249  THR B O   1 
ATOM   4258  C  CB  . THR B  1 162 ? -5.792  -6.629  66.734  1.00 11.02  ? 249  THR B CB  1 
ATOM   4259  O  OG1 . THR B  1 162 ? -6.183  -7.584  67.724  1.00 11.27  ? 249  THR B OG1 1 
ATOM   4260  C  CG2 . THR B  1 162 ? -7.038  -5.855  66.242  1.00 11.75  ? 249  THR B CG2 1 
ATOM   4261  N  N   . ASP B  1 163 ? -5.595  -6.202  63.512  1.00 10.27  ? 250  ASP B N   1 
ATOM   4262  C  CA  . ASP B  1 163 ? -5.396  -5.246  62.431  1.00 11.60  ? 250  ASP B CA  1 
ATOM   4263  C  C   . ASP B  1 163 ? -6.804  -4.697  62.162  1.00 11.74  ? 250  ASP B C   1 
ATOM   4264  O  O   . ASP B  1 163 ? -7.737  -5.467  62.011  1.00 11.78  ? 250  ASP B O   1 
ATOM   4265  C  CB  . ASP B  1 163 ? -4.837  -5.990  61.205  1.00 11.58  ? 250  ASP B CB  1 
ATOM   4266  C  CG  . ASP B  1 163 ? -4.241  -5.063  60.147  1.00 12.06  ? 250  ASP B CG  1 
ATOM   4267  O  OD1 . ASP B  1 163 ? -3.510  -5.582  59.282  1.00 13.37  ? 250  ASP B OD1 1 
ATOM   4268  O  OD2 . ASP B  1 163 ? -4.482  -3.839  60.156  1.00 12.92  ? 250  ASP B OD2 1 
ATOM   4269  N  N   . GLY B  1 164 ? -6.950  -3.380  62.126  1.00 11.66  ? 251  GLY B N   1 
ATOM   4270  C  CA  . GLY B  1 164 ? -8.272  -2.763  62.020  1.00 12.91  ? 251  GLY B CA  1 
ATOM   4271  C  C   . GLY B  1 164 ? -8.464  -1.625  63.020  1.00 13.62  ? 251  GLY B C   1 
ATOM   4272  O  O   . GLY B  1 164 ? -7.540  -1.298  63.778  1.00 13.84  ? 251  GLY B O   1 
ATOM   4273  N  N   . PRO B  1 165 ? -9.658  -0.989  63.021  1.00 13.82  ? 252  PRO B N   1 
ATOM   4274  C  CA  . PRO B  1 165 ? -9.891  0.161   63.908  1.00 14.63  ? 252  PRO B CA  1 
ATOM   4275  C  C   . PRO B  1 165 ? -9.763  -0.208  65.386  1.00 14.65  ? 252  PRO B C   1 
ATOM   4276  O  O   . PRO B  1 165 ? -10.031 -1.360  65.774  1.00 15.18  ? 252  PRO B O   1 
ATOM   4277  C  CB  . PRO B  1 165 ? -11.347 0.566   63.613  1.00 14.32  ? 252  PRO B CB  1 
ATOM   4278  C  CG  . PRO B  1 165 ? -11.688 -0.066  62.328  1.00 15.05  ? 252  PRO B CG  1 
ATOM   4279  C  CD  . PRO B  1 165 ? -10.840 -1.306  62.198  1.00 14.33  ? 252  PRO B CD  1 
ATOM   4280  N  N   . ALA B  1 166 ? -9.328  0.769   66.178  1.00 15.19  ? 253  ALA B N   1 
ATOM   4281  C  CA  . ALA B  1 166 ? -9.258  0.653   67.636  1.00 15.65  ? 253  ALA B CA  1 
ATOM   4282  C  C   . ALA B  1 166 ? -10.631 0.872   68.282  1.00 15.96  ? 253  ALA B C   1 
ATOM   4283  O  O   . ALA B  1 166 ? -10.834 0.505   69.434  1.00 15.47  ? 253  ALA B O   1 
ATOM   4284  C  CB  . ALA B  1 166 ? -8.242  1.667   68.200  1.00 16.14  ? 253  ALA B CB  1 
ATOM   4285  N  N   . ASN B  1 167 ? -11.573 1.431   67.522  1.00 16.21  ? 254  ASN B N   1 
ATOM   4286  C  CA  . ASN B  1 167 ? -12.840 1.928   68.069  1.00 17.24  ? 254  ASN B CA  1 
ATOM   4287  C  C   . ASN B  1 167 ? -14.056 1.374   67.333  1.00 17.33  ? 254  ASN B C   1 
ATOM   4288  O  O   . ASN B  1 167 ? -15.137 1.979   67.324  1.00 17.27  ? 254  ASN B O   1 
ATOM   4289  C  CB  . ASN B  1 167 ? -12.852 3.448   67.976  1.00 17.50  ? 254  ASN B CB  1 
ATOM   4290  C  CG  . ASN B  1 167 ? -12.888 3.943   66.529  1.00 19.20  ? 254  ASN B CG  1 
ATOM   4291  O  OD1 . ASN B  1 167 ? -12.594 3.199   65.580  1.00 18.54  ? 254  ASN B OD1 1 
ATOM   4292  N  ND2 . ASN B  1 167 ? -13.258 5.208   66.358  1.00 20.94  ? 254  ASN B ND2 1 
ATOM   4293  N  N   . ASN B  1 168 ? -13.851 0.242   66.672  1.00 16.79  ? 255  ASN B N   1 
ATOM   4294  C  CA  . ASN B  1 168 ? -14.904 -0.482  66.007  1.00 16.86  ? 255  ASN B CA  1 
ATOM   4295  C  C   . ASN B  1 168 ? -14.432 -1.917  65.824  1.00 16.75  ? 255  ASN B C   1 
ATOM   4296  O  O   . ASN B  1 168 ? -13.337 -2.275  66.288  1.00 16.98  ? 255  ASN B O   1 
ATOM   4297  C  CB  . ASN B  1 168 ? -15.249 0.153   64.652  1.00 17.23  ? 255  ASN B CB  1 
ATOM   4298  C  CG  . ASN B  1 168 ? -16.736 0.078   64.346  1.00 18.03  ? 255  ASN B CG  1 
ATOM   4299  O  OD1 . ASN B  1 168 ? -17.351 -0.977  64.429  1.00 17.81  ? 255  ASN B OD1 1 
ATOM   4300  N  ND2 . ASN B  1 168 ? -17.327 1.219   64.048  1.00 23.63  ? 255  ASN B ND2 1 
ATOM   4301  N  N   . ARG B  1 169 ? -15.241 -2.723  65.144  1.00 16.28  ? 256  ARG B N   1 
ATOM   4302  C  CA  . ARG B  1 169 ? -14.908 -4.105  64.856  1.00 16.36  ? 256  ARG B CA  1 
ATOM   4303  C  C   . ARG B  1 169 ? -13.575 -4.170  64.080  1.00 15.47  ? 256  ARG B C   1 
ATOM   4304  O  O   . ARG B  1 169 ? -13.347 -3.368  63.180  1.00 14.61  ? 256  ARG B O   1 
ATOM   4305  C  CB  . ARG B  1 169 ? -16.033 -4.748  64.044  1.00 17.34  ? 256  ARG B CB  1 
ATOM   4306  C  CG  . ARG B  1 169 ? -15.917 -6.241  63.932  1.00 19.43  ? 256  ARG B CG  1 
ATOM   4307  C  CD  . ARG B  1 169 ? -17.234 -6.912  63.493  1.00 25.65  ? 256  ARG B CD  1 
ATOM   4308  N  NE  . ARG B  1 169 ? -18.377 -6.753  64.411  1.00 27.81  ? 256  ARG B NE  1 
ATOM   4309  C  CZ  . ARG B  1 169 ? -18.536 -7.375  65.588  1.00 30.39  ? 256  ARG B CZ  1 
ATOM   4310  N  NH1 . ARG B  1 169 ? -19.640 -7.150  66.295  1.00 29.80  ? 256  ARG B NH1 1 
ATOM   4311  N  NH2 . ARG B  1 169 ? -17.603 -8.201  66.090  1.00 30.31  ? 256  ARG B NH2 1 
ATOM   4312  N  N   . ALA B  1 170 ? -12.714 -5.119  64.444  1.00 14.46  ? 257  ALA B N   1 
ATOM   4313  C  CA  . ALA B  1 170 ? -11.387 -5.251  63.811  1.00 13.42  ? 257  ALA B CA  1 
ATOM   4314  C  C   . ALA B  1 170 ? -11.149 -6.702  63.442  1.00 13.14  ? 257  ALA B C   1 
ATOM   4315  O  O   . ALA B  1 170 ? -11.997 -7.553  63.721  1.00 13.57  ? 257  ALA B O   1 
ATOM   4316  C  CB  . ALA B  1 170 ? -10.277 -4.712  64.741  1.00 13.01  ? 257  ALA B CB  1 
ATOM   4317  N  N   . ALA B  1 171 ? -10.003 -6.994  62.825  1.00 12.04  ? 258  ALA B N   1 
ATOM   4318  C  CA  . ALA B  1 171 ? -9.712  -8.329  62.350  1.00 11.86  ? 258  ALA B CA  1 
ATOM   4319  C  C   . ALA B  1 171 ? -8.580  -8.919  63.171  1.00 12.18  ? 258  ALA B C   1 
ATOM   4320  O  O   . ALA B  1 171 ? -7.411  -8.596  62.952  1.00 12.30  ? 258  ALA B O   1 
ATOM   4321  C  CB  . ALA B  1 171 ? -9.350  -8.311  60.849  1.00 11.37  ? 258  ALA B CB  1 
ATOM   4322  N  N   . THR B  1 172 ? -8.949  -9.766  64.123  1.00 11.02  ? 259  THR B N   1 
ATOM   4323  C  CA  . THR B  1 172 ? -8.005  -10.395 65.030  1.00 11.38  ? 259  THR B CA  1 
ATOM   4324  C  C   . THR B  1 172 ? -7.709  -11.807 64.529  1.00 11.84  ? 259  THR B C   1 
ATOM   4325  O  O   . THR B  1 172 ? -8.613  -12.521 64.055  1.00 11.06  ? 259  THR B O   1 
ATOM   4326  C  CB  . THR B  1 172 ? -8.564  -10.412 66.472  1.00 10.73  ? 259  THR B CB  1 
ATOM   4327  O  OG1 . THR B  1 172 ? -8.554  -9.068  66.986  1.00 10.74  ? 259  THR B OG1 1 
ATOM   4328  C  CG2 . THR B  1 172 ? -7.732  -11.341 67.399  1.00 10.50  ? 259  THR B CG2 1 
ATOM   4329  N  N   . LYS B  1 173 ? -6.435  -12.180 64.598  1.00 11.52  ? 260  LYS B N   1 
ATOM   4330  C  CA  . LYS B  1 173 ? -6.022  -13.545 64.290  1.00 12.34  ? 260  LYS B CA  1 
ATOM   4331  C  C   . LYS B  1 173 ? -5.139  -14.163 65.384  1.00 12.45  ? 260  LYS B C   1 
ATOM   4332  O  O   . LYS B  1 173 ? -4.433  -13.458 66.120  1.00 12.18  ? 260  LYS B O   1 
ATOM   4333  C  CB  . LYS B  1 173 ? -5.304  -13.602 62.932  1.00 12.24  ? 260  LYS B CB  1 
ATOM   4334  C  CG  . LYS B  1 173 ? -6.093  -12.979 61.793  1.00 12.37  ? 260  LYS B CG  1 
ATOM   4335  C  CD  . LYS B  1 173 ? -5.426  -13.217 60.441  1.00 13.24  ? 260  LYS B CD  1 
ATOM   4336  C  CE  . LYS B  1 173 ? -6.308  -12.667 59.343  1.00 16.04  ? 260  LYS B CE  1 
ATOM   4337  N  NZ  . LYS B  1 173 ? -5.556  -12.648 58.060  1.00 19.18  ? 260  LYS B NZ  1 
ATOM   4338  N  N   . ILE B  1 174 ? -5.210  -15.478 65.494  1.00 12.67  ? 261  ILE B N   1 
ATOM   4339  C  CA  . ILE B  1 174 ? -4.274  -16.237 66.332  1.00 13.25  ? 261  ILE B CA  1 
ATOM   4340  C  C   . ILE B  1 174 ? -3.339  -16.960 65.379  1.00 13.29  ? 261  ILE B C   1 
ATOM   4341  O  O   . ILE B  1 174 ? -3.788  -17.726 64.516  1.00 13.11  ? 261  ILE B O   1 
ATOM   4342  C  CB  . ILE B  1 174 ? -4.950  -17.282 67.227  1.00 13.87  ? 261  ILE B CB  1 
ATOM   4343  C  CG1 . ILE B  1 174 ? -6.252  -16.773 67.892  1.00 14.70  ? 261  ILE B CG1 1 
ATOM   4344  C  CG2 . ILE B  1 174 ? -3.926  -17.920 68.219  1.00 12.72  ? 261  ILE B CG2 1 
ATOM   4345  C  CD1 . ILE B  1 174 ? -6.192  -15.482 68.578  1.00 17.69  ? 261  ILE B CD1 1 
ATOM   4346  N  N   . ILE B  1 175 ? -2.047  -16.690 65.520  1.00 12.57  ? 262  ILE B N   1 
ATOM   4347  C  CA  . ILE B  1 175 ? -1.050  -17.296 64.643  1.00 13.15  ? 262  ILE B CA  1 
ATOM   4348  C  C   . ILE B  1 175 ? -0.144  -18.191 65.478  1.00 13.20  ? 262  ILE B C   1 
ATOM   4349  O  O   . ILE B  1 175 ? 0.408   -17.758 66.498  1.00 13.78  ? 262  ILE B O   1 
ATOM   4350  C  CB  . ILE B  1 175 ? -0.275  -16.235 63.782  1.00 13.53  ? 262  ILE B CB  1 
ATOM   4351  C  CG1 . ILE B  1 175 ? -1.277  -15.410 62.929  1.00 13.09  ? 262  ILE B CG1 1 
ATOM   4352  C  CG2 . ILE B  1 175 ? 0.783   -16.930 62.884  1.00 11.52  ? 262  ILE B CG2 1 
ATOM   4353  C  CD1 . ILE B  1 175 ? -0.700  -14.187 62.202  1.00 14.80  ? 262  ILE B CD1 1 
ATOM   4354  N  N   . TYR B  1 176 ? -0.062  -19.456 65.061  1.00 13.02  ? 263  TYR B N   1 
ATOM   4355  C  CA  . TYR B  1 176 ? 0.672   -20.495 65.769  1.00 12.34  ? 263  TYR B CA  1 
ATOM   4356  C  C   . TYR B  1 176 ? 2.036   -20.632 65.111  1.00 12.72  ? 263  TYR B C   1 
ATOM   4357  O  O   . TYR B  1 176 ? 2.133   -20.957 63.924  1.00 13.31  ? 263  TYR B O   1 
ATOM   4358  C  CB  . TYR B  1 176 ? -0.108  -21.824 65.750  1.00 12.35  ? 263  TYR B CB  1 
ATOM   4359  C  CG  . TYR B  1 176 ? -1.498  -21.722 66.362  1.00 11.94  ? 263  TYR B CG  1 
ATOM   4360  C  CD1 . TYR B  1 176 ? -2.596  -21.314 65.597  1.00 12.78  ? 263  TYR B CD1 1 
ATOM   4361  C  CD2 . TYR B  1 176 ? -1.706  -22.020 67.711  1.00 12.56  ? 263  TYR B CD2 1 
ATOM   4362  C  CE1 . TYR B  1 176 ? -3.873  -21.208 66.172  1.00 12.81  ? 263  TYR B CE1 1 
ATOM   4363  C  CE2 . TYR B  1 176 ? -2.961  -21.941 68.288  1.00 12.04  ? 263  TYR B CE2 1 
ATOM   4364  C  CZ  . TYR B  1 176 ? -4.038  -21.530 67.521  1.00 13.18  ? 263  TYR B CZ  1 
ATOM   4365  O  OH  . TYR B  1 176 ? -5.287  -21.437 68.094  1.00 12.53  ? 263  TYR B OH  1 
ATOM   4366  N  N   . PHE B  1 177 ? 3.083   -20.378 65.887  1.00 12.50  ? 264  PHE B N   1 
ATOM   4367  C  CA  . PHE B  1 177 ? 4.462   -20.462 65.394  1.00 12.71  ? 264  PHE B CA  1 
ATOM   4368  C  C   . PHE B  1 177 ? 5.219   -21.660 65.964  1.00 13.26  ? 264  PHE B C   1 
ATOM   4369  O  O   . PHE B  1 177 ? 4.990   -22.071 67.102  1.00 13.48  ? 264  PHE B O   1 
ATOM   4370  C  CB  . PHE B  1 177 ? 5.251   -19.185 65.756  1.00 12.76  ? 264  PHE B CB  1 
ATOM   4371  C  CG  . PHE B  1 177 ? 4.730   -17.935 65.119  1.00 12.40  ? 264  PHE B CG  1 
ATOM   4372  C  CD1 . PHE B  1 177 ? 3.900   -17.065 65.840  1.00 12.26  ? 264  PHE B CD1 1 
ATOM   4373  C  CD2 . PHE B  1 177 ? 5.065   -17.616 63.802  1.00 10.53  ? 264  PHE B CD2 1 
ATOM   4374  C  CE1 . PHE B  1 177 ? 3.404   -15.899 65.255  1.00 12.15  ? 264  PHE B CE1 1 
ATOM   4375  C  CE2 . PHE B  1 177 ? 4.586   -16.464 63.202  1.00 10.26  ? 264  PHE B CE2 1 
ATOM   4376  C  CZ  . PHE B  1 177 ? 3.765   -15.582 63.940  1.00 11.89  ? 264  PHE B CZ  1 
ATOM   4377  N  N   . LYS B  1 178 ? 6.143   -22.194 65.168  1.00 13.57  ? 265  LYS B N   1 
ATOM   4378  C  CA  . LYS B  1 178 ? 7.171   -23.129 65.647  1.00 13.72  ? 265  LYS B CA  1 
ATOM   4379  C  C   . LYS B  1 178 ? 8.507   -22.770 64.995  1.00 13.85  ? 265  LYS B C   1 
ATOM   4380  O  O   . LYS B  1 178 ? 8.608   -22.729 63.769  1.00 13.16  ? 265  LYS B O   1 
ATOM   4381  C  CB  . LYS B  1 178 ? 6.789   -24.595 65.358  1.00 14.10  ? 265  LYS B CB  1 
ATOM   4382  C  CG  . LYS B  1 178 ? 7.839   -25.600 65.815  1.00 15.31  ? 265  LYS B CG  1 
ATOM   4383  C  CD  . LYS B  1 178 ? 7.253   -26.988 65.901  1.00 18.36  ? 265  LYS B CD  1 
ATOM   4384  C  CE  . LYS B  1 178 ? 8.350   -28.008 66.145  1.00 23.28  ? 265  LYS B CE  1 
ATOM   4385  N  NZ  . LYS B  1 178 ? 7.776   -29.377 66.223  1.00 25.42  ? 265  LYS B NZ  1 
ATOM   4386  N  N   . GLU B  1 179 ? 9.515   -22.479 65.821  1.00 14.11  ? 266  GLU B N   1 
ATOM   4387  C  CA  . GLU B  1 179 ? 10.820  -22.014 65.339  1.00 15.07  ? 266  GLU B CA  1 
ATOM   4388  C  C   . GLU B  1 179 ? 10.677  -20.807 64.395  1.00 14.20  ? 266  GLU B C   1 
ATOM   4389  O  O   . GLU B  1 179 ? 11.371  -20.688 63.380  1.00 13.63  ? 266  GLU B O   1 
ATOM   4390  C  CB  . GLU B  1 179 ? 11.609  -23.179 64.710  1.00 14.58  ? 266  GLU B CB  1 
ATOM   4391  C  CG  . GLU B  1 179 ? 11.780  -24.308 65.709  1.00 17.28  ? 266  GLU B CG  1 
ATOM   4392  C  CD  . GLU B  1 179 ? 12.531  -25.520 65.193  1.00 18.99  ? 266  GLU B CD  1 
ATOM   4393  O  OE1 . GLU B  1 179 ? 12.502  -25.806 63.968  1.00 23.13  ? 266  GLU B OE1 1 
ATOM   4394  O  OE2 . GLU B  1 179 ? 13.133  -26.205 66.046  1.00 24.22  ? 266  GLU B OE2 1 
ATOM   4395  N  N   . GLY B  1 180 ? 9.720   -19.933 64.725  1.00 13.94  ? 267  GLY B N   1 
ATOM   4396  C  CA  . GLY B  1 180 ? 9.451   -18.716 63.945  1.00 13.51  ? 267  GLY B CA  1 
ATOM   4397  C  C   . GLY B  1 180 ? 8.698   -18.926 62.630  1.00 13.89  ? 267  GLY B C   1 
ATOM   4398  O  O   . GLY B  1 180 ? 8.475   -17.966 61.902  1.00 14.23  ? 267  GLY B O   1 
ATOM   4399  N  N   . LYS B  1 181 ? 8.292   -20.165 62.326  1.00 14.06  ? 268  LYS B N   1 
ATOM   4400  C  CA  . LYS B  1 181 ? 7.556   -20.447 61.074  1.00 14.70  ? 268  LYS B CA  1 
ATOM   4401  C  C   . LYS B  1 181 ? 6.061   -20.607 61.368  1.00 13.25  ? 268  LYS B C   1 
ATOM   4402  O  O   . LYS B  1 181 ? 5.696   -21.198 62.375  1.00 12.63  ? 268  LYS B O   1 
ATOM   4403  C  CB  . LYS B  1 181 ? 8.075   -21.722 60.391  1.00 14.61  ? 268  LYS B CB  1 
ATOM   4404  C  CG  . LYS B  1 181 ? 9.591   -21.767 60.124  1.00 15.64  ? 268  LYS B CG  1 
ATOM   4405  C  CD  . LYS B  1 181 ? 9.992   -23.160 59.614  1.00 18.08  ? 268  LYS B CD  1 
ATOM   4406  C  CE  . LYS B  1 181 ? 11.524  -23.395 59.608  1.00 21.93  ? 268  LYS B CE  1 
ATOM   4407  N  NZ  . LYS B  1 181 ? 12.084  -23.984 60.912  1.00 24.86  ? 268  LYS B NZ  1 
ATOM   4408  N  N   . ILE B  1 182 ? 5.210   -20.100 60.479  1.00 12.62  ? 269  ILE B N   1 
ATOM   4409  C  CA  . ILE B  1 182 ? 3.744   -20.176 60.677  1.00 13.23  ? 269  ILE B CA  1 
ATOM   4410  C  C   . ILE B  1 182 ? 3.250   -21.631 60.498  1.00 13.18  ? 269  ILE B C   1 
ATOM   4411  O  O   . ILE B  1 182 ? 3.498   -22.252 59.462  1.00 13.69  ? 269  ILE B O   1 
ATOM   4412  C  CB  . ILE B  1 182 ? 2.987   -19.202 59.741  1.00 12.57  ? 269  ILE B CB  1 
ATOM   4413  C  CG1 . ILE B  1 182 ? 3.346   -17.737 60.079  1.00 12.90  ? 269  ILE B CG1 1 
ATOM   4414  C  CG2 . ILE B  1 182 ? 1.449   -19.425 59.819  1.00 14.65  ? 269  ILE B CG2 1 
ATOM   4415  C  CD1 . ILE B  1 182 ? 2.889   -16.718 59.043  1.00 13.63  ? 269  ILE B CD1 1 
ATOM   4416  N  N   . GLN B  1 183 ? 2.593   -22.165 61.522  1.00 12.66  ? 270  GLN B N   1 
ATOM   4417  C  CA  . GLN B  1 183 ? 2.061   -23.525 61.479  1.00 12.30  ? 270  GLN B CA  1 
ATOM   4418  C  C   . GLN B  1 183 ? 0.578   -23.493 61.095  1.00 12.49  ? 270  GLN B C   1 
ATOM   4419  O  O   . GLN B  1 183 ? 0.086   -24.407 60.419  1.00 11.44  ? 270  GLN B O   1 
ATOM   4420  C  CB  . GLN B  1 183 ? 2.256   -24.204 62.832  1.00 12.62  ? 270  GLN B CB  1 
ATOM   4421  C  CG  . GLN B  1 183 ? 3.706   -24.181 63.326  1.00 13.50  ? 270  GLN B CG  1 
ATOM   4422  C  CD  . GLN B  1 183 ? 4.663   -24.928 62.384  1.00 17.01  ? 270  GLN B CD  1 
ATOM   4423  O  OE1 . GLN B  1 183 ? 5.498   -24.322 61.712  1.00 19.04  ? 270  GLN B OE1 1 
ATOM   4424  N  NE2 . GLN B  1 183 ? 4.530   -26.247 62.333  1.00 17.03  ? 270  GLN B NE2 1 
ATOM   4425  N  N   . LYS B  1 184 ? -0.116  -22.420 61.508  1.00 11.38  ? 271  LYS B N   1 
ATOM   4426  C  CA  . LYS B  1 184 ? -1.569  -22.292 61.327  1.00 12.03  ? 271  LYS B CA  1 
ATOM   4427  C  C   . LYS B  1 184 ? -1.956  -20.858 61.660  1.00 12.75  ? 271  LYS B C   1 
ATOM   4428  O  O   . LYS B  1 184 ? -1.322  -20.220 62.521  1.00 12.53  ? 271  LYS B O   1 
ATOM   4429  C  CB  . LYS B  1 184 ? -2.348  -23.281 62.236  1.00 12.01  ? 271  LYS B CB  1 
ATOM   4430  C  CG  . LYS B  1 184 ? -3.900  -23.371 61.987  1.00 11.35  ? 271  LYS B CG  1 
ATOM   4431  C  CD  . LYS B  1 184 ? -4.526  -24.367 62.979  1.00 12.32  ? 271  LYS B CD  1 
ATOM   4432  C  CE  . LYS B  1 184 ? -6.024  -24.499 62.814  1.00 13.15  ? 271  LYS B CE  1 
ATOM   4433  N  NZ  . LYS B  1 184 ? -6.550  -25.453 63.822  1.00 16.48  ? 271  LYS B NZ  1 
ATOM   4434  N  N   . ILE B  1 185 ? -2.977  -20.361 60.969  1.00 13.31  ? 272  ILE B N   1 
ATOM   4435  C  CA  . ILE B  1 185 ? -3.558  -19.035 61.218  1.00 14.37  ? 272  ILE B CA  1 
ATOM   4436  C  C   . ILE B  1 185 ? -5.056  -19.244 61.409  1.00 15.07  ? 272  ILE B C   1 
ATOM   4437  O  O   . ILE B  1 185 ? -5.703  -19.885 60.562  1.00 14.70  ? 272  ILE B O   1 
ATOM   4438  C  CB  . ILE B  1 185 ? -3.339  -18.050 60.031  1.00 14.45  ? 272  ILE B CB  1 
ATOM   4439  C  CG1 . ILE B  1 185 ? -1.851  -17.791 59.777  1.00 15.01  ? 272  ILE B CG1 1 
ATOM   4440  C  CG2 . ILE B  1 185 ? -4.031  -16.711 60.279  1.00 13.78  ? 272  ILE B CG2 1 
ATOM   4441  C  CD1 . ILE B  1 185 ? -1.564  -17.144 58.434  1.00 15.52  ? 272  ILE B CD1 1 
ATOM   4442  N  N   . GLU B  1 186 ? -5.599  -18.733 62.518  1.00 15.36  ? 273  GLU B N   1 
ATOM   4443  C  CA  . GLU B  1 186 ? -7.056  -18.731 62.752  1.00 16.16  ? 273  GLU B CA  1 
ATOM   4444  C  C   . GLU B  1 186 ? -7.634  -17.314 62.891  1.00 15.69  ? 273  GLU B C   1 
ATOM   4445  O  O   . GLU B  1 186 ? -7.028  -16.440 63.535  1.00 15.31  ? 273  GLU B O   1 
ATOM   4446  C  CB  . GLU B  1 186 ? -7.425  -19.508 64.019  1.00 16.05  ? 273  GLU B CB  1 
ATOM   4447  C  CG  . GLU B  1 186 ? -7.080  -20.989 64.041  1.00 17.15  ? 273  GLU B CG  1 
ATOM   4448  C  CD  . GLU B  1 186 ? -7.665  -21.655 65.272  1.00 17.53  ? 273  GLU B CD  1 
ATOM   4449  O  OE1 . GLU B  1 186 ? -7.355  -21.224 66.419  1.00 16.75  ? 273  GLU B OE1 1 
ATOM   4450  O  OE2 . GLU B  1 186 ? -8.470  -22.594 65.089  1.00 20.19  ? 273  GLU B OE2 1 
ATOM   4451  N  N   . GLU B  1 187 ? -8.816  -17.098 62.315  1.00 15.11  ? 274  GLU B N   1 
ATOM   4452  C  CA  . GLU B  1 187 ? -9.566  -15.867 62.559  1.00 15.55  ? 274  GLU B CA  1 
ATOM   4453  C  C   . GLU B  1 187 ? -10.187 -15.998 63.925  1.00 14.73  ? 274  GLU B C   1 
ATOM   4454  O  O   . GLU B  1 187 ? -10.593 -17.103 64.306  1.00 14.22  ? 274  GLU B O   1 
ATOM   4455  C  CB  . GLU B  1 187 ? -10.673 -15.691 61.523  1.00 16.68  ? 274  GLU B CB  1 
ATOM   4456  C  CG  . GLU B  1 187 ? -10.134 -15.467 60.120  1.00 22.52  ? 274  GLU B CG  1 
ATOM   4457  C  CD  . GLU B  1 187 ? -11.216 -15.570 59.052  1.00 30.06  ? 274  GLU B CD  1 
ATOM   4458  O  OE1 . GLU B  1 187 ? -12.382 -15.190 59.342  1.00 32.11  ? 274  GLU B OE1 1 
ATOM   4459  O  OE2 . GLU B  1 187 ? -10.892 -16.043 57.929  1.00 34.22  ? 274  GLU B OE2 1 
ATOM   4460  N  N   . LEU B  1 188 ? -10.266 -14.889 64.666  1.00 13.62  ? 275  LEU B N   1 
ATOM   4461  C  CA  . LEU B  1 188 ? -10.853 -14.923 66.008  1.00 13.26  ? 275  LEU B CA  1 
ATOM   4462  C  C   . LEU B  1 188 ? -12.314 -15.389 65.901  1.00 13.20  ? 275  LEU B C   1 
ATOM   4463  O  O   . LEU B  1 188 ? -13.049 -14.945 65.011  1.00 12.54  ? 275  LEU B O   1 
ATOM   4464  C  CB  . LEU B  1 188 ? -10.758 -13.549 66.675  1.00 12.82  ? 275  LEU B CB  1 
ATOM   4465  C  CG  . LEU B  1 188 ? -11.479 -13.376 68.021  1.00 13.83  ? 275  LEU B CG  1 
ATOM   4466  C  CD1 . LEU B  1 188 ? -10.635 -13.988 69.144  1.00 12.50  ? 275  LEU B CD1 1 
ATOM   4467  C  CD2 . LEU B  1 188 ? -11.818 -11.905 68.299  1.00 12.91  ? 275  LEU B CD2 1 
ATOM   4468  N  N   . ALA B  1 189 ? -12.693 -16.322 66.776  1.00 13.34  ? 276  ALA B N   1 
ATOM   4469  C  CA  . ALA B  1 189 ? -14.059 -16.849 66.841  1.00 13.95  ? 276  ALA B CA  1 
ATOM   4470  C  C   . ALA B  1 189 ? -14.550 -16.638 68.262  1.00 14.34  ? 276  ALA B C   1 
ATOM   4471  O  O   . ALA B  1 189 ? -13.761 -16.278 69.148  1.00 14.06  ? 276  ALA B O   1 
ATOM   4472  C  CB  . ALA B  1 189 ? -14.068 -18.352 66.503  1.00 14.10  ? 276  ALA B CB  1 
ATOM   4473  N  N   . GLY B  1 190 ? -15.845 -16.864 68.476  1.00 14.10  ? 277  GLY B N   1 
ATOM   4474  C  CA  . GLY B  1 190 ? -16.426 -16.775 69.819  1.00 13.98  ? 277  GLY B CA  1 
ATOM   4475  C  C   . GLY B  1 190 ? -17.073 -15.439 70.125  1.00 13.92  ? 277  GLY B C   1 
ATOM   4476  O  O   . GLY B  1 190 ? -17.415 -14.667 69.211  1.00 13.84  ? 277  GLY B O   1 
ATOM   4477  N  N   . ASN B  1 191 ? -17.241 -15.151 71.413  1.00 13.50  ? 278  ASN B N   1 
ATOM   4478  C  CA  . ASN B  1 191 ? -18.059 -13.999 71.836  1.00 13.17  ? 278  ASN B CA  1 
ATOM   4479  C  C   . ASN B  1 191 ? -17.302 -12.705 72.139  1.00 12.80  ? 278  ASN B C   1 
ATOM   4480  O  O   . ASN B  1 191 ? -17.924 -11.681 72.368  1.00 11.90  ? 278  ASN B O   1 
ATOM   4481  C  CB  . ASN B  1 191 ? -18.967 -14.386 73.013  1.00 14.14  ? 278  ASN B CB  1 
ATOM   4482  C  CG  . ASN B  1 191 ? -20.001 -15.438 72.622  1.00 15.45  ? 278  ASN B CG  1 
ATOM   4483  O  OD1 . ASN B  1 191 ? -20.350 -15.565 71.449  1.00 19.10  ? 278  ASN B OD1 1 
ATOM   4484  N  ND2 . ASN B  1 191 ? -20.486 -16.187 73.589  1.00 19.11  ? 278  ASN B ND2 1 
ATOM   4485  N  N   . ALA B  1 192 ? -15.971 -12.748 72.149  1.00 12.03  ? 279  ALA B N   1 
ATOM   4486  C  CA  . ALA B  1 192 ? -15.199 -11.516 72.321  1.00 12.46  ? 279  ALA B CA  1 
ATOM   4487  C  C   . ALA B  1 192 ? -15.423 -10.599 71.114  1.00 12.33  ? 279  ALA B C   1 
ATOM   4488  O  O   . ALA B  1 192 ? -15.253 -11.033 69.973  1.00 12.19  ? 279  ALA B O   1 
ATOM   4489  C  CB  . ALA B  1 192 ? -13.701 -11.846 72.517  1.00 12.16  ? 279  ALA B CB  1 
ATOM   4490  N  N   . GLN B  1 193 ? -15.830 -9.349  71.354  1.00 11.85  ? 280  GLN B N   1 
ATOM   4491  C  CA  . GLN B  1 193 ? -16.212 -8.463  70.246  1.00 12.72  ? 280  GLN B CA  1 
ATOM   4492  C  C   . GLN B  1 193 ? -15.076 -7.592  69.705  1.00 12.38  ? 280  GLN B C   1 
ATOM   4493  O  O   . GLN B  1 193 ? -15.172 -7.024  68.603  1.00 12.14  ? 280  GLN B O   1 
ATOM   4494  C  CB  . GLN B  1 193 ? -17.422 -7.602  70.611  1.00 12.49  ? 280  GLN B CB  1 
ATOM   4495  C  CG  . GLN B  1 193 ? -18.679 -8.396  70.878  1.00 15.57  ? 280  GLN B CG  1 
ATOM   4496  C  CD  . GLN B  1 193 ? -19.934 -7.545  70.858  1.00 20.41  ? 280  GLN B CD  1 
ATOM   4497  O  OE1 . GLN B  1 193 ? -19.947 -6.464  70.279  1.00 20.18  ? 280  GLN B OE1 1 
ATOM   4498  N  NE2 . GLN B  1 193 ? -21.013 -8.046  71.485  1.00 20.20  ? 280  GLN B NE2 1 
ATOM   4499  N  N   . HIS B  1 194 ? -14.006 -7.469  70.491  1.00 12.10  ? 281  HIS B N   1 
ATOM   4500  C  CA  . HIS B  1 194 ? -12.836 -6.705  70.069  1.00 12.10  ? 281  HIS B CA  1 
ATOM   4501  C  C   . HIS B  1 194 ? -11.663 -7.147  70.948  1.00 11.46  ? 281  HIS B C   1 
ATOM   4502  O  O   . HIS B  1 194 ? -11.836 -7.341  72.154  1.00 11.33  ? 281  HIS B O   1 
ATOM   4503  C  CB  . HIS B  1 194 ? -13.098 -5.203  70.224  1.00 11.19  ? 281  HIS B CB  1 
ATOM   4504  C  CG  . HIS B  1 194 ? -12.011 -4.328  69.685  1.00 13.19  ? 281  HIS B CG  1 
ATOM   4505  N  ND1 . HIS B  1 194 ? -12.024 -3.826  68.397  1.00 14.43  ? 281  HIS B ND1 1 
ATOM   4506  C  CD2 . HIS B  1 194 ? -10.895 -3.831  70.272  1.00 11.34  ? 281  HIS B CD2 1 
ATOM   4507  C  CE1 . HIS B  1 194 ? -10.954 -3.071  68.212  1.00 12.96  ? 281  HIS B CE1 1 
ATOM   4508  N  NE2 . HIS B  1 194 ? -10.250 -3.065  69.331  1.00 15.48  ? 281  HIS B NE2 1 
ATOM   4509  N  N   . ILE B  1 195 ? -10.489 -7.286  70.340  1.00 10.73  ? 282  ILE B N   1 
ATOM   4510  C  CA  . ILE B  1 195 ? -9.316  -7.811  71.028  1.00 10.68  ? 282  ILE B CA  1 
ATOM   4511  C  C   . ILE B  1 195 ? -8.085  -6.911  70.826  1.00 10.82  ? 282  ILE B C   1 
ATOM   4512  O  O   . ILE B  1 195 ? -7.687  -6.615  69.685  1.00 10.82  ? 282  ILE B O   1 
ATOM   4513  C  CB  . ILE B  1 195 ? -8.976  -9.266  70.560  1.00 11.02  ? 282  ILE B CB  1 
ATOM   4514  C  CG1 . ILE B  1 195 ? -10.044 -10.288 71.019  1.00 10.49  ? 282  ILE B CG1 1 
ATOM   4515  C  CG2 . ILE B  1 195 ? -7.570  -9.680  71.040  1.00 10.70  ? 282  ILE B CG2 1 
ATOM   4516  C  CD1 . ILE B  1 195 ? -10.168 -10.452 72.537  1.00 10.40  ? 282  ILE B CD1 1 
ATOM   4517  N  N   . GLU B  1 196 ? -7.478  -6.492  71.936  1.00 10.64  ? 283  GLU B N   1 
ATOM   4518  C  CA  . GLU B  1 196 ? -6.189  -5.804  71.913  1.00 10.97  ? 283  GLU B CA  1 
ATOM   4519  C  C   . GLU B  1 196 ? -5.270  -6.347  72.995  1.00 10.76  ? 283  GLU B C   1 
ATOM   4520  O  O   . GLU B  1 196 ? -5.741  -6.748  74.072  1.00 10.75  ? 283  GLU B O   1 
ATOM   4521  C  CB  . GLU B  1 196 ? -6.357  -4.304  72.185  1.00 11.08  ? 283  GLU B CB  1 
ATOM   4522  C  CG  . GLU B  1 196 ? -7.327  -3.575  71.284  1.00 13.78  ? 283  GLU B CG  1 
ATOM   4523  C  CD  . GLU B  1 196 ? -6.712  -3.085  70.001  1.00 16.79  ? 283  GLU B CD  1 
ATOM   4524  O  OE1 . GLU B  1 196 ? -5.567  -3.467  69.663  1.00 18.11  ? 283  GLU B OE1 1 
ATOM   4525  O  OE2 . GLU B  1 196 ? -7.382  -2.283  69.320  1.00 19.06  ? 283  GLU B OE2 1 
ATOM   4526  N  N   . GLU B  1 197 ? -3.966  -6.316  72.729  1.00 9.63   ? 284  GLU B N   1 
ATOM   4527  C  CA  . GLU B  1 197 ? -2.969  -6.372  73.815  1.00 10.15  ? 284  GLU B CA  1 
ATOM   4528  C  C   . GLU B  1 197 ? -3.171  -7.532  74.809  1.00 9.90   ? 284  GLU B C   1 
ATOM   4529  O  O   . GLU B  1 197 ? -3.223  -7.337  76.033  1.00 9.72   ? 284  GLU B O   1 
ATOM   4530  C  CB  . GLU B  1 197 ? -2.947  -5.013  74.549  1.00 10.41  ? 284  GLU B CB  1 
ATOM   4531  C  CG  . GLU B  1 197 ? -2.448  -3.880  73.633  1.00 8.81   ? 284  GLU B CG  1 
ATOM   4532  C  CD  . GLU B  1 197 ? -2.624  -2.492  74.208  1.00 10.62  ? 284  GLU B CD  1 
ATOM   4533  O  OE1 . GLU B  1 197 ? -3.298  -2.337  75.248  1.00 9.31   ? 284  GLU B OE1 1 
ATOM   4534  O  OE2 . GLU B  1 197 ? -2.070  -1.534  73.615  1.00 9.55   ? 284  GLU B OE2 1 
ATOM   4535  N  N   . CYS B  1 198 ? -3.247  -8.755  74.288  1.00 9.55   ? 285  CYS B N   1 
ATOM   4536  C  CA  . CYS B  1 198 ? -3.518  -9.920  75.146  1.00 9.91   ? 285  CYS B CA  1 
ATOM   4537  C  C   . CYS B  1 198 ? -2.371  -10.219 76.118  1.00 9.85   ? 285  CYS B C   1 
ATOM   4538  O  O   . CYS B  1 198 ? -1.197  -10.151 75.726  1.00 9.18   ? 285  CYS B O   1 
ATOM   4539  C  CB  . CYS B  1 198 ? -3.812  -11.156 74.301  1.00 9.29   ? 285  CYS B CB  1 
ATOM   4540  S  SG  . CYS B  1 198 ? -5.403  -11.024 73.435  1.00 11.76  ? 285  CYS B SG  1 
ATOM   4541  N  N   . SER B  1 199 ? -2.723  -10.483 77.382  1.00 9.69   ? 286  SER B N   1 
ATOM   4542  C  CA  . SER B  1 199 ? -1.776  -10.980 78.398  1.00 9.79   ? 286  SER B CA  1 
ATOM   4543  C  C   . SER B  1 199 ? -2.054  -12.465 78.627  1.00 10.39  ? 286  SER B C   1 
ATOM   4544  O  O   . SER B  1 199 ? -3.152  -12.843 79.085  1.00 11.55  ? 286  SER B O   1 
ATOM   4545  C  CB  . SER B  1 199 ? -1.902  -10.207 79.718  1.00 9.47   ? 286  SER B CB  1 
ATOM   4546  O  OG  . SER B  1 199 ? -1.648  -8.819  79.561  1.00 9.02   ? 286  SER B OG  1 
ATOM   4547  N  N   . CYS B  1 200 ? -1.060  -13.294 78.313  1.00 10.43  ? 287  CYS B N   1 
ATOM   4548  C  CA  . CYS B  1 200 ? -1.230  -14.751 78.223  1.00 10.75  ? 287  CYS B CA  1 
ATOM   4549  C  C   . CYS B  1 200 ? -0.311  -15.536 79.163  1.00 11.25  ? 287  CYS B C   1 
ATOM   4550  O  O   . CYS B  1 200 ? 0.835   -15.148 79.427  1.00 11.24  ? 287  CYS B O   1 
ATOM   4551  C  CB  . CYS B  1 200 ? -1.020  -15.247 76.776  1.00 10.89  ? 287  CYS B CB  1 
ATOM   4552  S  SG  . CYS B  1 200 ? -1.903  -14.279 75.480  1.00 11.85  ? 287  CYS B SG  1 
ATOM   4553  N  N   . TYR B  1 201 ? -0.821  -16.661 79.652  1.00 11.60  ? 288  TYR B N   1 
ATOM   4554  C  CA  . TYR B  1 201 ? -0.017  -17.588 80.468  1.00 11.40  ? 288  TYR B CA  1 
ATOM   4555  C  C   . TYR B  1 201 ? -0.565  -18.994 80.246  1.00 11.87  ? 288  TYR B C   1 
ATOM   4556  O  O   . TYR B  1 201 ? -1.726  -19.159 79.831  1.00 11.85  ? 288  TYR B O   1 
ATOM   4557  C  CB  . TYR B  1 201 ? -0.079  -17.211 81.956  1.00 11.57  ? 288  TYR B CB  1 
ATOM   4558  C  CG  . TYR B  1 201 ? -1.430  -17.531 82.559  1.00 12.11  ? 288  TYR B CG  1 
ATOM   4559  C  CD1 . TYR B  1 201 ? -2.491  -16.612 82.470  1.00 12.89  ? 288  TYR B CD1 1 
ATOM   4560  C  CD2 . TYR B  1 201 ? -1.670  -18.775 83.159  1.00 11.83  ? 288  TYR B CD2 1 
ATOM   4561  C  CE1 . TYR B  1 201 ? -3.761  -16.915 82.987  1.00 12.67  ? 288  TYR B CE1 1 
ATOM   4562  C  CE2 . TYR B  1 201 ? -2.931  -19.088 83.664  1.00 11.95  ? 288  TYR B CE2 1 
ATOM   4563  C  CZ  . TYR B  1 201 ? -3.962  -18.158 83.574  1.00 11.95  ? 288  TYR B CZ  1 
ATOM   4564  O  OH  . TYR B  1 201 ? -5.195  -18.481 84.079  1.00 12.95  ? 288  TYR B OH  1 
ATOM   4565  N  N   . GLY B  1 202 ? 0.244   -20.011 80.545  1.00 12.23  ? 289  GLY B N   1 
ATOM   4566  C  CA  . GLY B  1 202 ? -0.205  -21.392 80.402  1.00 13.27  ? 289  GLY B CA  1 
ATOM   4567  C  C   . GLY B  1 202 ? -0.127  -22.204 81.692  1.00 13.96  ? 289  GLY B C   1 
ATOM   4568  O  O   . GLY B  1 202 ? 0.675   -21.905 82.591  1.00 13.37  ? 289  GLY B O   1 
ATOM   4569  N  N   . ALA B  1 203 ? -0.974  -23.233 81.766  1.00 14.68  ? 290  ALA B N   1 
ATOM   4570  C  CA  . ALA B  1 203 ? -1.026  -24.168 82.884  1.00 14.79  ? 290  ALA B CA  1 
ATOM   4571  C  C   . ALA B  1 203 ? -1.871  -25.357 82.446  1.00 14.90  ? 290  ALA B C   1 
ATOM   4572  O  O   . ALA B  1 203 ? -2.889  -25.177 81.769  1.00 14.74  ? 290  ALA B O   1 
ATOM   4573  C  CB  . ALA B  1 203 ? -1.641  -23.512 84.117  1.00 14.96  ? 290  ALA B CB  1 
ATOM   4574  N  N   . GLY B  1 204 ? -1.440  -26.564 82.815  1.00 14.50  ? 291  GLY B N   1 
ATOM   4575  C  CA  . GLY B  1 204 ? -2.175  -27.800 82.456  1.00 15.23  ? 291  GLY B CA  1 
ATOM   4576  C  C   . GLY B  1 204 ? -2.573  -27.920 80.991  1.00 14.97  ? 291  GLY B C   1 
ATOM   4577  O  O   . GLY B  1 204 ? -3.708  -28.283 80.673  1.00 15.82  ? 291  GLY B O   1 
ATOM   4578  N  N   . GLY B  1 205 ? -1.637  -27.586 80.105  1.00 15.32  ? 292  GLY B N   1 
ATOM   4579  C  CA  . GLY B  1 205 ? -1.805  -27.689 78.660  1.00 15.34  ? 292  GLY B CA  1 
ATOM   4580  C  C   . GLY B  1 205 ? -2.737  -26.687 78.001  1.00 15.51  ? 292  GLY B C   1 
ATOM   4581  O  O   . GLY B  1 205 ? -3.046  -26.827 76.822  1.00 15.82  ? 292  GLY B O   1 
ATOM   4582  N  N   . VAL B  1 206 ? -3.181  -25.682 78.755  1.00 14.88  ? 293  VAL B N   1 
ATOM   4583  C  CA  . VAL B  1 206 ? -4.114  -24.676 78.258  1.00 14.71  ? 293  VAL B CA  1 
ATOM   4584  C  C   . VAL B  1 206 ? -3.452  -23.289 78.373  1.00 14.22  ? 293  VAL B C   1 
ATOM   4585  O  O   . VAL B  1 206 ? -2.856  -22.968 79.395  1.00 14.05  ? 293  VAL B O   1 
ATOM   4586  C  CB  . VAL B  1 206 ? -5.447  -24.696 79.078  1.00 14.47  ? 293  VAL B CB  1 
ATOM   4587  C  CG1 . VAL B  1 206 ? -6.368  -23.528 78.699  1.00 15.03  ? 293  VAL B CG1 1 
ATOM   4588  C  CG2 . VAL B  1 206 ? -6.182  -26.034 78.923  1.00 15.80  ? 293  VAL B CG2 1 
ATOM   4589  N  N   . ILE B  1 207 ? -3.556  -22.494 77.320  1.00 14.03  ? 294  ILE B N   1 
ATOM   4590  C  CA  . ILE B  1 207 ? -3.149  -21.098 77.359  1.00 13.76  ? 294  ILE B CA  1 
ATOM   4591  C  C   . ILE B  1 207 ? -4.377  -20.172 77.454  1.00 13.65  ? 294  ILE B C   1 
ATOM   4592  O  O   . ILE B  1 207 ? -5.311  -20.279 76.649  1.00 13.45  ? 294  ILE B O   1 
ATOM   4593  C  CB  . ILE B  1 207 ? -2.297  -20.740 76.132  1.00 13.59  ? 294  ILE B CB  1 
ATOM   4594  C  CG1 . ILE B  1 207 ? -0.962  -21.491 76.181  1.00 14.50  ? 294  ILE B CG1 1 
ATOM   4595  C  CG2 . ILE B  1 207 ? -2.058  -19.216 76.042  1.00 12.67  ? 294  ILE B CG2 1 
ATOM   4596  C  CD1 . ILE B  1 207 ? -0.189  -21.434 74.867  1.00 13.79  ? 294  ILE B CD1 1 
ATOM   4597  N  N   . LYS B  1 208 ? -4.363  -19.275 78.435  1.00 12.23  ? 295  LYS B N   1 
ATOM   4598  C  CA  . LYS B  1 208 ? -5.437  -18.304 78.602  1.00 13.20  ? 295  LYS B CA  1 
ATOM   4599  C  C   . LYS B  1 208 ? -4.931  -16.881 78.388  1.00 12.02  ? 295  LYS B C   1 
ATOM   4600  O  O   . LYS B  1 208 ? -3.971  -16.450 79.028  1.00 12.45  ? 295  LYS B O   1 
ATOM   4601  C  CB  . LYS B  1 208 ? -6.068  -18.435 79.989  1.00 13.28  ? 295  LYS B CB  1 
ATOM   4602  C  CG  . LYS B  1 208 ? -6.927  -19.677 80.165  1.00 14.02  ? 295  LYS B CG  1 
ATOM   4603  C  CD  . LYS B  1 208 ? -7.594  -19.698 81.531  1.00 12.29  ? 295  LYS B CD  1 
ATOM   4604  C  CE  . LYS B  1 208 ? -8.272  -21.033 81.793  1.00 13.03  ? 295  LYS B CE  1 
ATOM   4605  N  NZ  . LYS B  1 208 ? -8.889  -21.085 83.147  1.00 13.10  ? 295  LYS B NZ  1 
ATOM   4606  N  N   . CYS B  1 209 ? -5.584  -16.156 77.486  1.00 11.32  ? 296  CYS B N   1 
ATOM   4607  C  CA  . CYS B  1 209 ? -5.160  -14.802 77.132  1.00 10.80  ? 296  CYS B CA  1 
ATOM   4608  C  C   . CYS B  1 209 ? -6.231  -13.823 77.596  1.00 11.12  ? 296  CYS B C   1 
ATOM   4609  O  O   . CYS B  1 209 ? -7.403  -13.958 77.210  1.00 10.94  ? 296  CYS B O   1 
ATOM   4610  C  CB  . CYS B  1 209 ? -4.961  -14.676 75.624  1.00 11.55  ? 296  CYS B CB  1 
ATOM   4611  S  SG  . CYS B  1 209 ? -3.469  -15.483 74.942  1.00 12.20  ? 296  CYS B SG  1 
ATOM   4612  N  N   . ILE B  1 210 ? -5.838  -12.886 78.458  1.00 9.97   ? 297  ILE B N   1 
ATOM   4613  C  CA  . ILE B  1 210 ? -6.774  -11.931 79.033  1.00 10.15  ? 297  ILE B CA  1 
ATOM   4614  C  C   . ILE B  1 210 ? -6.472  -10.586 78.367  1.00 10.12  ? 297  ILE B C   1 
ATOM   4615  O  O   . ILE B  1 210 ? -5.345  -10.083 78.464  1.00 10.80  ? 297  ILE B O   1 
ATOM   4616  C  CB  . ILE B  1 210 ? -6.667  -11.857 80.590  1.00 9.61   ? 297  ILE B CB  1 
ATOM   4617  C  CG1 . ILE B  1 210 ? -7.301  -13.075 81.294  1.00 11.87  ? 297  ILE B CG1 1 
ATOM   4618  C  CG2 . ILE B  1 210 ? -7.436  -10.639 81.092  1.00 9.93   ? 297  ILE B CG2 1 
ATOM   4619  C  CD1 . ILE B  1 210 ? -6.727  -14.457 80.934  1.00 12.11  ? 297  ILE B CD1 1 
ATOM   4620  N  N   . CYS B  1 211 ? -7.451  -10.035 77.656  1.00 9.23   ? 298  CYS B N   1 
ATOM   4621  C  CA  . CYS B  1 211 ? -7.169  -8.968  76.679  1.00 10.43  ? 298  CYS B CA  1 
ATOM   4622  C  C   . CYS B  1 211 ? -7.855  -7.643  77.002  1.00 9.70   ? 298  CYS B C   1 
ATOM   4623  O  O   . CYS B  1 211 ? -8.416  -7.474  78.099  1.00 9.95   ? 298  CYS B O   1 
ATOM   4624  C  CB  . CYS B  1 211 ? -7.465  -9.460  75.237  1.00 10.01  ? 298  CYS B CB  1 
ATOM   4625  S  SG  . CYS B  1 211 ? -6.846  -11.172 74.927  1.00 11.53  ? 298  CYS B SG  1 
ATOM   4626  N  N   . ARG B  1 212 ? -7.791  -6.707  76.057  1.00 9.77   ? 299  ARG B N   1 
ATOM   4627  C  CA  . ARG B  1 212 ? -8.427  -5.385  76.174  1.00 10.09  ? 299  ARG B CA  1 
ATOM   4628  C  C   . ARG B  1 212 ? -9.463  -5.215  75.059  1.00 10.52  ? 299  ARG B C   1 
ATOM   4629  O  O   . ARG B  1 212 ? -9.114  -5.239  73.873  1.00 10.46  ? 299  ARG B O   1 
ATOM   4630  C  CB  . ARG B  1 212 ? -7.355  -4.308  76.037  1.00 10.64  ? 299  ARG B CB  1 
ATOM   4631  C  CG  . ARG B  1 212 ? -7.848  -2.882  75.781  1.00 8.33   ? 299  ARG B CG  1 
ATOM   4632  C  CD  . ARG B  1 212 ? -6.618  -1.994  75.580  1.00 8.15   ? 299  ARG B CD  1 
ATOM   4633  N  NE  . ARG B  1 212 ? -6.940  -0.657  75.094  1.00 8.74   ? 299  ARG B NE  1 
ATOM   4634  C  CZ  . ARG B  1 212 ? -6.035  0.308   74.975  1.00 10.98  ? 299  ARG B CZ  1 
ATOM   4635  N  NH1 . ARG B  1 212 ? -4.780  0.075   75.350  1.00 10.80  ? 299  ARG B NH1 1 
ATOM   4636  N  NH2 . ARG B  1 212 ? -6.385  1.515   74.527  1.00 11.16  ? 299  ARG B NH2 1 
ATOM   4637  N  N   . ASP B  1 213 ? -10.728 -5.044  75.435  1.00 10.64  ? 300  ASP B N   1 
ATOM   4638  C  CA  . ASP B  1 213 ? -11.781 -4.732  74.450  1.00 10.37  ? 300  ASP B CA  1 
ATOM   4639  C  C   . ASP B  1 213 ? -11.799 -3.220  74.368  1.00 10.62  ? 300  ASP B C   1 
ATOM   4640  O  O   . ASP B  1 213 ? -12.273 -2.558  75.299  1.00 9.84   ? 300  ASP B O   1 
ATOM   4641  C  CB  . ASP B  1 213 ? -13.137 -5.281  74.910  1.00 9.98   ? 300  ASP B CB  1 
ATOM   4642  C  CG  . ASP B  1 213 ? -14.294 -4.876  74.002  1.00 11.11  ? 300  ASP B CG  1 
ATOM   4643  O  OD1 . ASP B  1 213 ? -15.403 -5.440  74.179  1.00 10.76  ? 300  ASP B OD1 1 
ATOM   4644  O  OD2 . ASP B  1 213 ? -14.131 -3.972  73.150  1.00 10.95  ? 300  ASP B OD2 1 
ATOM   4645  N  N   . ASN B  1 214 ? -11.239 -2.666  73.294  1.00 10.77  ? 301  ASN B N   1 
ATOM   4646  C  CA  . ASN B  1 214 ? -11.173 -1.200  73.160  1.00 11.47  ? 301  ASN B CA  1 
ATOM   4647  C  C   . ASN B  1 214 ? -12.435 -0.584  72.544  1.00 12.51  ? 301  ASN B C   1 
ATOM   4648  O  O   . ASN B  1 214 ? -12.565 0.648   72.443  1.00 12.52  ? 301  ASN B O   1 
ATOM   4649  C  CB  . ASN B  1 214 ? -9.940  -0.768  72.343  1.00 11.43  ? 301  ASN B CB  1 
ATOM   4650  C  CG  . ASN B  1 214 ? -9.430  0.612   72.746  1.00 11.51  ? 301  ASN B CG  1 
ATOM   4651  O  OD1 . ASN B  1 214 ? -9.043  0.828   73.890  1.00 13.10  ? 301  ASN B OD1 1 
ATOM   4652  N  ND2 . ASN B  1 214 ? -9.445  1.564   71.803  1.00 12.62  ? 301  ASN B ND2 1 
ATOM   4653  N  N   . TRP B  1 215 ? -13.357 -1.440  72.117  1.00 12.90  ? 302  TRP B N   1 
ATOM   4654  C  CA  . TRP B  1 215 ? -14.558 -0.970  71.433  1.00 13.16  ? 302  TRP B CA  1 
ATOM   4655  C  C   . TRP B  1 215 ? -15.758 -0.762  72.388  1.00 13.16  ? 302  TRP B C   1 
ATOM   4656  O  O   . TRP B  1 215 ? -16.396 0.304   72.384  1.00 13.37  ? 302  TRP B O   1 
ATOM   4657  C  CB  . TRP B  1 215 ? -14.899 -1.945  70.311  1.00 13.14  ? 302  TRP B CB  1 
ATOM   4658  C  CG  . TRP B  1 215 ? -16.092 -1.564  69.437  1.00 14.31  ? 302  TRP B CG  1 
ATOM   4659  C  CD1 . TRP B  1 215 ? -16.611 -0.315  69.229  1.00 15.30  ? 302  TRP B CD1 1 
ATOM   4660  C  CD2 . TRP B  1 215 ? -16.871 -2.461  68.642  1.00 14.41  ? 302  TRP B CD2 1 
ATOM   4661  N  NE1 . TRP B  1 215 ? -17.697 -0.389  68.364  1.00 15.01  ? 302  TRP B NE1 1 
ATOM   4662  C  CE2 . TRP B  1 215 ? -17.872 -1.693  67.991  1.00 14.38  ? 302  TRP B CE2 1 
ATOM   4663  C  CE3 . TRP B  1 215 ? -16.839 -3.852  68.432  1.00 15.13  ? 302  TRP B CE3 1 
ATOM   4664  C  CZ2 . TRP B  1 215 ? -18.825 -2.268  67.136  1.00 15.03  ? 302  TRP B CZ2 1 
ATOM   4665  C  CZ3 . TRP B  1 215 ? -17.799 -4.425  67.577  1.00 15.58  ? 302  TRP B CZ3 1 
ATOM   4666  C  CH2 . TRP B  1 215 ? -18.772 -3.629  66.946  1.00 15.03  ? 302  TRP B CH2 1 
ATOM   4667  N  N   . LYS B  1 216 ? -16.050 -1.775  73.193  1.00 12.50  ? 303  LYS B N   1 
ATOM   4668  C  CA  . LYS B  1 216 ? -17.228 -1.757  74.077  1.00 12.95  ? 303  LYS B CA  1 
ATOM   4669  C  C   . LYS B  1 216 ? -16.957 -2.059  75.564  1.00 13.18  ? 303  LYS B C   1 
ATOM   4670  O  O   . LYS B  1 216 ? -17.272 -1.253  76.462  1.00 13.08  ? 303  LYS B O   1 
ATOM   4671  C  CB  . LYS B  1 216 ? -18.259 -2.752  73.541  1.00 12.70  ? 303  LYS B CB  1 
ATOM   4672  C  CG  . LYS B  1 216 ? -18.833 -2.389  72.179  1.00 13.64  ? 303  LYS B CG  1 
ATOM   4673  C  CD  . LYS B  1 216 ? -19.748 -3.500  71.692  1.00 12.82  ? 303  LYS B CD  1 
ATOM   4674  C  CE  . LYS B  1 216 ? -20.396 -3.136  70.356  1.00 16.99  ? 303  LYS B CE  1 
ATOM   4675  N  NZ  . LYS B  1 216 ? -21.352 -4.218  69.935  1.00 15.33  ? 303  LYS B NZ  1 
ATOM   4676  N  N   . GLY B  1 217 ? -16.390 -3.232  75.821  1.00 12.75  ? 304  GLY B N   1 
ATOM   4677  C  CA  . GLY B  1 217 ? -16.346 -3.771  77.177  1.00 12.61  ? 304  GLY B CA  1 
ATOM   4678  C  C   . GLY B  1 217 ? -15.370 -3.159  78.167  1.00 12.24  ? 304  GLY B C   1 
ATOM   4679  O  O   . GLY B  1 217 ? -14.190 -2.978  77.865  1.00 11.94  ? 304  GLY B O   1 
ATOM   4680  N  N   . ALA B  1 218 ? -15.876 -2.882  79.368  1.00 11.52  ? 305  ALA B N   1 
ATOM   4681  C  CA  . ALA B  1 218 ? -15.047 -2.603  80.546  1.00 11.52  ? 305  ALA B CA  1 
ATOM   4682  C  C   . ALA B  1 218 ? -14.685 -3.901  81.281  1.00 11.34  ? 305  ALA B C   1 
ATOM   4683  O  O   . ALA B  1 218 ? -13.806 -3.922  82.159  1.00 10.86  ? 305  ALA B O   1 
ATOM   4684  C  CB  . ALA B  1 218 ? -15.767 -1.629  81.484  1.00 12.89  ? 305  ALA B CB  1 
ATOM   4685  N  N   . ASN B  1 219 ? -15.395 -4.978  80.951  1.00 10.53  ? 306  ASN B N   1 
ATOM   4686  C  CA  . ASN B  1 219 ? -14.947 -6.325  81.309  1.00 11.08  ? 306  ASN B CA  1 
ATOM   4687  C  C   . ASN B  1 219 ? -13.942 -6.814  80.238  1.00 10.90  ? 306  ASN B C   1 
ATOM   4688  O  O   . ASN B  1 219 ? -14.032 -6.408  79.063  1.00 10.46  ? 306  ASN B O   1 
ATOM   4689  C  CB  . ASN B  1 219 ? -16.139 -7.296  81.501  1.00 10.42  ? 306  ASN B CB  1 
ATOM   4690  C  CG  . ASN B  1 219 ? -17.114 -7.305  80.303  1.00 11.49  ? 306  ASN B CG  1 
ATOM   4691  O  OD1 . ASN B  1 219 ? -17.131 -6.382  79.456  1.00 12.23  ? 306  ASN B OD1 1 
ATOM   4692  N  ND2 . ASN B  1 219 ? -17.931 -8.358  80.232  1.00 10.14  ? 306  ASN B ND2 1 
ATOM   4693  N  N   . ARG B  1 220 ? -13.000 -7.677  80.625  1.00 10.87  ? 307  ARG B N   1 
ATOM   4694  C  CA  . ARG B  1 220 ? -11.944 -8.094  79.693  1.00 11.13  ? 307  ARG B CA  1 
ATOM   4695  C  C   . ARG B  1 220 ? -12.271 -9.345  78.919  1.00 10.84  ? 307  ARG B C   1 
ATOM   4696  O  O   . ARG B  1 220 ? -12.750 -10.327 79.487  1.00 11.72  ? 307  ARG B O   1 
ATOM   4697  C  CB  . ARG B  1 220 ? -10.602 -8.306  80.422  1.00 11.13  ? 307  ARG B CB  1 
ATOM   4698  C  CG  . ARG B  1 220 ? -10.042 -7.033  81.016  1.00 10.36  ? 307  ARG B CG  1 
ATOM   4699  C  CD  . ARG B  1 220 ? -8.618  -7.213  81.571  1.00 10.08  ? 307  ARG B CD  1 
ATOM   4700  N  NE  . ARG B  1 220 ? -8.071  -5.900  81.971  1.00 10.99  ? 307  ARG B NE  1 
ATOM   4701  C  CZ  . ARG B  1 220 ? -7.700  -4.939  81.123  1.00 8.82   ? 307  ARG B CZ  1 
ATOM   4702  N  NH1 . ARG B  1 220 ? -7.220  -3.778  81.591  1.00 10.85  ? 307  ARG B NH1 1 
ATOM   4703  N  NH2 . ARG B  1 220 ? -7.752  -5.147  79.801  1.00 9.88   ? 307  ARG B NH2 1 
ATOM   4704  N  N   . PRO B  1 221 ? -11.984 -9.336  77.616  1.00 11.38  ? 308  PRO B N   1 
ATOM   4705  C  CA  . PRO B  1 221 ? -12.135 -10.589 76.876  1.00 11.64  ? 308  PRO B CA  1 
ATOM   4706  C  C   . PRO B  1 221 ? -11.118 -11.639 77.316  1.00 12.24  ? 308  PRO B C   1 
ATOM   4707  O  O   . PRO B  1 221 ? -10.020 -11.281 77.786  1.00 12.93  ? 308  PRO B O   1 
ATOM   4708  C  CB  . PRO B  1 221 ? -11.900 -10.180 75.411  1.00 12.13  ? 308  PRO B CB  1 
ATOM   4709  C  CG  . PRO B  1 221 ? -11.855 -8.716  75.366  1.00 10.85  ? 308  PRO B CG  1 
ATOM   4710  C  CD  . PRO B  1 221 ? -11.564 -8.214  76.761  1.00 10.59  ? 308  PRO B CD  1 
ATOM   4711  N  N   . VAL B  1 222 ? -11.500 -12.910 77.179  1.00 11.81  ? 309  VAL B N   1 
ATOM   4712  C  CA  . VAL B  1 222 ? -10.669 -14.067 77.546  1.00 12.01  ? 309  VAL B CA  1 
ATOM   4713  C  C   . VAL B  1 222 ? -10.669 -15.036 76.363  1.00 11.79  ? 309  VAL B C   1 
ATOM   4714  O  O   . VAL B  1 222 ? -11.737 -15.567 75.960  1.00 11.32  ? 309  VAL B O   1 
ATOM   4715  C  CB  . VAL B  1 222 ? -11.169 -14.812 78.827  1.00 12.26  ? 309  VAL B CB  1 
ATOM   4716  C  CG1 . VAL B  1 222 ? -10.255 -16.022 79.145  1.00 11.73  ? 309  VAL B CG1 1 
ATOM   4717  C  CG2 . VAL B  1 222 ? -11.247 -13.839 80.031  1.00 11.88  ? 309  VAL B CG2 1 
ATOM   4718  N  N   . ILE B  1 223 ? -9.485  -15.226 75.787  1.00 10.84  ? 310  ILE B N   1 
ATOM   4719  C  CA  . ILE B  1 223 ? -9.293  -16.201 74.731  1.00 11.72  ? 310  ILE B CA  1 
ATOM   4720  C  C   . ILE B  1 223 ? -8.625  -17.420 75.342  1.00 12.04  ? 310  ILE B C   1 
ATOM   4721  O  O   . ILE B  1 223 ? -7.571  -17.292 75.989  1.00 11.83  ? 310  ILE B O   1 
ATOM   4722  C  CB  . ILE B  1 223 ? -8.411  -15.665 73.578  1.00 11.03  ? 310  ILE B CB  1 
ATOM   4723  C  CG1 . ILE B  1 223 ? -9.028  -14.378 72.979  1.00 11.32  ? 310  ILE B CG1 1 
ATOM   4724  C  CG2 . ILE B  1 223 ? -8.218  -16.742 72.527  1.00 10.33  ? 310  ILE B CG2 1 
ATOM   4725  C  CD1 . ILE B  1 223 ? -8.119  -13.601 71.990  1.00 12.18  ? 310  ILE B CD1 1 
ATOM   4726  N  N   . THR B  1 224 ? -9.236  -18.585 75.137  1.00 12.04  ? 311  THR B N   1 
ATOM   4727  C  CA  . THR B  1 224 ? -8.688  -19.876 75.622  1.00 12.56  ? 311  THR B CA  1 
ATOM   4728  C  C   . THR B  1 224 ? -8.131  -20.706 74.457  1.00 12.69  ? 311  THR B C   1 
ATOM   4729  O  O   . THR B  1 224 ? -8.867  -21.043 73.534  1.00 12.66  ? 311  THR B O   1 
ATOM   4730  C  CB  . THR B  1 224 ? -9.763  -20.694 76.391  1.00 13.03  ? 311  THR B CB  1 
ATOM   4731  O  OG1 . THR B  1 224 ? -10.225 -19.935 77.514  1.00 14.18  ? 311  THR B OG1 1 
ATOM   4732  C  CG2 . THR B  1 224 ? -9.204  -22.046 76.904  1.00 13.41  ? 311  THR B CG2 1 
ATOM   4733  N  N   . ILE B  1 225 ? -6.838  -21.025 74.514  1.00 11.85  ? 312  ILE B N   1 
ATOM   4734  C  CA  . ILE B  1 225 ? -6.130  -21.628 73.381  1.00 12.71  ? 312  ILE B CA  1 
ATOM   4735  C  C   . ILE B  1 225 ? -5.588  -23.002 73.755  1.00 13.11  ? 312  ILE B C   1 
ATOM   4736  O  O   . ILE B  1 225 ? -4.972  -23.171 74.811  1.00 13.07  ? 312  ILE B O   1 
ATOM   4737  C  CB  . ILE B  1 225 ? -4.962  -20.739 72.902  1.00 12.84  ? 312  ILE B CB  1 
ATOM   4738  C  CG1 . ILE B  1 225 ? -5.461  -19.327 72.550  1.00 11.88  ? 312  ILE B CG1 1 
ATOM   4739  C  CG2 . ILE B  1 225 ? -4.212  -21.365 71.699  1.00 12.51  ? 312  ILE B CG2 1 
ATOM   4740  C  CD1 . ILE B  1 225 ? -4.326  -18.336 72.290  1.00 12.90  ? 312  ILE B CD1 1 
ATOM   4741  N  N   . ASP B  1 226 ? -5.855  -23.967 72.874  1.00 14.01  ? 313  ASP B N   1 
ATOM   4742  C  CA  . ASP B  1 226 ? -5.284  -25.304 72.924  1.00 15.30  ? 313  ASP B CA  1 
ATOM   4743  C  C   . ASP B  1 226 ? -4.096  -25.324 71.963  1.00 15.45  ? 313  ASP B C   1 
ATOM   4744  O  O   . ASP B  1 226 ? -4.284  -25.369 70.737  1.00 15.80  ? 313  ASP B O   1 
ATOM   4745  C  CB  . ASP B  1 226 ? -6.320  -26.346 72.492  1.00 15.70  ? 313  ASP B CB  1 
ATOM   4746  C  CG  . ASP B  1 226 ? -5.817  -27.773 72.624  1.00 17.08  ? 313  ASP B CG  1 
ATOM   4747  O  OD1 . ASP B  1 226 ? -6.655  -28.650 72.898  1.00 19.60  ? 313  ASP B OD1 1 
ATOM   4748  O  OD2 . ASP B  1 226 ? -4.600  -28.032 72.462  1.00 18.12  ? 313  ASP B OD2 1 
ATOM   4749  N  N   . PRO B  1 227 ? -2.871  -25.312 72.509  1.00 15.34  ? 314  PRO B N   1 
ATOM   4750  C  CA  . PRO B  1 227 ? -1.686  -25.197 71.658  1.00 16.18  ? 314  PRO B CA  1 
ATOM   4751  C  C   . PRO B  1 227 ? -1.311  -26.498 70.915  1.00 16.39  ? 314  PRO B C   1 
ATOM   4752  O  O   . PRO B  1 227 ? -0.451  -26.465 70.018  1.00 16.12  ? 314  PRO B O   1 
ATOM   4753  C  CB  . PRO B  1 227 ? -0.587  -24.814 72.657  1.00 15.97  ? 314  PRO B CB  1 
ATOM   4754  C  CG  . PRO B  1 227 ? -1.015  -25.455 73.938  1.00 15.04  ? 314  PRO B CG  1 
ATOM   4755  C  CD  . PRO B  1 227 ? -2.525  -25.404 73.945  1.00 15.72  ? 314  PRO B CD  1 
ATOM   4756  N  N   . GLU B  1 228 ? -1.917  -27.626 71.302  1.00 17.14  ? 315  GLU B N   1 
ATOM   4757  C  CA  . GLU B  1 228 ? -1.691  -28.894 70.576  1.00 18.16  ? 315  GLU B CA  1 
ATOM   4758  C  C   . GLU B  1 228 ? -2.648  -29.052 69.400  1.00 18.25  ? 315  GLU B C   1 
ATOM   4759  O  O   . GLU B  1 228 ? -2.212  -29.357 68.288  1.00 18.66  ? 315  GLU B O   1 
ATOM   4760  C  CB  . GLU B  1 228 ? -1.786  -30.113 71.497  1.00 17.96  ? 315  GLU B CB  1 
ATOM   4761  C  CG  . GLU B  1 228 ? -0.717  -30.161 72.558  1.00 20.14  ? 315  GLU B CG  1 
ATOM   4762  C  CD  . GLU B  1 228 ? -0.611  -31.526 73.215  1.00 24.57  ? 315  GLU B CD  1 
ATOM   4763  O  OE1 . GLU B  1 228 ? -1.091  -32.502 72.610  1.00 28.81  ? 315  GLU B OE1 1 
ATOM   4764  O  OE2 . GLU B  1 228 ? -0.051  -31.631 74.324  1.00 25.31  ? 315  GLU B OE2 1 
ATOM   4765  N  N   . MET B  1 229 ? -3.941  -28.853 69.651  1.00 18.15  ? 316  MET B N   1 
ATOM   4766  C  CA  . MET B  1 229 ? -4.956  -28.892 68.601  1.00 18.72  ? 316  MET B CA  1 
ATOM   4767  C  C   . MET B  1 229 ? -4.875  -27.640 67.739  1.00 18.65  ? 316  MET B C   1 
ATOM   4768  O  O   . MET B  1 229 ? -5.379  -27.626 66.608  1.00 17.78  ? 316  MET B O   1 
ATOM   4769  C  CB  . MET B  1 229 ? -6.368  -29.037 69.189  1.00 18.98  ? 316  MET B CB  1 
ATOM   4770  C  CG  . MET B  1 229 ? -6.629  -30.358 69.936  1.00 21.48  ? 316  MET B CG  1 
ATOM   4771  S  SD  . MET B  1 229 ? -6.417  -31.842 68.912  1.00 23.44  ? 316  MET B SD  1 
ATOM   4772  C  CE  . MET B  1 229 ? -4.729  -32.294 69.328  1.00 24.70  ? 316  MET B CE  1 
ATOM   4773  N  N   . MET B  1 230 ? -4.228  -26.606 68.285  1.00 18.07  ? 317  MET B N   1 
ATOM   4774  C  CA  . MET B  1 230 ? -4.178  -25.250 67.693  1.00 17.97  ? 317  MET B CA  1 
ATOM   4775  C  C   . MET B  1 230 ? -5.579  -24.728 67.375  1.00 17.12  ? 317  MET B C   1 
ATOM   4776  O  O   . MET B  1 230 ? -5.892  -24.360 66.233  1.00 16.79  ? 317  MET B O   1 
ATOM   4777  C  CB  . MET B  1 230 ? -3.236  -25.174 66.480  1.00 18.12  ? 317  MET B CB  1 
ATOM   4778  C  CG  . MET B  1 230 ? -1.843  -25.770 66.723  1.00 18.82  ? 317  MET B CG  1 
ATOM   4779  S  SD  . MET B  1 230 ? -0.680  -25.488 65.349  1.00 19.82  ? 317  MET B SD  1 
ATOM   4780  C  CE  . MET B  1 230 ? -1.404  -26.463 64.049  1.00 22.98  ? 317  MET B CE  1 
ATOM   4781  N  N   . THR B  1 231 ? -6.419  -24.710 68.406  1.00 16.69  ? 318  THR B N   1 
ATOM   4782  C  CA  . THR B  1 231 ? -7.782  -24.186 68.307  1.00 16.62  ? 318  THR B CA  1 
ATOM   4783  C  C   . THR B  1 231 ? -8.041  -23.259 69.496  1.00 16.59  ? 318  THR B C   1 
ATOM   4784  O  O   . THR B  1 231 ? -7.259  -23.248 70.463  1.00 16.08  ? 318  THR B O   1 
ATOM   4785  C  CB  . THR B  1 231 ? -8.835  -25.323 68.282  1.00 16.94  ? 318  THR B CB  1 
ATOM   4786  O  OG1 . THR B  1 231 ? -8.665  -26.152 69.432  1.00 18.38  ? 318  THR B OG1 1 
ATOM   4787  C  CG2 . THR B  1 231 ? -8.679  -26.174 67.020  1.00 16.44  ? 318  THR B CG2 1 
ATOM   4788  N  N   . HIS B  1 232 ? -9.115  -22.471 69.426  1.00 15.98  ? 319  HIS B N   1 
ATOM   4789  C  CA  . HIS B  1 232 ? -9.419  -21.518 70.509  1.00 16.05  ? 319  HIS B CA  1 
ATOM   4790  C  C   . HIS B  1 232 ? -10.907 -21.263 70.642  1.00 15.57  ? 319  HIS B C   1 
ATOM   4791  O  O   . HIS B  1 232 ? -11.701 -21.563 69.730  1.00 15.62  ? 319  HIS B O   1 
ATOM   4792  C  CB  . HIS B  1 232 ? -8.706  -20.180 70.274  1.00 15.46  ? 319  HIS B CB  1 
ATOM   4793  C  CG  . HIS B  1 232 ? -9.386  -19.316 69.262  1.00 15.71  ? 319  HIS B CG  1 
ATOM   4794  N  ND1 . HIS B  1 232 ? -9.186  -19.470 67.912  1.00 14.03  ? 319  HIS B ND1 1 
ATOM   4795  C  CD2 . HIS B  1 232 ? -10.282 -18.306 69.398  1.00 16.51  ? 319  HIS B CD2 1 
ATOM   4796  C  CE1 . HIS B  1 232 ? -9.925  -18.597 67.251  1.00 15.55  ? 319  HIS B CE1 1 
ATOM   4797  N  NE2 . HIS B  1 232 ? -10.598 -17.875 68.128  1.00 15.60  ? 319  HIS B NE2 1 
ATOM   4798  N  N   . THR B  1 233 ? -11.279 -20.711 71.787  1.00 14.93  ? 320  THR B N   1 
ATOM   4799  C  CA  . THR B  1 233 ? -12.608 -20.147 71.990  1.00 15.27  ? 320  THR B CA  1 
ATOM   4800  C  C   . THR B  1 233 ? -12.416 -18.752 72.621  1.00 14.70  ? 320  THR B C   1 
ATOM   4801  O  O   . THR B  1 233 ? -11.336 -18.435 73.126  1.00 14.47  ? 320  THR B O   1 
ATOM   4802  C  CB  . THR B  1 233 ? -13.468 -21.050 72.904  1.00 15.99  ? 320  THR B CB  1 
ATOM   4803  O  OG1 . THR B  1 233 ? -12.802 -21.227 74.159  1.00 17.42  ? 320  THR B OG1 1 
ATOM   4804  C  CG2 . THR B  1 233 ? -13.697 -22.453 72.274  1.00 15.65  ? 320  THR B CG2 1 
ATOM   4805  N  N   . SER B  1 234 ? -13.438 -17.908 72.566  1.00 14.15  ? 321  SER B N   1 
ATOM   4806  C  CA  . SER B  1 234 ? -13.373 -16.628 73.276  1.00 13.37  ? 321  SER B CA  1 
ATOM   4807  C  C   . SER B  1 234 ? -14.687 -16.276 73.964  1.00 12.85  ? 321  SER B C   1 
ATOM   4808  O  O   . SER B  1 234 ? -15.757 -16.735 73.556  1.00 11.38  ? 321  SER B O   1 
ATOM   4809  C  CB  . SER B  1 234 ? -12.896 -15.477 72.357  1.00 12.78  ? 321  SER B CB  1 
ATOM   4810  O  OG  . SER B  1 234 ? -13.945 -14.950 71.531  1.00 14.62  ? 321  SER B OG  1 
ATOM   4811  N  N   . LYS B  1 235 ? -14.584 -15.443 75.003  1.00 12.60  ? 322  LYS B N   1 
ATOM   4812  C  CA  . LYS B  1 235 ? -15.748 -14.847 75.688  1.00 12.91  ? 322  LYS B CA  1 
ATOM   4813  C  C   . LYS B  1 235 ? -15.224 -13.717 76.547  1.00 12.54  ? 322  LYS B C   1 
ATOM   4814  O  O   . LYS B  1 235 ? -14.134 -13.194 76.275  1.00 11.81  ? 322  LYS B O   1 
ATOM   4815  C  CB  . LYS B  1 235 ? -16.521 -15.888 76.522  1.00 12.68  ? 322  LYS B CB  1 
ATOM   4816  C  CG  . LYS B  1 235 ? -15.684 -16.603 77.593  1.00 13.61  ? 322  LYS B CG  1 
ATOM   4817  C  CD  . LYS B  1 235 ? -16.377 -17.866 78.084  1.00 14.59  ? 322  LYS B CD  1 
ATOM   4818  C  CE  . LYS B  1 235 ? -17.740 -17.612 78.654  1.00 16.73  ? 322  LYS B CE  1 
ATOM   4819  N  NZ  . LYS B  1 235 ? -18.221 -18.862 79.327  1.00 20.91  ? 322  LYS B NZ  1 
ATOM   4820  N  N   . TYR B  1 236 ? -15.993 -13.322 77.557  1.00 12.47  ? 323  TYR B N   1 
ATOM   4821  C  CA  . TYR B  1 236 ? -15.535 -12.309 78.503  1.00 13.01  ? 323  TYR B CA  1 
ATOM   4822  C  C   . TYR B  1 236 ? -15.358 -12.912 79.889  1.00 13.01  ? 323  TYR B C   1 
ATOM   4823  O  O   . TYR B  1 236 ? -15.966 -13.946 80.201  1.00 13.14  ? 323  TYR B O   1 
ATOM   4824  C  CB  . TYR B  1 236 ? -16.532 -11.148 78.547  1.00 13.04  ? 323  TYR B CB  1 
ATOM   4825  C  CG  . TYR B  1 236 ? -16.497 -10.262 77.328  1.00 12.77  ? 323  TYR B CG  1 
ATOM   4826  C  CD1 . TYR B  1 236 ? -17.180 -10.625 76.148  1.00 12.49  ? 323  TYR B CD1 1 
ATOM   4827  C  CD2 . TYR B  1 236 ? -15.814 -9.045  77.358  1.00 9.59   ? 323  TYR B CD2 1 
ATOM   4828  C  CE1 . TYR B  1 236 ? -17.144 -9.811  75.011  1.00 11.88  ? 323  TYR B CE1 1 
ATOM   4829  C  CE2 . TYR B  1 236 ? -15.766 -8.218  76.231  1.00 12.64  ? 323  TYR B CE2 1 
ATOM   4830  C  CZ  . TYR B  1 236 ? -16.430 -8.612  75.060  1.00 13.00  ? 323  TYR B CZ  1 
ATOM   4831  O  OH  . TYR B  1 236 ? -16.405 -7.781  73.964  1.00 12.86  ? 323  TYR B OH  1 
ATOM   4832  N  N   . LEU B  1 237 ? -14.517 -12.284 80.716  1.00 13.14  ? 324  LEU B N   1 
ATOM   4833  C  CA  . LEU B  1 237 ? -14.499 -12.570 82.156  1.00 13.48  ? 324  LEU B CA  1 
ATOM   4834  C  C   . LEU B  1 237 ? -15.929 -12.445 82.694  1.00 13.75  ? 324  LEU B C   1 
ATOM   4835  O  O   . LEU B  1 237 ? -16.575 -11.433 82.442  1.00 14.03  ? 324  LEU B O   1 
ATOM   4836  C  CB  . LEU B  1 237 ? -13.596 -11.565 82.901  1.00 14.35  ? 324  LEU B CB  1 
ATOM   4837  C  CG  . LEU B  1 237 ? -12.128 -11.861 83.180  1.00 16.15  ? 324  LEU B CG  1 
ATOM   4838  C  CD1 . LEU B  1 237 ? -11.520 -10.708 83.988  1.00 14.44  ? 324  LEU B CD1 1 
ATOM   4839  C  CD2 . LEU B  1 237 ? -11.984 -13.152 83.949  1.00 16.93  ? 324  LEU B CD2 1 
ATOM   4840  N  N   . CYS B  1 238 ? -16.420 -13.468 83.407  1.00 13.65  ? 325  CYS B N   1 
ATOM   4841  C  CA  . CYS B  1 238 ? -17.805 -13.448 83.950  1.00 14.02  ? 325  CYS B CA  1 
ATOM   4842  C  C   . CYS B  1 238 ? -18.035 -12.421 85.073  1.00 13.10  ? 325  CYS B C   1 
ATOM   4843  O  O   . CYS B  1 238 ? -19.130 -11.877 85.208  1.00 12.87  ? 325  CYS B O   1 
ATOM   4844  C  CB  . CYS B  1 238 ? -18.206 -14.837 84.459  1.00 13.96  ? 325  CYS B CB  1 
ATOM   4845  S  SG  . CYS B  1 238 ? -18.334 -16.081 83.160  1.00 15.46  ? 325  CYS B SG  1 
ATOM   4846  N  N   . SER B  1 239 ? -17.005 -12.182 85.889  1.00 13.02  ? 326  SER B N   1 
ATOM   4847  C  CA  . SER B  1 239 ? -17.136 -11.430 87.153  1.00 12.27  ? 326  SER B CA  1 
ATOM   4848  C  C   . SER B  1 239 ? -17.683 -10.022 86.992  1.00 12.27  ? 326  SER B C   1 
ATOM   4849  O  O   . SER B  1 239 ? -17.308 -9.317  86.053  1.00 12.48  ? 326  SER B O   1 
ATOM   4850  C  CB  . SER B  1 239 ? -15.773 -11.348 87.877  1.00 11.74  ? 326  SER B CB  1 
ATOM   4851  O  OG  . SER B  1 239 ? -15.890 -10.598 89.086  1.00 10.65  ? 326  SER B OG  1 
ATOM   4852  N  N   . LYS B  1 240 ? -18.527 -9.605  87.941  1.00 11.69  ? 327  LYS B N   1 
ATOM   4853  C  CA  . LYS B  1 240 ? -19.007 -8.226  88.037  1.00 11.75  ? 327  LYS B CA  1 
ATOM   4854  C  C   . LYS B  1 240 ? -17.864 -7.244  88.345  1.00 11.43  ? 327  LYS B C   1 
ATOM   4855  O  O   . LYS B  1 240 ? -18.045 -6.019  88.215  1.00 11.92  ? 327  LYS B O   1 
ATOM   4856  C  CB  . LYS B  1 240 ? -20.083 -8.107  89.125  1.00 11.75  ? 327  LYS B CB  1 
ATOM   4857  C  CG  . LYS B  1 240 ? -19.526 -8.266  90.526  1.00 11.73  ? 327  LYS B CG  1 
ATOM   4858  C  CD  . LYS B  1 240 ? -20.612 -8.661  91.523  1.00 14.32  ? 327  LYS B CD  1 
ATOM   4859  C  CE  . LYS B  1 240 ? -20.020 -8.832  92.922  1.00 16.62  ? 327  LYS B CE  1 
ATOM   4860  N  NZ  . LYS B  1 240 ? -21.034 -9.458  93.832  1.00 17.35  ? 327  LYS B NZ  1 
ATOM   4861  N  N   . VAL B  1 241 ? -16.706 -7.778  88.770  1.00 11.75  ? 328  VAL B N   1 
ATOM   4862  C  CA  . VAL B  1 241 ? -15.536 -6.944  89.063  1.00 11.94  ? 328  VAL B CA  1 
ATOM   4863  C  C   . VAL B  1 241 ? -14.887 -6.538  87.734  1.00 11.71  ? 328  VAL B C   1 
ATOM   4864  O  O   . VAL B  1 241 ? -14.154 -7.322  87.126  1.00 11.78  ? 328  VAL B O   1 
ATOM   4865  C  CB  . VAL B  1 241 ? -14.511 -7.629  90.017  1.00 11.35  ? 328  VAL B CB  1 
ATOM   4866  C  CG1 . VAL B  1 241 ? -13.306 -6.700  90.259  1.00 11.36  ? 328  VAL B CG1 1 
ATOM   4867  C  CG2 . VAL B  1 241 ? -15.192 -8.013  91.340  1.00 11.19  ? 328  VAL B CG2 1 
ATOM   4868  N  N   . LEU B  1 242 ? -15.183 -5.315  87.288  1.00 11.22  ? 329  LEU B N   1 
ATOM   4869  C  CA  . LEU B  1 242 ? -14.706 -4.842  85.982  1.00 10.39  ? 329  LEU B CA  1 
ATOM   4870  C  C   . LEU B  1 242 ? -13.251 -4.379  86.078  1.00 9.98   ? 329  LEU B C   1 
ATOM   4871  O  O   . LEU B  1 242 ? -12.871 -3.719  87.045  1.00 9.23   ? 329  LEU B O   1 
ATOM   4872  C  CB  . LEU B  1 242 ? -15.579 -3.713  85.462  1.00 10.68  ? 329  LEU B CB  1 
ATOM   4873  C  CG  . LEU B  1 242 ? -17.092 -3.994  85.366  1.00 10.49  ? 329  LEU B CG  1 
ATOM   4874  C  CD1 . LEU B  1 242 ? -17.821 -2.726  84.897  1.00 7.82   ? 329  LEU B CD1 1 
ATOM   4875  C  CD2 . LEU B  1 242 ? -17.416 -5.206  84.480  1.00 11.90  ? 329  LEU B CD2 1 
ATOM   4876  N  N   . THR B  1 243 ? -12.444 -4.719  85.079  1.00 9.44   ? 330  THR B N   1 
ATOM   4877  C  CA  . THR B  1 243 ? -10.984 -4.537  85.245  1.00 9.78   ? 330  THR B CA  1 
ATOM   4878  C  C   . THR B  1 243 ? -10.277 -3.763  84.115  1.00 9.72   ? 330  THR B C   1 
ATOM   4879  O  O   . THR B  1 243 ? -9.046  -3.632  84.136  1.00 10.37  ? 330  THR B O   1 
ATOM   4880  C  CB  . THR B  1 243 ? -10.247 -5.876  85.529  1.00 9.41   ? 330  THR B CB  1 
ATOM   4881  O  OG1 . THR B  1 243 ? -10.364 -6.743  84.406  1.00 8.49   ? 330  THR B OG1 1 
ATOM   4882  C  CG2 . THR B  1 243 ? -10.798 -6.596  86.781  1.00 9.38   ? 330  THR B CG2 1 
ATOM   4883  N  N   . ASP B  1 244 ? -11.028 -3.269  83.134  1.00 9.84   ? 331  ASP B N   1 
ATOM   4884  C  CA  . ASP B  1 244 ? -10.443 -2.333  82.160  1.00 10.22  ? 331  ASP B CA  1 
ATOM   4885  C  C   . ASP B  1 244 ? -10.490 -0.894  82.728  1.00 10.12  ? 331  ASP B C   1 
ATOM   4886  O  O   . ASP B  1 244 ? -11.055 -0.646  83.813  1.00 9.70   ? 331  ASP B O   1 
ATOM   4887  C  CB  . ASP B  1 244 ? -11.158 -2.468  80.800  1.00 10.44  ? 331  ASP B CB  1 
ATOM   4888  C  CG  . ASP B  1 244 ? -10.259 -2.131  79.608  1.00 11.45  ? 331  ASP B CG  1 
ATOM   4889  O  OD1 . ASP B  1 244 ? -9.128  -1.598  79.804  1.00 10.94  ? 331  ASP B OD1 1 
ATOM   4890  O  OD2 . ASP B  1 244 ? -10.715 -2.376  78.465  1.00 10.85  ? 331  ASP B OD2 1 
ATOM   4891  N  N   . THR B  1 245 ? -9.875  0.044   82.013  1.00 10.22  ? 332  THR B N   1 
ATOM   4892  C  CA  . THR B  1 245 ? -9.893  1.476   82.371  1.00 11.00  ? 332  THR B CA  1 
ATOM   4893  C  C   . THR B  1 245 ? -10.008 2.256   81.068  1.00 10.95  ? 332  THR B C   1 
ATOM   4894  O  O   . THR B  1 245 ? -9.184  2.055   80.196  1.00 10.56  ? 332  THR B O   1 
ATOM   4895  C  CB  . THR B  1 245 ? -8.578  1.918   83.074  1.00 11.01  ? 332  THR B CB  1 
ATOM   4896  O  OG1 . THR B  1 245 ? -8.329  1.081   84.210  1.00 12.06  ? 332  THR B OG1 1 
ATOM   4897  C  CG2 . THR B  1 245 ? -8.661  3.404   83.502  1.00 11.24  ? 332  THR B CG2 1 
ATOM   4898  N  N   . SER B  1 246 ? -10.968 3.173   80.912  1.00 11.42  ? 333  SER B N   1 
ATOM   4899  C  CA  . SER B  1 246 ? -11.932 3.586   81.920  1.00 11.30  ? 333  SER B CA  1 
ATOM   4900  C  C   . SER B  1 246 ? -13.094 2.568   82.026  1.00 11.01  ? 333  SER B C   1 
ATOM   4901  O  O   . SER B  1 246 ? -13.400 1.804   81.075  1.00 11.85  ? 333  SER B O   1 
ATOM   4902  C  CB  . SER B  1 246 ? -12.473 4.996   81.580  1.00 11.15  ? 333  SER B CB  1 
ATOM   4903  O  OG  . SER B  1 246 ? -11.433 5.977   81.436  1.00 9.81   ? 333  SER B OG  1 
ATOM   4904  N  N   . ARG B  1 247 ? -13.723 2.546   83.195  1.00 11.38  ? 334  ARG B N   1 
ATOM   4905  C  CA  . ARG B  1 247 ? -14.831 1.625   83.469  1.00 10.62  ? 334  ARG B CA  1 
ATOM   4906  C  C   . ARG B  1 247 ? -15.922 2.324   84.306  1.00 11.86  ? 334  ARG B C   1 
ATOM   4907  O  O   . ARG B  1 247 ? -15.643 3.303   84.995  1.00 11.46  ? 334  ARG B O   1 
ATOM   4908  C  CB  . ARG B  1 247 ? -14.306 0.349   84.172  1.00 10.71  ? 334  ARG B CB  1 
ATOM   4909  C  CG  . ARG B  1 247 ? -13.616 0.618   85.539  1.00 8.39   ? 334  ARG B CG  1 
ATOM   4910  C  CD  . ARG B  1 247 ? -13.155 -0.652  86.264  1.00 9.83   ? 334  ARG B CD  1 
ATOM   4911  N  NE  . ARG B  1 247 ? -12.602 -0.324  87.588  1.00 8.96   ? 334  ARG B NE  1 
ATOM   4912  C  CZ  . ARG B  1 247 ? -11.334 0.035   87.826  1.00 10.33  ? 334  ARG B CZ  1 
ATOM   4913  N  NH1 . ARG B  1 247 ? -10.433 0.082   86.837  1.00 6.55   ? 334  ARG B NH1 1 
ATOM   4914  N  NH2 . ARG B  1 247 ? -10.953 0.334   89.074  1.00 8.11   ? 334  ARG B NH2 1 
ATOM   4915  N  N   . PRO B  1 248 ? -17.177 1.823   84.242  1.00 12.20  ? 335  PRO B N   1 
ATOM   4916  C  CA  . PRO B  1 248 ? -18.175 2.310   85.205  1.00 12.86  ? 335  PRO B CA  1 
ATOM   4917  C  C   . PRO B  1 248 ? -18.012 1.592   86.546  1.00 13.50  ? 335  PRO B C   1 
ATOM   4918  O  O   . PRO B  1 248 ? -17.153 0.704   86.674  1.00 13.31  ? 335  PRO B O   1 
ATOM   4919  C  CB  . PRO B  1 248 ? -19.502 1.894   84.552  1.00 12.44  ? 335  PRO B CB  1 
ATOM   4920  C  CG  . PRO B  1 248 ? -19.167 0.599   83.854  1.00 12.41  ? 335  PRO B CG  1 
ATOM   4921  C  CD  . PRO B  1 248 ? -17.730 0.792   83.339  1.00 12.25  ? 335  PRO B CD  1 
ATOM   4922  N  N   . ASN B  1 249 ? -18.828 1.964   87.542  1.00 14.38  ? 336  ASN B N   1 
ATOM   4923  C  CA  . ASN B  1 249 ? -18.948 1.167   88.775  1.00 15.09  ? 336  ASN B CA  1 
ATOM   4924  C  C   . ASN B  1 249 ? -19.281 -0.290  88.464  1.00 14.09  ? 336  ASN B C   1 
ATOM   4925  O  O   . ASN B  1 249 ? -19.970 -0.564  87.477  1.00 13.88  ? 336  ASN B O   1 
ATOM   4926  C  CB  . ASN B  1 249 ? -20.059 1.720   89.674  1.00 15.87  ? 336  ASN B CB  1 
ATOM   4927  C  CG  . ASN B  1 249 ? -19.775 3.127   90.140  1.00 19.69  ? 336  ASN B CG  1 
ATOM   4928  O  OD1 . ASN B  1 249 ? -18.614 3.514   90.342  1.00 22.63  ? 336  ASN B OD1 1 
ATOM   4929  N  ND2 . ASN B  1 249 ? -20.837 3.911   90.316  1.00 22.41  ? 336  ASN B ND2 1 
ATOM   4930  N  N   . ASP B  1 250 ? -18.766 -1.211  89.284  1.00 13.23  ? 337  ASP B N   1 
ATOM   4931  C  CA  . ASP B  1 250 ? -19.047 -2.640  89.118  1.00 13.65  ? 337  ASP B CA  1 
ATOM   4932  C  C   . ASP B  1 250 ? -20.563 -2.850  89.255  1.00 14.63  ? 337  ASP B C   1 
ATOM   4933  O  O   . ASP B  1 250 ? -21.156 -2.368  90.234  1.00 15.27  ? 337  ASP B O   1 
ATOM   4934  C  CB  . ASP B  1 250 ? -18.298 -3.476  90.166  1.00 13.28  ? 337  ASP B CB  1 
ATOM   4935  C  CG  . ASP B  1 250 ? -16.777 -3.445  89.967  1.00 11.36  ? 337  ASP B CG  1 
ATOM   4936  O  OD1 . ASP B  1 250 ? -16.025 -3.739  90.922  1.00 14.69  ? 337  ASP B OD1 1 
ATOM   4937  O  OD2 . ASP B  1 250 ? -16.327 -3.126  88.854  1.00 12.63  ? 337  ASP B OD2 1 
ATOM   4938  N  N   . PRO B  1 251 ? -21.190 -3.525  88.268  1.00 14.56  ? 338  PRO B N   1 
ATOM   4939  C  CA  . PRO B  1 251 ? -22.622 -3.831  88.327  1.00 14.47  ? 338  PRO B CA  1 
ATOM   4940  C  C   . PRO B  1 251 ? -22.939 -4.943  89.340  1.00 13.75  ? 338  PRO B C   1 
ATOM   4941  O  O   . PRO B  1 251 ? -22.034 -5.494  89.966  1.00 12.85  ? 338  PRO B O   1 
ATOM   4942  C  CB  . PRO B  1 251 ? -22.937 -4.267  86.889  1.00 15.03  ? 338  PRO B CB  1 
ATOM   4943  C  CG  . PRO B  1 251 ? -21.679 -4.870  86.405  1.00 15.32  ? 338  PRO B CG  1 
ATOM   4944  C  CD  . PRO B  1 251 ? -20.586 -4.024  87.015  1.00 14.52  ? 338  PRO B CD  1 
ATOM   4945  N  N   . THR B  1 252 ? -24.226 -5.227  89.533  1.00 12.58  ? 339  THR B N   1 
ATOM   4946  C  CA  . THR B  1 252 ? -24.658 -6.354  90.347  1.00 13.23  ? 339  THR B CA  1 
ATOM   4947  C  C   . THR B  1 252 ? -24.179 -7.693  89.774  1.00 13.22  ? 339  THR B C   1 
ATOM   4948  O  O   . THR B  1 252 ? -23.766 -8.575  90.528  1.00 12.86  ? 339  THR B O   1 
ATOM   4949  C  CB  . THR B  1 252 ? -26.205 -6.362  90.464  1.00 12.83  ? 339  THR B CB  1 
ATOM   4950  O  OG1 . THR B  1 252 ? -26.612 -5.120  91.029  1.00 15.57  ? 339  THR B OG1 1 
ATOM   4951  C  CG2 . THR B  1 252 ? -26.670 -7.466  91.373  1.00 15.36  ? 339  THR B CG2 1 
ATOM   4952  N  N   . ASN B  1 253 ? -24.239 -7.839  88.445  1.00 13.30  ? 340  ASN B N   1 
ATOM   4953  C  CA  . ASN B  1 253 ? -23.789 -9.057  87.765  1.00 14.82  ? 340  ASN B CA  1 
ATOM   4954  C  C   . ASN B  1 253 ? -22.882 -8.676  86.612  1.00 13.65  ? 340  ASN B C   1 
ATOM   4955  O  O   . ASN B  1 253 ? -23.186 -7.733  85.875  1.00 13.68  ? 340  ASN B O   1 
ATOM   4956  C  CB  . ASN B  1 253 ? -24.940 -9.833  87.089  1.00 15.51  ? 340  ASN B CB  1 
ATOM   4957  C  CG  . ASN B  1 253 ? -25.981 -10.388 88.045  1.00 19.00  ? 340  ASN B CG  1 
ATOM   4958  O  OD1 . ASN B  1 253 ? -27.085 -10.712 87.598  1.00 23.09  ? 340  ASN B OD1 1 
ATOM   4959  N  ND2 . ASN B  1 253 ? -25.649 -10.539 89.328  1.00 19.92  ? 340  ASN B ND2 1 
ATOM   4960  N  N   . GLY B  1 254 ? -21.822 -9.450  86.394  1.00 13.77  ? 341  GLY B N   1 
ATOM   4961  C  CA  . GLY B  1 254 ? -21.094 -9.376  85.123  1.00 13.77  ? 341  GLY B CA  1 
ATOM   4962  C  C   . GLY B  1 254 ? -21.824 -10.110 84.000  1.00 14.49  ? 341  GLY B C   1 
ATOM   4963  O  O   . GLY B  1 254 ? -22.990 -10.486 84.138  1.00 14.98  ? 341  GLY B O   1 
ATOM   4964  N  N   . ASN B  1 255 ? -21.119 -10.329 82.890  1.00 14.47  ? 342  ASN B N   1 
ATOM   4965  C  CA  . ASN B  1 255 ? -21.653 -10.992 81.719  1.00 14.44  ? 342  ASN B CA  1 
ATOM   4966  C  C   . ASN B  1 255 ? -20.528 -11.774 81.059  1.00 14.68  ? 342  ASN B C   1 
ATOM   4967  O  O   . ASN B  1 255 ? -19.549 -11.181 80.597  1.00 12.98  ? 342  ASN B O   1 
ATOM   4968  C  CB  . ASN B  1 255 ? -22.209 -9.944  80.729  1.00 14.82  ? 342  ASN B CB  1 
ATOM   4969  C  CG  . ASN B  1 255 ? -23.145 -10.552 79.691  1.00 15.83  ? 342  ASN B CG  1 
ATOM   4970  O  OD1 . ASN B  1 255 ? -24.100 -9.910  79.249  1.00 18.16  ? 342  ASN B OD1 1 
ATOM   4971  N  ND2 . ASN B  1 255 ? -22.876 -11.795 79.301  1.00 11.54  ? 342  ASN B ND2 1 
ATOM   4972  N  N   . CYS B  1 256 ? -20.665 -13.104 81.051  1.00 14.89  ? 343  CYS B N   1 
ATOM   4973  C  CA  . CYS B  1 256 ? -19.698 -14.009 80.424  1.00 15.46  ? 343  CYS B CA  1 
ATOM   4974  C  C   . CYS B  1 256 ? -19.592 -13.843 78.904  1.00 15.97  ? 343  CYS B C   1 
ATOM   4975  O  O   . CYS B  1 256 ? -18.559 -14.132 78.327  1.00 16.25  ? 343  CYS B O   1 
ATOM   4976  C  CB  . CYS B  1 256 ? -20.067 -15.474 80.724  1.00 15.15  ? 343  CYS B CB  1 
ATOM   4977  S  SG  . CYS B  1 256 ? -20.246 -15.868 82.485  1.00 16.67  ? 343  CYS B SG  1 
ATOM   4978  N  N   . ASP B  1 257 ? -20.659 -13.404 78.250  1.00 15.98  ? 344  ASP B N   1 
ATOM   4979  C  CA  . ASP B  1 257 ? -20.718 -13.545 76.793  1.00 16.75  ? 344  ASP B CA  1 
ATOM   4980  C  C   . ASP B  1 257 ? -20.929 -12.267 76.001  1.00 16.07  ? 344  ASP B C   1 
ATOM   4981  O  O   . ASP B  1 257 ? -21.132 -12.307 74.791  1.00 16.28  ? 344  ASP B O   1 
ATOM   4982  C  CB  . ASP B  1 257 ? -21.743 -14.615 76.416  1.00 17.77  ? 344  ASP B CB  1 
ATOM   4983  C  CG  . ASP B  1 257 ? -21.261 -16.011 76.792  1.00 20.01  ? 344  ASP B CG  1 
ATOM   4984  O  OD1 . ASP B  1 257 ? -21.806 -16.544 77.761  1.00 20.90  ? 344  ASP B OD1 1 
ATOM   4985  O  OD2 . ASP B  1 257 ? -20.306 -16.536 76.153  1.00 22.45  ? 344  ASP B OD2 1 
ATOM   4986  N  N   . ALA B  1 258 ? -20.853 -11.127 76.675  1.00 15.05  ? 345  ALA B N   1 
ATOM   4987  C  CA  . ALA B  1 258 ? -21.040 -9.858  76.007  1.00 14.82  ? 345  ALA B CA  1 
ATOM   4988  C  C   . ALA B  1 258 ? -20.396 -8.750  76.835  1.00 14.88  ? 345  ALA B C   1 
ATOM   4989  O  O   . ALA B  1 258 ? -20.255 -8.891  78.052  1.00 14.57  ? 345  ALA B O   1 
ATOM   4990  C  CB  . ALA B  1 258 ? -22.525 -9.577  75.789  1.00 14.94  ? 345  ALA B CB  1 
ATOM   4991  N  N   . PRO B  1 259 ? -19.977 -7.661  76.172  1.00 14.85  ? 346  PRO B N   1 
ATOM   4992  C  CA  . PRO B  1 259 ? -19.339 -6.559  76.908  1.00 14.83  ? 346  PRO B CA  1 
ATOM   4993  C  C   . PRO B  1 259 ? -20.274 -5.840  77.876  1.00 14.72  ? 346  PRO B C   1 
ATOM   4994  O  O   . PRO B  1 259 ? -21.462 -5.635  77.567  1.00 13.58  ? 346  PRO B O   1 
ATOM   4995  C  CB  . PRO B  1 259 ? -18.890 -5.600  75.791  1.00 14.87  ? 346  PRO B CB  1 
ATOM   4996  C  CG  . PRO B  1 259 ? -19.743 -5.966  74.588  1.00 15.76  ? 346  PRO B CG  1 
ATOM   4997  C  CD  . PRO B  1 259 ? -19.996 -7.427  74.712  1.00 15.04  ? 346  PRO B CD  1 
ATOM   4998  N  N   . ILE B  1 260 ? -19.728 -5.499  79.044  1.00 14.88  ? 347  ILE B N   1 
ATOM   4999  C  CA  . ILE B  1 260 ? -20.304 -4.488  79.944  1.00 15.06  ? 347  ILE B CA  1 
ATOM   5000  C  C   . ILE B  1 260 ? -19.694 -3.134  79.590  1.00 15.14  ? 347  ILE B C   1 
ATOM   5001  O  O   . ILE B  1 260 ? -18.488 -2.902  79.798  1.00 13.94  ? 347  ILE B O   1 
ATOM   5002  C  CB  . ILE B  1 260 ? -19.987 -4.811  81.433  1.00 15.07  ? 347  ILE B CB  1 
ATOM   5003  C  CG1 . ILE B  1 260 ? -20.404 -6.243  81.807  1.00 16.52  ? 347  ILE B CG1 1 
ATOM   5004  C  CG2 . ILE B  1 260 ? -20.566 -3.735  82.374  1.00 14.83  ? 347  ILE B CG2 1 
ATOM   5005  C  CD1 . ILE B  1 260 ? -21.837 -6.423  82.283  1.00 18.80  ? 347  ILE B CD1 1 
ATOM   5006  N  N   . THR B  1 261 ? -20.520 -2.232  79.055  1.00 14.03  ? 348  THR B N   1 
ATOM   5007  C  CA  . THR B  1 261 ? -20.031 -0.956  78.540  1.00 14.42  ? 348  THR B CA  1 
ATOM   5008  C  C   . THR B  1 261 ? -20.108 0.163   79.568  1.00 14.25  ? 348  THR B C   1 
ATOM   5009  O  O   . THR B  1 261 ? -20.637 -0.020  80.677  1.00 14.23  ? 348  THR B O   1 
ATOM   5010  C  CB  . THR B  1 261 ? -20.770 -0.535  77.258  1.00 14.37  ? 348  THR B CB  1 
ATOM   5011  O  OG1 . THR B  1 261 ? -22.152 -0.292  77.577  1.00 14.35  ? 348  THR B OG1 1 
ATOM   5012  C  CG2 . THR B  1 261 ? -20.660 -1.659  76.172  1.00 15.20  ? 348  THR B CG2 1 
ATOM   5013  N  N   . GLY B  1 262 ? -19.559 1.312   79.205  1.00 14.57  ? 349  GLY B N   1 
ATOM   5014  C  CA  . GLY B  1 262 ? -19.578 2.481   80.074  1.00 14.78  ? 349  GLY B CA  1 
ATOM   5015  C  C   . GLY B  1 262 ? -18.200 2.932   80.504  1.00 14.87  ? 349  GLY B C   1 
ATOM   5016  O  O   . GLY B  1 262 ? -17.190 2.358   80.098  1.00 14.75  ? 349  GLY B O   1 
ATOM   5017  N  N   . GLY B  1 263 ? -18.175 3.963   81.338  1.00 14.80  ? 350  GLY B N   1 
ATOM   5018  C  CA  . GLY B  1 263 ? -16.936 4.564   81.797  1.00 15.26  ? 350  GLY B CA  1 
ATOM   5019  C  C   . GLY B  1 263 ? -16.473 5.699   80.903  1.00 15.19  ? 350  GLY B C   1 
ATOM   5020  O  O   . GLY B  1 263 ? -16.856 5.788   79.734  1.00 14.77  ? 350  GLY B O   1 
ATOM   5021  N  N   . SER B  1 264 ? -15.623 6.549   81.467  1.00 15.01  ? 351  SER B N   1 
ATOM   5022  C  CA  . SER B  1 264 ? -15.165 7.769   80.827  1.00 15.24  ? 351  SER B CA  1 
ATOM   5023  C  C   . SER B  1 264 ? -13.818 8.175   81.424  1.00 14.07  ? 351  SER B C   1 
ATOM   5024  O  O   . SER B  1 264 ? -13.617 7.994   82.626  1.00 13.46  ? 351  SER B O   1 
ATOM   5025  C  CB  . SER B  1 264 ? -16.169 8.885   81.110  1.00 15.05  ? 351  SER B CB  1 
ATOM   5026  O  OG  . SER B  1 264 ? -15.688 10.080  80.552  1.00 19.86  ? 351  SER B OG  1 
ATOM   5027  N  N   . PRO B  1 265 ? -12.921 8.786   80.627  1.00 13.96  ? 352  PRO B N   1 
ATOM   5028  C  CA  . PRO B  1 265 ? -12.976 9.155   79.210  1.00 14.08  ? 352  PRO B CA  1 
ATOM   5029  C  C   . PRO B  1 265 ? -12.298 8.203   78.231  1.00 14.19  ? 352  PRO B C   1 
ATOM   5030  O  O   . PRO B  1 265 ? -12.399 8.432   77.026  1.00 14.27  ? 352  PRO B O   1 
ATOM   5031  C  CB  . PRO B  1 265 ? -12.217 10.488  79.188  1.00 14.54  ? 352  PRO B CB  1 
ATOM   5032  C  CG  . PRO B  1 265 ? -11.142 10.318  80.258  1.00 14.22  ? 352  PRO B CG  1 
ATOM   5033  C  CD  . PRO B  1 265 ? -11.691 9.299   81.269  1.00 14.08  ? 352  PRO B CD  1 
ATOM   5034  N  N   . ASP B  1 266 ? -11.617 7.163   78.734  1.00 13.98  ? 353  ASP B N   1 
ATOM   5035  C  CA  . ASP B  1 266 ? -10.781 6.300   77.896  1.00 13.80  ? 353  ASP B CA  1 
ATOM   5036  C  C   . ASP B  1 266 ? -11.341 4.902   77.631  1.00 12.99  ? 353  ASP B C   1 
ATOM   5037  O  O   . ASP B  1 266 ? -11.955 4.285   78.514  1.00 12.49  ? 353  ASP B O   1 
ATOM   5038  C  CB  . ASP B  1 266 ? -9.368  6.229   78.475  1.00 14.39  ? 353  ASP B CB  1 
ATOM   5039  C  CG  . ASP B  1 266 ? -8.700  7.602   78.523  1.00 14.88  ? 353  ASP B CG  1 
ATOM   5040  O  OD1 . ASP B  1 266 ? -8.914  8.410   77.591  1.00 19.60  ? 353  ASP B OD1 1 
ATOM   5041  O  OD2 . ASP B  1 266 ? -7.996  7.887   79.506  1.00 15.63  ? 353  ASP B OD2 1 
ATOM   5042  N  N   . PRO B  1 267 ? -11.144 4.405   76.402  1.00 12.38  ? 354  PRO B N   1 
ATOM   5043  C  CA  . PRO B  1 267 ? -11.727 3.134   75.992  1.00 11.78  ? 354  PRO B CA  1 
ATOM   5044  C  C   . PRO B  1 267 ? -11.016 1.857   76.478  1.00 11.53  ? 354  PRO B C   1 
ATOM   5045  O  O   . PRO B  1 267 ? -11.564 0.774   76.310  1.00 11.72  ? 354  PRO B O   1 
ATOM   5046  C  CB  . PRO B  1 267 ? -11.636 3.192   74.459  1.00 11.92  ? 354  PRO B CB  1 
ATOM   5047  C  CG  . PRO B  1 267 ? -10.415 4.018   74.193  1.00 12.47  ? 354  PRO B CG  1 
ATOM   5048  C  CD  . PRO B  1 267 ? -10.402 5.062   75.301  1.00 12.88  ? 354  PRO B CD  1 
ATOM   5049  N  N   . GLY B  1 268 ? -9.805  1.958   77.028  1.00 11.21  ? 355  GLY B N   1 
ATOM   5050  C  CA  . GLY B  1 268 ? -9.096  0.743   77.449  1.00 10.01  ? 355  GLY B CA  1 
ATOM   5051  C  C   . GLY B  1 268 ? -7.660  0.913   77.906  1.00 9.54   ? 355  GLY B C   1 
ATOM   5052  O  O   . GLY B  1 268 ? -7.066  1.972   77.709  1.00 8.62   ? 355  GLY B O   1 
ATOM   5053  N  N   . VAL B  1 269 ? -7.134  -0.149  78.534  1.00 9.19   ? 356  VAL B N   1 
ATOM   5054  C  CA  . VAL B  1 269 ? -5.735  -0.235  78.944  1.00 8.87   ? 356  VAL B CA  1 
ATOM   5055  C  C   . VAL B  1 269 ? -5.367  -1.703  78.927  1.00 9.05   ? 356  VAL B C   1 
ATOM   5056  O  O   . VAL B  1 269 ? -6.211  -2.563  79.197  1.00 8.54   ? 356  VAL B O   1 
ATOM   5057  C  CB  . VAL B  1 269 ? -5.486  0.379   80.362  1.00 8.26   ? 356  VAL B CB  1 
ATOM   5058  C  CG1 . VAL B  1 269 ? -6.112  -0.473  81.476  1.00 8.86   ? 356  VAL B CG1 1 
ATOM   5059  C  CG2 . VAL B  1 269 ? -3.950  0.587   80.629  1.00 8.81   ? 356  VAL B CG2 1 
ATOM   5060  N  N   . LYS B  1 270 ? -4.106  -2.001  78.603  1.00 8.80   ? 357  LYS B N   1 
ATOM   5061  C  CA  . LYS B  1 270 ? -3.644  -3.383  78.692  1.00 7.86   ? 357  LYS B CA  1 
ATOM   5062  C  C   . LYS B  1 270 ? -3.677  -3.865  80.134  1.00 8.09   ? 357  LYS B C   1 
ATOM   5063  O  O   . LYS B  1 270 ? -3.208  -3.160  81.039  1.00 7.81   ? 357  LYS B O   1 
ATOM   5064  C  CB  . LYS B  1 270 ? -2.210  -3.541  78.150  1.00 7.25   ? 357  LYS B CB  1 
ATOM   5065  C  CG  . LYS B  1 270 ? -1.724  -4.997  78.169  1.00 7.38   ? 357  LYS B CG  1 
ATOM   5066  C  CD  . LYS B  1 270 ? -0.280  -5.124  77.632  1.00 6.96   ? 357  LYS B CD  1 
ATOM   5067  C  CE  . LYS B  1 270 ? 0.270   -6.529  77.872  1.00 5.81   ? 357  LYS B CE  1 
ATOM   5068  N  NZ  . LYS B  1 270 ? -0.435  -7.612  77.110  1.00 8.14   ? 357  LYS B NZ  1 
ATOM   5069  N  N   . GLY B  1 271 ? -4.192  -5.079  80.327  1.00 8.13   ? 358  GLY B N   1 
ATOM   5070  C  CA  . GLY B  1 271 ? -4.304  -5.678  81.660  1.00 8.97   ? 358  GLY B CA  1 
ATOM   5071  C  C   . GLY B  1 271 ? -4.196  -7.185  81.618  1.00 8.79   ? 358  GLY B C   1 
ATOM   5072  O  O   . GLY B  1 271 ? -3.861  -7.777  80.579  1.00 9.31   ? 358  GLY B O   1 
ATOM   5073  N  N   . PHE B  1 272 ? -4.487  -7.823  82.750  1.00 8.80   ? 359  PHE B N   1 
ATOM   5074  C  CA  . PHE B  1 272 ? -4.271  -9.252  82.863  1.00 9.04   ? 359  PHE B CA  1 
ATOM   5075  C  C   . PHE B  1 272 ? -5.093  -9.833  84.008  1.00 8.97   ? 359  PHE B C   1 
ATOM   5076  O  O   . PHE B  1 272 ? -5.635  -9.092  84.840  1.00 9.70   ? 359  PHE B O   1 
ATOM   5077  C  CB  . PHE B  1 272 ? -2.770  -9.558  83.117  1.00 8.21   ? 359  PHE B CB  1 
ATOM   5078  C  CG  . PHE B  1 272 ? -2.362  -9.386  84.560  1.00 9.75   ? 359  PHE B CG  1 
ATOM   5079  C  CD1 . PHE B  1 272 ? -2.098  -8.113  85.059  1.00 9.19   ? 359  PHE B CD1 1 
ATOM   5080  C  CD2 . PHE B  1 272 ? -2.288  -10.488 85.427  1.00 7.64   ? 359  PHE B CD2 1 
ATOM   5081  C  CE1 . PHE B  1 272 ? -1.738  -7.923  86.411  1.00 10.72  ? 359  PHE B CE1 1 
ATOM   5082  C  CE2 . PHE B  1 272 ? -1.939  -10.316 86.774  1.00 9.68   ? 359  PHE B CE2 1 
ATOM   5083  C  CZ  . PHE B  1 272 ? -1.670  -9.025  87.272  1.00 8.90   ? 359  PHE B CZ  1 
ATOM   5084  N  N   . ALA B  1 273 ? -5.170  -11.160 84.032  1.00 9.15   ? 360  ALA B N   1 
ATOM   5085  C  CA  . ALA B  1 273 ? -5.735  -11.896 85.173  1.00 9.76   ? 360  ALA B CA  1 
ATOM   5086  C  C   . ALA B  1 273 ? -5.194  -13.325 85.171  1.00 10.28  ? 360  ALA B C   1 
ATOM   5087  O  O   . ALA B  1 273 ? -4.778  -13.852 84.128  1.00 10.75  ? 360  ALA B O   1 
ATOM   5088  C  CB  . ALA B  1 273 ? -7.264  -11.917 85.106  1.00 9.20   ? 360  ALA B CB  1 
ATOM   5089  N  N   . PHE B  1 274 ? -5.205  -13.952 86.341  1.00 10.25  ? 361  PHE B N   1 
ATOM   5090  C  CA  . PHE B  1 274 ? -4.954  -15.399 86.439  1.00 10.43  ? 361  PHE B CA  1 
ATOM   5091  C  C   . PHE B  1 274 ? -6.231  -16.076 86.862  1.00 10.89  ? 361  PHE B C   1 
ATOM   5092  O  O   . PHE B  1 274 ? -6.843  -15.682 87.847  1.00 10.64  ? 361  PHE B O   1 
ATOM   5093  C  CB  . PHE B  1 274 ? -3.812  -15.706 87.412  1.00 10.61  ? 361  PHE B CB  1 
ATOM   5094  C  CG  . PHE B  1 274 ? -2.468  -15.263 86.891  1.00 8.87   ? 361  PHE B CG  1 
ATOM   5095  C  CD1 . PHE B  1 274 ? -1.761  -16.067 86.002  1.00 9.64   ? 361  PHE B CD1 1 
ATOM   5096  C  CD2 . PHE B  1 274 ? -1.945  -14.015 87.247  1.00 9.97   ? 361  PHE B CD2 1 
ATOM   5097  C  CE1 . PHE B  1 274 ? -0.522  -15.658 85.483  1.00 10.88  ? 361  PHE B CE1 1 
ATOM   5098  C  CE2 . PHE B  1 274 ? -0.712  -13.590 86.735  1.00 9.91   ? 361  PHE B CE2 1 
ATOM   5099  C  CZ  . PHE B  1 274 ? -0.005  -14.418 85.851  1.00 9.91   ? 361  PHE B CZ  1 
ATOM   5100  N  N   . LEU B  1 275 ? -6.622  -17.097 86.099  1.00 11.70  ? 362  LEU B N   1 
ATOM   5101  C  CA  . LEU B  1 275 ? -7.947  -17.714 86.238  1.00 12.13  ? 362  LEU B CA  1 
ATOM   5102  C  C   . LEU B  1 275 ? -7.818  -19.216 86.514  1.00 12.74  ? 362  LEU B C   1 
ATOM   5103  O  O   . LEU B  1 275 ? -7.421  -19.977 85.637  1.00 12.44  ? 362  LEU B O   1 
ATOM   5104  C  CB  . LEU B  1 275 ? -8.762  -17.446 84.967  1.00 11.97  ? 362  LEU B CB  1 
ATOM   5105  C  CG  . LEU B  1 275 ? -8.936  -15.993 84.530  1.00 11.50  ? 362  LEU B CG  1 
ATOM   5106  C  CD1 . LEU B  1 275 ? -9.669  -15.961 83.168  1.00 10.78  ? 362  LEU B CD1 1 
ATOM   5107  C  CD2 . LEU B  1 275 ? -9.671  -15.171 85.617  1.00 10.43  ? 362  LEU B CD2 1 
ATOM   5108  N  N   . ASP B  1 276 ? -8.140  -19.617 87.745  1.00 13.29  ? 363  ASP B N   1 
ATOM   5109  C  CA  . ASP B  1 276 ? -7.935  -20.997 88.212  1.00 13.97  ? 363  ASP B CA  1 
ATOM   5110  C  C   . ASP B  1 276 ? -8.949  -21.299 89.326  1.00 14.27  ? 363  ASP B C   1 
ATOM   5111  O  O   . ASP B  1 276 ? -8.585  -21.580 90.481  1.00 14.31  ? 363  ASP B O   1 
ATOM   5112  C  CB  . ASP B  1 276 ? -6.474  -21.162 88.683  1.00 13.67  ? 363  ASP B CB  1 
ATOM   5113  C  CG  . ASP B  1 276 ? -6.135  -22.586 89.133  1.00 15.12  ? 363  ASP B CG  1 
ATOM   5114  O  OD1 . ASP B  1 276 ? -5.330  -22.724 90.082  1.00 15.27  ? 363  ASP B OD1 1 
ATOM   5115  O  OD2 . ASP B  1 276 ? -6.651  -23.554 88.531  1.00 14.81  ? 363  ASP B OD2 1 
ATOM   5116  N  N   . GLY B  1 277 ? -10.236 -21.216 88.977  1.00 14.38  ? 364  GLY B N   1 
ATOM   5117  C  CA  . GLY B  1 277 ? -11.309 -21.490 89.941  1.00 15.05  ? 364  GLY B CA  1 
ATOM   5118  C  C   . GLY B  1 277 ? -11.252 -20.549 91.136  1.00 14.90  ? 364  GLY B C   1 
ATOM   5119  O  O   . GLY B  1 277 ? -11.243 -19.336 90.967  1.00 14.68  ? 364  GLY B O   1 
ATOM   5120  N  N   . GLU B  1 278 ? -11.230 -21.120 92.343  1.00 15.62  ? 365  GLU B N   1 
ATOM   5121  C  CA  . GLU B  1 278 ? -11.054 -20.359 93.585  1.00 15.93  ? 365  GLU B CA  1 
ATOM   5122  C  C   . GLU B  1 278 ? -9.740  -19.552 93.603  1.00 15.41  ? 365  GLU B C   1 
ATOM   5123  O  O   . GLU B  1 278 ? -9.673  -18.457 94.196  1.00 15.12  ? 365  GLU B O   1 
ATOM   5124  C  CB  . GLU B  1 278 ? -11.062 -21.323 94.779  1.00 17.31  ? 365  GLU B CB  1 
ATOM   5125  C  CG  . GLU B  1 278 ? -12.352 -22.112 94.946  1.00 22.55  ? 365  GLU B CG  1 
ATOM   5126  C  CD  . GLU B  1 278 ? -13.510 -21.249 95.380  1.00 29.04  ? 365  GLU B CD  1 
ATOM   5127  O  OE1 . GLU B  1 278 ? -14.631 -21.492 94.872  1.00 34.02  ? 365  GLU B OE1 1 
ATOM   5128  O  OE2 . GLU B  1 278 ? -13.302 -20.332 96.224  1.00 33.14  ? 365  GLU B OE2 1 
ATOM   5129  N  N   . ASN B  1 279 ? -8.716  -20.106 92.948  1.00 14.15  ? 366  ASN B N   1 
ATOM   5130  C  CA  . ASN B  1 279 ? -7.368  -19.508 92.879  1.00 14.36  ? 366  ASN B CA  1 
ATOM   5131  C  C   . ASN B  1 279 ? -7.275  -18.491 91.736  1.00 13.60  ? 366  ASN B C   1 
ATOM   5132  O  O   . ASN B  1 279 ? -6.428  -18.635 90.841  1.00 13.58  ? 366  ASN B O   1 
ATOM   5133  C  CB  . ASN B  1 279 ? -6.334  -20.625 92.659  1.00 14.14  ? 366  ASN B CB  1 
ATOM   5134  C  CG  . ASN B  1 279 ? -4.886  -20.146 92.810  1.00 15.24  ? 366  ASN B CG  1 
ATOM   5135  O  OD1 . ASN B  1 279 ? -4.556  -19.333 93.696  1.00 16.15  ? 366  ASN B OD1 1 
ATOM   5136  N  ND2 . ASN B  1 279 ? -4.016  -20.645 91.928  1.00 13.23  ? 366  ASN B ND2 1 
ATOM   5137  N  N   . SER B  1 280 ? -8.148  -17.477 91.756  1.00 13.03  ? 367  SER B N   1 
ATOM   5138  C  CA  . SER B  1 280 ? -8.238  -16.502 90.654  1.00 11.90  ? 367  SER B CA  1 
ATOM   5139  C  C   . SER B  1 280 ? -7.968  -15.088 91.150  1.00 11.49  ? 367  SER B C   1 
ATOM   5140  O  O   . SER B  1 280 ? -8.538  -14.668 92.170  1.00 11.21  ? 367  SER B O   1 
ATOM   5141  C  CB  . SER B  1 280 ? -9.614  -16.561 89.958  1.00 12.31  ? 367  SER B CB  1 
ATOM   5142  O  OG  . SER B  1 280 ? -9.856  -17.837 89.362  1.00 11.18  ? 367  SER B OG  1 
ATOM   5143  N  N   . TRP B  1 281 ? -7.111  -14.376 90.414  1.00 11.19  ? 368  TRP B N   1 
ATOM   5144  C  CA  . TRP B  1 281 ? -6.704  -12.997 90.722  1.00 11.42  ? 368  TRP B CA  1 
ATOM   5145  C  C   . TRP B  1 281 ? -6.856  -12.057 89.521  1.00 11.54  ? 368  TRP B C   1 
ATOM   5146  O  O   . TRP B  1 281 ? -6.395  -12.365 88.397  1.00 11.75  ? 368  TRP B O   1 
ATOM   5147  C  CB  . TRP B  1 281 ? -5.245  -12.961 91.191  1.00 11.13  ? 368  TRP B CB  1 
ATOM   5148  C  CG  . TRP B  1 281 ? -5.003  -13.457 92.589  1.00 11.22  ? 368  TRP B CG  1 
ATOM   5149  C  CD1 . TRP B  1 281 ? -4.760  -14.762 92.979  1.00 10.03  ? 368  TRP B CD1 1 
ATOM   5150  C  CD2 . TRP B  1 281 ? -4.926  -12.659 93.776  1.00 9.37   ? 368  TRP B CD2 1 
ATOM   5151  N  NE1 . TRP B  1 281 ? -4.564  -14.813 94.344  1.00 11.63  ? 368  TRP B NE1 1 
ATOM   5152  C  CE2 . TRP B  1 281 ? -4.647  -13.537 94.854  1.00 11.35  ? 368  TRP B CE2 1 
ATOM   5153  C  CE3 . TRP B  1 281 ? -5.077  -11.289 94.039  1.00 10.15  ? 368  TRP B CE3 1 
ATOM   5154  C  CZ2 . TRP B  1 281 ? -4.528  -13.086 96.172  1.00 11.23  ? 368  TRP B CZ2 1 
ATOM   5155  C  CZ3 . TRP B  1 281 ? -4.935  -10.834 95.353  1.00 11.43  ? 368  TRP B CZ3 1 
ATOM   5156  C  CH2 . TRP B  1 281 ? -4.651  -11.735 96.398  1.00 10.85  ? 368  TRP B CH2 1 
ATOM   5157  N  N   . LEU B  1 282 ? -7.495  -10.918 89.762  1.00 11.36  ? 369  LEU B N   1 
ATOM   5158  C  CA  . LEU B  1 282 ? -7.685  -9.882  88.746  1.00 11.73  ? 369  LEU B CA  1 
ATOM   5159  C  C   . LEU B  1 282 ? -6.894  -8.653  89.139  1.00 11.14  ? 369  LEU B C   1 
ATOM   5160  O  O   . LEU B  1 282 ? -7.003  -8.190  90.275  1.00 11.31  ? 369  LEU B O   1 
ATOM   5161  C  CB  . LEU B  1 282 ? -9.171  -9.475  88.612  1.00 12.17  ? 369  LEU B CB  1 
ATOM   5162  C  CG  . LEU B  1 282 ? -10.290 -10.527 88.590  1.00 15.05  ? 369  LEU B CG  1 
ATOM   5163  C  CD1 . LEU B  1 282 ? -11.653 -9.895  88.236  1.00 12.81  ? 369  LEU B CD1 1 
ATOM   5164  C  CD2 . LEU B  1 282 ? -9.966  -11.756 87.700  1.00 15.21  ? 369  LEU B CD2 1 
ATOM   5165  N  N   . GLY B  1 283 ? -6.070  -8.147  88.221  1.00 10.81  ? 370  GLY B N   1 
ATOM   5166  C  CA  . GLY B  1 283 ? -5.428  -6.837  88.421  1.00 10.53  ? 370  GLY B CA  1 
ATOM   5167  C  C   . GLY B  1 283 ? -6.297  -5.742  87.825  1.00 10.44  ? 370  GLY B C   1 
ATOM   5168  O  O   . GLY B  1 283 ? -7.037  -5.991  86.879  1.00 10.71  ? 370  GLY B O   1 
ATOM   5169  N  N   . ARG B  1 284 ? -6.217  -4.533  88.378  1.00 10.35  ? 371  ARG B N   1 
ATOM   5170  C  CA  . ARG B  1 284 ? -6.786  -3.342  87.728  1.00 10.19  ? 371  ARG B CA  1 
ATOM   5171  C  C   . ARG B  1 284 ? -6.216  -2.051  88.332  1.00 9.85   ? 371  ARG B C   1 
ATOM   5172  O  O   . ARG B  1 284 ? -5.672  -2.063  89.457  1.00 10.06  ? 371  ARG B O   1 
ATOM   5173  C  CB  . ARG B  1 284 ? -8.338  -3.355  87.819  1.00 9.62   ? 371  ARG B CB  1 
ATOM   5174  C  CG  . ARG B  1 284 ? -8.889  -3.193  89.240  1.00 9.84   ? 371  ARG B CG  1 
ATOM   5175  C  CD  . ARG B  1 284 ? -10.438 -3.073  89.209  1.00 10.96  ? 371  ARG B CD  1 
ATOM   5176  N  NE  . ARG B  1 284 ? -10.995 -2.898  90.552  1.00 12.82  ? 371  ARG B NE  1 
ATOM   5177  C  CZ  . ARG B  1 284 ? -12.299 -2.903  90.839  1.00 13.13  ? 371  ARG B CZ  1 
ATOM   5178  N  NH1 . ARG B  1 284 ? -13.197 -3.060  89.880  1.00 13.78  ? 371  ARG B NH1 1 
ATOM   5179  N  NH2 . ARG B  1 284 ? -12.704 -2.720  92.089  1.00 14.49  ? 371  ARG B NH2 1 
ATOM   5180  N  N   . THR B  1 285 ? -6.336  -0.943  87.599  1.00 9.81   ? 372  THR B N   1 
ATOM   5181  C  CA  . THR B  1 285 ? -6.034  0.378   88.152  1.00 9.95   ? 372  THR B CA  1 
ATOM   5182  C  C   . THR B  1 285 ? -7.011  0.638   89.289  1.00 10.60  ? 372  THR B C   1 
ATOM   5183  O  O   . THR B  1 285 ? -8.148  0.149   89.259  1.00 10.98  ? 372  THR B O   1 
ATOM   5184  C  CB  . THR B  1 285 ? -6.116  1.505   87.072  1.00 10.45  ? 372  THR B CB  1 
ATOM   5185  O  OG1 . THR B  1 285 ? -7.483  1.678   86.631  1.00 10.49  ? 372  THR B OG1 1 
ATOM   5186  C  CG2 . THR B  1 285 ? -5.235  1.141   85.859  1.00 9.58   ? 372  THR B CG2 1 
ATOM   5187  N  N   . ILE B  1 286 ? -6.569  1.350   90.316  1.00 11.17  ? 373  ILE B N   1 
ATOM   5188  C  CA  . ILE B  1 286 ? -7.483  1.687   91.428  1.00 11.43  ? 373  ILE B CA  1 
ATOM   5189  C  C   . ILE B  1 286 ? -8.542  2.681   90.939  1.00 12.14  ? 373  ILE B C   1 
ATOM   5190  O  O   . ILE B  1 286 ? -9.741  2.468   91.153  1.00 12.37  ? 373  ILE B O   1 
ATOM   5191  C  CB  . ILE B  1 286 ? -6.714  2.204   92.677  1.00 11.29  ? 373  ILE B CB  1 
ATOM   5192  C  CG1 . ILE B  1 286 ? -5.820  1.092   93.242  1.00 11.56  ? 373  ILE B CG1 1 
ATOM   5193  C  CG2 . ILE B  1 286 ? -7.699  2.735   93.755  1.00 11.71  ? 373  ILE B CG2 1 
ATOM   5194  C  CD1 . ILE B  1 286 ? -4.846  1.583   94.341  1.00 10.85  ? 373  ILE B CD1 1 
ATOM   5195  N  N   . SER B  1 287 ? -8.112  3.747   90.263  1.00 11.90  ? 374  SER B N   1 
ATOM   5196  C  CA  . SER B  1 287 ? -9.056  4.663   89.625  1.00 12.71  ? 374  SER B CA  1 
ATOM   5197  C  C   . SER B  1 287 ? -9.859  3.967   88.530  1.00 12.16  ? 374  SER B C   1 
ATOM   5198  O  O   . SER B  1 287 ? -9.324  3.223   87.708  1.00 12.59  ? 374  SER B O   1 
ATOM   5199  C  CB  . SER B  1 287 ? -8.342  5.871   89.021  1.00 12.21  ? 374  SER B CB  1 
ATOM   5200  O  OG  . SER B  1 287 ? -9.264  6.687   88.303  1.00 13.69  ? 374  SER B OG  1 
ATOM   5201  N  N   . LYS B  1 288 ? -11.155 4.220   88.506  1.00 12.89  ? 375  LYS B N   1 
ATOM   5202  C  CA  . LYS B  1 288 ? -11.965 3.682   87.433  1.00 13.51  ? 375  LYS B CA  1 
ATOM   5203  C  C   . LYS B  1 288 ? -11.894 4.566   86.168  1.00 13.37  ? 375  LYS B C   1 
ATOM   5204  O  O   . LYS B  1 288 ? -12.281 4.145   85.091  1.00 13.26  ? 375  LYS B O   1 
ATOM   5205  C  CB  . LYS B  1 288 ? -13.392 3.396   87.930  1.00 15.23  ? 375  LYS B CB  1 
ATOM   5206  C  CG  . LYS B  1 288 ? -14.297 4.558   87.944  1.00 17.43  ? 375  LYS B CG  1 
ATOM   5207  C  CD  . LYS B  1 288 ? -15.660 4.166   88.550  1.00 21.97  ? 375  LYS B CD  1 
ATOM   5208  C  CE  . LYS B  1 288 ? -16.766 5.063   87.956  1.00 24.90  ? 375  LYS B CE  1 
ATOM   5209  N  NZ  . LYS B  1 288 ? -16.345 6.510   87.888  1.00 24.90  ? 375  LYS B NZ  1 
ATOM   5210  N  N   . ASP B  1 289 ? -11.364 5.780   86.302  1.00 12.93  ? 376  ASP B N   1 
ATOM   5211  C  CA  . ASP B  1 289 ? -11.255 6.697   85.174  1.00 13.04  ? 376  ASP B CA  1 
ATOM   5212  C  C   . ASP B  1 289 ? -9.866  6.706   84.533  1.00 12.84  ? 376  ASP B C   1 
ATOM   5213  O  O   . ASP B  1 289 ? -9.736  6.687   83.314  1.00 12.61  ? 376  ASP B O   1 
ATOM   5214  C  CB  . ASP B  1 289 ? -11.590 8.137   85.594  1.00 13.29  ? 376  ASP B CB  1 
ATOM   5215  C  CG  . ASP B  1 289 ? -12.986 8.281   86.223  1.00 14.97  ? 376  ASP B CG  1 
ATOM   5216  O  OD1 . ASP B  1 289 ? -13.926 7.504   85.950  1.00 16.97  ? 376  ASP B OD1 1 
ATOM   5217  O  OD2 . ASP B  1 289 ? -13.119 9.205   87.034  1.00 19.40  ? 376  ASP B OD2 1 
ATOM   5218  N  N   . SER B  1 290 ? -8.827  6.735   85.359  1.00 13.01  ? 377  SER B N   1 
ATOM   5219  C  CA  . SER B  1 290 ? -7.484  7.009   84.848  1.00 13.01  ? 377  SER B CA  1 
ATOM   5220  C  C   . SER B  1 290 ? -6.483  5.925   85.225  1.00 12.15  ? 377  SER B C   1 
ATOM   5221  O  O   . SER B  1 290 ? -6.755  5.066   86.087  1.00 11.58  ? 377  SER B O   1 
ATOM   5222  C  CB  . SER B  1 290 ? -7.008  8.402   85.300  1.00 13.81  ? 377  SER B CB  1 
ATOM   5223  O  OG  . SER B  1 290 ? -6.765  8.403   86.696  1.00 18.26  ? 377  SER B OG  1 
ATOM   5224  N  N   . ARG B  1 291 ? -5.324  5.964   84.562  1.00 11.03  ? 378  ARG B N   1 
ATOM   5225  C  CA  . ARG B  1 291 ? -4.241  5.001   84.803  1.00 11.04  ? 378  ARG B CA  1 
ATOM   5226  C  C   . ARG B  1 291 ? -3.446  5.379   86.068  1.00 12.05  ? 378  ARG B C   1 
ATOM   5227  O  O   . ARG B  1 291 ? -2.253  5.723   86.002  1.00 12.23  ? 378  ARG B O   1 
ATOM   5228  C  CB  . ARG B  1 291 ? -3.342  4.897   83.556  1.00 11.12  ? 378  ARG B CB  1 
ATOM   5229  C  CG  . ARG B  1 291 ? -4.085  4.337   82.352  1.00 10.91  ? 378  ARG B CG  1 
ATOM   5230  C  CD  . ARG B  1 291 ? -3.328  4.501   81.046  1.00 10.45  ? 378  ARG B CD  1 
ATOM   5231  N  NE  . ARG B  1 291 ? -4.092  3.933   79.940  1.00 11.25  ? 378  ARG B NE  1 
ATOM   5232  C  CZ  . ARG B  1 291 ? -3.634  3.775   78.700  1.00 12.19  ? 378  ARG B CZ  1 
ATOM   5233  N  NH1 . ARG B  1 291 ? -2.409  4.181   78.377  1.00 9.54   ? 378  ARG B NH1 1 
ATOM   5234  N  NH2 . ARG B  1 291 ? -4.414  3.212   77.776  1.00 11.11  ? 378  ARG B NH2 1 
ATOM   5235  N  N   . SER B  1 292 ? -4.138  5.357   87.212  1.00 11.87  ? 379  SER B N   1 
ATOM   5236  C  CA  . SER B  1 292 ? -3.507  5.599   88.518  1.00 11.88  ? 379  SER B CA  1 
ATOM   5237  C  C   . SER B  1 292 ? -3.844  4.502   89.509  1.00 10.68  ? 379  SER B C   1 
ATOM   5238  O  O   . SER B  1 292 ? -4.959  3.988   89.517  1.00 10.53  ? 379  SER B O   1 
ATOM   5239  C  CB  . SER B  1 292 ? -3.872  6.963   89.117  1.00 12.54  ? 379  SER B CB  1 
ATOM   5240  O  OG  . SER B  1 292 ? -5.226  7.013   89.483  1.00 15.84  ? 379  SER B OG  1 
ATOM   5241  N  N   . GLY B  1 293 ? -2.864  4.171   90.343  1.00 10.31  ? 380  GLY B N   1 
ATOM   5242  C  CA  . GLY B  1 293 ? -2.967  3.080   91.294  1.00 9.31   ? 380  GLY B CA  1 
ATOM   5243  C  C   . GLY B  1 293 ? -2.960  1.715   90.621  1.00 9.49   ? 380  GLY B C   1 
ATOM   5244  O  O   . GLY B  1 293 ? -3.134  1.589   89.394  1.00 9.06   ? 380  GLY B O   1 
ATOM   5245  N  N   . TYR B  1 294 ? -2.725  0.683   91.421  1.00 9.69   ? 381  TYR B N   1 
ATOM   5246  C  CA  . TYR B  1 294 ? -2.873  -0.681  90.923  1.00 10.40  ? 381  TYR B CA  1 
ATOM   5247  C  C   . TYR B  1 294 ? -3.188  -1.584  92.099  1.00 10.83  ? 381  TYR B C   1 
ATOM   5248  O  O   . TYR B  1 294 ? -2.534  -1.471  93.130  1.00 10.80  ? 381  TYR B O   1 
ATOM   5249  C  CB  . TYR B  1 294 ? -1.621  -1.168  90.127  1.00 9.59   ? 381  TYR B CB  1 
ATOM   5250  C  CG  . TYR B  1 294 ? -2.026  -2.249  89.150  1.00 10.24  ? 381  TYR B CG  1 
ATOM   5251  C  CD1 . TYR B  1 294 ? -2.084  -3.596  89.548  1.00 9.55   ? 381  TYR B CD1 1 
ATOM   5252  C  CD2 . TYR B  1 294 ? -2.469  -1.915  87.857  1.00 10.76  ? 381  TYR B CD2 1 
ATOM   5253  C  CE1 . TYR B  1 294 ? -2.528  -4.592  88.654  1.00 8.56   ? 381  TYR B CE1 1 
ATOM   5254  C  CE2 . TYR B  1 294 ? -2.918  -2.890  86.971  1.00 9.54   ? 381  TYR B CE2 1 
ATOM   5255  C  CZ  . TYR B  1 294 ? -2.931  -4.222  87.376  1.00 9.60   ? 381  TYR B CZ  1 
ATOM   5256  O  OH  . TYR B  1 294 ? -3.394  -5.177  86.518  1.00 10.68  ? 381  TYR B OH  1 
ATOM   5257  N  N   . GLU B  1 295 ? -4.203  -2.444  91.931  1.00 11.19  ? 382  GLU B N   1 
ATOM   5258  C  CA  . GLU B  1 295 ? -4.643  -3.374  92.959  1.00 11.44  ? 382  GLU B CA  1 
ATOM   5259  C  C   . GLU B  1 295 ? -4.813  -4.798  92.400  1.00 11.23  ? 382  GLU B C   1 
ATOM   5260  O  O   . GLU B  1 295 ? -5.232  -4.984  91.239  1.00 11.78  ? 382  GLU B O   1 
ATOM   5261  C  CB  . GLU B  1 295 ? -5.958  -2.856  93.599  1.00 11.14  ? 382  GLU B CB  1 
ATOM   5262  C  CG  . GLU B  1 295 ? -7.113  -2.633  92.571  1.00 10.60  ? 382  GLU B CG  1 
ATOM   5263  C  CD  . GLU B  1 295 ? -8.375  -2.099  93.211  1.00 12.88  ? 382  GLU B CD  1 
ATOM   5264  O  OE1 . GLU B  1 295 ? -8.438  -2.068  94.460  1.00 15.83  ? 382  GLU B OE1 1 
ATOM   5265  O  OE2 . GLU B  1 295 ? -9.295  -1.682  92.477  1.00 14.67  ? 382  GLU B OE2 1 
ATOM   5266  N  N   . MET B  1 296 ? -4.478  -5.804  93.218  1.00 10.37  ? 383  MET B N   1 
ATOM   5267  C  CA  . MET B  1 296 ? -4.759  -7.191  92.901  1.00 10.27  ? 383  MET B CA  1 
ATOM   5268  C  C   . MET B  1 296 ? -5.931  -7.626  93.772  1.00 10.70  ? 383  MET B C   1 
ATOM   5269  O  O   . MET B  1 296 ? -5.950  -7.357  94.986  1.00 11.31  ? 383  MET B O   1 
ATOM   5270  C  CB  . MET B  1 296 ? -3.538  -8.086  93.161  1.00 10.19  ? 383  MET B CB  1 
ATOM   5271  C  CG  . MET B  1 296 ? -2.360  -7.768  92.255  1.00 9.55   ? 383  MET B CG  1 
ATOM   5272  S  SD  . MET B  1 296 ? -2.797  -8.021  90.522  1.00 9.59   ? 383  MET B SD  1 
ATOM   5273  C  CE  . MET B  1 296 ? -3.191  -9.782  90.474  1.00 11.90  ? 383  MET B CE  1 
ATOM   5274  N  N   . LEU B  1 297 ? -6.895  -8.282  93.139  1.00 10.52  ? 384  LEU B N   1 
ATOM   5275  C  CA  . LEU B  1 297 ? -8.143  -8.690  93.786  1.00 11.52  ? 384  LEU B CA  1 
ATOM   5276  C  C   . LEU B  1 297 ? -8.313  -10.187 93.606  1.00 10.64  ? 384  LEU B C   1 
ATOM   5277  O  O   . LEU B  1 297 ? -8.332  -10.678 92.461  1.00 10.81  ? 384  LEU B O   1 
ATOM   5278  C  CB  . LEU B  1 297 ? -9.343  -7.940  93.171  1.00 11.75  ? 384  LEU B CB  1 
ATOM   5279  C  CG  . LEU B  1 297 ? -9.283  -6.408  93.187  1.00 14.27  ? 384  LEU B CG  1 
ATOM   5280  C  CD1 . LEU B  1 297 ? -10.488 -5.820  92.449  1.00 16.88  ? 384  LEU B CD1 1 
ATOM   5281  C  CD2 . LEU B  1 297 ? -9.185  -5.866  94.589  1.00 14.96  ? 384  LEU B CD2 1 
ATOM   5282  N  N   . LYS B  1 298 ? -8.394  -10.919 94.721  1.00 10.58  ? 385  LYS B N   1 
ATOM   5283  C  CA  . LYS B  1 298 ? -8.667  -12.360 94.654  1.00 10.60  ? 385  LYS B CA  1 
ATOM   5284  C  C   . LYS B  1 298 ? -10.175 -12.537 94.484  1.00 11.06  ? 385  LYS B C   1 
ATOM   5285  O  O   . LYS B  1 298 ? -10.953 -12.174 95.373  1.00 10.90  ? 385  LYS B O   1 
ATOM   5286  C  CB  . LYS B  1 298 ? -8.174  -13.120 95.888  1.00 10.95  ? 385  LYS B CB  1 
ATOM   5287  C  CG  . LYS B  1 298 ? -8.209  -14.622 95.677  1.00 10.83  ? 385  LYS B CG  1 
ATOM   5288  C  CD  . LYS B  1 298 ? -7.367  -15.353 96.694  1.00 13.35  ? 385  LYS B CD  1 
ATOM   5289  C  CE  . LYS B  1 298 ? -7.240  -16.816 96.307  1.00 14.02  ? 385  LYS B CE  1 
ATOM   5290  N  NZ  . LYS B  1 298 ? -6.545  -17.584 97.391  1.00 17.71  ? 385  LYS B NZ  1 
ATOM   5291  N  N   . VAL B  1 299 ? -10.569 -13.038 93.319  1.00 10.75  ? 386  VAL B N   1 
ATOM   5292  C  CA  . VAL B  1 299 ? -11.977 -13.101 92.936  1.00 11.10  ? 386  VAL B CA  1 
ATOM   5293  C  C   . VAL B  1 299 ? -12.289 -14.549 92.558  1.00 11.66  ? 386  VAL B C   1 
ATOM   5294  O  O   . VAL B  1 299 ? -12.187 -14.933 91.400  1.00 12.06  ? 386  VAL B O   1 
ATOM   5295  C  CB  . VAL B  1 299 ? -12.326 -12.090 91.812  1.00 10.48  ? 386  VAL B CB  1 
ATOM   5296  C  CG1 . VAL B  1 299 ? -13.836 -12.177 91.443  1.00 11.61  ? 386  VAL B CG1 1 
ATOM   5297  C  CG2 . VAL B  1 299 ? -11.947 -10.620 92.233  1.00 8.52   ? 386  VAL B CG2 1 
ATOM   5298  N  N   . PRO B  1 300 ? -12.644 -15.372 93.554  1.00 12.58  ? 387  PRO B N   1 
ATOM   5299  C  CA  . PRO B  1 300 ? -12.897 -16.788 93.256  1.00 12.76  ? 387  PRO B CA  1 
ATOM   5300  C  C   . PRO B  1 300 ? -13.936 -16.991 92.131  1.00 12.39  ? 387  PRO B C   1 
ATOM   5301  O  O   . PRO B  1 300 ? -14.978 -16.340 92.133  1.00 12.70  ? 387  PRO B O   1 
ATOM   5302  C  CB  . PRO B  1 300 ? -13.395 -17.336 94.601  1.00 12.67  ? 387  PRO B CB  1 
ATOM   5303  C  CG  . PRO B  1 300 ? -12.698 -16.459 95.614  1.00 13.17  ? 387  PRO B CG  1 
ATOM   5304  C  CD  . PRO B  1 300 ? -12.796 -15.082 94.995  1.00 12.72  ? 387  PRO B CD  1 
ATOM   5305  N  N   . ASN B  1 301 ? -13.612 -17.858 91.171  1.00 12.38  ? 388  ASN B N   1 
ATOM   5306  C  CA  . ASN B  1 301 ? -14.503 -18.202 90.047  1.00 12.59  ? 388  ASN B CA  1 
ATOM   5307  C  C   . ASN B  1 301 ? -14.842 -17.024 89.113  1.00 12.95  ? 388  ASN B C   1 
ATOM   5308  O  O   . ASN B  1 301 ? -15.885 -17.022 88.434  1.00 12.77  ? 388  ASN B O   1 
ATOM   5309  C  CB  . ASN B  1 301 ? -15.758 -18.958 90.545  1.00 12.65  ? 388  ASN B CB  1 
ATOM   5310  C  CG  . ASN B  1 301 ? -15.387 -20.219 91.353  1.00 14.94  ? 388  ASN B CG  1 
ATOM   5311  O  OD1 . ASN B  1 301 ? -14.624 -21.068 90.882  1.00 16.96  ? 388  ASN B OD1 1 
ATOM   5312  N  ND2 . ASN B  1 301 ? -15.899 -20.319 92.586  1.00 17.92  ? 388  ASN B ND2 1 
ATOM   5313  N  N   . ALA B  1 302 ? -13.947 -16.032 89.074  1.00 12.48  ? 389  ALA B N   1 
ATOM   5314  C  CA  . ALA B  1 302 ? -14.104 -14.873 88.175  1.00 12.52  ? 389  ALA B CA  1 
ATOM   5315  C  C   . ALA B  1 302 ? -14.362 -15.295 86.726  1.00 12.82  ? 389  ALA B C   1 
ATOM   5316  O  O   . ALA B  1 302 ? -15.068 -14.599 85.997  1.00 12.48  ? 389  ALA B O   1 
ATOM   5317  C  CB  . ALA B  1 302 ? -12.883 -13.962 88.245  1.00 12.74  ? 389  ALA B CB  1 
ATOM   5318  N  N   . GLU B  1 303 ? -13.817 -16.438 86.320  1.00 13.17  ? 390  GLU B N   1 
ATOM   5319  C  CA  . GLU B  1 303 ? -13.968 -16.896 84.935  1.00 14.26  ? 390  GLU B CA  1 
ATOM   5320  C  C   . GLU B  1 303 ? -15.342 -17.518 84.629  1.00 14.22  ? 390  GLU B C   1 
ATOM   5321  O  O   . GLU B  1 303 ? -15.700 -17.692 83.458  1.00 14.62  ? 390  GLU B O   1 
ATOM   5322  C  CB  . GLU B  1 303 ? -12.864 -17.887 84.574  1.00 14.45  ? 390  GLU B CB  1 
ATOM   5323  C  CG  . GLU B  1 303 ? -12.739 -18.138 83.077  1.00 15.16  ? 390  GLU B CG  1 
ATOM   5324  C  CD  . GLU B  1 303 ? -11.626 -19.099 82.715  1.00 15.02  ? 390  GLU B CD  1 
ATOM   5325  O  OE1 . GLU B  1 303 ? -11.333 -19.199 81.505  1.00 17.56  ? 390  GLU B OE1 1 
ATOM   5326  O  OE2 . GLU B  1 303 ? -11.053 -19.760 83.616  1.00 14.06  ? 390  GLU B OE2 1 
ATOM   5327  N  N   . THR B  1 304 ? -16.104 -17.866 85.666  1.00 14.16  ? 391  THR B N   1 
ATOM   5328  C  CA  . THR B  1 304 ? -17.340 -18.642 85.461  1.00 14.78  ? 391  THR B CA  1 
ATOM   5329  C  C   . THR B  1 304 ? -18.600 -18.091 86.148  1.00 15.12  ? 391  THR B C   1 
ATOM   5330  O  O   . THR B  1 304 ? -19.722 -18.484 85.793  1.00 15.68  ? 391  THR B O   1 
ATOM   5331  C  CB  . THR B  1 304 ? -17.141 -20.119 85.901  1.00 15.03  ? 391  THR B CB  1 
ATOM   5332  O  OG1 . THR B  1 304 ? -16.798 -20.170 87.297  1.00 15.74  ? 391  THR B OG1 1 
ATOM   5333  C  CG2 . THR B  1 304 ? -16.051 -20.804 85.063  1.00 15.07  ? 391  THR B CG2 1 
ATOM   5334  N  N   . ASP B  1 305 ? -18.422 -17.178 87.099  1.00 14.45  ? 392  ASP B N   1 
ATOM   5335  C  CA  . ASP B  1 305 ? -19.501 -16.753 87.987  1.00 14.69  ? 392  ASP B CA  1 
ATOM   5336  C  C   . ASP B  1 305 ? -19.754 -15.239 87.899  1.00 14.34  ? 392  ASP B C   1 
ATOM   5337  O  O   . ASP B  1 305 ? -18.943 -14.436 88.352  1.00 14.08  ? 392  ASP B O   1 
ATOM   5338  C  CB  . ASP B  1 305 ? -19.168 -17.189 89.422  1.00 14.70  ? 392  ASP B CB  1 
ATOM   5339  C  CG  . ASP B  1 305 ? -20.190 -16.722 90.458  1.00 17.19  ? 392  ASP B CG  1 
ATOM   5340  O  OD1 . ASP B  1 305 ? -21.289 -16.198 90.109  1.00 14.84  ? 392  ASP B OD1 1 
ATOM   5341  O  OD2 . ASP B  1 305 ? -19.860 -16.876 91.665  1.00 19.64  ? 392  ASP B OD2 1 
ATOM   5342  N  N   . ILE B  1 306 ? -20.895 -14.859 87.339  1.00 13.82  ? 393  ILE B N   1 
ATOM   5343  C  CA  . ILE B  1 306 ? -21.219 -13.434 87.150  1.00 14.09  ? 393  ILE B CA  1 
ATOM   5344  C  C   . ILE B  1 306 ? -21.415 -12.659 88.462  1.00 13.84  ? 393  ILE B C   1 
ATOM   5345  O  O   . ILE B  1 306 ? -21.399 -11.425 88.480  1.00 14.07  ? 393  ILE B O   1 
ATOM   5346  C  CB  . ILE B  1 306 ? -22.445 -13.229 86.204  1.00 14.66  ? 393  ILE B CB  1 
ATOM   5347  C  CG1 . ILE B  1 306 ? -23.674 -13.964 86.754  1.00 15.26  ? 393  ILE B CG1 1 
ATOM   5348  C  CG2 . ILE B  1 306 ? -22.086 -13.670 84.764  1.00 15.47  ? 393  ILE B CG2 1 
ATOM   5349  C  CD1 . ILE B  1 306 ? -25.010 -13.544 86.123  1.00 15.38  ? 393  ILE B CD1 1 
ATOM   5350  N  N   . GLN B  1 307 ? -21.595 -13.376 89.570  1.00 13.80  ? 394  GLN B N   1 
ATOM   5351  C  CA  . GLN B  1 307 ? -21.766 -12.699 90.842  1.00 14.50  ? 394  GLN B CA  1 
ATOM   5352  C  C   . GLN B  1 307 ? -20.491 -12.652 91.672  1.00 13.94  ? 394  GLN B C   1 
ATOM   5353  O  O   . GLN B  1 307 ? -20.503 -12.116 92.773  1.00 14.25  ? 394  GLN B O   1 
ATOM   5354  C  CB  . GLN B  1 307 ? -22.906 -13.328 91.632  1.00 15.25  ? 394  GLN B CB  1 
ATOM   5355  C  CG  . GLN B  1 307 ? -24.204 -13.313 90.863  1.00 19.41  ? 394  GLN B CG  1 
ATOM   5356  C  CD  . GLN B  1 307 ? -25.379 -13.500 91.759  1.00 24.07  ? 394  GLN B CD  1 
ATOM   5357  O  OE1 . GLN B  1 307 ? -25.708 -14.627 92.132  1.00 27.24  ? 394  GLN B OE1 1 
ATOM   5358  N  NE2 . GLN B  1 307 ? -26.032 -12.391 92.126  1.00 25.95  ? 394  GLN B NE2 1 
ATOM   5359  N  N   . SER B  1 308 ? -19.398 -13.196 91.135  1.00 14.19  ? 395  SER B N   1 
ATOM   5360  C  CA  . SER B  1 308 ? -18.143 -13.299 91.891  1.00 13.86  ? 395  SER B CA  1 
ATOM   5361  C  C   . SER B  1 308 ? -17.559 -11.927 92.241  1.00 13.36  ? 395  SER B C   1 
ATOM   5362  O  O   . SER B  1 308 ? -17.443 -11.044 91.386  1.00 13.86  ? 395  SER B O   1 
ATOM   5363  C  CB  . SER B  1 308 ? -17.112 -14.159 91.150  1.00 14.01  ? 395  SER B CB  1 
ATOM   5364  O  OG  . SER B  1 308 ? -16.786 -13.593 89.887  1.00 10.78  ? 395  SER B OG  1 
ATOM   5365  N  N   . GLY B  1 309 ? -17.226 -11.758 93.519  1.00 13.49  ? 396  GLY B N   1 
ATOM   5366  C  CA  . GLY B  1 309 ? -16.579 -10.557 94.045  1.00 12.94  ? 396  GLY B CA  1 
ATOM   5367  C  C   . GLY B  1 309 ? -15.265 -10.869 94.782  1.00 12.96  ? 396  GLY B C   1 
ATOM   5368  O  O   . GLY B  1 309 ? -14.915 -12.036 94.974  1.00 12.18  ? 396  GLY B O   1 
ATOM   5369  N  N   . PRO B  1 310 ? -14.526 -9.824  95.190  1.00 12.58  ? 397  PRO B N   1 
ATOM   5370  C  CA  . PRO B  1 310 ? -13.215 -9.999  95.850  1.00 13.19  ? 397  PRO B CA  1 
ATOM   5371  C  C   . PRO B  1 310 ? -13.327 -10.474 97.303  1.00 13.44  ? 397  PRO B C   1 
ATOM   5372  O  O   . PRO B  1 310 ? -14.240 -10.052 98.020  1.00 13.35  ? 397  PRO B O   1 
ATOM   5373  C  CB  . PRO B  1 310 ? -12.608 -8.582  95.826  1.00 13.63  ? 397  PRO B CB  1 
ATOM   5374  C  CG  . PRO B  1 310 ? -13.459 -7.805  94.858  1.00 13.32  ? 397  PRO B CG  1 
ATOM   5375  C  CD  . PRO B  1 310 ? -14.838 -8.402  94.988  1.00 12.41  ? 397  PRO B CD  1 
ATOM   5376  N  N   . ILE B  1 311 ? -12.396 -11.337 97.715  1.00 13.40  ? 398  ILE B N   1 
ATOM   5377  C  CA  . ILE B  1 311 ? -12.316 -11.850 99.081  1.00 13.30  ? 398  ILE B CA  1 
ATOM   5378  C  C   . ILE B  1 311 ? -11.001 -11.386 99.741  1.00 13.63  ? 398  ILE B C   1 
ATOM   5379  O  O   . ILE B  1 311 ? -10.827 -11.477 100.952 1.00 12.92  ? 398  ILE B O   1 
ATOM   5380  C  CB  . ILE B  1 311 ? -12.506 -13.403 99.109  1.00 13.37  ? 398  ILE B CB  1 
ATOM   5381  C  CG1 . ILE B  1 311 ? -11.320 -14.148 98.444  1.00 13.61  ? 398  ILE B CG1 1 
ATOM   5382  C  CG2 . ILE B  1 311 ? -13.872 -13.764 98.450  1.00 14.55  ? 398  ILE B CG2 1 
ATOM   5383  C  CD1 . ILE B  1 311 ? -11.197 -15.662 98.817  1.00 14.22  ? 398  ILE B CD1 1 
ATOM   5384  N  N   . SER B  1 312 ? -10.080 -10.883 98.928  1.00 13.57  ? 399  SER B N   1 
ATOM   5385  C  CA  . SER B  1 312 ? -8.883  -10.216 99.443  1.00 14.86  ? 399  SER B CA  1 
ATOM   5386  C  C   . SER B  1 312 ? -8.394  -9.193  98.411  1.00 14.49  ? 399  SER B C   1 
ATOM   5387  O  O   . SER B  1 312 ? -8.805  -9.219  97.239  1.00 13.76  ? 399  SER B O   1 
ATOM   5388  C  CB  . SER B  1 312 ? -7.781  -11.218 99.802  1.00 15.31  ? 399  SER B CB  1 
ATOM   5389  O  OG  . SER B  1 312 ? -7.267  -11.788 98.627  1.00 19.45  ? 399  SER B OG  1 
ATOM   5390  N  N   . ASN B  1 313 ? -7.556  -8.273  98.862  1.00 14.42  ? 400  ASN B N   1 
ATOM   5391  C  CA  . ASN B  1 313 ? -6.970  -7.278  97.971  1.00 14.47  ? 400  ASN B CA  1 
ATOM   5392  C  C   . ASN B  1 313 ? -5.541  -6.967  98.380  1.00 13.71  ? 400  ASN B C   1 
ATOM   5393  O  O   . ASN B  1 313 ? -5.175  -7.101  99.552  1.00 14.28  ? 400  ASN B O   1 
ATOM   5394  C  CB  . ASN B  1 313 ? -7.808  -6.006  97.936  1.00 15.01  ? 400  ASN B CB  1 
ATOM   5395  C  CG  . ASN B  1 313 ? -7.687  -5.201  99.200  1.00 18.69  ? 400  ASN B CG  1 
ATOM   5396  O  OD1 . ASN B  1 313 ? -8.251  -5.559  100.246 1.00 22.70  ? 400  ASN B OD1 1 
ATOM   5397  N  ND2 . ASN B  1 313 ? -6.939  -4.106  99.124  1.00 21.26  ? 400  ASN B ND2 1 
ATOM   5398  N  N   . GLN B  1 314 ? -4.726  -6.586  97.408  1.00 12.52  ? 401  GLN B N   1 
ATOM   5399  C  CA  . GLN B  1 314 ? -3.378  -6.086  97.702  1.00 11.65  ? 401  GLN B CA  1 
ATOM   5400  C  C   . GLN B  1 314 ? -3.115  -4.866  96.846  1.00 11.30  ? 401  GLN B C   1 
ATOM   5401  O  O   . GLN B  1 314 ? -3.197  -4.956  95.629  1.00 11.54  ? 401  GLN B O   1 
ATOM   5402  C  CB  . GLN B  1 314 ? -2.315  -7.155  97.436  1.00 11.58  ? 401  GLN B CB  1 
ATOM   5403  C  CG  . GLN B  1 314 ? -0.905  -6.727  97.909  1.00 11.11  ? 401  GLN B CG  1 
ATOM   5404  C  CD  . GLN B  1 314 ? 0.128   -7.835  97.831  1.00 11.61  ? 401  GLN B CD  1 
ATOM   5405  O  OE1 . GLN B  1 314 ? -0.191  -9.036  97.914  1.00 12.24  ? 401  GLN B OE1 1 
ATOM   5406  N  NE2 . GLN B  1 314 ? 1.388   -7.436  97.644  1.00 12.86  ? 401  GLN B NE2 1 
ATOM   5407  N  N   . VAL B  1 315 ? -2.844  -3.732  97.490  1.00 10.24  ? 402  VAL B N   1 
ATOM   5408  C  CA  . VAL B  1 315 ? -2.455  -2.515  96.782  1.00 10.77  ? 402  VAL B CA  1 
ATOM   5409  C  C   . VAL B  1 315 ? -1.001  -2.679  96.323  1.00 10.36  ? 402  VAL B C   1 
ATOM   5410  O  O   . VAL B  1 315 ? -0.113  -2.931  97.141  1.00 10.38  ? 402  VAL B O   1 
ATOM   5411  C  CB  . VAL B  1 315 ? -2.608  -1.249  97.641  1.00 10.98  ? 402  VAL B CB  1 
ATOM   5412  C  CG1 . VAL B  1 315 ? -1.896  -0.050  96.975  1.00 10.51  ? 402  VAL B CG1 1 
ATOM   5413  C  CG2 . VAL B  1 315 ? -4.089  -0.938  97.889  1.00 12.66  ? 402  VAL B CG2 1 
ATOM   5414  N  N   . ILE B  1 316 ? -0.792  -2.565  95.009  1.00 9.59   ? 403  ILE B N   1 
ATOM   5415  C  CA  . ILE B  1 316 ? 0.543   -2.701  94.409  1.00 9.40   ? 403  ILE B CA  1 
ATOM   5416  C  C   . ILE B  1 316 ? 1.162   -1.318  94.174  1.00 10.23  ? 403  ILE B C   1 
ATOM   5417  O  O   . ILE B  1 316 ? 2.381   -1.113  94.378  1.00 10.23  ? 403  ILE B O   1 
ATOM   5418  C  CB  . ILE B  1 316 ? 0.477   -3.529  93.073  1.00 9.37   ? 403  ILE B CB  1 
ATOM   5419  C  CG1 . ILE B  1 316 ? -0.260  -4.887  93.276  1.00 9.77   ? 403  ILE B CG1 1 
ATOM   5420  C  CG2 . ILE B  1 316 ? 1.903   -3.662  92.424  1.00 8.43   ? 403  ILE B CG2 1 
ATOM   5421  C  CD1 . ILE B  1 316 ? 0.340   -5.830  94.329  1.00 8.45   ? 403  ILE B CD1 1 
ATOM   5422  N  N   . VAL B  1 317 ? 0.310   -0.373  93.765  1.00 9.48   ? 404  VAL B N   1 
ATOM   5423  C  CA  . VAL B  1 317 ? 0.705   1.032   93.570  1.00 9.87   ? 404  VAL B CA  1 
ATOM   5424  C  C   . VAL B  1 317 ? -0.406  1.884   94.163  1.00 10.25  ? 404  VAL B C   1 
ATOM   5425  O  O   . VAL B  1 317 ? -1.597  1.691   93.824  1.00 9.78   ? 404  VAL B O   1 
ATOM   5426  C  CB  . VAL B  1 317 ? 0.866   1.382   92.065  1.00 9.37   ? 404  VAL B CB  1 
ATOM   5427  C  CG1 . VAL B  1 317 ? 1.229   2.885   91.879  1.00 8.37   ? 404  VAL B CG1 1 
ATOM   5428  C  CG2 . VAL B  1 317 ? 1.927   0.495   91.401  1.00 9.20   ? 404  VAL B CG2 1 
ATOM   5429  N  N   . ASN B  1 318 ? -0.067  2.812   95.054  1.00 12.01  ? 405  ASN B N   1 
ATOM   5430  C  CA  . ASN B  1 318 ? -1.144  3.641   95.642  1.00 12.73  ? 405  ASN B CA  1 
ATOM   5431  C  C   . ASN B  1 318 ? -1.827  4.579   94.637  1.00 12.82  ? 405  ASN B C   1 
ATOM   5432  O  O   . ASN B  1 318 ? -1.237  4.945   93.606  1.00 11.72  ? 405  ASN B O   1 
ATOM   5433  C  CB  . ASN B  1 318 ? -0.721  4.357   96.951  1.00 13.83  ? 405  ASN B CB  1 
ATOM   5434  C  CG  . ASN B  1 318 ? 0.293   5.438   96.735  1.00 15.96  ? 405  ASN B CG  1 
ATOM   5435  O  OD1 . ASN B  1 318 ? 1.210   5.618   97.558  1.00 21.02  ? 405  ASN B OD1 1 
ATOM   5436  N  ND2 . ASN B  1 318 ? 0.158   6.170   95.641  1.00 15.07  ? 405  ASN B ND2 1 
ATOM   5437  N  N   . ASN B  1 319 ? -3.071  4.964   94.934  1.00 12.95  ? 406  ASN B N   1 
ATOM   5438  C  CA  . ASN B  1 319 ? -3.861  5.713   93.958  1.00 13.74  ? 406  ASN B CA  1 
ATOM   5439  C  C   . ASN B  1 319 ? -3.413  7.170   93.829  1.00 13.81  ? 406  ASN B C   1 
ATOM   5440  O  O   . ASN B  1 319 ? -4.008  7.935   93.079  1.00 14.92  ? 406  ASN B O   1 
ATOM   5441  C  CB  . ASN B  1 319 ? -5.373  5.601   94.244  1.00 13.76  ? 406  ASN B CB  1 
ATOM   5442  C  CG  . ASN B  1 319 ? -6.246  6.066   93.055  1.00 14.80  ? 406  ASN B CG  1 
ATOM   5443  O  OD1 . ASN B  1 319 ? -7.320  6.674   93.252  1.00 20.53  ? 406  ASN B OD1 1 
ATOM   5444  N  ND2 . ASN B  1 319 ? -5.791  5.807   91.837  1.00 10.94  ? 406  ASN B ND2 1 
ATOM   5445  N  N   . GLN B  1 320 ? -2.366  7.558   94.559  1.00 13.46  ? 407  GLN B N   1 
ATOM   5446  C  CA  . GLN B  1 320 ? -1.760  8.881   94.354  1.00 13.91  ? 407  GLN B CA  1 
ATOM   5447  C  C   . GLN B  1 320 ? -0.615  8.797   93.368  1.00 13.28  ? 407  GLN B C   1 
ATOM   5448  O  O   . GLN B  1 320 ? 0.057   9.803   93.116  1.00 13.96  ? 407  GLN B O   1 
ATOM   5449  C  CB  . GLN B  1 320 ? -1.258  9.496   95.666  1.00 14.47  ? 407  GLN B CB  1 
ATOM   5450  C  CG  . GLN B  1 320 ? -2.376  9.740   96.672  1.00 18.12  ? 407  GLN B CG  1 
ATOM   5451  C  CD  . GLN B  1 320 ? -2.808  8.440   97.332  1.00 22.76  ? 407  GLN B CD  1 
ATOM   5452  O  OE1 . GLN B  1 320 ? -2.004  7.777   97.984  1.00 24.76  ? 407  GLN B OE1 1 
ATOM   5453  N  NE2 . GLN B  1 320 ? -4.070  8.055   97.140  1.00 27.39  ? 407  GLN B NE2 1 
ATOM   5454  N  N   . ASN B  1 321 ? -0.388  7.606   92.821  1.00 12.01  ? 408  ASN B N   1 
ATOM   5455  C  CA  . ASN B  1 321 ? 0.702   7.406   91.859  1.00 11.26  ? 408  ASN B CA  1 
ATOM   5456  C  C   . ASN B  1 321 ? 0.229   6.879   90.525  1.00 10.87  ? 408  ASN B C   1 
ATOM   5457  O  O   . ASN B  1 321 ? -0.791  6.209   90.460  1.00 11.34  ? 408  ASN B O   1 
ATOM   5458  C  CB  . ASN B  1 321 ? 1.803   6.509   92.453  1.00 10.85  ? 408  ASN B CB  1 
ATOM   5459  C  CG  . ASN B  1 321 ? 2.625   7.242   93.499  1.00 10.85  ? 408  ASN B CG  1 
ATOM   5460  O  OD1 . ASN B  1 321 ? 2.405   7.090   94.707  1.00 14.63  ? 408  ASN B OD1 1 
ATOM   5461  N  ND2 . ASN B  1 321 ? 3.542   8.077   93.037  1.00 11.49  ? 408  ASN B ND2 1 
ATOM   5462  N  N   . TRP B  1 322 ? 0.980   7.188   89.468  1.00 10.86  ? 409  TRP B N   1 
ATOM   5463  C  CA  . TRP B  1 322 ? 0.620   6.768   88.113  1.00 10.93  ? 409  TRP B CA  1 
ATOM   5464  C  C   . TRP B  1 322 ? 0.981   5.309   87.852  1.00 10.19  ? 409  TRP B C   1 
ATOM   5465  O  O   . TRP B  1 322 ? 2.048   4.840   88.268  1.00 11.03  ? 409  TRP B O   1 
ATOM   5466  C  CB  . TRP B  1 322 ? 1.282   7.686   87.075  1.00 11.36  ? 409  TRP B CB  1 
ATOM   5467  C  CG  . TRP B  1 322 ? 0.863   9.122   87.244  1.00 13.65  ? 409  TRP B CG  1 
ATOM   5468  C  CD1 . TRP B  1 322 ? 1.658   10.185  87.606  1.00 14.45  ? 409  TRP B CD1 1 
ATOM   5469  C  CD2 . TRP B  1 322 ? -0.469  9.638   87.127  1.00 14.71  ? 409  TRP B CD2 1 
ATOM   5470  N  NE1 . TRP B  1 322 ? 0.898   11.326  87.703  1.00 14.44  ? 409  TRP B NE1 1 
ATOM   5471  C  CE2 . TRP B  1 322 ? -0.409  11.020  87.412  1.00 14.49  ? 409  TRP B CE2 1 
ATOM   5472  C  CE3 . TRP B  1 322 ? -1.713  9.062   86.793  1.00 13.80  ? 409  TRP B CE3 1 
ATOM   5473  C  CZ2 . TRP B  1 322 ? -1.546  11.847  87.364  1.00 14.27  ? 409  TRP B CZ2 1 
ATOM   5474  C  CZ3 . TRP B  1 322 ? -2.847  9.883   86.756  1.00 13.40  ? 409  TRP B CZ3 1 
ATOM   5475  C  CH2 . TRP B  1 322 ? -2.751  11.259  87.030  1.00 13.56  ? 409  TRP B CH2 1 
ATOM   5476  N  N   . SER B  1 323 ? 0.095   4.595   87.164  1.00 9.70   ? 410  SER B N   1 
ATOM   5477  C  CA  . SER B  1 323 ? 0.392   3.226   86.751  1.00 9.32   ? 410  SER B CA  1 
ATOM   5478  C  C   . SER B  1 323 ? 0.430   3.199   85.223  1.00 9.33   ? 410  SER B C   1 
ATOM   5479  O  O   . SER B  1 323 ? 1.060   4.070   84.610  1.00 9.27   ? 410  SER B O   1 
ATOM   5480  C  CB  . SER B  1 323 ? -0.582  2.204   87.387  1.00 9.05   ? 410  SER B CB  1 
ATOM   5481  O  OG  . SER B  1 323 ? -1.967  2.458   87.082  1.00 8.61   ? 410  SER B OG  1 
ATOM   5482  N  N   . GLY B  1 324 ? -0.252  2.242   84.602  1.00 9.18   ? 411  GLY B N   1 
ATOM   5483  C  CA  . GLY B  1 324 ? -0.126  2.071   83.134  1.00 9.54   ? 411  GLY B CA  1 
ATOM   5484  C  C   . GLY B  1 324 ? -0.516  0.662   82.732  1.00 8.67   ? 411  GLY B C   1 
ATOM   5485  O  O   . GLY B  1 324 ? -1.368  0.034   83.376  1.00 8.66   ? 411  GLY B O   1 
ATOM   5486  N  N   . TYR B  1 325 ? 0.107   0.165   81.668  1.00 8.19   ? 412  TYR B N   1 
ATOM   5487  C  CA  . TYR B  1 325 ? -0.111  -1.237  81.229  1.00 7.97   ? 412  TYR B CA  1 
ATOM   5488  C  C   . TYR B  1 325 ? 0.282   -2.245  82.310  1.00 8.11   ? 412  TYR B C   1 
ATOM   5489  O  O   . TYR B  1 325 ? 1.141   -1.965  83.144  1.00 9.41   ? 412  TYR B O   1 
ATOM   5490  C  CB  . TYR B  1 325 ? 0.670   -1.488  79.928  1.00 8.28   ? 412  TYR B CB  1 
ATOM   5491  C  CG  . TYR B  1 325 ? 0.034   -0.931  78.665  1.00 8.15   ? 412  TYR B CG  1 
ATOM   5492  C  CD1 . TYR B  1 325 ? -1.011  0.016   78.723  1.00 7.34   ? 412  TYR B CD1 1 
ATOM   5493  C  CD2 . TYR B  1 325 ? 0.503   -1.314  77.407  1.00 7.53   ? 412  TYR B CD2 1 
ATOM   5494  C  CE1 . TYR B  1 325 ? -1.594  0.525   77.550  1.00 9.04   ? 412  TYR B CE1 1 
ATOM   5495  C  CE2 . TYR B  1 325 ? -0.072  -0.819  76.234  1.00 9.37   ? 412  TYR B CE2 1 
ATOM   5496  C  CZ  . TYR B  1 325 ? -1.115  0.101   76.313  1.00 9.00   ? 412  TYR B CZ  1 
ATOM   5497  O  OH  . TYR B  1 325 ? -1.680  0.598   75.151  1.00 9.13   ? 412  TYR B OH  1 
ATOM   5498  N  N   . SER B  1 326 ? -0.348  -3.422  82.299  1.00 7.85   ? 413  SER B N   1 
ATOM   5499  C  CA  . SER B  1 326 ? 0.078   -4.526  83.135  1.00 7.56   ? 413  SER B CA  1 
ATOM   5500  C  C   . SER B  1 326 ? -0.076  -5.816  82.333  1.00 8.25   ? 413  SER B C   1 
ATOM   5501  O  O   . SER B  1 326 ? -0.924  -5.884  81.425  1.00 8.41   ? 413  SER B O   1 
ATOM   5502  C  CB  . SER B  1 326 ? -0.729  -4.597  84.441  1.00 7.42   ? 413  SER B CB  1 
ATOM   5503  O  OG  . SER B  1 326 ? -2.135  -4.699  84.213  1.00 7.40   ? 413  SER B OG  1 
ATOM   5504  N  N   . GLY B  1 327 ? 0.724   -6.825  82.683  1.00 8.41   ? 414  GLY B N   1 
ATOM   5505  C  CA  . GLY B  1 327 ? 0.732   -8.082  81.953  1.00 8.00   ? 414  GLY B CA  1 
ATOM   5506  C  C   . GLY B  1 327 ? 1.213   -9.257  82.763  1.00 8.32   ? 414  GLY B C   1 
ATOM   5507  O  O   . GLY B  1 327 ? 1.844   -9.097  83.812  1.00 8.31   ? 414  GLY B O   1 
ATOM   5508  N  N   . ALA B  1 328 ? 0.913   -10.443 82.250  1.00 8.18   ? 415  ALA B N   1 
ATOM   5509  C  CA  . ALA B  1 328 ? 1.287   -11.711 82.857  1.00 8.34   ? 415  ALA B CA  1 
ATOM   5510  C  C   . ALA B  1 328 ? 2.594   -12.256 82.300  1.00 8.40   ? 415  ALA B C   1 
ATOM   5511  O  O   . ALA B  1 328 ? 2.877   -12.078 81.125  1.00 9.20   ? 415  ALA B O   1 
ATOM   5512  C  CB  . ALA B  1 328 ? 0.164   -12.733 82.614  1.00 7.87   ? 415  ALA B CB  1 
ATOM   5513  N  N   . PHE B  1 329 ? 3.362   -12.931 83.154  1.00 8.95   ? 416  PHE B N   1 
ATOM   5514  C  CA  . PHE B  1 329 ? 4.481   -13.801 82.750  1.00 8.82   ? 416  PHE B CA  1 
ATOM   5515  C  C   . PHE B  1 329 ? 4.666   -14.860 83.822  1.00 9.37   ? 416  PHE B C   1 
ATOM   5516  O  O   . PHE B  1 329 ? 4.191   -14.692 84.960  1.00 9.67   ? 416  PHE B O   1 
ATOM   5517  C  CB  . PHE B  1 329 ? 5.793   -13.016 82.484  1.00 8.28   ? 416  PHE B CB  1 
ATOM   5518  C  CG  . PHE B  1 329 ? 6.415   -12.378 83.717  1.00 9.58   ? 416  PHE B CG  1 
ATOM   5519  C  CD1 . PHE B  1 329 ? 5.898   -11.193 84.253  1.00 9.61   ? 416  PHE B CD1 1 
ATOM   5520  C  CD2 . PHE B  1 329 ? 7.538   -12.945 84.314  1.00 8.84   ? 416  PHE B CD2 1 
ATOM   5521  C  CE1 . PHE B  1 329 ? 6.463   -10.612 85.386  1.00 8.35   ? 416  PHE B CE1 1 
ATOM   5522  C  CE2 . PHE B  1 329 ? 8.122   -12.371 85.464  1.00 9.26   ? 416  PHE B CE2 1 
ATOM   5523  C  CZ  . PHE B  1 329 ? 7.589   -11.191 85.990  1.00 7.42   ? 416  PHE B CZ  1 
ATOM   5524  N  N   . ILE B  1 330 ? 5.341   -15.949 83.462  1.00 9.27   ? 417  ILE B N   1 
ATOM   5525  C  CA  . ILE B  1 330 ? 5.680   -16.989 84.431  1.00 10.32  ? 417  ILE B CA  1 
ATOM   5526  C  C   . ILE B  1 330 ? 7.106   -17.444 84.148  1.00 10.34  ? 417  ILE B C   1 
ATOM   5527  O  O   . ILE B  1 330 ? 7.512   -17.537 82.990  1.00 10.31  ? 417  ILE B O   1 
ATOM   5528  C  CB  . ILE B  1 330 ? 4.679   -18.191 84.376  1.00 9.98   ? 417  ILE B CB  1 
ATOM   5529  C  CG1 . ILE B  1 330 ? 3.241   -17.749 84.745  1.00 11.24  ? 417  ILE B CG1 1 
ATOM   5530  C  CG2 . ILE B  1 330 ? 5.153   -19.374 85.262  1.00 10.35  ? 417  ILE B CG2 1 
ATOM   5531  C  CD1 . ILE B  1 330 ? 2.191   -18.867 84.658  1.00 10.44  ? 417  ILE B CD1 1 
ATOM   5532  N  N   . ASP B  1 331 ? 7.874   -17.694 85.208  1.00 11.35  ? 418  ASP B N   1 
ATOM   5533  C  CA  . ASP B  1 331 ? 9.128   -18.432 85.051  1.00 11.36  ? 418  ASP B CA  1 
ATOM   5534  C  C   . ASP B  1 331 ? 8.790   -19.923 84.908  1.00 11.81  ? 418  ASP B C   1 
ATOM   5535  O  O   . ASP B  1 331 ? 8.782   -20.667 85.909  1.00 11.40  ? 418  ASP B O   1 
ATOM   5536  C  CB  . ASP B  1 331 ? 10.053  -18.237 86.245  1.00 11.78  ? 418  ASP B CB  1 
ATOM   5537  C  CG  . ASP B  1 331 ? 11.428  -18.884 86.013  1.00 13.39  ? 418  ASP B CG  1 
ATOM   5538  O  OD1 . ASP B  1 331 ? 11.656  -19.428 84.899  1.00 12.28  ? 418  ASP B OD1 1 
ATOM   5539  O  OD2 . ASP B  1 331 ? 12.268  -18.847 86.939  1.00 14.88  ? 418  ASP B OD2 1 
ATOM   5540  N  N   . TYR B  1 332 ? 8.543   -20.357 83.666  1.00 11.66  ? 419  TYR B N   1 
ATOM   5541  C  CA  . TYR B  1 332 ? 8.182   -21.757 83.375  1.00 11.77  ? 419  TYR B CA  1 
ATOM   5542  C  C   . TYR B  1 332 ? 9.314   -22.755 83.670  1.00 12.34  ? 419  TYR B C   1 
ATOM   5543  O  O   . TYR B  1 332 ? 9.082   -23.967 83.639  1.00 13.11  ? 419  TYR B O   1 
ATOM   5544  C  CB  . TYR B  1 332 ? 7.686   -21.909 81.928  1.00 11.67  ? 419  TYR B CB  1 
ATOM   5545  C  CG  . TYR B  1 332 ? 6.396   -21.147 81.664  1.00 9.61   ? 419  TYR B CG  1 
ATOM   5546  C  CD1 . TYR B  1 332 ? 5.167   -21.674 82.042  1.00 9.47   ? 419  TYR B CD1 1 
ATOM   5547  C  CD2 . TYR B  1 332 ? 6.418   -19.864 81.074  1.00 8.67   ? 419  TYR B CD2 1 
ATOM   5548  C  CE1 . TYR B  1 332 ? 3.968   -20.957 81.836  1.00 9.67   ? 419  TYR B CE1 1 
ATOM   5549  C  CE2 . TYR B  1 332 ? 5.232   -19.146 80.842  1.00 8.05   ? 419  TYR B CE2 1 
ATOM   5550  C  CZ  . TYR B  1 332 ? 4.014   -19.703 81.242  1.00 10.58  ? 419  TYR B CZ  1 
ATOM   5551  O  OH  . TYR B  1 332 ? 2.845   -19.018 81.055  1.00 9.53   ? 419  TYR B OH  1 
ATOM   5552  N  N   . TRP B  1 333 ? 10.503  -22.241 83.971  1.00 12.48  ? 420  TRP B N   1 
ATOM   5553  C  CA  . TRP B  1 333 ? 11.698  -23.071 84.178  1.00 13.77  ? 420  TRP B CA  1 
ATOM   5554  C  C   . TRP B  1 333 ? 12.140  -23.121 85.632  1.00 14.34  ? 420  TRP B C   1 
ATOM   5555  O  O   . TRP B  1 333 ? 13.237  -23.624 85.946  1.00 14.26  ? 420  TRP B O   1 
ATOM   5556  C  CB  . TRP B  1 333 ? 12.845  -22.626 83.250  1.00 13.93  ? 420  TRP B CB  1 
ATOM   5557  C  CG  . TRP B  1 333 ? 12.452  -22.791 81.812  1.00 14.12  ? 420  TRP B CG  1 
ATOM   5558  C  CD1 . TRP B  1 333 ? 12.617  -23.914 81.022  1.00 14.53  ? 420  TRP B CD1 1 
ATOM   5559  C  CD2 . TRP B  1 333 ? 11.731  -21.841 81.013  1.00 14.12  ? 420  TRP B CD2 1 
ATOM   5560  N  NE1 . TRP B  1 333 ? 12.066  -23.691 79.771  1.00 14.57  ? 420  TRP B NE1 1 
ATOM   5561  C  CE2 . TRP B  1 333 ? 11.524  -22.430 79.739  1.00 14.88  ? 420  TRP B CE2 1 
ATOM   5562  C  CE3 . TRP B  1 333 ? 11.255  -20.541 81.245  1.00 14.26  ? 420  TRP B CE3 1 
ATOM   5563  C  CZ2 . TRP B  1 333 ? 10.861  -21.761 78.704  1.00 14.41  ? 420  TRP B CZ2 1 
ATOM   5564  C  CZ3 . TRP B  1 333 ? 10.591  -19.872 80.213  1.00 13.85  ? 420  TRP B CZ3 1 
ATOM   5565  C  CH2 . TRP B  1 333 ? 10.403  -20.487 78.960  1.00 13.73  ? 420  TRP B CH2 1 
ATOM   5566  N  N   . ALA B  1 334 ? 11.280  -22.624 86.518  1.00 14.60  ? 421  ALA B N   1 
ATOM   5567  C  CA  . ALA B  1 334 ? 11.523  -22.678 87.964  1.00 15.92  ? 421  ALA B CA  1 
ATOM   5568  C  C   . ALA B  1 334 ? 11.571  -24.134 88.436  1.00 16.57  ? 421  ALA B C   1 
ATOM   5569  O  O   . ALA B  1 334 ? 10.957  -25.011 87.821  1.00 16.58  ? 421  ALA B O   1 
ATOM   5570  C  CB  . ALA B  1 334 ? 10.433  -21.916 88.720  1.00 15.63  ? 421  ALA B CB  1 
ATOM   5571  N  N   . ASN B  1 335 ? 12.303  -24.369 89.530  1.00 17.93  ? 422  ASN B N   1 
ATOM   5572  C  CA  . ASN B  1 335 ? 12.408  -25.687 90.155  1.00 19.15  ? 422  ASN B CA  1 
ATOM   5573  C  C   . ASN B  1 335 ? 11.285  -25.810 91.181  1.00 19.47  ? 422  ASN B C   1 
ATOM   5574  O  O   . ASN B  1 335 ? 11.521  -25.801 92.389  1.00 19.43  ? 422  ASN B O   1 
ATOM   5575  C  CB  . ASN B  1 335 ? 13.801  -25.841 90.792  1.00 19.66  ? 422  ASN B CB  1 
ATOM   5576  C  CG  . ASN B  1 335 ? 14.031  -27.203 91.450  1.00 22.89  ? 422  ASN B CG  1 
ATOM   5577  O  OD1 . ASN B  1 335 ? 14.888  -27.319 92.347  1.00 26.61  ? 422  ASN B OD1 1 
ATOM   5578  N  ND2 . ASN B  1 335 ? 13.305  -28.235 91.010  1.00 23.27  ? 422  ASN B ND2 1 
ATOM   5579  N  N   . LYS B  1 336 ? 10.059  -25.909 90.674  1.00 19.95  ? 423  LYS B N   1 
ATOM   5580  C  CA  . LYS B  1 336 ? 8.848   -25.975 91.496  1.00 21.05  ? 423  LYS B CA  1 
ATOM   5581  C  C   . LYS B  1 336 ? 7.880   -26.906 90.792  1.00 20.13  ? 423  LYS B C   1 
ATOM   5582  O  O   . LYS B  1 336 ? 7.961   -27.062 89.582  1.00 20.30  ? 423  LYS B O   1 
ATOM   5583  C  CB  . LYS B  1 336 ? 8.214   -24.580 91.654  1.00 21.07  ? 423  LYS B CB  1 
ATOM   5584  C  CG  . LYS B  1 336 ? 8.985   -23.615 92.556  1.00 23.78  ? 423  LYS B CG  1 
ATOM   5585  C  CD  . LYS B  1 336 ? 8.228   -22.292 92.773  1.00 23.25  ? 423  LYS B CD  1 
ATOM   5586  C  CE  . LYS B  1 336 ? 9.125   -21.235 93.478  1.00 25.08  ? 423  LYS B CE  1 
ATOM   5587  N  NZ  . LYS B  1 336 ? 8.596   -19.799 93.509  1.00 26.30  ? 423  LYS B NZ  1 
ATOM   5588  N  N   . GLU B  1 337 ? 6.945   -27.489 91.544  1.00 20.27  ? 424  GLU B N   1 
ATOM   5589  C  CA  . GLU B  1 337 ? 5.977   -28.446 90.995  1.00 19.91  ? 424  GLU B CA  1 
ATOM   5590  C  C   . GLU B  1 337 ? 4.790   -27.776 90.295  1.00 18.21  ? 424  GLU B C   1 
ATOM   5591  O  O   . GLU B  1 337 ? 4.001   -28.428 89.618  1.00 17.83  ? 424  GLU B O   1 
ATOM   5592  C  CB  . GLU B  1 337 ? 5.447   -29.372 92.094  1.00 21.17  ? 424  GLU B CB  1 
ATOM   5593  C  CG  . GLU B  1 337 ? 6.522   -30.139 92.844  1.00 26.05  ? 424  GLU B CG  1 
ATOM   5594  C  CD  . GLU B  1 337 ? 6.063   -31.519 93.278  1.00 31.85  ? 424  GLU B CD  1 
ATOM   5595  O  OE1 . GLU B  1 337 ? 4.864   -31.695 93.615  1.00 33.99  ? 424  GLU B OE1 1 
ATOM   5596  O  OE2 . GLU B  1 337 ? 6.911   -32.441 93.273  1.00 35.73  ? 424  GLU B OE2 1 
ATOM   5597  N  N   . CYS B  1 338 ? 4.662   -26.472 90.474  1.00 16.49  ? 425  CYS B N   1 
ATOM   5598  C  CA  . CYS B  1 338 ? 3.557   -25.731 89.865  1.00 15.27  ? 425  CYS B CA  1 
ATOM   5599  C  C   . CYS B  1 338 ? 4.138   -24.484 89.190  1.00 14.14  ? 425  CYS B C   1 
ATOM   5600  O  O   . CYS B  1 338 ? 5.236   -24.058 89.544  1.00 13.07  ? 425  CYS B O   1 
ATOM   5601  C  CB  . CYS B  1 338 ? 2.535   -25.342 90.936  1.00 15.50  ? 425  CYS B CB  1 
ATOM   5602  S  SG  . CYS B  1 338 ? 3.247   -24.464 92.385  1.00 16.44  ? 425  CYS B SG  1 
ATOM   5603  N  N   . PHE B  1 339 ? 3.393   -23.916 88.235  1.00 13.49  ? 426  PHE B N   1 
ATOM   5604  C  CA  . PHE B  1 339 ? 3.767   -22.652 87.589  1.00 12.56  ? 426  PHE B CA  1 
ATOM   5605  C  C   . PHE B  1 339 ? 3.259   -21.499 88.452  1.00 12.54  ? 426  PHE B C   1 
ATOM   5606  O  O   . PHE B  1 339 ? 2.042   -21.412 88.720  1.00 12.92  ? 426  PHE B O   1 
ATOM   5607  C  CB  . PHE B  1 339 ? 3.151   -22.523 86.178  1.00 12.10  ? 426  PHE B CB  1 
ATOM   5608  C  CG  . PHE B  1 339 ? 3.651   -23.541 85.161  1.00 12.98  ? 426  PHE B CG  1 
ATOM   5609  C  CD1 . PHE B  1 339 ? 4.977   -23.959 85.145  1.00 13.80  ? 426  PHE B CD1 1 
ATOM   5610  C  CD2 . PHE B  1 339 ? 2.786   -24.024 84.171  1.00 14.83  ? 426  PHE B CD2 1 
ATOM   5611  C  CE1 . PHE B  1 339 ? 5.435   -24.886 84.192  1.00 14.15  ? 426  PHE B CE1 1 
ATOM   5612  C  CE2 . PHE B  1 339 ? 3.226   -24.953 83.202  1.00 14.93  ? 426  PHE B CE2 1 
ATOM   5613  C  CZ  . PHE B  1 339 ? 4.565   -25.383 83.216  1.00 14.24  ? 426  PHE B CZ  1 
ATOM   5614  N  N   . ASN B  1 340 ? 4.167   -20.607 88.855  1.00 11.51  ? 427  ASN B N   1 
ATOM   5615  C  CA  . ASN B  1 340 ? 3.810   -19.502 89.748  1.00 11.06  ? 427  ASN B CA  1 
ATOM   5616  C  C   . ASN B  1 340 ? 3.485   -18.219 88.961  1.00 10.59  ? 427  ASN B C   1 
ATOM   5617  O  O   . ASN B  1 340 ? 4.344   -17.700 88.252  1.00 10.48  ? 427  ASN B O   1 
ATOM   5618  C  CB  . ASN B  1 340 ? 4.923   -19.281 90.788  1.00 10.81  ? 427  ASN B CB  1 
ATOM   5619  C  CG  . ASN B  1 340 ? 4.486   -18.418 91.964  1.00 10.48  ? 427  ASN B CG  1 
ATOM   5620  O  OD1 . ASN B  1 340 ? 5.297   -17.640 92.488  1.00 13.95  ? 427  ASN B OD1 1 
ATOM   5621  N  ND2 . ASN B  1 340 ? 3.237   -18.559 92.408  1.00 8.44   ? 427  ASN B ND2 1 
ATOM   5622  N  N   . PRO B  1 341 ? 2.227   -17.734 89.051  1.00 10.31  ? 428  PRO B N   1 
ATOM   5623  C  CA  . PRO B  1 341 ? 1.886   -16.456 88.413  1.00 9.99   ? 428  PRO B CA  1 
ATOM   5624  C  C   . PRO B  1 341 ? 2.862   -15.326 88.769  1.00 10.09  ? 428  PRO B C   1 
ATOM   5625  O  O   . PRO B  1 341 ? 3.218   -15.179 89.935  1.00 10.79  ? 428  PRO B O   1 
ATOM   5626  C  CB  . PRO B  1 341 ? 0.497   -16.142 89.008  1.00 9.99   ? 428  PRO B CB  1 
ATOM   5627  C  CG  . PRO B  1 341 ? -0.127  -17.534 89.202  1.00 10.82  ? 428  PRO B CG  1 
ATOM   5628  C  CD  . PRO B  1 341 ? 1.048   -18.359 89.699  1.00 10.16  ? 428  PRO B CD  1 
ATOM   5629  N  N   . CYS B  1 342 ? 3.271   -14.536 87.772  1.00 9.63   ? 429  CYS B N   1 
ATOM   5630  C  CA  . CYS B  1 342 ? 3.924   -13.243 87.998  1.00 8.87   ? 429  CYS B CA  1 
ATOM   5631  C  C   . CYS B  1 342 ? 3.229   -12.198 87.144  1.00 8.97   ? 429  CYS B C   1 
ATOM   5632  O  O   . CYS B  1 342 ? 2.515   -12.534 86.190  1.00 9.35   ? 429  CYS B O   1 
ATOM   5633  C  CB  . CYS B  1 342 ? 5.412   -13.270 87.615  1.00 8.04   ? 429  CYS B CB  1 
ATOM   5634  S  SG  . CYS B  1 342 ? 6.398   -14.536 88.485  1.00 10.78  ? 429  CYS B SG  1 
ATOM   5635  N  N   . PHE B  1 343 ? 3.475   -10.933 87.464  1.00 8.39   ? 430  PHE B N   1 
ATOM   5636  C  CA  . PHE B  1 343 ? 2.948   -9.831  86.685  1.00 8.48   ? 430  PHE B CA  1 
ATOM   5637  C  C   . PHE B  1 343 ? 3.841   -8.607  86.845  1.00 8.66   ? 430  PHE B C   1 
ATOM   5638  O  O   . PHE B  1 343 ? 4.643   -8.524  87.788  1.00 8.98   ? 430  PHE B O   1 
ATOM   5639  C  CB  . PHE B  1 343 ? 1.489   -9.534  87.079  1.00 8.58   ? 430  PHE B CB  1 
ATOM   5640  C  CG  . PHE B  1 343 ? 1.336   -8.798  88.391  1.00 8.93   ? 430  PHE B CG  1 
ATOM   5641  C  CD1 . PHE B  1 343 ? 1.254   -7.395  88.423  1.00 7.34   ? 430  PHE B CD1 1 
ATOM   5642  C  CD2 . PHE B  1 343 ? 1.289   -9.511  89.593  1.00 10.15  ? 430  PHE B CD2 1 
ATOM   5643  C  CE1 . PHE B  1 343 ? 1.094   -6.722  89.633  1.00 7.99   ? 430  PHE B CE1 1 
ATOM   5644  C  CE2 . PHE B  1 343 ? 1.135   -8.854  90.802  1.00 8.67   ? 430  PHE B CE2 1 
ATOM   5645  C  CZ  . PHE B  1 343 ? 1.051   -7.444  90.838  1.00 7.57   ? 430  PHE B CZ  1 
ATOM   5646  N  N   . TYR B  1 344 ? 3.713   -7.667  85.918  1.00 7.79   ? 431  TYR B N   1 
ATOM   5647  C  CA  . TYR B  1 344 ? 4.415   -6.394  86.026  1.00 7.95   ? 431  TYR B CA  1 
ATOM   5648  C  C   . TYR B  1 344 ? 3.391   -5.281  85.895  1.00 8.13   ? 431  TYR B C   1 
ATOM   5649  O  O   . TYR B  1 344 ? 2.294   -5.481  85.345  1.00 8.76   ? 431  TYR B O   1 
ATOM   5650  C  CB  . TYR B  1 344 ? 5.472   -6.258  84.904  1.00 7.72   ? 431  TYR B CB  1 
ATOM   5651  C  CG  . TYR B  1 344 ? 4.805   -6.170  83.555  1.00 7.67   ? 431  TYR B CG  1 
ATOM   5652  C  CD1 . TYR B  1 344 ? 4.553   -7.329  82.806  1.00 7.60   ? 431  TYR B CD1 1 
ATOM   5653  C  CD2 . TYR B  1 344 ? 4.373   -4.933  83.048  1.00 7.67   ? 431  TYR B CD2 1 
ATOM   5654  C  CE1 . TYR B  1 344 ? 3.884   -7.253  81.576  1.00 7.89   ? 431  TYR B CE1 1 
ATOM   5655  C  CE2 . TYR B  1 344 ? 3.696   -4.843  81.842  1.00 5.98   ? 431  TYR B CE2 1 
ATOM   5656  C  CZ  . TYR B  1 344 ? 3.465   -5.989  81.102  1.00 7.39   ? 431  TYR B CZ  1 
ATOM   5657  O  OH  . TYR B  1 344 ? 2.803   -5.892  79.890  1.00 8.37   ? 431  TYR B OH  1 
ATOM   5658  N  N   . VAL B  1 345 ? 3.747   -4.114  86.408  1.00 8.36   ? 432  VAL B N   1 
ATOM   5659  C  CA  . VAL B  1 345 ? 2.980   -2.904  86.184  1.00 8.43   ? 432  VAL B CA  1 
ATOM   5660  C  C   . VAL B  1 345 ? 3.958   -1.893  85.594  1.00 8.81   ? 432  VAL B C   1 
ATOM   5661  O  O   . VAL B  1 345 ? 5.077   -1.726  86.104  1.00 8.83   ? 432  VAL B O   1 
ATOM   5662  C  CB  . VAL B  1 345 ? 2.386   -2.328  87.494  1.00 8.77   ? 432  VAL B CB  1 
ATOM   5663  C  CG1 . VAL B  1 345 ? 1.541   -1.058  87.188  1.00 7.95   ? 432  VAL B CG1 1 
ATOM   5664  C  CG2 . VAL B  1 345 ? 1.571   -3.403  88.227  1.00 8.45   ? 432  VAL B CG2 1 
ATOM   5665  N  N   . GLU B  1 346 ? 3.534   -1.256  84.506  1.00 8.10   ? 433  GLU B N   1 
ATOM   5666  C  CA  . GLU B  1 346 ? 4.258   -0.173  83.868  1.00 8.40   ? 433  GLU B CA  1 
ATOM   5667  C  C   . GLU B  1 346 ? 3.906   1.104   84.610  1.00 7.97   ? 433  GLU B C   1 
ATOM   5668  O  O   . GLU B  1 346 ? 2.729   1.411   84.791  1.00 8.69   ? 433  GLU B O   1 
ATOM   5669  C  CB  . GLU B  1 346 ? 3.834   -0.048  82.389  1.00 8.01   ? 433  GLU B CB  1 
ATOM   5670  C  CG  . GLU B  1 346 ? 4.357   1.214   81.665  1.00 8.80   ? 433  GLU B CG  1 
ATOM   5671  C  CD  . GLU B  1 346 ? 3.689   1.461   80.309  1.00 9.18   ? 433  GLU B CD  1 
ATOM   5672  O  OE1 . GLU B  1 346 ? 4.386   1.925   79.364  1.00 8.55   ? 433  GLU B OE1 1 
ATOM   5673  O  OE2 . GLU B  1 346 ? 2.462   1.226   80.200  1.00 9.97   ? 433  GLU B OE2 1 
ATOM   5674  N  N   . LEU B  1 347 ? 4.923   1.847   85.028  1.00 6.82   ? 434  LEU B N   1 
ATOM   5675  C  CA  . LEU B  1 347 ? 4.692   3.034   85.835  1.00 7.39   ? 434  LEU B CA  1 
ATOM   5676  C  C   . LEU B  1 347 ? 4.991   4.225   84.942  1.00 6.93   ? 434  LEU B C   1 
ATOM   5677  O  O   . LEU B  1 347 ? 6.143   4.622   84.799  1.00 6.13   ? 434  LEU B O   1 
ATOM   5678  C  CB  . LEU B  1 347 ? 5.573   2.980   87.108  1.00 7.13   ? 434  LEU B CB  1 
ATOM   5679  C  CG  . LEU B  1 347 ? 5.444   1.694   87.953  1.00 7.78   ? 434  LEU B CG  1 
ATOM   5680  C  CD1 . LEU B  1 347 ? 6.542   1.602   89.002  1.00 8.32   ? 434  LEU B CD1 1 
ATOM   5681  C  CD2 . LEU B  1 347 ? 4.063   1.564   88.604  1.00 8.58   ? 434  LEU B CD2 1 
ATOM   5682  N  N   . ILE B  1 348 ? 3.951   4.755   84.282  1.00 7.37   ? 435  ILE B N   1 
ATOM   5683  C  CA  . ILE B  1 348 ? 4.137   5.822   83.279  1.00 7.90   ? 435  ILE B CA  1 
ATOM   5684  C  C   . ILE B  1 348 ? 4.374   7.187   83.939  1.00 8.64   ? 435  ILE B C   1 
ATOM   5685  O  O   . ILE B  1 348 ? 3.618   7.587   84.823  1.00 9.37   ? 435  ILE B O   1 
ATOM   5686  C  CB  . ILE B  1 348 ? 2.929   5.940   82.295  1.00 7.90   ? 435  ILE B CB  1 
ATOM   5687  C  CG1 . ILE B  1 348 ? 2.691   4.613   81.568  1.00 7.75   ? 435  ILE B CG1 1 
ATOM   5688  C  CG2 . ILE B  1 348 ? 3.161   7.143   81.297  1.00 7.25   ? 435  ILE B CG2 1 
ATOM   5689  C  CD1 . ILE B  1 348 ? 1.305   4.529   80.809  1.00 8.17   ? 435  ILE B CD1 1 
ATOM   5690  N  N   . ARG B  1 349 ? 5.417   7.884   83.480  1.00 8.41   ? 436  ARG B N   1 
ATOM   5691  C  CA  . ARG B  1 349 ? 5.749   9.217   83.927  1.00 8.91   ? 436  ARG B CA  1 
ATOM   5692  C  C   . ARG B  1 349 ? 5.774   10.171  82.733  1.00 9.23   ? 436  ARG B C   1 
ATOM   5693  O  O   . ARG B  1 349 ? 6.052   9.765   81.610  1.00 9.12   ? 436  ARG B O   1 
ATOM   5694  C  CB  . ARG B  1 349 ? 7.094   9.225   84.662  1.00 8.14   ? 436  ARG B CB  1 
ATOM   5695  C  CG  . ARG B  1 349 ? 7.136   8.355   85.919  1.00 7.74   ? 436  ARG B CG  1 
ATOM   5696  C  CD  . ARG B  1 349 ? 6.000   8.692   86.923  1.00 6.85   ? 436  ARG B CD  1 
ATOM   5697  N  NE  . ARG B  1 349 ? 6.013   10.086  87.400  1.00 9.45   ? 436  ARG B NE  1 
ATOM   5698  C  CZ  . ARG B  1 349 ? 6.673   10.525  88.468  1.00 11.17  ? 436  ARG B CZ  1 
ATOM   5699  N  NH1 . ARG B  1 349 ? 7.452   9.707   89.178  1.00 9.62   ? 436  ARG B NH1 1 
ATOM   5700  N  NH2 . ARG B  1 349 ? 6.562   11.800  88.819  1.00 12.02  ? 436  ARG B NH2 1 
ATOM   5701  N  N   . GLY B  1 350 ? 5.476   11.445  82.974  1.00 8.91   ? 437  GLY B N   1 
ATOM   5702  C  CA  . GLY B  1 350 ? 5.478   12.391  81.883  1.00 9.44   ? 437  GLY B CA  1 
ATOM   5703  C  C   . GLY B  1 350 ? 4.097   12.495  81.253  1.00 9.45   ? 437  GLY B C   1 
ATOM   5704  O  O   . GLY B  1 350 ? 3.083   12.312  81.922  1.00 9.39   ? 437  GLY B O   1 
ATOM   5705  N  N   . ARG B  1 351 ? 4.060   12.829  79.968  1.00 10.60  ? 438  ARG B N   1 
ATOM   5706  C  CA  . ARG B  1 351 ? 2.798   13.167  79.292  1.00 11.33  ? 438  ARG B CA  1 
ATOM   5707  C  C   . ARG B  1 351 ? 1.872   11.968  79.075  1.00 12.12  ? 438  ARG B C   1 
ATOM   5708  O  O   . ARG B  1 351 ? 2.349   10.846  78.913  1.00 11.25  ? 438  ARG B O   1 
ATOM   5709  C  CB  . ARG B  1 351 ? 3.102   13.850  77.960  1.00 11.85  ? 438  ARG B CB  1 
ATOM   5710  C  CG  . ARG B  1 351 ? 3.884   15.106  78.145  1.00 14.39  ? 438  ARG B CG  1 
ATOM   5711  C  CD  . ARG B  1 351 ? 4.068   15.825  76.844  1.00 20.13  ? 438  ARG B CD  1 
ATOM   5712  N  NE  . ARG B  1 351 ? 4.459   17.196  77.106  1.00 25.47  ? 438  ARG B NE  1 
ATOM   5713  C  CZ  . ARG B  1 351 ? 3.623   18.229  77.148  1.00 27.66  ? 438  ARG B CZ  1 
ATOM   5714  N  NH1 . ARG B  1 351 ? 2.321   18.059  76.931  1.00 31.56  ? 438  ARG B NH1 1 
ATOM   5715  N  NH2 . ARG B  1 351 ? 4.094   19.440  77.402  1.00 26.01  ? 438  ARG B NH2 1 
ATOM   5716  N  N   . PRO B  1 352 ? 0.534   12.207  79.042  1.00 12.26  ? 439  PRO B N   1 
ATOM   5717  C  CA  . PRO B  1 352 ? -0.116  13.525  79.156  1.00 12.45  ? 439  PRO B CA  1 
ATOM   5718  C  C   . PRO B  1 352 ? -0.463  13.950  80.585  1.00 12.81  ? 439  PRO B C   1 
ATOM   5719  O  O   . PRO B  1 352 ? -0.848  15.108  80.805  1.00 12.91  ? 439  PRO B O   1 
ATOM   5720  C  CB  . PRO B  1 352 ? -1.414  13.329  78.372  1.00 12.01  ? 439  PRO B CB  1 
ATOM   5721  C  CG  . PRO B  1 352 ? -1.777  11.878  78.608  1.00 12.66  ? 439  PRO B CG  1 
ATOM   5722  C  CD  . PRO B  1 352 ? -0.442  11.121  78.811  1.00 12.91  ? 439  PRO B CD  1 
ATOM   5723  N  N   . LYS B  1 353 ? -0.345  13.033  81.543  1.00 12.31  ? 440  LYS B N   1 
ATOM   5724  C  CA  . LYS B  1 353 ? -0.765  13.330  82.922  1.00 13.14  ? 440  LYS B CA  1 
ATOM   5725  C  C   . LYS B  1 353 ? 0.140   14.334  83.616  1.00 12.96  ? 440  LYS B C   1 
ATOM   5726  O  O   . LYS B  1 353 ? -0.339  15.121  84.438  1.00 13.36  ? 440  LYS B O   1 
ATOM   5727  C  CB  . LYS B  1 353 ? -0.933  12.057  83.764  1.00 13.36  ? 440  LYS B CB  1 
ATOM   5728  C  CG  . LYS B  1 353 ? -2.119  11.154  83.339  1.00 13.70  ? 440  LYS B CG  1 
ATOM   5729  C  CD  . LYS B  1 353 ? -3.473  11.842  83.561  1.00 17.32  ? 440  LYS B CD  1 
ATOM   5730  C  CE  . LYS B  1 353 ? -4.637  10.880  83.319  1.00 16.62  ? 440  LYS B CE  1 
ATOM   5731  N  NZ  . LYS B  1 353 ? -5.062  10.889  81.903  1.00 19.00  ? 440  LYS B NZ  1 
ATOM   5732  N  N   . GLU B  1 354 ? 1.428   14.320  83.276  1.00 12.25  ? 441  GLU B N   1 
ATOM   5733  C  CA  . GLU B  1 354 ? 2.413   15.265  83.835  1.00 12.50  ? 441  GLU B CA  1 
ATOM   5734  C  C   . GLU B  1 354 ? 2.993   16.115  82.705  1.00 13.36  ? 441  GLU B C   1 
ATOM   5735  O  O   . GLU B  1 354 ? 3.976   15.742  82.070  1.00 12.76  ? 441  GLU B O   1 
ATOM   5736  C  CB  . GLU B  1 354 ? 3.515   14.508  84.618  1.00 11.90  ? 441  GLU B CB  1 
ATOM   5737  C  CG  . GLU B  1 354 ? 2.937   13.626  85.735  1.00 11.41  ? 441  GLU B CG  1 
ATOM   5738  C  CD  . GLU B  1 354 ? 3.952   12.691  86.382  1.00 13.36  ? 441  GLU B CD  1 
ATOM   5739  O  OE1 . GLU B  1 354 ? 4.202   12.832  87.596  1.00 12.69  ? 441  GLU B OE1 1 
ATOM   5740  O  OE2 . GLU B  1 354 ? 4.489   11.807  85.682  1.00 12.34  ? 441  GLU B OE2 1 
ATOM   5741  N  N   . SER B  1 355 ? 2.351   17.256  82.430  1.00 14.06  ? 442  SER B N   1 
ATOM   5742  C  CA  . SER B  1 355 ? 2.695   18.044  81.245  1.00 14.69  ? 442  SER B CA  1 
ATOM   5743  C  C   . SER B  1 355 ? 3.770   19.093  81.482  1.00 14.43  ? 442  SER B C   1 
ATOM   5744  O  O   . SER B  1 355 ? 4.080   19.871  80.568  1.00 14.36  ? 442  SER B O   1 
ATOM   5745  C  CB  . SER B  1 355 ? 1.434   18.696  80.665  1.00 15.33  ? 442  SER B CB  1 
ATOM   5746  O  OG  . SER B  1 355 ? 0.875   19.580  81.618  1.00 17.83  ? 442  SER B OG  1 
ATOM   5747  N  N   . SER B  1 356 ? 4.350   19.119  82.688  1.00 14.07  ? 443  SER B N   1 
ATOM   5748  C  CA  . SER B  1 356 ? 5.491   19.999  82.989  1.00 13.66  ? 443  SER B CA  1 
ATOM   5749  C  C   . SER B  1 356 ? 6.822   19.531  82.357  1.00 13.24  ? 443  SER B C   1 
ATOM   5750  O  O   . SER B  1 356 ? 7.841   20.228  82.456  1.00 13.44  ? 443  SER B O   1 
ATOM   5751  C  CB  . SER B  1 356 ? 5.666   20.179  84.499  1.00 13.19  ? 443  SER B CB  1 
ATOM   5752  O  OG  . SER B  1 356 ? 6.180   19.003  85.127  1.00 15.78  ? 443  SER B OG  1 
ATOM   5753  N  N   . VAL B  1 357 ? 6.799   18.350  81.733  1.00 13.03  ? 444  VAL B N   1 
ATOM   5754  C  CA  . VAL B  1 357 ? 7.912   17.811  80.957  1.00 11.99  ? 444  VAL B CA  1 
ATOM   5755  C  C   . VAL B  1 357 ? 7.447   17.519  79.532  1.00 12.20  ? 444  VAL B C   1 
ATOM   5756  O  O   . VAL B  1 357 ? 6.232   17.398  79.272  1.00 12.52  ? 444  VAL B O   1 
ATOM   5757  C  CB  . VAL B  1 357 ? 8.522   16.513  81.594  1.00 12.54  ? 444  VAL B CB  1 
ATOM   5758  C  CG1 . VAL B  1 357 ? 9.094   16.831  82.969  1.00 11.60  ? 444  VAL B CG1 1 
ATOM   5759  C  CG2 . VAL B  1 357 ? 7.477   15.354  81.652  1.00 11.14  ? 444  VAL B CG2 1 
ATOM   5760  N  N   . LEU B  1 358 ? 8.407   17.386  78.611  1.00 11.34  ? 445  LEU B N   1 
ATOM   5761  C  CA  . LEU B  1 358 ? 8.096   17.233  77.186  1.00 10.92  ? 445  LEU B CA  1 
ATOM   5762  C  C   . LEU B  1 358 ? 8.041   15.774  76.729  1.00 11.21  ? 445  LEU B C   1 
ATOM   5763  O  O   . LEU B  1 358 ? 7.759   15.500  75.548  1.00 10.83  ? 445  LEU B O   1 
ATOM   5764  C  CB  . LEU B  1 358 ? 9.126   17.993  76.341  1.00 11.15  ? 445  LEU B CB  1 
ATOM   5765  C  CG  . LEU B  1 358 ? 9.086   19.530  76.492  1.00 12.24  ? 445  LEU B CG  1 
ATOM   5766  C  CD1 . LEU B  1 358 ? 10.367  20.164  75.898  1.00 11.34  ? 445  LEU B CD1 1 
ATOM   5767  C  CD2 . LEU B  1 358 ? 7.816   20.098  75.844  1.00 12.75  ? 445  LEU B CD2 1 
ATOM   5768  N  N   . TRP B  1 359 ? 8.324   14.860  77.661  1.00 10.29  ? 446  TRP B N   1 
ATOM   5769  C  CA  . TRP B  1 359 ? 8.521   13.446  77.328  1.00 9.87   ? 446  TRP B CA  1 
ATOM   5770  C  C   . TRP B  1 359 ? 7.476   12.556  77.987  1.00 9.63   ? 446  TRP B C   1 
ATOM   5771  O  O   . TRP B  1 359 ? 6.714   13.005  78.851  1.00 10.04  ? 446  TRP B O   1 
ATOM   5772  C  CB  . TRP B  1 359 ? 9.946   12.982  77.727  1.00 10.44  ? 446  TRP B CB  1 
ATOM   5773  C  CG  . TRP B  1 359 ? 10.349  13.327  79.166  1.00 10.23  ? 446  TRP B CG  1 
ATOM   5774  C  CD1 . TRP B  1 359 ? 11.121  14.387  79.562  1.00 11.14  ? 446  TRP B CD1 1 
ATOM   5775  C  CD2 . TRP B  1 359 ? 10.020  12.601  80.376  1.00 11.09  ? 446  TRP B CD2 1 
ATOM   5776  N  NE1 . TRP B  1 359 ? 11.283  14.381  80.934  1.00 11.01  ? 446  TRP B NE1 1 
ATOM   5777  C  CE2 . TRP B  1 359 ? 10.621  13.299  81.458  1.00 11.51  ? 446  TRP B CE2 1 
ATOM   5778  C  CE3 . TRP B  1 359 ? 9.277   11.427  80.650  1.00 10.35  ? 446  TRP B CE3 1 
ATOM   5779  C  CZ2 . TRP B  1 359 ? 10.510  12.869  82.795  1.00 9.91   ? 446  TRP B CZ2 1 
ATOM   5780  C  CZ3 . TRP B  1 359 ? 9.159   11.004  81.984  1.00 10.89  ? 446  TRP B CZ3 1 
ATOM   5781  C  CH2 . TRP B  1 359 ? 9.771   11.720  83.036  1.00 10.91  ? 446  TRP B CH2 1 
ATOM   5782  N  N   . THR B  1 360 ? 7.432   11.307  77.530  1.00 8.61   ? 447  THR B N   1 
ATOM   5783  C  CA  . THR B  1 360 ? 6.666   10.239  78.138  1.00 8.32   ? 447  THR B CA  1 
ATOM   5784  C  C   . THR B  1 360 ? 7.587   9.036   78.201  1.00 8.21   ? 447  THR B C   1 
ATOM   5785  O  O   . THR B  1 360 ? 8.223   8.666   77.207  1.00 7.45   ? 447  THR B O   1 
ATOM   5786  C  CB  . THR B  1 360 ? 5.423   9.851   77.285  1.00 8.62   ? 447  THR B CB  1 
ATOM   5787  O  OG1 . THR B  1 360 ? 4.528   10.977  77.180  1.00 8.44   ? 447  THR B OG1 1 
ATOM   5788  C  CG2 . THR B  1 360 ? 4.666   8.664   77.924  1.00 7.89   ? 447  THR B CG2 1 
ATOM   5789  N  N   . SER B  1 361 ? 7.672   8.427   79.377  1.00 8.36   ? 448  SER B N   1 
ATOM   5790  C  CA  . SER B  1 361 ? 8.440   7.188   79.556  1.00 8.29   ? 448  SER B CA  1 
ATOM   5791  C  C   . SER B  1 361 ? 7.823   6.399   80.731  1.00 8.38   ? 448  SER B C   1 
ATOM   5792  O  O   . SER B  1 361 ? 6.712   6.711   81.169  1.00 8.57   ? 448  SER B O   1 
ATOM   5793  C  CB  . SER B  1 361 ? 9.935   7.512   79.810  1.00 8.70   ? 448  SER B CB  1 
ATOM   5794  O  OG  . SER B  1 361 ? 10.720  6.321   79.674  1.00 9.18   ? 448  SER B OG  1 
ATOM   5795  N  N   . ASN B  1 362 ? 8.530   5.391   81.231  1.00 7.35   ? 449  ASN B N   1 
ATOM   5796  C  CA  . ASN B  1 362 ? 8.051   4.572   82.353  1.00 7.60   ? 449  ASN B CA  1 
ATOM   5797  C  C   . ASN B  1 362 ? 9.198   3.910   83.103  1.00 7.25   ? 449  ASN B C   1 
ATOM   5798  O  O   . ASN B  1 362 ? 10.337  3.881   82.614  1.00 7.23   ? 449  ASN B O   1 
ATOM   5799  C  CB  . ASN B  1 362 ? 7.135   3.451   81.849  1.00 7.11   ? 449  ASN B CB  1 
ATOM   5800  C  CG  . ASN B  1 362 ? 7.914   2.353   81.101  1.00 7.18   ? 449  ASN B CG  1 
ATOM   5801  O  OD1 . ASN B  1 362 ? 8.183   1.254   81.642  1.00 10.98  ? 449  ASN B OD1 1 
ATOM   5802  N  ND2 . ASN B  1 362 ? 8.275   2.644   79.868  1.00 5.36   ? 449  ASN B ND2 1 
ATOM   5803  N  N   . SER B  1 363 ? 8.890   3.379   84.292  1.00 7.43   ? 450  SER B N   1 
ATOM   5804  C  CA  . SER B  1 363 ? 9.736   2.371   84.904  1.00 7.58   ? 450  SER B CA  1 
ATOM   5805  C  C   . SER B  1 363 ? 8.885   1.117   85.075  1.00 8.28   ? 450  SER B C   1 
ATOM   5806  O  O   . SER B  1 363 ? 7.703   1.087   84.664  1.00 7.42   ? 450  SER B O   1 
ATOM   5807  C  CB  . SER B  1 363 ? 10.325  2.854   86.243  1.00 7.98   ? 450  SER B CB  1 
ATOM   5808  O  OG  . SER B  1 363 ? 9.302   3.018   87.223  1.00 7.70   ? 450  SER B OG  1 
ATOM   5809  N  N   . ILE B  1 364 ? 9.467   0.098   85.697  1.00 8.06   ? 451  ILE B N   1 
ATOM   5810  C  CA  . ILE B  1 364 ? 8.811   -1.209  85.830  1.00 8.81   ? 451  ILE B CA  1 
ATOM   5811  C  C   . ILE B  1 364 ? 8.844   -1.702  87.285  1.00 9.07   ? 451  ILE B C   1 
ATOM   5812  O  O   . ILE B  1 364 ? 9.852   -1.546  87.970  1.00 9.34   ? 451  ILE B O   1 
ATOM   5813  C  CB  . ILE B  1 364 ? 9.509   -2.286  84.938  1.00 9.26   ? 451  ILE B CB  1 
ATOM   5814  C  CG1 . ILE B  1 364 ? 9.553   -1.880  83.446  1.00 8.30   ? 451  ILE B CG1 1 
ATOM   5815  C  CG2 . ILE B  1 364 ? 8.880   -3.691  85.141  1.00 9.51   ? 451  ILE B CG2 1 
ATOM   5816  C  CD1 . ILE B  1 364 ? 10.482  -2.799  82.623  1.00 7.55   ? 451  ILE B CD1 1 
ATOM   5817  N  N   . VAL B  1 365 ? 7.734   -2.295  87.744  1.00 8.76   ? 452  VAL B N   1 
ATOM   5818  C  CA  . VAL B  1 365 ? 7.757   -3.173  88.918  1.00 8.65   ? 452  VAL B CA  1 
ATOM   5819  C  C   . VAL B  1 365 ? 7.142   -4.531  88.533  1.00 8.33   ? 452  VAL B C   1 
ATOM   5820  O  O   . VAL B  1 365 ? 6.223   -4.598  87.694  1.00 7.73   ? 452  VAL B O   1 
ATOM   5821  C  CB  . VAL B  1 365 ? 7.007   -2.537  90.131  1.00 8.40   ? 452  VAL B CB  1 
ATOM   5822  C  CG1 . VAL B  1 365 ? 5.507   -2.321  89.799  1.00 9.07   ? 452  VAL B CG1 1 
ATOM   5823  C  CG2 . VAL B  1 365 ? 7.193   -3.391  91.409  1.00 8.87   ? 452  VAL B CG2 1 
ATOM   5824  N  N   . ALA B  1 366 ? 7.667   -5.603  89.130  1.00 8.32   ? 453  ALA B N   1 
ATOM   5825  C  CA  . ALA B  1 366 ? 7.181   -6.956  88.914  1.00 8.44   ? 453  ALA B CA  1 
ATOM   5826  C  C   . ALA B  1 366 ? 7.073   -7.719  90.246  1.00 8.35   ? 453  ALA B C   1 
ATOM   5827  O  O   . ALA B  1 366 ? 7.917   -7.568  91.148  1.00 8.60   ? 453  ALA B O   1 
ATOM   5828  C  CB  . ALA B  1 366 ? 8.097   -7.702  87.942  1.00 7.65   ? 453  ALA B CB  1 
ATOM   5829  N  N   . LEU B  1 367 ? 6.033   -8.543  90.345  1.00 9.24   ? 454  LEU B N   1 
ATOM   5830  C  CA  . LEU B  1 367 ? 5.727   -9.326  91.552  1.00 9.15   ? 454  LEU B CA  1 
ATOM   5831  C  C   . LEU B  1 367 ? 5.313   -10.745 91.145  1.00 9.46   ? 454  LEU B C   1 
ATOM   5832  O  O   . LEU B  1 367 ? 4.855   -10.958 90.018  1.00 9.95   ? 454  LEU B O   1 
ATOM   5833  C  CB  . LEU B  1 367 ? 4.604   -8.643  92.366  1.00 9.08   ? 454  LEU B CB  1 
ATOM   5834  C  CG  . LEU B  1 367 ? 4.880   -7.249  92.956  1.00 9.45   ? 454  LEU B CG  1 
ATOM   5835  C  CD1 . LEU B  1 367 ? 4.420   -6.086  92.053  1.00 8.52   ? 454  LEU B CD1 1 
ATOM   5836  C  CD2 . LEU B  1 367 ? 4.250   -7.123  94.352  1.00 10.81  ? 454  LEU B CD2 1 
ATOM   5837  N  N   . CYS B  1 368 ? 5.490   -11.717 92.041  1.00 9.36   ? 455  CYS B N   1 
ATOM   5838  C  CA  . CYS B  1 368 ? 5.003   -13.077 91.795  1.00 9.27   ? 455  CYS B CA  1 
ATOM   5839  C  C   . CYS B  1 368 ? 4.182   -13.555 92.999  1.00 9.02   ? 455  CYS B C   1 
ATOM   5840  O  O   . CYS B  1 368 ? 4.259   -12.968 94.071  1.00 8.60   ? 455  CYS B O   1 
ATOM   5841  C  CB  . CYS B  1 368 ? 6.165   -14.032 91.513  1.00 9.57   ? 455  CYS B CB  1 
ATOM   5842  S  SG  . CYS B  1 368 ? 7.201   -13.551 90.092  1.00 10.90  ? 455  CYS B SG  1 
ATOM   5843  N  N   . GLY B  1 369 ? 3.420   -14.623 92.813  1.00 8.69   ? 456  GLY B N   1 
ATOM   5844  C  CA  . GLY B  1 369 ? 2.566   -15.147 93.884  1.00 9.27   ? 456  GLY B CA  1 
ATOM   5845  C  C   . GLY B  1 369 ? 3.329   -15.730 95.067  1.00 10.03  ? 456  GLY B C   1 
ATOM   5846  O  O   . GLY B  1 369 ? 4.447   -16.272 94.932  1.00 8.92   ? 456  GLY B O   1 
ATOM   5847  N  N   . SER B  1 370 ? 2.717   -15.619 96.237  1.00 10.76  ? 457  SER B N   1 
ATOM   5848  C  CA  . SER B  1 370 ? 3.182   -16.331 97.420  1.00 12.17  ? 457  SER B CA  1 
ATOM   5849  C  C   . SER B  1 370 ? 1.997   -17.069 98.017  1.00 13.12  ? 457  SER B C   1 
ATOM   5850  O  O   . SER B  1 370 ? 0.878   -16.553 98.002  1.00 12.48  ? 457  SER B O   1 
ATOM   5851  C  CB  . SER B  1 370 ? 3.759   -15.360 98.456  1.00 12.16  ? 457  SER B CB  1 
ATOM   5852  O  OG  . SER B  1 370 ? 4.066   -16.044 99.663  1.00 13.41  ? 457  SER B OG  1 
ATOM   5853  N  N   . LYS B  1 371 ? 2.250   -18.268 98.538  1.00 14.10  ? 458  LYS B N   1 
ATOM   5854  C  CA  . LYS B  1 371 ? 1.243   -19.024 99.296  1.00 16.30  ? 458  LYS B CA  1 
ATOM   5855  C  C   . LYS B  1 371 ? 1.073   -18.435 100.705 1.00 16.11  ? 458  LYS B C   1 
ATOM   5856  O  O   . LYS B  1 371 ? 0.045   -18.655 101.360 1.00 16.57  ? 458  LYS B O   1 
ATOM   5857  C  CB  . LYS B  1 371 ? 1.632   -20.518 99.332  1.00 15.53  ? 458  LYS B CB  1 
ATOM   5858  C  CG  . LYS B  1 371 ? 0.487   -21.515 99.393  1.00 19.26  ? 458  LYS B CG  1 
ATOM   5859  C  CD  . LYS B  1 371 ? 1.067   -22.940 99.237  1.00 20.20  ? 458  LYS B CD  1 
ATOM   5860  C  CE  . LYS B  1 371 ? 0.019   -24.037 99.458  1.00 27.13  ? 458  LYS B CE  1 
ATOM   5861  N  NZ  . LYS B  1 371 ? -0.542  -24.581 98.149  1.00 31.56  ? 458  LYS B NZ  1 
ATOM   5862  N  N   . LYS B  1 372 ? 2.061   -17.664 101.152 1.00 16.49  ? 459  LYS B N   1 
ATOM   5863  C  CA  . LYS B  1 372 ? 2.025   -16.977 102.449 1.00 16.74  ? 459  LYS B CA  1 
ATOM   5864  C  C   . LYS B  1 372 ? 1.124   -15.750 102.407 1.00 16.91  ? 459  LYS B C   1 
ATOM   5865  O  O   . LYS B  1 372 ? 0.736   -15.286 101.327 1.00 17.04  ? 459  LYS B O   1 
ATOM   5866  C  CB  . LYS B  1 372 ? 3.431   -16.530 102.879 1.00 16.67  ? 459  LYS B CB  1 
ATOM   5867  C  CG  . LYS B  1 372 ? 4.527   -17.590 102.783 1.00 18.89  ? 459  LYS B CG  1 
ATOM   5868  C  CD  . LYS B  1 372 ? 4.435   -18.602 103.901 1.00 19.85  ? 459  LYS B CD  1 
ATOM   5869  C  CE  . LYS B  1 372 ? 5.346   -19.801 103.652 1.00 21.84  ? 459  LYS B CE  1 
ATOM   5870  N  NZ  . LYS B  1 372 ? 6.769   -19.489 103.951 1.00 21.65  ? 459  LYS B NZ  1 
ATOM   5871  N  N   . ARG B  1 373 ? 0.812   -15.223 103.591 1.00 17.07  ? 460  ARG B N   1 
ATOM   5872  C  CA  . ARG B  1 373 ? 0.110   -13.947 103.711 1.00 17.56  ? 460  ARG B CA  1 
ATOM   5873  C  C   . ARG B  1 373 ? 1.111   -12.828 104.015 1.00 16.55  ? 460  ARG B C   1 
ATOM   5874  O  O   . ARG B  1 373 ? 1.397   -12.506 105.183 1.00 16.39  ? 460  ARG B O   1 
ATOM   5875  C  CB  . ARG B  1 373 ? -0.977  -14.033 104.797 1.00 18.69  ? 460  ARG B CB  1 
ATOM   5876  C  CG  . ARG B  1 373 ? -2.375  -14.174 104.253 1.00 23.51  ? 460  ARG B CG  1 
ATOM   5877  C  CD  . ARG B  1 373 ? -2.690  -15.584 103.823 1.00 29.11  ? 460  ARG B CD  1 
ATOM   5878  N  NE  . ARG B  1 373 ? -4.059  -15.664 103.309 1.00 34.97  ? 460  ARG B NE  1 
ATOM   5879  C  CZ  . ARG B  1 373 ? -4.721  -16.796 103.073 1.00 36.42  ? 460  ARG B CZ  1 
ATOM   5880  N  NH1 . ARG B  1 373 ? -5.962  -16.738 102.597 1.00 38.64  ? 460  ARG B NH1 1 
ATOM   5881  N  NH2 . ARG B  1 373 ? -4.160  -17.981 103.313 1.00 36.26  ? 460  ARG B NH2 1 
ATOM   5882  N  N   . LEU B  1 374 ? 1.671   -12.248 102.959 1.00 15.13  ? 461  LEU B N   1 
ATOM   5883  C  CA  . LEU B  1 374 ? 2.742   -11.263 103.121 1.00 14.30  ? 461  LEU B CA  1 
ATOM   5884  C  C   . LEU B  1 374 ? 2.180   -9.855  103.253 1.00 14.69  ? 461  LEU B C   1 
ATOM   5885  O  O   . LEU B  1 374 ? 1.160   -9.536  102.648 1.00 14.88  ? 461  LEU B O   1 
ATOM   5886  C  CB  . LEU B  1 374 ? 3.685   -11.310 101.909 1.00 13.70  ? 461  LEU B CB  1 
ATOM   5887  C  CG  . LEU B  1 374 ? 4.350   -12.646 101.576 1.00 13.25  ? 461  LEU B CG  1 
ATOM   5888  C  CD1 . LEU B  1 374 ? 5.154   -12.448 100.308 1.00 13.24  ? 461  LEU B CD1 1 
ATOM   5889  C  CD2 . LEU B  1 374 ? 5.253   -13.128 102.726 1.00 11.46  ? 461  LEU B CD2 1 
ATOM   5890  N  N   . GLY B  1 375 ? 2.865   -9.019  104.032 1.00 14.56  ? 462  GLY B N   1 
ATOM   5891  C  CA  . GLY B  1 375 ? 2.578   -7.587  104.109 1.00 13.85  ? 462  GLY B CA  1 
ATOM   5892  C  C   . GLY B  1 375 ? 2.850   -6.882  102.790 1.00 13.99  ? 462  GLY B C   1 
ATOM   5893  O  O   . GLY B  1 375 ? 3.561   -7.398  101.914 1.00 13.16  ? 462  GLY B O   1 
ATOM   5894  N  N   . SER B  1 376 ? 2.289   -5.697  102.624 1.00 13.88  ? 463  SER B N   1 
ATOM   5895  C  CA  . SER B  1 376 ? 2.465   -5.018  101.331 1.00 14.27  ? 463  SER B CA  1 
ATOM   5896  C  C   . SER B  1 376 ? 2.822   -3.546  101.463 1.00 13.37  ? 463  SER B C   1 
ATOM   5897  O  O   . SER B  1 376 ? 2.550   -2.914  102.487 1.00 13.31  ? 463  SER B O   1 
ATOM   5898  C  CB  . SER B  1 376 ? 1.211   -5.212  100.470 1.00 14.29  ? 463  SER B CB  1 
ATOM   5899  O  OG  . SER B  1 376 ? 0.177   -4.373  100.936 1.00 16.66  ? 463  SER B OG  1 
ATOM   5900  N  N   . TRP B  1 377 ? 3.422   -3.035  100.387 1.00 12.70  ? 464  TRP B N   1 
ATOM   5901  C  CA  . TRP B  1 377 ? 3.885   -1.689  100.204 1.00 13.26  ? 464  TRP B CA  1 
ATOM   5902  C  C   . TRP B  1 377 ? 3.519   -1.226  98.808  1.00 12.13  ? 464  TRP B C   1 
ATOM   5903  O  O   . TRP B  1 377 ? 3.456   -2.051  97.901  1.00 11.69  ? 464  TRP B O   1 
ATOM   5904  C  CB  . TRP B  1 377 ? 5.421   -1.736  100.177 1.00 14.22  ? 464  TRP B CB  1 
ATOM   5905  C  CG  . TRP B  1 377 ? 6.017   -0.760  100.995 1.00 15.09  ? 464  TRP B CG  1 
ATOM   5906  C  CD1 . TRP B  1 377 ? 5.384   0.062   101.860 1.00 17.12  ? 464  TRP B CD1 1 
ATOM   5907  C  CD2 . TRP B  1 377 ? 7.414   -0.494  101.111 1.00 14.78  ? 464  TRP B CD2 1 
ATOM   5908  N  NE1 . TRP B  1 377 ? 6.315   0.860   102.507 1.00 18.01  ? 464  TRP B NE1 1 
ATOM   5909  C  CE2 . TRP B  1 377 ? 7.567   0.529   102.067 1.00 14.79  ? 464  TRP B CE2 1 
ATOM   5910  C  CE3 . TRP B  1 377 ? 8.552   -1.022  100.489 1.00 14.13  ? 464  TRP B CE3 1 
ATOM   5911  C  CZ2 . TRP B  1 377 ? 8.830   1.043   102.441 1.00 14.56  ? 464  TRP B CZ2 1 
ATOM   5912  C  CZ3 . TRP B  1 377 ? 9.812   -0.522  100.862 1.00 14.19  ? 464  TRP B CZ3 1 
ATOM   5913  C  CH2 . TRP B  1 377 ? 9.935   0.506   101.821 1.00 14.21  ? 464  TRP B CH2 1 
ATOM   5914  N  N   . SER B  1 378 ? 3.343   0.086   98.633  1.00 10.90  ? 465  SER B N   1 
ATOM   5915  C  CA  . SER B  1 378 ? 3.238   0.699   97.297  1.00 10.14  ? 465  SER B CA  1 
ATOM   5916  C  C   . SER B  1 378 ? 4.616   0.762   96.614  1.00 9.81   ? 465  SER B C   1 
ATOM   5917  O  O   . SER B  1 378 ? 5.588   1.236   97.209  1.00 9.03   ? 465  SER B O   1 
ATOM   5918  C  CB  . SER B  1 378 ? 2.662   2.122   97.372  1.00 10.66  ? 465  SER B CB  1 
ATOM   5919  O  OG  . SER B  1 378 ? 2.571   2.690   96.075  1.00 9.87   ? 465  SER B OG  1 
ATOM   5920  N  N   . TRP B  1 379 ? 4.660   0.275   95.373  1.00 9.09   ? 466  TRP B N   1 
ATOM   5921  C  CA  . TRP B  1 379 ? 5.887   0.180   94.578  1.00 9.32   ? 466  TRP B CA  1 
ATOM   5922  C  C   . TRP B  1 379 ? 5.797   1.155   93.416  1.00 9.49   ? 466  TRP B C   1 
ATOM   5923  O  O   . TRP B  1 379 ? 5.966   0.775   92.243  1.00 8.89   ? 466  TRP B O   1 
ATOM   5924  C  CB  . TRP B  1 379 ? 6.073   -1.250  94.042  1.00 9.22   ? 466  TRP B CB  1 
ATOM   5925  C  CG  . TRP B  1 379 ? 6.284   -2.294  95.127  1.00 9.41   ? 466  TRP B CG  1 
ATOM   5926  C  CD1 . TRP B  1 379 ? 5.354   -3.191  95.621  1.00 9.67   ? 466  TRP B CD1 1 
ATOM   5927  C  CD2 . TRP B  1 379 ? 7.499   -2.541  95.834  1.00 7.63   ? 466  TRP B CD2 1 
ATOM   5928  N  NE1 . TRP B  1 379 ? 5.938   -3.978  96.603  1.00 8.35   ? 466  TRP B NE1 1 
ATOM   5929  C  CE2 . TRP B  1 379 ? 7.254   -3.604  96.741  1.00 8.90   ? 466  TRP B CE2 1 
ATOM   5930  C  CE3 . TRP B  1 379 ? 8.795   -1.976  95.773  1.00 8.25   ? 466  TRP B CE3 1 
ATOM   5931  C  CZ2 . TRP B  1 379 ? 8.242   -4.094  97.602  1.00 9.62   ? 466  TRP B CZ2 1 
ATOM   5932  C  CZ3 . TRP B  1 379 ? 9.772   -2.469  96.618  1.00 8.41   ? 466  TRP B CZ3 1 
ATOM   5933  C  CH2 . TRP B  1 379 ? 9.497   -3.531  97.512  1.00 9.22   ? 466  TRP B CH2 1 
ATOM   5934  N  N   . HIS B  1 380 ? 5.493   2.408   93.749  1.00 8.74   ? 467  HIS B N   1 
ATOM   5935  C  CA  . HIS B  1 380 ? 5.407   3.488   92.758  1.00 10.00  ? 467  HIS B CA  1 
ATOM   5936  C  C   . HIS B  1 380 ? 6.774   3.838   92.153  1.00 10.64  ? 467  HIS B C   1 
ATOM   5937  O  O   . HIS B  1 380 ? 7.836   3.407   92.660  1.00 8.69   ? 467  HIS B O   1 
ATOM   5938  C  CB  . HIS B  1 380 ? 4.700   4.717   93.356  1.00 9.65   ? 467  HIS B CB  1 
ATOM   5939  C  CG  . HIS B  1 380 ? 5.149   5.059   94.752  1.00 10.41  ? 467  HIS B CG  1 
ATOM   5940  N  ND1 . HIS B  1 380 ? 6.063   6.062   95.018  1.00 13.00  ? 467  HIS B ND1 1 
ATOM   5941  C  CD2 . HIS B  1 380 ? 4.824   4.522   95.951  1.00 9.99   ? 467  HIS B CD2 1 
ATOM   5942  C  CE1 . HIS B  1 380 ? 6.277   6.130   96.324  1.00 9.32   ? 467  HIS B CE1 1 
ATOM   5943  N  NE2 . HIS B  1 380 ? 5.544   5.201   96.911  1.00 13.71  ? 467  HIS B NE2 1 
ATOM   5944  N  N   . ASP B  1 381 ? 6.732   4.595   91.057  1.00 11.23  ? 468  ASP B N   1 
ATOM   5945  C  CA  . ASP B  1 381 ? 7.943   5.059   90.390  1.00 13.46  ? 468  ASP B CA  1 
ATOM   5946  C  C   . ASP B  1 381 ? 8.499   6.125   91.311  1.00 14.88  ? 468  ASP B C   1 
ATOM   5947  O  O   . ASP B  1 381 ? 7.860   7.131   91.550  1.00 19.79  ? 468  ASP B O   1 
ATOM   5948  C  CB  . ASP B  1 381 ? 7.617   5.761   89.084  1.00 12.20  ? 468  ASP B CB  1 
ATOM   5949  C  CG  . ASP B  1 381 ? 8.853   6.322   88.413  1.00 10.96  ? 468  ASP B CG  1 
ATOM   5950  O  OD1 . ASP B  1 381 ? 9.544   5.502   87.769  1.00 8.81   ? 468  ASP B OD1 1 
ATOM   5951  O  OD2 . ASP B  1 381 ? 9.127   7.553   88.511  1.00 7.51   ? 468  ASP B OD2 1 
ATOM   5952  N  N   . GLY B  1 382 ? 9.667   5.980   91.845  1.00 16.48  ? 469  GLY B N   1 
ATOM   5953  C  CA  . GLY B  1 382 ? 9.937   6.999   92.873  1.00 14.11  ? 469  GLY B CA  1 
ATOM   5954  C  C   . GLY B  1 382 ? 10.526  8.339   92.457  1.00 13.00  ? 469  GLY B C   1 
ATOM   5955  O  O   . GLY B  1 382 ? 11.224  8.968   93.264  1.00 12.19  ? 469  GLY B O   1 
ATOM   5956  N  N   . ALA B  1 383 ? 10.302  8.770   91.214  1.00 11.70  ? 470  ALA B N   1 
ATOM   5957  C  CA  . ALA B  1 383 ? 10.955  9.992   90.730  1.00 11.20  ? 470  ALA B CA  1 
ATOM   5958  C  C   . ALA B  1 383 ? 10.170  11.252  91.056  1.00 11.58  ? 470  ALA B C   1 
ATOM   5959  O  O   . ALA B  1 383 ? 8.929   11.215  91.178  1.00 10.63  ? 470  ALA B O   1 
ATOM   5960  C  CB  . ALA B  1 383 ? 11.267  9.931   89.231  1.00 11.80  ? 470  ALA B CB  1 
ATOM   5961  N  N   . GLU B  1 384 ? 10.922  12.341  91.227  1.00 11.25  ? 471  GLU B N   1 
ATOM   5962  C  CA  . GLU B  1 384 ? 10.373  13.666  91.490  1.00 12.64  ? 471  GLU B CA  1 
ATOM   5963  C  C   . GLU B  1 384 ? 10.329  14.426  90.190  1.00 11.62  ? 471  GLU B C   1 
ATOM   5964  O  O   . GLU B  1 384 ? 11.377  14.792  89.651  1.00 11.94  ? 471  GLU B O   1 
ATOM   5965  C  CB  . GLU B  1 384 ? 11.231  14.441  92.511  1.00 13.29  ? 471  GLU B CB  1 
ATOM   5966  C  CG  . GLU B  1 384 ? 11.196  13.886  93.908  1.00 17.81  ? 471  GLU B CG  1 
ATOM   5967  C  CD  . GLU B  1 384 ? 9.789   13.962  94.507  1.00 25.01  ? 471  GLU B CD  1 
ATOM   5968  O  OE1 . GLU B  1 384 ? 9.346   12.930  95.058  1.00 26.50  ? 471  GLU B OE1 1 
ATOM   5969  O  OE2 . GLU B  1 384 ? 9.130   15.042  94.392  1.00 24.73  ? 471  GLU B OE2 1 
ATOM   5970  N  N   . ILE B  1 385 ? 9.117   14.665  89.690  1.00 11.38  ? 472  ILE B N   1 
ATOM   5971  C  CA  . ILE B  1 385 ? 8.952   15.338  88.403  1.00 11.60  ? 472  ILE B CA  1 
ATOM   5972  C  C   . ILE B  1 385 ? 9.613   16.731  88.423  1.00 11.74  ? 472  ILE B C   1 
ATOM   5973  O  O   . ILE B  1 385 ? 10.133  17.165  87.403  1.00 12.09  ? 472  ILE B O   1 
ATOM   5974  C  CB  . ILE B  1 385 ? 7.459   15.398  87.943  1.00 11.80  ? 472  ILE B CB  1 
ATOM   5975  C  CG1 . ILE B  1 385 ? 7.342   15.565  86.416  1.00 12.85  ? 472  ILE B CG1 1 
ATOM   5976  C  CG2 . ILE B  1 385 ? 6.687   16.516  88.685  1.00 11.28  ? 472  ILE B CG2 1 
ATOM   5977  C  CD1 . ILE B  1 385 ? 7.555   14.278  85.611  1.00 15.19  ? 472  ILE B CD1 1 
ATOM   5978  N  N   . ILE B  1 386 ? 9.633   17.402  89.584  1.00 12.29  ? 473  ILE B N   1 
ATOM   5979  C  CA  . ILE B  1 386 ? 10.222  18.765  89.668  1.00 13.44  ? 473  ILE B CA  1 
ATOM   5980  C  C   . ILE B  1 386 ? 11.701  18.763  89.265  1.00 12.55  ? 473  ILE B C   1 
ATOM   5981  O  O   . ILE B  1 386 ? 12.210  19.744  88.720  1.00 12.29  ? 473  ILE B O   1 
ATOM   5982  C  CB  . ILE B  1 386 ? 10.038  19.429  91.081  1.00 13.54  ? 473  ILE B CB  1 
ATOM   5983  C  CG1 . ILE B  1 386 ? 10.559  20.872  91.064  1.00 14.95  ? 473  ILE B CG1 1 
ATOM   5984  C  CG2 . ILE B  1 386 ? 10.760  18.649  92.148  1.00 14.84  ? 473  ILE B CG2 1 
ATOM   5985  C  CD1 . ILE B  1 386 ? 10.355  21.652  92.341  1.00 16.66  ? 473  ILE B CD1 1 
ATOM   5986  N  N   . TYR B  1 387 ? 12.387  17.649  89.529  1.00 12.64  ? 474  TYR B N   1 
ATOM   5987  C  CA  . TYR B  1 387 ? 13.803  17.520  89.158  1.00 12.54  ? 474  TYR B CA  1 
ATOM   5988  C  C   . TYR B  1 387 ? 14.029  17.607  87.644  1.00 12.49  ? 474  TYR B C   1 
ATOM   5989  O  O   . TYR B  1 387 ? 15.116  17.985  87.193  1.00 12.92  ? 474  TYR B O   1 
ATOM   5990  C  CB  . TYR B  1 387 ? 14.367  16.194  89.690  1.00 12.49  ? 474  TYR B CB  1 
ATOM   5991  C  CG  . TYR B  1 387 ? 14.553  16.147  91.196  1.00 13.14  ? 474  TYR B CG  1 
ATOM   5992  C  CD1 . TYR B  1 387 ? 14.640  14.918  91.861  1.00 13.66  ? 474  TYR B CD1 1 
ATOM   5993  C  CD2 . TYR B  1 387 ? 14.665  17.325  91.956  1.00 14.13  ? 474  TYR B CD2 1 
ATOM   5994  C  CE1 . TYR B  1 387 ? 14.821  14.856  93.254  1.00 12.78  ? 474  TYR B CE1 1 
ATOM   5995  C  CE2 . TYR B  1 387 ? 14.836  17.273  93.361  1.00 13.42  ? 474  TYR B CE2 1 
ATOM   5996  C  CZ  . TYR B  1 387 ? 14.921  16.039  93.991  1.00 12.99  ? 474  TYR B CZ  1 
ATOM   5997  O  OH  . TYR B  1 387 ? 15.097  15.959  95.344  1.00 13.10  ? 474  TYR B OH  1 
ATOM   5998  N  N   . PHE B  1 388 ? 13.006  17.233  86.879  1.00 12.01  ? 475  PHE B N   1 
ATOM   5999  C  CA  . PHE B  1 388 ? 13.024  17.257  85.413  1.00 12.16  ? 475  PHE B CA  1 
ATOM   6000  C  C   . PHE B  1 388 ? 12.529  18.592  84.817  1.00 13.11  ? 475  PHE B C   1 
ATOM   6001  O  O   . PHE B  1 388 ? 12.545  18.787  83.589  1.00 12.94  ? 475  PHE B O   1 
ATOM   6002  C  CB  . PHE B  1 388 ? 12.186  16.104  84.860  1.00 11.38  ? 475  PHE B CB  1 
ATOM   6003  C  CG  . PHE B  1 388 ? 12.789  14.734  85.083  1.00 11.96  ? 475  PHE B CG  1 
ATOM   6004  C  CD1 . PHE B  1 388 ? 13.672  14.187  84.144  1.00 10.82  ? 475  PHE B CD1 1 
ATOM   6005  C  CD2 . PHE B  1 388 ? 12.466  13.988  86.220  1.00 11.19  ? 475  PHE B CD2 1 
ATOM   6006  C  CE1 . PHE B  1 388 ? 14.226  12.919  84.324  1.00 9.47   ? 475  PHE B CE1 1 
ATOM   6007  C  CE2 . PHE B  1 388 ? 13.023  12.698  86.418  1.00 12.12  ? 475  PHE B CE2 1 
ATOM   6008  C  CZ  . PHE B  1 388 ? 13.882  12.175  85.465  1.00 10.87  ? 475  PHE B CZ  1 
ATOM   6009  N  N   . GLU B  1 389 ? 12.102  19.507  85.680  1.00 13.98  ? 476  GLU B N   1 
ATOM   6010  C  CA  . GLU B  1 389 ? 11.639  20.836  85.228  1.00 15.81  ? 476  GLU B CA  1 
ATOM   6011  C  C   . GLU B  1 389 ? 12.769  21.848  85.089  1.00 16.61  ? 476  GLU B C   1 
ATOM   6012  O  O   . GLU B  1 389 ? 13.942  21.568  85.369  1.00 17.45  ? 476  GLU B O   1 
ATOM   6013  C  CB  . GLU B  1 389 ? 10.516  21.349  86.131  1.00 14.83  ? 476  GLU B CB  1 
ATOM   6014  C  CG  . GLU B  1 389 ? 9.273   20.444  86.069  1.00 16.57  ? 476  GLU B CG  1 
ATOM   6015  C  CD  . GLU B  1 389 ? 8.203   20.805  87.082  1.00 16.80  ? 476  GLU B CD  1 
ATOM   6016  O  OE1 . GLU B  1 389 ? 8.308   21.862  87.737  1.00 18.89  ? 476  GLU B OE1 1 
ATOM   6017  O  OE2 . GLU B  1 389 ? 7.248   20.023  87.228  1.00 18.08  ? 476  GLU B OE2 1 
ATOM   6018  O  OXT . GLU B  1 389 ? 12.532  22.979  84.659  1.00 17.85  ? 476  GLU B OXT 1 
ATOM   6019  N  N   . ARG C  1 1   ? 44.758  -26.328 77.447  1.00 28.65  ? 88   ARG C N   1 
ATOM   6020  C  CA  . ARG C  1 1   ? 45.700  -25.385 78.140  1.00 28.09  ? 88   ARG C CA  1 
ATOM   6021  C  C   . ARG C  1 1   ? 46.893  -26.056 78.816  1.00 26.90  ? 88   ARG C C   1 
ATOM   6022  O  O   . ARG C  1 1   ? 46.747  -26.998 79.599  1.00 27.64  ? 88   ARG C O   1 
ATOM   6023  C  CB  . ARG C  1 1   ? 44.963  -24.476 79.133  1.00 28.81  ? 88   ARG C CB  1 
ATOM   6024  C  CG  . ARG C  1 1   ? 44.233  -23.312 78.451  1.00 31.00  ? 88   ARG C CG  1 
ATOM   6025  C  CD  . ARG C  1 1   ? 44.195  -22.048 79.317  1.00 35.31  ? 88   ARG C CD  1 
ATOM   6026  N  NE  . ARG C  1 1   ? 43.502  -20.963 78.622  1.00 38.15  ? 88   ARG C NE  1 
ATOM   6027  C  CZ  . ARG C  1 1   ? 43.353  -19.725 79.090  1.00 39.79  ? 88   ARG C CZ  1 
ATOM   6028  N  NH1 . ARG C  1 1   ? 43.844  -19.375 80.273  1.00 39.99  ? 88   ARG C NH1 1 
ATOM   6029  N  NH2 . ARG C  1 1   ? 42.701  -18.828 78.365  1.00 41.01  ? 88   ARG C NH2 1 
ATOM   6030  N  N   . THR C  1 2   ? 48.081  -25.557 78.500  1.00 25.15  ? 89   THR C N   1 
ATOM   6031  C  CA  . THR C  1 2   ? 49.325  -26.030 79.098  1.00 23.24  ? 89   THR C CA  1 
ATOM   6032  C  C   . THR C  1 2   ? 50.181  -24.803 79.403  1.00 20.88  ? 89   THR C C   1 
ATOM   6033  O  O   . THR C  1 2   ? 49.911  -23.705 78.891  1.00 19.31  ? 89   THR C O   1 
ATOM   6034  C  CB  . THR C  1 2   ? 50.136  -26.936 78.136  1.00 23.66  ? 89   THR C CB  1 
ATOM   6035  O  OG1 . THR C  1 2   ? 50.341  -26.246 76.900  1.00 25.40  ? 89   THR C OG1 1 
ATOM   6036  C  CG2 . THR C  1 2   ? 49.418  -28.264 77.859  1.00 25.12  ? 89   THR C CG2 1 
ATOM   6037  N  N   . PHE C  1 3   ? 51.212  -24.996 80.222  1.00 18.38  ? 90   PHE C N   1 
ATOM   6038  C  CA  . PHE C  1 3   ? 52.203  -23.934 80.443  1.00 16.42  ? 90   PHE C CA  1 
ATOM   6039  C  C   . PHE C  1 3   ? 52.886  -23.527 79.140  1.00 15.68  ? 90   PHE C C   1 
ATOM   6040  O  O   . PHE C  1 3   ? 53.238  -24.357 78.311  1.00 15.25  ? 90   PHE C O   1 
ATOM   6041  C  CB  . PHE C  1 3   ? 53.274  -24.354 81.455  1.00 16.46  ? 90   PHE C CB  1 
ATOM   6042  C  CG  . PHE C  1 3   ? 52.797  -24.398 82.890  1.00 15.22  ? 90   PHE C CG  1 
ATOM   6043  C  CD1 . PHE C  1 3   ? 53.112  -25.488 83.697  1.00 16.19  ? 90   PHE C CD1 1 
ATOM   6044  C  CD2 . PHE C  1 3   ? 52.050  -23.353 83.439  1.00 14.12  ? 90   PHE C CD2 1 
ATOM   6045  C  CE1 . PHE C  1 3   ? 52.694  -25.543 85.029  1.00 16.72  ? 90   PHE C CE1 1 
ATOM   6046  C  CE2 . PHE C  1 3   ? 51.611  -23.403 84.774  1.00 13.06  ? 90   PHE C CE2 1 
ATOM   6047  C  CZ  . PHE C  1 3   ? 51.935  -24.491 85.567  1.00 16.67  ? 90   PHE C CZ  1 
ATOM   6048  N  N   . LEU C  1 4   ? 53.064  -22.224 78.966  1.00 14.83  ? 91   LEU C N   1 
ATOM   6049  C  CA  . LEU C  1 4   ? 53.853  -21.699 77.879  1.00 14.14  ? 91   LEU C CA  1 
ATOM   6050  C  C   . LEU C  1 4   ? 55.336  -22.072 78.069  1.00 14.27  ? 91   LEU C C   1 
ATOM   6051  O  O   . LEU C  1 4   ? 55.908  -21.895 79.161  1.00 13.42  ? 91   LEU C O   1 
ATOM   6052  C  CB  . LEU C  1 4   ? 53.714  -20.173 77.836  1.00 14.38  ? 91   LEU C CB  1 
ATOM   6053  C  CG  . LEU C  1 4   ? 54.745  -19.438 76.983  1.00 14.49  ? 91   LEU C CG  1 
ATOM   6054  C  CD1 . LEU C  1 4   ? 54.459  -19.685 75.510  1.00 12.23  ? 91   LEU C CD1 1 
ATOM   6055  C  CD2 . LEU C  1 4   ? 54.772  -17.950 77.310  1.00 13.77  ? 91   LEU C CD2 1 
ATOM   6056  N  N   . ASN C  1 5   ? 55.938  -22.588 76.997  1.00 13.96  ? 92   ASN C N   1 
ATOM   6057  C  CA  . ASN C  1 5   ? 57.386  -22.788 76.933  1.00 14.60  ? 92   ASN C CA  1 
ATOM   6058  C  C   . ASN C  1 5   ? 57.979  -21.867 75.884  1.00 14.23  ? 92   ASN C C   1 
ATOM   6059  O  O   . ASN C  1 5   ? 57.438  -21.764 74.780  1.00 13.51  ? 92   ASN C O   1 
ATOM   6060  C  CB  . ASN C  1 5   ? 57.730  -24.248 76.583  1.00 14.92  ? 92   ASN C CB  1 
ATOM   6061  C  CG  . ASN C  1 5   ? 57.118  -25.249 77.548  1.00 15.99  ? 92   ASN C CG  1 
ATOM   6062  O  OD1 . ASN C  1 5   ? 56.841  -24.944 78.715  1.00 14.43  ? 92   ASN C OD1 1 
ATOM   6063  N  ND2 . ASN C  1 5   ? 56.900  -26.466 77.056  1.00 21.75  ? 92   ASN C ND2 1 
ATOM   6064  N  N   . LEU C  1 6   ? 59.090  -21.224 76.228  1.00 14.66  ? 93   LEU C N   1 
ATOM   6065  C  CA  . LEU C  1 6   ? 59.781  -20.277 75.342  1.00 15.77  ? 93   LEU C CA  1 
ATOM   6066  C  C   . LEU C  1 6   ? 60.644  -21.007 74.296  1.00 16.39  ? 93   LEU C C   1 
ATOM   6067  O  O   . LEU C  1 6   ? 61.864  -20.822 74.217  1.00 17.00  ? 93   LEU C O   1 
ATOM   6068  C  CB  . LEU C  1 6   ? 60.600  -19.273 76.172  1.00 16.09  ? 93   LEU C CB  1 
ATOM   6069  C  CG  . LEU C  1 6   ? 59.812  -18.456 77.218  1.00 15.53  ? 93   LEU C CG  1 
ATOM   6070  C  CD1 . LEU C  1 6   ? 60.730  -17.645 78.171  1.00 15.61  ? 93   LEU C CD1 1 
ATOM   6071  C  CD2 . LEU C  1 6   ? 58.736  -17.551 76.567  1.00 14.21  ? 93   LEU C CD2 1 
ATOM   6072  N  N   . THR C  1 7   ? 59.987  -21.837 73.495  1.00 17.18  ? 94   THR C N   1 
ATOM   6073  C  CA  . THR C  1 7   ? 60.678  -22.732 72.549  1.00 18.20  ? 94   THR C CA  1 
ATOM   6074  C  C   . THR C  1 7   ? 61.021  -22.083 71.203  1.00 17.99  ? 94   THR C C   1 
ATOM   6075  O  O   . THR C  1 7   ? 61.736  -22.675 70.396  1.00 18.05  ? 94   THR C O   1 
ATOM   6076  C  CB  . THR C  1 7   ? 59.850  -24.020 72.259  1.00 18.52  ? 94   THR C CB  1 
ATOM   6077  O  OG1 . THR C  1 7   ? 58.629  -23.675 71.584  1.00 20.65  ? 94   THR C OG1 1 
ATOM   6078  C  CG2 . THR C  1 7   ? 59.540  -24.769 73.531  1.00 19.44  ? 94   THR C CG2 1 
ATOM   6079  N  N   . LYS C  1 8   ? 60.513  -20.877 70.956  1.00 16.52  ? 95   LYS C N   1 
ATOM   6080  C  CA  . LYS C  1 8   ? 60.631  -20.260 69.630  1.00 15.46  ? 95   LYS C CA  1 
ATOM   6081  C  C   . LYS C  1 8   ? 61.668  -19.156 69.603  1.00 14.90  ? 95   LYS C C   1 
ATOM   6082  O  O   . LYS C  1 8   ? 61.878  -18.495 70.620  1.00 14.05  ? 95   LYS C O   1 
ATOM   6083  C  CB  . LYS C  1 8   ? 59.267  -19.748 69.155  1.00 15.17  ? 95   LYS C CB  1 
ATOM   6084  C  CG  . LYS C  1 8   ? 58.257  -20.876 69.042  1.00 15.05  ? 95   LYS C CG  1 
ATOM   6085  C  CD  . LYS C  1 8   ? 56.877  -20.408 68.618  1.00 13.79  ? 95   LYS C CD  1 
ATOM   6086  C  CE  . LYS C  1 8   ? 55.937  -21.611 68.535  1.00 14.85  ? 95   LYS C CE  1 
ATOM   6087  N  NZ  . LYS C  1 8   ? 54.552  -21.214 68.211  1.00 13.53  ? 95   LYS C NZ  1 
ATOM   6088  N  N   . PRO C  1 9   ? 62.315  -18.940 68.432  1.00 14.54  ? 96   PRO C N   1 
ATOM   6089  C  CA  . PRO C  1 9   ? 63.194  -17.778 68.279  1.00 14.15  ? 96   PRO C CA  1 
ATOM   6090  C  C   . PRO C  1 9   ? 62.365  -16.509 68.009  1.00 14.00  ? 96   PRO C C   1 
ATOM   6091  O  O   . PRO C  1 9   ? 61.149  -16.618 67.729  1.00 13.23  ? 96   PRO C O   1 
ATOM   6092  C  CB  . PRO C  1 9   ? 64.010  -18.141 67.026  1.00 14.50  ? 96   PRO C CB  1 
ATOM   6093  C  CG  . PRO C  1 9   ? 63.040  -18.936 66.192  1.00 15.09  ? 96   PRO C CG  1 
ATOM   6094  C  CD  . PRO C  1 9   ? 62.266  -19.762 67.197  1.00 14.65  ? 96   PRO C CD  1 
ATOM   6095  N  N   . LEU C  1 10  ? 62.994  -15.331 68.064  1.00 13.63  ? 97   LEU C N   1 
ATOM   6096  C  CA  . LEU C  1 10  ? 62.296  -14.092 67.659  1.00 13.70  ? 97   LEU C CA  1 
ATOM   6097  C  C   . LEU C  1 10  ? 62.174  -14.048 66.149  1.00 13.87  ? 97   LEU C C   1 
ATOM   6098  O  O   . LEU C  1 10  ? 63.085  -14.495 65.426  1.00 12.46  ? 97   LEU C O   1 
ATOM   6099  C  CB  . LEU C  1 10  ? 63.011  -12.802 68.108  1.00 13.99  ? 97   LEU C CB  1 
ATOM   6100  C  CG  . LEU C  1 10  ? 63.109  -12.327 69.561  1.00 13.53  ? 97   LEU C CG  1 
ATOM   6101  C  CD1 . LEU C  1 10  ? 63.828  -11.015 69.604  1.00 12.27  ? 97   LEU C CD1 1 
ATOM   6102  C  CD2 . LEU C  1 10  ? 61.716  -12.197 70.206  1.00 11.84  ? 97   LEU C CD2 1 
ATOM   6103  N  N   . CYS C  1 11  ? 61.051  -13.507 65.677  1.00 13.30  ? 98   CYS C N   1 
ATOM   6104  C  CA  . CYS C  1 11  ? 60.862  -13.252 64.249  1.00 13.42  ? 98   CYS C CA  1 
ATOM   6105  C  C   . CYS C  1 11  ? 61.809  -12.153 63.759  1.00 13.61  ? 98   CYS C C   1 
ATOM   6106  O  O   . CYS C  1 11  ? 62.149  -11.213 64.492  1.00 12.80  ? 98   CYS C O   1 
ATOM   6107  C  CB  . CYS C  1 11  ? 59.414  -12.807 63.966  1.00 13.83  ? 98   CYS C CB  1 
ATOM   6108  S  SG  . CYS C  1 11  ? 58.112  -13.930 64.541  1.00 13.89  ? 98   CYS C SG  1 
ATOM   6109  N  N   . GLU C  1 12  ? 62.205  -12.267 62.497  1.00 13.26  ? 99   GLU C N   1 
ATOM   6110  C  CA  . GLU C  1 12  ? 62.909  -11.205 61.819  1.00 14.04  ? 99   GLU C CA  1 
ATOM   6111  C  C   . GLU C  1 12  ? 62.026  -9.971  61.766  1.00 13.32  ? 99   GLU C C   1 
ATOM   6112  O  O   . GLU C  1 12  ? 60.848  -10.050 61.395  1.00 13.59  ? 99   GLU C O   1 
ATOM   6113  C  CB  . GLU C  1 12  ? 63.238  -11.662 60.402  1.00 14.52  ? 99   GLU C CB  1 
ATOM   6114  C  CG  . GLU C  1 12  ? 63.876  -10.624 59.533  1.00 16.05  ? 99   GLU C CG  1 
ATOM   6115  C  CD  . GLU C  1 12  ? 64.172  -11.163 58.141  1.00 20.36  ? 99   GLU C CD  1 
ATOM   6116  O  OE1 . GLU C  1 12  ? 64.325  -10.341 57.224  1.00 20.39  ? 99   GLU C OE1 1 
ATOM   6117  O  OE2 . GLU C  1 12  ? 64.259  -12.403 57.975  1.00 20.37  ? 99   GLU C OE2 1 
ATOM   6118  N  N   . VAL C  1 13  ? 62.587  -8.831  62.155  1.00 13.00  ? 100  VAL C N   1 
ATOM   6119  C  CA  . VAL C  1 13  ? 61.867  -7.555  62.097  1.00 12.02  ? 100  VAL C CA  1 
ATOM   6120  C  C   . VAL C  1 13  ? 62.609  -6.504  61.251  1.00 12.14  ? 100  VAL C C   1 
ATOM   6121  O  O   . VAL C  1 13  ? 63.771  -6.137  61.549  1.00 11.55  ? 100  VAL C O   1 
ATOM   6122  C  CB  . VAL C  1 13  ? 61.612  -6.990  63.532  1.00 12.30  ? 100  VAL C CB  1 
ATOM   6123  C  CG1 . VAL C  1 13  ? 60.947  -5.604  63.496  1.00 10.54  ? 100  VAL C CG1 1 
ATOM   6124  C  CG2 . VAL C  1 13  ? 60.775  -7.981  64.355  1.00 11.00  ? 100  VAL C CG2 1 
ATOM   6125  N  N   . ASN C  1 14  ? 61.915  -6.009  60.218  1.00 12.25  ? 101  ASN C N   1 
ATOM   6126  C  CA  . ASN C  1 14  ? 62.422  -4.963  59.315  1.00 11.58  ? 101  ASN C CA  1 
ATOM   6127  C  C   . ASN C  1 14  ? 61.665  -3.633  59.384  1.00 12.05  ? 101  ASN C C   1 
ATOM   6128  O  O   . ASN C  1 14  ? 62.186  -2.585  58.989  1.00 10.05  ? 101  ASN C O   1 
ATOM   6129  C  CB  . ASN C  1 14  ? 62.471  -5.506  57.872  1.00 12.37  ? 101  ASN C CB  1 
ATOM   6130  C  CG  . ASN C  1 14  ? 63.384  -6.731  57.741  1.00 13.35  ? 101  ASN C CG  1 
ATOM   6131  O  OD1 . ASN C  1 14  ? 64.521  -6.709  58.218  1.00 14.62  ? 101  ASN C OD1 1 
ATOM   6132  N  ND2 . ASN C  1 14  ? 62.891  -7.798  57.104  1.00 13.62  ? 101  ASN C ND2 1 
ATOM   6133  N  N   . SER C  1 15  ? 60.455  -3.687  59.944  1.00 11.07  ? 102  SER C N   1 
ATOM   6134  C  CA  . SER C  1 15  ? 59.500  -2.588  59.989  1.00 12.36  ? 102  SER C CA  1 
ATOM   6135  C  C   . SER C  1 15  ? 58.599  -2.850  61.219  1.00 11.07  ? 102  SER C C   1 
ATOM   6136  O  O   . SER C  1 15  ? 58.572  -3.984  61.727  1.00 10.80  ? 102  SER C O   1 
ATOM   6137  C  CB  . SER C  1 15  ? 58.611  -2.671  58.730  1.00 12.10  ? 102  SER C CB  1 
ATOM   6138  O  OG  . SER C  1 15  ? 58.127  -1.410  58.417  1.00 19.57  ? 102  SER C OG  1 
ATOM   6139  N  N   . TRP C  1 16  ? 57.854  -1.830  61.663  1.00 10.81  ? 103  TRP C N   1 
ATOM   6140  C  CA  . TRP C  1 16  ? 56.836  -1.983  62.720  1.00 9.74   ? 103  TRP C CA  1 
ATOM   6141  C  C   . TRP C  1 16  ? 55.432  -1.582  62.202  1.00 9.66   ? 103  TRP C C   1 
ATOM   6142  O  O   . TRP C  1 16  ? 55.252  -0.482  61.671  1.00 9.99   ? 103  TRP C O   1 
ATOM   6143  C  CB  . TRP C  1 16  ? 57.221  -1.165  63.972  1.00 9.13   ? 103  TRP C CB  1 
ATOM   6144  C  CG  . TRP C  1 16  ? 58.587  -1.565  64.504  1.00 9.75   ? 103  TRP C CG  1 
ATOM   6145  C  CD1 . TRP C  1 16  ? 59.814  -1.064  64.108  1.00 10.59  ? 103  TRP C CD1 1 
ATOM   6146  C  CD2 . TRP C  1 16  ? 58.864  -2.590  65.464  1.00 8.91   ? 103  TRP C CD2 1 
ATOM   6147  N  NE1 . TRP C  1 16  ? 60.835  -1.719  64.793  1.00 10.43  ? 103  TRP C NE1 1 
ATOM   6148  C  CE2 . TRP C  1 16  ? 60.272  -2.649  65.633  1.00 9.70   ? 103  TRP C CE2 1 
ATOM   6149  C  CE3 . TRP C  1 16  ? 58.057  -3.448  66.224  1.00 8.64   ? 103  TRP C CE3 1 
ATOM   6150  C  CZ2 . TRP C  1 16  ? 60.888  -3.554  66.525  1.00 9.63   ? 103  TRP C CZ2 1 
ATOM   6151  C  CZ3 . TRP C  1 16  ? 58.658  -4.315  67.127  1.00 10.15  ? 103  TRP C CZ3 1 
ATOM   6152  C  CH2 . TRP C  1 16  ? 60.071  -4.368  67.270  1.00 11.00  ? 103  TRP C CH2 1 
ATOM   6153  N  N   . HIS C  1 17  ? 54.453  -2.469  62.379  1.00 9.30   ? 104  HIS C N   1 
ATOM   6154  C  CA  . HIS C  1 17  ? 53.052  -2.194  61.972  1.00 9.64   ? 104  HIS C CA  1 
ATOM   6155  C  C   . HIS C  1 17  ? 52.208  -1.836  63.200  1.00 9.41   ? 104  HIS C C   1 
ATOM   6156  O  O   . HIS C  1 17  ? 52.507  -2.271  64.322  1.00 9.08   ? 104  HIS C O   1 
ATOM   6157  C  CB  . HIS C  1 17  ? 52.436  -3.397  61.217  1.00 9.77   ? 104  HIS C CB  1 
ATOM   6158  C  CG  . HIS C  1 17  ? 52.006  -4.525  62.109  1.00 11.45  ? 104  HIS C CG  1 
ATOM   6159  N  ND1 . HIS C  1 17  ? 50.790  -4.537  62.763  1.00 11.14  ? 104  HIS C ND1 1 
ATOM   6160  C  CD2 . HIS C  1 17  ? 52.627  -5.674  62.455  1.00 11.57  ? 104  HIS C CD2 1 
ATOM   6161  C  CE1 . HIS C  1 17  ? 50.680  -5.646  63.466  1.00 12.94  ? 104  HIS C CE1 1 
ATOM   6162  N  NE2 . HIS C  1 17  ? 51.786  -6.347  63.310  1.00 14.44  ? 104  HIS C NE2 1 
ATOM   6163  N  N   . ILE C  1 18  ? 51.140  -1.079  62.974  1.00 8.87   ? 105  ILE C N   1 
ATOM   6164  C  CA  . ILE C  1 18  ? 50.241  -0.683  64.059  1.00 8.08   ? 105  ILE C CA  1 
ATOM   6165  C  C   . ILE C  1 18  ? 49.432  -1.909  64.551  1.00 7.95   ? 105  ILE C C   1 
ATOM   6166  O  O   . ILE C  1 18  ? 48.850  -2.635  63.736  1.00 7.16   ? 105  ILE C O   1 
ATOM   6167  C  CB  . ILE C  1 18  ? 49.321  0.501   63.606  1.00 8.12   ? 105  ILE C CB  1 
ATOM   6168  C  CG1 . ILE C  1 18  ? 48.521  1.083   64.782  1.00 7.49   ? 105  ILE C CG1 1 
ATOM   6169  C  CG2 . ILE C  1 18  ? 48.414  0.087   62.463  1.00 6.82   ? 105  ILE C CG2 1 
ATOM   6170  C  CD1 . ILE C  1 18  ? 49.385  1.793   65.810  1.00 8.20   ? 105  ILE C CD1 1 
ATOM   6171  N  N   . LEU C  1 19  ? 49.438  -2.126  65.876  1.00 7.68   ? 106  LEU C N   1 
ATOM   6172  C  CA  . LEU C  1 19  ? 48.637  -3.174  66.564  1.00 8.18   ? 106  LEU C CA  1 
ATOM   6173  C  C   . LEU C  1 19  ? 47.363  -2.591  67.197  1.00 8.25   ? 106  LEU C C   1 
ATOM   6174  O  O   . LEU C  1 19  ? 46.242  -3.082  66.970  1.00 7.71   ? 106  LEU C O   1 
ATOM   6175  C  CB  . LEU C  1 19  ? 49.475  -3.840  67.657  1.00 8.37   ? 106  LEU C CB  1 
ATOM   6176  C  CG  . LEU C  1 19  ? 48.791  -5.031  68.348  1.00 8.23   ? 106  LEU C CG  1 
ATOM   6177  C  CD1 . LEU C  1 19  ? 48.795  -6.246  67.416  1.00 8.05   ? 106  LEU C CD1 1 
ATOM   6178  C  CD2 . LEU C  1 19  ? 49.509  -5.317  69.670  1.00 5.91   ? 106  LEU C CD2 1 
ATOM   6179  N  N   . SER C  1 20  ? 47.545  -1.545  68.002  1.00 7.85   ? 107  SER C N   1 
ATOM   6180  C  CA  . SER C  1 20  ? 46.433  -0.934  68.719  1.00 7.86   ? 107  SER C CA  1 
ATOM   6181  C  C   . SER C  1 20  ? 46.738  0.505   69.160  1.00 8.24   ? 107  SER C C   1 
ATOM   6182  O  O   . SER C  1 20  ? 47.909  0.904   69.278  1.00 8.39   ? 107  SER C O   1 
ATOM   6183  C  CB  . SER C  1 20  ? 46.061  -1.782  69.936  1.00 7.72   ? 107  SER C CB  1 
ATOM   6184  O  OG  . SER C  1 20  ? 44.806  -1.374  70.423  1.00 8.51   ? 107  SER C OG  1 
ATOM   6185  N  N   . LYS C  1 21  ? 45.670  1.259   69.403  1.00 6.99   ? 108  LYS C N   1 
ATOM   6186  C  CA  . LYS C  1 21  ? 45.729  2.646   69.882  1.00 8.12   ? 108  LYS C CA  1 
ATOM   6187  C  C   . LYS C  1 21  ? 44.373  2.899   70.515  1.00 8.86   ? 108  LYS C C   1 
ATOM   6188  O  O   . LYS C  1 21  ? 43.354  2.590   69.900  1.00 9.43   ? 108  LYS C O   1 
ATOM   6189  C  CB  . LYS C  1 21  ? 45.950  3.628   68.715  1.00 7.47   ? 108  LYS C CB  1 
ATOM   6190  C  CG  . LYS C  1 21  ? 46.439  5.017   69.141  1.00 8.53   ? 108  LYS C CG  1 
ATOM   6191  C  CD  . LYS C  1 21  ? 46.429  6.002   67.947  1.00 8.08   ? 108  LYS C CD  1 
ATOM   6192  C  CE  . LYS C  1 21  ? 47.049  7.352   68.328  1.00 9.19   ? 108  LYS C CE  1 
ATOM   6193  N  NZ  . LYS C  1 21  ? 46.280  8.061   69.383  1.00 8.09   ? 108  LYS C NZ  1 
ATOM   6194  N  N   . ASP C  1 22  ? 44.359  3.442   71.734  1.00 9.03   ? 109  ASP C N   1 
ATOM   6195  C  CA  . ASP C  1 22  ? 43.099  3.593   72.461  1.00 8.75   ? 109  ASP C CA  1 
ATOM   6196  C  C   . ASP C  1 22  ? 42.524  5.013   72.450  1.00 7.94   ? 109  ASP C C   1 
ATOM   6197  O  O   . ASP C  1 22  ? 41.361  5.205   72.792  1.00 8.29   ? 109  ASP C O   1 
ATOM   6198  C  CB  . ASP C  1 22  ? 43.170  2.993   73.878  1.00 8.67   ? 109  ASP C CB  1 
ATOM   6199  C  CG  . ASP C  1 22  ? 44.025  3.809   74.853  1.00 11.16  ? 109  ASP C CG  1 
ATOM   6200  O  OD1 . ASP C  1 22  ? 44.743  4.731   74.426  1.00 10.16  ? 109  ASP C OD1 1 
ATOM   6201  O  OD2 . ASP C  1 22  ? 43.968  3.499   76.070  1.00 10.72  ? 109  ASP C OD2 1 
ATOM   6202  N  N   . ASN C  1 23  ? 43.335  5.996   72.054  1.00 8.23   ? 110  ASN C N   1 
ATOM   6203  C  CA  . ASN C  1 23  ? 42.867  7.393   71.940  1.00 7.85   ? 110  ASN C CA  1 
ATOM   6204  C  C   . ASN C  1 23  ? 42.142  7.852   73.203  1.00 7.83   ? 110  ASN C C   1 
ATOM   6205  O  O   . ASN C  1 23  ? 41.123  8.545   73.124  1.00 7.77   ? 110  ASN C O   1 
ATOM   6206  C  CB  . ASN C  1 23  ? 41.953  7.536   70.720  1.00 7.84   ? 110  ASN C CB  1 
ATOM   6207  C  CG  . ASN C  1 23  ? 42.703  7.277   69.395  1.00 8.41   ? 110  ASN C CG  1 
ATOM   6208  O  OD1 . ASN C  1 23  ? 43.591  8.041   69.040  1.00 10.09  ? 110  ASN C OD1 1 
ATOM   6209  N  ND2 . ASN C  1 23  ? 42.373  6.175   68.704  1.00 9.20   ? 110  ASN C ND2 1 
ATOM   6210  N  N   . ALA C  1 24  ? 42.695  7.488   74.361  1.00 7.60   ? 111  ALA C N   1 
ATOM   6211  C  CA  . ALA C  1 24  ? 41.982  7.630   75.635  1.00 8.20   ? 111  ALA C CA  1 
ATOM   6212  C  C   . ALA C  1 24  ? 41.717  9.082   76.034  1.00 8.64   ? 111  ALA C C   1 
ATOM   6213  O  O   . ALA C  1 24  ? 40.646  9.394   76.580  1.00 8.56   ? 111  ALA C O   1 
ATOM   6214  C  CB  . ALA C  1 24  ? 42.716  6.886   76.743  1.00 7.97   ? 111  ALA C CB  1 
ATOM   6215  N  N   . ILE C  1 25  ? 42.687  9.960   75.757  1.00 7.71   ? 112  ILE C N   1 
ATOM   6216  C  CA  . ILE C  1 25  ? 42.562  11.375  76.148  1.00 8.01   ? 112  ILE C CA  1 
ATOM   6217  C  C   . ILE C  1 25  ? 41.507  12.079  75.273  1.00 7.69   ? 112  ILE C C   1 
ATOM   6218  O  O   . ILE C  1 25  ? 40.653  12.818  75.800  1.00 8.54   ? 112  ILE C O   1 
ATOM   6219  C  CB  . ILE C  1 25  ? 43.927  12.109  76.152  1.00 7.78   ? 112  ILE C CB  1 
ATOM   6220  C  CG1 . ILE C  1 25  ? 44.943  11.351  77.038  1.00 8.03   ? 112  ILE C CG1 1 
ATOM   6221  C  CG2 . ILE C  1 25  ? 43.772  13.595  76.632  1.00 6.85   ? 112  ILE C CG2 1 
ATOM   6222  C  CD1 . ILE C  1 25  ? 44.502  11.201  78.477  1.00 7.01   ? 112  ILE C CD1 1 
ATOM   6223  N  N   . ARG C  1 26  ? 41.561  11.834  73.960  1.00 7.06   ? 113  ARG C N   1 
ATOM   6224  C  CA  . ARG C  1 26  ? 40.543  12.356  73.039  1.00 6.92   ? 113  ARG C CA  1 
ATOM   6225  C  C   . ARG C  1 26  ? 39.138  11.949  73.517  1.00 7.37   ? 113  ARG C C   1 
ATOM   6226  O  O   . ARG C  1 26  ? 38.265  12.789  73.709  1.00 7.83   ? 113  ARG C O   1 
ATOM   6227  C  CB  . ARG C  1 26  ? 40.773  11.845  71.625  1.00 5.95   ? 113  ARG C CB  1 
ATOM   6228  C  CG  . ARG C  1 26  ? 41.944  12.528  70.879  1.00 7.14   ? 113  ARG C CG  1 
ATOM   6229  C  CD  . ARG C  1 26  ? 42.201  11.813  69.574  1.00 6.94   ? 113  ARG C CD  1 
ATOM   6230  N  NE  . ARG C  1 26  ? 41.020  11.805  68.715  1.00 7.26   ? 113  ARG C NE  1 
ATOM   6231  C  CZ  . ARG C  1 26  ? 40.661  12.798  67.893  1.00 11.04  ? 113  ARG C CZ  1 
ATOM   6232  N  NH1 . ARG C  1 26  ? 41.384  13.928  67.813  1.00 9.47   ? 113  ARG C NH1 1 
ATOM   6233  N  NH2 . ARG C  1 26  ? 39.563  12.662  67.139  1.00 9.36   ? 113  ARG C NH2 1 
ATOM   6234  N  N   . ILE C  1 27  ? 38.942  10.645  73.711  1.00 7.05   ? 114  ILE C N   1 
ATOM   6235  C  CA  . ILE C  1 27  ? 37.644  10.113  74.108  1.00 6.70   ? 114  ILE C CA  1 
ATOM   6236  C  C   . ILE C  1 27  ? 37.247  10.619  75.510  1.00 7.16   ? 114  ILE C C   1 
ATOM   6237  O  O   . ILE C  1 27  ? 36.113  11.098  75.701  1.00 7.85   ? 114  ILE C O   1 
ATOM   6238  C  CB  . ILE C  1 27  ? 37.661  8.559   74.044  1.00 6.61   ? 114  ILE C CB  1 
ATOM   6239  C  CG1 . ILE C  1 27  ? 37.753  8.118   72.580  1.00 7.74   ? 114  ILE C CG1 1 
ATOM   6240  C  CG2 . ILE C  1 27  ? 36.389  7.950   74.727  1.00 6.45   ? 114  ILE C CG2 1 
ATOM   6241  C  CD1 . ILE C  1 27  ? 38.181  6.635   72.380  1.00 6.95   ? 114  ILE C CD1 1 
ATOM   6242  N  N   . GLY C  1 28  ? 38.199  10.541  76.454  1.00 6.74   ? 115  GLY C N   1 
ATOM   6243  C  CA  . GLY C  1 28  ? 38.010  10.962  77.848  1.00 8.14   ? 115  GLY C CA  1 
ATOM   6244  C  C   . GLY C  1 28  ? 37.710  12.440  78.077  1.00 8.06   ? 115  GLY C C   1 
ATOM   6245  O  O   . GLY C  1 28  ? 37.314  12.831  79.181  1.00 9.03   ? 115  GLY C O   1 
ATOM   6246  N  N   . GLU C  1 29  ? 37.902  13.268  77.050  1.00 8.42   ? 116  GLU C N   1 
ATOM   6247  C  CA  . GLU C  1 29  ? 37.451  14.678  77.110  1.00 9.02   ? 116  GLU C CA  1 
ATOM   6248  C  C   . GLU C  1 29  ? 35.919  14.784  77.361  1.00 10.09  ? 116  GLU C C   1 
ATOM   6249  O  O   . GLU C  1 29  ? 35.434  15.779  77.898  1.00 10.65  ? 116  GLU C O   1 
ATOM   6250  C  CB  . GLU C  1 29  ? 37.836  15.415  75.805  1.00 8.98   ? 116  GLU C CB  1 
ATOM   6251  C  CG  . GLU C  1 29  ? 37.618  16.939  75.803  1.00 8.90   ? 116  GLU C CG  1 
ATOM   6252  C  CD  . GLU C  1 29  ? 36.159  17.345  75.541  1.00 12.24  ? 116  GLU C CD  1 
ATOM   6253  O  OE1 . GLU C  1 29  ? 35.733  18.382  76.110  1.00 10.57  ? 116  GLU C OE1 1 
ATOM   6254  O  OE2 . GLU C  1 29  ? 35.435  16.617  74.812  1.00 11.13  ? 116  GLU C OE2 1 
ATOM   6255  N  N   . ASP C  1 30  ? 35.161  13.783  76.938  1.00 11.26  ? 117  ASP C N   1 
ATOM   6256  C  CA  . ASP C  1 30  ? 33.708  13.811  77.133  1.00 13.21  ? 117  ASP C CA  1 
ATOM   6257  C  C   . ASP C  1 30  ? 33.176  12.549  77.828  1.00 13.71  ? 117  ASP C C   1 
ATOM   6258  O  O   . ASP C  1 30  ? 32.274  12.621  78.668  1.00 16.65  ? 117  ASP C O   1 
ATOM   6259  C  CB  . ASP C  1 30  ? 33.006  14.067  75.798  1.00 13.74  ? 117  ASP C CB  1 
ATOM   6260  C  CG  . ASP C  1 30  ? 31.482  14.110  75.932  1.00 18.23  ? 117  ASP C CG  1 
ATOM   6261  O  OD1 . ASP C  1 30  ? 30.791  13.372  75.173  1.00 21.94  ? 117  ASP C OD1 1 
ATOM   6262  O  OD2 . ASP C  1 30  ? 30.997  14.870  76.816  1.00 21.11  ? 117  ASP C OD2 1 
ATOM   6263  N  N   . ALA C  1 31  ? 33.763  11.403  77.536  1.00 12.54  ? 118  ALA C N   1 
ATOM   6264  C  CA  . ALA C  1 31  ? 33.258  10.123  78.062  1.00 11.38  ? 118  ALA C CA  1 
ATOM   6265  C  C   . ALA C  1 31  ? 33.897  9.815   79.424  1.00 10.72  ? 118  ALA C C   1 
ATOM   6266  O  O   . ALA C  1 31  ? 34.832  10.494  79.833  1.00 11.51  ? 118  ALA C O   1 
ATOM   6267  C  CB  . ALA C  1 31  ? 33.517  9.020   77.066  1.00 10.39  ? 118  ALA C CB  1 
ATOM   6268  N  N   . HIS C  1 32  ? 33.357  8.840   80.149  1.00 10.33  ? 119  HIS C N   1 
ATOM   6269  C  CA  . HIS C  1 32  ? 33.862  8.551   81.509  1.00 8.87   ? 119  HIS C CA  1 
ATOM   6270  C  C   . HIS C  1 32  ? 35.110  7.667   81.383  1.00 8.46   ? 119  HIS C C   1 
ATOM   6271  O  O   . HIS C  1 32  ? 35.016  6.455   81.339  1.00 8.43   ? 119  HIS C O   1 
ATOM   6272  C  CB  . HIS C  1 32  ? 32.767  7.913   82.388  1.00 9.28   ? 119  HIS C CB  1 
ATOM   6273  C  CG  . HIS C  1 32  ? 31.562  8.791   82.572  1.00 7.03   ? 119  HIS C CG  1 
ATOM   6274  N  ND1 . HIS C  1 32  ? 30.296  8.292   82.800  1.00 9.65   ? 119  HIS C ND1 1 
ATOM   6275  C  CD2 . HIS C  1 32  ? 31.431  10.142  82.549  1.00 7.69   ? 119  HIS C CD2 1 
ATOM   6276  C  CE1 . HIS C  1 32  ? 29.438  9.290   82.915  1.00 8.50   ? 119  HIS C CE1 1 
ATOM   6277  N  NE2 . HIS C  1 32  ? 30.096  10.424  82.755  1.00 8.19   ? 119  HIS C NE2 1 
ATOM   6278  N  N   . ILE C  1 33  ? 36.272  8.303   81.315  1.00 8.17   ? 120  ILE C N   1 
ATOM   6279  C  CA  . ILE C  1 33  ? 37.538  7.600   81.107  1.00 7.95   ? 120  ILE C CA  1 
ATOM   6280  C  C   . ILE C  1 33  ? 38.400  7.812   82.329  1.00 7.79   ? 120  ILE C C   1 
ATOM   6281  O  O   . ILE C  1 33  ? 38.582  8.931   82.766  1.00 8.04   ? 120  ILE C O   1 
ATOM   6282  C  CB  . ILE C  1 33  ? 38.252  8.058   79.807  1.00 8.23   ? 120  ILE C CB  1 
ATOM   6283  C  CG1 . ILE C  1 33  ? 37.356  7.795   78.566  1.00 8.71   ? 120  ILE C CG1 1 
ATOM   6284  C  CG2 . ILE C  1 33  ? 39.660  7.380   79.656  1.00 7.31   ? 120  ILE C CG2 1 
ATOM   6285  C  CD1 . ILE C  1 33  ? 36.962  6.318   78.350  1.00 8.45   ? 120  ILE C CD1 1 
ATOM   6286  N  N   . LEU C  1 34  ? 38.900  6.718   82.891  1.00 7.28   ? 121  LEU C N   1 
ATOM   6287  C  CA  . LEU C  1 34  ? 39.759  6.770   84.081  1.00 7.25   ? 121  LEU C CA  1 
ATOM   6288  C  C   . LEU C  1 34  ? 41.111  7.456   83.796  1.00 7.73   ? 121  LEU C C   1 
ATOM   6289  O  O   . LEU C  1 34  ? 41.689  7.254   82.726  1.00 7.74   ? 121  LEU C O   1 
ATOM   6290  C  CB  . LEU C  1 34  ? 40.009  5.343   84.567  1.00 7.13   ? 121  LEU C CB  1 
ATOM   6291  C  CG  . LEU C  1 34  ? 38.809  4.596   85.167  1.00 7.67   ? 121  LEU C CG  1 
ATOM   6292  C  CD1 . LEU C  1 34  ? 39.200  3.149   85.432  1.00 9.89   ? 121  LEU C CD1 1 
ATOM   6293  C  CD2 . LEU C  1 34  ? 38.290  5.273   86.461  1.00 8.30   ? 121  LEU C CD2 1 
ATOM   6294  N  N   . VAL C  1 35  ? 41.585  8.279   84.744  1.00 7.58   ? 122  VAL C N   1 
ATOM   6295  C  CA  . VAL C  1 35  ? 42.982  8.758   84.721  1.00 7.76   ? 122  VAL C CA  1 
ATOM   6296  C  C   . VAL C  1 35  ? 43.924  7.597   84.996  1.00 8.06   ? 122  VAL C C   1 
ATOM   6297  O  O   . VAL C  1 35  ? 43.683  6.801   85.913  1.00 8.35   ? 122  VAL C O   1 
ATOM   6298  C  CB  . VAL C  1 35  ? 43.233  9.903   85.748  1.00 8.82   ? 122  VAL C CB  1 
ATOM   6299  C  CG1 . VAL C  1 35  ? 44.719  10.262  85.799  1.00 7.04   ? 122  VAL C CG1 1 
ATOM   6300  C  CG2 . VAL C  1 35  ? 42.407  11.129  85.390  1.00 6.01   ? 122  VAL C CG2 1 
ATOM   6301  N  N   . THR C  1 36  ? 44.975  7.478   84.183  1.00 7.93   ? 123  THR C N   1 
ATOM   6302  C  CA  . THR C  1 36  ? 45.966  6.391   84.321  1.00 8.10   ? 123  THR C CA  1 
ATOM   6303  C  C   . THR C  1 36  ? 47.407  6.941   84.193  1.00 7.89   ? 123  THR C C   1 
ATOM   6304  O  O   . THR C  1 36  ? 47.611  8.147   83.974  1.00 8.78   ? 123  THR C O   1 
ATOM   6305  C  CB  . THR C  1 36  ? 45.727  5.212   83.280  1.00 8.26   ? 123  THR C CB  1 
ATOM   6306  O  OG1 . THR C  1 36  ? 45.896  5.683   81.937  1.00 9.53   ? 123  THR C OG1 1 
ATOM   6307  C  CG2 . THR C  1 36  ? 44.312  4.596   83.410  1.00 7.57   ? 123  THR C CG2 1 
ATOM   6308  N  N   . ARG C  1 37  ? 48.379  6.058   84.395  1.00 7.91   ? 124  ARG C N   1 
ATOM   6309  C  CA  . ARG C  1 37  ? 49.760  6.159   83.892  1.00 7.47   ? 124  ARG C CA  1 
ATOM   6310  C  C   . ARG C  1 37  ? 50.378  4.759   84.031  1.00 7.86   ? 124  ARG C C   1 
ATOM   6311  O  O   . ARG C  1 37  ? 49.710  3.829   84.518  1.00 8.65   ? 124  ARG C O   1 
ATOM   6312  C  CB  . ARG C  1 37  ? 50.609  7.246   84.606  1.00 7.57   ? 124  ARG C CB  1 
ATOM   6313  C  CG  . ARG C  1 37  ? 50.680  8.587   83.833  1.00 7.90   ? 124  ARG C CG  1 
ATOM   6314  C  CD  . ARG C  1 37  ? 52.095  9.280   83.964  1.00 8.97   ? 124  ARG C CD  1 
ATOM   6315  N  NE  . ARG C  1 37  ? 53.152  8.391   83.456  1.00 10.19  ? 124  ARG C NE  1 
ATOM   6316  C  CZ  . ARG C  1 37  ? 54.393  8.325   83.943  1.00 11.42  ? 124  ARG C CZ  1 
ATOM   6317  N  NH1 . ARG C  1 37  ? 55.258  7.457   83.426  1.00 10.52  ? 124  ARG C NH1 1 
ATOM   6318  N  NH2 . ARG C  1 37  ? 54.767  9.128   84.957  1.00 10.75  ? 124  ARG C NH2 1 
ATOM   6319  N  N   . GLU C  1 38  ? 51.638  4.617   83.620  1.00 7.55   ? 125  GLU C N   1 
ATOM   6320  C  CA  . GLU C  1 38  ? 52.384  3.345   83.661  1.00 7.50   ? 125  GLU C CA  1 
ATOM   6321  C  C   . GLU C  1 38  ? 51.598  2.174   83.004  1.00 7.41   ? 125  GLU C C   1 
ATOM   6322  O  O   . GLU C  1 38  ? 51.389  1.140   83.620  1.00 7.98   ? 125  GLU C O   1 
ATOM   6323  C  CB  . GLU C  1 38  ? 52.793  2.990   85.104  1.00 7.86   ? 125  GLU C CB  1 
ATOM   6324  C  CG  . GLU C  1 38  ? 53.708  4.018   85.793  1.00 6.58   ? 125  GLU C CG  1 
ATOM   6325  C  CD  . GLU C  1 38  ? 52.967  5.226   86.356  1.00 10.43  ? 125  GLU C CD  1 
ATOM   6326  O  OE1 . GLU C  1 38  ? 53.618  6.295   86.442  1.00 9.43   ? 125  GLU C OE1 1 
ATOM   6327  O  OE2 . GLU C  1 38  ? 51.764  5.116   86.734  1.00 7.90   ? 125  GLU C OE2 1 
ATOM   6328  N  N   . PRO C  1 39  ? 51.188  2.346   81.736  1.00 7.65   ? 126  PRO C N   1 
ATOM   6329  C  CA  . PRO C  1 39  ? 50.434  1.320   81.030  1.00 7.57   ? 126  PRO C CA  1 
ATOM   6330  C  C   . PRO C  1 39  ? 51.356  0.272   80.427  1.00 8.14   ? 126  PRO C C   1 
ATOM   6331  O  O   . PRO C  1 39  ? 52.590  0.447   80.387  1.00 9.41   ? 126  PRO C O   1 
ATOM   6332  C  CB  . PRO C  1 39  ? 49.773  2.106   79.902  1.00 7.47   ? 126  PRO C CB  1 
ATOM   6333  C  CG  . PRO C  1 39  ? 50.882  3.115   79.519  1.00 8.17   ? 126  PRO C CG  1 
ATOM   6334  C  CD  . PRO C  1 39  ? 51.444  3.522   80.880  1.00 7.20   ? 126  PRO C CD  1 
ATOM   6335  N  N   . TYR C  1 40  ? 50.739  -0.791  79.947  1.00 8.01   ? 127  TYR C N   1 
ATOM   6336  C  CA  . TYR C  1 40  ? 51.397  -1.821  79.146  1.00 7.78   ? 127  TYR C CA  1 
ATOM   6337  C  C   . TYR C  1 40  ? 50.369  -2.711  78.503  1.00 8.09   ? 127  TYR C C   1 
ATOM   6338  O  O   . TYR C  1 40  ? 49.166  -2.469  78.639  1.00 9.01   ? 127  TYR C O   1 
ATOM   6339  C  CB  . TYR C  1 40  ? 52.408  -2.649  79.965  1.00 7.64   ? 127  TYR C CB  1 
ATOM   6340  C  CG  . TYR C  1 40  ? 51.952  -3.260  81.298  1.00 6.45   ? 127  TYR C CG  1 
ATOM   6341  C  CD1 . TYR C  1 40  ? 51.855  -2.486  82.453  1.00 6.15   ? 127  TYR C CD1 1 
ATOM   6342  C  CD2 . TYR C  1 40  ? 51.736  -4.647  81.409  1.00 7.31   ? 127  TYR C CD2 1 
ATOM   6343  C  CE1 . TYR C  1 40  ? 51.486  -3.036  83.665  1.00 3.58   ? 127  TYR C CE1 1 
ATOM   6344  C  CE2 . TYR C  1 40  ? 51.387  -5.223  82.635  1.00 7.70   ? 127  TYR C CE2 1 
ATOM   6345  C  CZ  . TYR C  1 40  ? 51.279  -4.411  83.756  1.00 6.93   ? 127  TYR C CZ  1 
ATOM   6346  O  OH  . TYR C  1 40  ? 50.956  -4.938  84.989  1.00 7.64   ? 127  TYR C OH  1 
ATOM   6347  N  N   . LEU C  1 41  ? 50.837  -3.728  77.778  1.00 7.99   ? 128  LEU C N   1 
ATOM   6348  C  CA  . LEU C  1 41  ? 49.941  -4.746  77.258  1.00 8.46   ? 128  LEU C CA  1 
ATOM   6349  C  C   . LEU C  1 41  ? 50.520  -6.082  77.669  1.00 8.73   ? 128  LEU C C   1 
ATOM   6350  O  O   . LEU C  1 41  ? 51.733  -6.207  77.883  1.00 8.22   ? 128  LEU C O   1 
ATOM   6351  C  CB  . LEU C  1 41  ? 49.840  -4.723  75.730  1.00 7.89   ? 128  LEU C CB  1 
ATOM   6352  C  CG  . LEU C  1 41  ? 49.389  -3.618  74.749  1.00 11.55  ? 128  LEU C CG  1 
ATOM   6353  C  CD1 . LEU C  1 41  ? 48.062  -3.886  74.088  1.00 10.74  ? 128  LEU C CD1 1 
ATOM   6354  C  CD2 . LEU C  1 41  ? 49.647  -2.152  75.123  1.00 8.61   ? 128  LEU C CD2 1 
ATOM   6355  N  N   . SER C  1 42  ? 49.631  -7.070  77.794  1.00 9.15   ? 129  SER C N   1 
ATOM   6356  C  CA  . SER C  1 42  ? 50.003  -8.433  78.069  1.00 9.19   ? 129  SER C CA  1 
ATOM   6357  C  C   . SER C  1 42  ? 48.951  -9.362  77.415  1.00 10.02  ? 129  SER C C   1 
ATOM   6358  O  O   . SER C  1 42  ? 47.749  -9.037  77.368  1.00 9.14   ? 129  SER C O   1 
ATOM   6359  C  CB  . SER C  1 42  ? 50.111  -8.649  79.590  1.00 9.00   ? 129  SER C CB  1 
ATOM   6360  O  OG  . SER C  1 42  ? 50.574  -9.955  79.906  1.00 7.94   ? 129  SER C OG  1 
ATOM   6361  N  N   . CYS C  1 43  ? 49.416  -10.488 76.889  1.00 10.45  ? 130  CYS C N   1 
ATOM   6362  C  CA  . CYS C  1 43  ? 48.555  -11.412 76.152  1.00 11.12  ? 130  CYS C CA  1 
ATOM   6363  C  C   . CYS C  1 43  ? 48.361  -12.715 76.916  1.00 11.41  ? 130  CYS C C   1 
ATOM   6364  O  O   . CYS C  1 43  ? 49.036  -12.978 77.914  1.00 10.70  ? 130  CYS C O   1 
ATOM   6365  C  CB  . CYS C  1 43  ? 49.122  -11.705 74.741  1.00 11.59  ? 130  CYS C CB  1 
ATOM   6366  S  SG  . CYS C  1 43  ? 49.483  -10.200 73.770  1.00 12.04  ? 130  CYS C SG  1 
ATOM   6367  N  N   . ASP C  1 44  ? 47.426  -13.527 76.423  1.00 12.49  ? 131  ASP C N   1 
ATOM   6368  C  CA  . ASP C  1 44  ? 47.136  -14.857 76.961  1.00 13.43  ? 131  ASP C CA  1 
ATOM   6369  C  C   . ASP C  1 44  ? 46.639  -15.729 75.783  1.00 13.64  ? 131  ASP C C   1 
ATOM   6370  O  O   . ASP C  1 44  ? 46.560  -15.248 74.647  1.00 13.62  ? 131  ASP C O   1 
ATOM   6371  C  CB  . ASP C  1 44  ? 46.109  -14.766 78.110  1.00 13.18  ? 131  ASP C CB  1 
ATOM   6372  C  CG  . ASP C  1 44  ? 44.773  -14.158 77.677  1.00 16.64  ? 131  ASP C CG  1 
ATOM   6373  O  OD1 . ASP C  1 44  ? 44.300  -13.203 78.339  1.00 20.90  ? 131  ASP C OD1 1 
ATOM   6374  O  OD2 . ASP C  1 44  ? 44.188  -14.610 76.679  1.00 18.14  ? 131  ASP C OD2 1 
ATOM   6375  N  N   . PRO C  1 45  ? 46.329  -17.012 76.028  1.00 14.70  ? 132  PRO C N   1 
ATOM   6376  C  CA  . PRO C  1 45  ? 45.895  -17.838 74.885  1.00 14.58  ? 132  PRO C CA  1 
ATOM   6377  C  C   . PRO C  1 45  ? 44.734  -17.277 74.052  1.00 15.24  ? 132  PRO C C   1 
ATOM   6378  O  O   . PRO C  1 45  ? 44.619  -17.604 72.869  1.00 15.82  ? 132  PRO C O   1 
ATOM   6379  C  CB  . PRO C  1 45  ? 45.512  -19.168 75.554  1.00 14.50  ? 132  PRO C CB  1 
ATOM   6380  C  CG  . PRO C  1 45  ? 46.446  -19.236 76.732  1.00 14.38  ? 132  PRO C CG  1 
ATOM   6381  C  CD  . PRO C  1 45  ? 46.424  -17.809 77.264  1.00 14.29  ? 132  PRO C CD  1 
ATOM   6382  N  N   . GLN C  1 46  ? 43.890  -16.447 74.655  1.00 15.85  ? 133  GLN C N   1 
ATOM   6383  C  CA  . GLN C  1 46  ? 42.681  -15.976 74.007  1.00 17.66  ? 133  GLN C CA  1 
ATOM   6384  C  C   . GLN C  1 46  ? 42.866  -14.632 73.288  1.00 17.91  ? 133  GLN C C   1 
ATOM   6385  O  O   . GLN C  1 46  ? 42.110  -14.287 72.386  1.00 18.12  ? 133  GLN C O   1 
ATOM   6386  C  CB  . GLN C  1 46  ? 41.558  -15.891 75.046  1.00 18.94  ? 133  GLN C CB  1 
ATOM   6387  C  CG  . GLN C  1 46  ? 40.634  -17.131 75.118  1.00 24.10  ? 133  GLN C CG  1 
ATOM   6388  C  CD  . GLN C  1 46  ? 41.345  -18.465 74.948  1.00 31.09  ? 133  GLN C CD  1 
ATOM   6389  O  OE1 . GLN C  1 46  ? 41.971  -18.975 75.883  1.00 35.71  ? 133  GLN C OE1 1 
ATOM   6390  N  NE2 . GLN C  1 46  ? 41.232  -19.054 73.752  1.00 34.27  ? 133  GLN C NE2 1 
ATOM   6391  N  N   . GLY C  1 47  ? 43.888  -13.880 73.670  1.00 17.65  ? 134  GLY C N   1 
ATOM   6392  C  CA  . GLY C  1 47  ? 44.110  -12.582 73.041  1.00 16.86  ? 134  GLY C CA  1 
ATOM   6393  C  C   . GLY C  1 47  ? 44.963  -11.691 73.918  1.00 16.25  ? 134  GLY C C   1 
ATOM   6394  O  O   . GLY C  1 47  ? 45.665  -12.187 74.813  1.00 16.20  ? 134  GLY C O   1 
ATOM   6395  N  N   . CYS C  1 48  ? 44.910  -10.389 73.647  1.00 13.72  ? 135  CYS C N   1 
ATOM   6396  C  CA  . CYS C  1 48  ? 45.763  -9.429  74.339  1.00 12.29  ? 135  CYS C CA  1 
ATOM   6397  C  C   . CYS C  1 48  ? 44.935  -8.359  75.042  1.00 10.91  ? 135  CYS C C   1 
ATOM   6398  O  O   . CYS C  1 48  ? 43.844  -8.012  74.596  1.00 10.29  ? 135  CYS C O   1 
ATOM   6399  C  CB  . CYS C  1 48  ? 46.757  -8.795  73.358  1.00 12.94  ? 135  CYS C CB  1 
ATOM   6400  S  SG  . CYS C  1 48  ? 47.869  -10.003 72.541  1.00 14.94  ? 135  CYS C SG  1 
ATOM   6401  N  N   . ARG C  1 49  ? 45.460  -7.849  76.151  1.00 10.33  ? 136  ARG C N   1 
ATOM   6402  C  CA  . ARG C  1 49  ? 44.774  -6.847  76.951  1.00 9.90   ? 136  ARG C CA  1 
ATOM   6403  C  C   . ARG C  1 49  ? 45.690  -5.661  77.242  1.00 9.29   ? 136  ARG C C   1 
ATOM   6404  O  O   . ARG C  1 49  ? 46.916  -5.797  77.287  1.00 9.39   ? 136  ARG C O   1 
ATOM   6405  C  CB  . ARG C  1 49  ? 44.262  -7.464  78.252  1.00 10.14  ? 136  ARG C CB  1 
ATOM   6406  C  CG  . ARG C  1 49  ? 43.082  -8.447  78.003  1.00 10.07  ? 136  ARG C CG  1 
ATOM   6407  C  CD  . ARG C  1 49  ? 42.713  -9.232  79.258  1.00 10.64  ? 136  ARG C CD  1 
ATOM   6408  N  NE  . ARG C  1 49  ? 42.107  -8.430  80.341  1.00 11.38  ? 136  ARG C NE  1 
ATOM   6409  C  CZ  . ARG C  1 49  ? 40.869  -7.912  80.314  1.00 11.67  ? 136  ARG C CZ  1 
ATOM   6410  N  NH1 . ARG C  1 49  ? 40.093  -8.050  79.241  1.00 11.38  ? 136  ARG C NH1 1 
ATOM   6411  N  NH2 . ARG C  1 49  ? 40.405  -7.225  81.357  1.00 10.59  ? 136  ARG C NH2 1 
ATOM   6412  N  N   . MET C  1 50  ? 45.087  -4.495  77.402  1.00 8.64   ? 137  MET C N   1 
ATOM   6413  C  CA  . MET C  1 50  ? 45.799  -3.329  77.908  1.00 8.52   ? 137  MET C CA  1 
ATOM   6414  C  C   . MET C  1 50  ? 45.750  -3.292  79.444  1.00 8.06   ? 137  MET C C   1 
ATOM   6415  O  O   . MET C  1 50  ? 44.751  -3.690  80.037  1.00 8.43   ? 137  MET C O   1 
ATOM   6416  C  CB  . MET C  1 50  ? 45.196  -2.041  77.325  1.00 8.12   ? 137  MET C CB  1 
ATOM   6417  C  CG  . MET C  1 50  ? 45.692  -1.732  75.919  1.00 10.44  ? 137  MET C CG  1 
ATOM   6418  S  SD  . MET C  1 50  ? 44.646  -0.551  75.060  1.00 8.91   ? 137  MET C SD  1 
ATOM   6419  C  CE  . MET C  1 50  ? 45.655  -0.285  73.556  1.00 5.91   ? 137  MET C CE  1 
ATOM   6420  N  N   . PHE C  1 51  ? 46.823  -2.783  80.059  1.00 8.04   ? 138  PHE C N   1 
ATOM   6421  C  CA  . PHE C  1 51  ? 46.977  -2.691  81.521  1.00 8.20   ? 138  PHE C CA  1 
ATOM   6422  C  C   . PHE C  1 51  ? 47.458  -1.273  81.848  1.00 8.08   ? 138  PHE C C   1 
ATOM   6423  O  O   . PHE C  1 51  ? 48.184  -0.682  81.041  1.00 8.25   ? 138  PHE C O   1 
ATOM   6424  C  CB  . PHE C  1 51  ? 48.046  -3.688  82.014  1.00 8.43   ? 138  PHE C CB  1 
ATOM   6425  C  CG  . PHE C  1 51  ? 47.605  -5.126  81.972  1.00 8.29   ? 138  PHE C CG  1 
ATOM   6426  C  CD1 . PHE C  1 51  ? 47.443  -5.789  80.750  1.00 7.56   ? 138  PHE C CD1 1 
ATOM   6427  C  CD2 . PHE C  1 51  ? 47.349  -5.817  83.155  1.00 8.97   ? 138  PHE C CD2 1 
ATOM   6428  C  CE1 . PHE C  1 51  ? 47.015  -7.127  80.698  1.00 8.56   ? 138  PHE C CE1 1 
ATOM   6429  C  CE2 . PHE C  1 51  ? 46.926  -7.159  83.119  1.00 8.45   ? 138  PHE C CE2 1 
ATOM   6430  C  CZ  . PHE C  1 51  ? 46.759  -7.816  81.889  1.00 5.82   ? 138  PHE C CZ  1 
ATOM   6431  N  N   . ALA C  1 52  ? 47.092  -0.747  83.025  1.00 7.20   ? 139  ALA C N   1 
ATOM   6432  C  CA  . ALA C  1 52  ? 47.632  0.546   83.520  1.00 7.55   ? 139  ALA C CA  1 
ATOM   6433  C  C   . ALA C  1 52  ? 47.332  0.717   85.000  1.00 7.60   ? 139  ALA C C   1 
ATOM   6434  O  O   . ALA C  1 52  ? 46.493  0.004   85.558  1.00 7.57   ? 139  ALA C O   1 
ATOM   6435  C  CB  . ALA C  1 52  ? 47.055  1.751   82.723  1.00 7.17   ? 139  ALA C CB  1 
ATOM   6436  N  N   . LEU C  1 53  ? 48.020  1.660   85.640  1.00 7.74   ? 140  LEU C N   1 
ATOM   6437  C  CA  . LEU C  1 53  ? 47.691  2.014   87.002  1.00 7.05   ? 140  LEU C CA  1 
ATOM   6438  C  C   . LEU C  1 53  ? 46.649  3.146   86.984  1.00 7.17   ? 140  LEU C C   1 
ATOM   6439  O  O   . LEU C  1 53  ? 46.960  4.319   86.677  1.00 6.53   ? 140  LEU C O   1 
ATOM   6440  C  CB  . LEU C  1 53  ? 48.944  2.423   87.783  1.00 7.14   ? 140  LEU C CB  1 
ATOM   6441  C  CG  . LEU C  1 53  ? 49.990  1.320   87.937  1.00 6.65   ? 140  LEU C CG  1 
ATOM   6442  C  CD1 . LEU C  1 53  ? 51.249  1.916   88.541  1.00 8.09   ? 140  LEU C CD1 1 
ATOM   6443  C  CD2 . LEU C  1 53  ? 49.435  0.209   88.818  1.00 7.16   ? 140  LEU C CD2 1 
ATOM   6444  N  N   . SER C  1 54  ? 45.411  2.799   87.321  1.00 6.46   ? 141  SER C N   1 
ATOM   6445  C  CA  . SER C  1 54  ? 44.381  3.843   87.523  1.00 6.96   ? 141  SER C CA  1 
ATOM   6446  C  C   . SER C  1 54  ? 44.770  4.806   88.640  1.00 7.10   ? 141  SER C C   1 
ATOM   6447  O  O   . SER C  1 54  ? 45.536  4.427   89.535  1.00 6.61   ? 141  SER C O   1 
ATOM   6448  C  CB  . SER C  1 54  ? 43.057  3.188   87.909  1.00 7.11   ? 141  SER C CB  1 
ATOM   6449  O  OG  . SER C  1 54  ? 42.034  4.177   87.991  1.00 6.97   ? 141  SER C OG  1 
ATOM   6450  N  N   . GLN C  1 55  ? 44.234  6.029   88.595  1.00 7.42   ? 142  GLN C N   1 
ATOM   6451  C  CA  . GLN C  1 55  ? 44.325  6.983   89.716  1.00 7.97   ? 142  GLN C CA  1 
ATOM   6452  C  C   . GLN C  1 55  ? 43.009  7.057   90.502  1.00 7.84   ? 142  GLN C C   1 
ATOM   6453  O  O   . GLN C  1 55  ? 42.878  7.896   91.398  1.00 8.97   ? 142  GLN C O   1 
ATOM   6454  C  CB  . GLN C  1 55  ? 44.734  8.376   89.218  1.00 7.31   ? 142  GLN C CB  1 
ATOM   6455  C  CG  . GLN C  1 55  ? 46.178  8.458   88.634  1.00 6.87   ? 142  GLN C CG  1 
ATOM   6456  C  CD  . GLN C  1 55  ? 47.235  8.738   89.718  1.00 8.34   ? 142  GLN C CD  1 
ATOM   6457  O  OE1 . GLN C  1 55  ? 47.008  8.504   90.897  1.00 7.82   ? 142  GLN C OE1 1 
ATOM   6458  N  NE2 . GLN C  1 55  ? 48.388  9.251   89.305  1.00 9.14   ? 142  GLN C NE2 1 
ATOM   6459  N  N   . GLY C  1 56  ? 42.054  6.173   90.187  1.00 7.82   ? 143  GLY C N   1 
ATOM   6460  C  CA  . GLY C  1 56  ? 40.780  6.106   90.957  1.00 8.05   ? 143  GLY C CA  1 
ATOM   6461  C  C   . GLY C  1 56  ? 39.951  7.387   90.800  1.00 7.35   ? 143  GLY C C   1 
ATOM   6462  O  O   . GLY C  1 56  ? 39.423  7.908   91.765  1.00 8.17   ? 143  GLY C O   1 
ATOM   6463  N  N   . THR C  1 57  ? 39.853  7.861   89.560  1.00 7.69   ? 144  THR C N   1 
ATOM   6464  C  CA  . THR C  1 57  ? 39.108  9.074   89.171  1.00 8.06   ? 144  THR C CA  1 
ATOM   6465  C  C   . THR C  1 57  ? 38.973  9.084   87.659  1.00 8.45   ? 144  THR C C   1 
ATOM   6466  O  O   . THR C  1 57  ? 39.794  8.500   86.959  1.00 7.97   ? 144  THR C O   1 
ATOM   6467  C  CB  . THR C  1 57  ? 39.781  10.413  89.654  1.00 9.04   ? 144  THR C CB  1 
ATOM   6468  O  OG1 . THR C  1 57  ? 38.987  11.531  89.222  1.00 8.94   ? 144  THR C OG1 1 
ATOM   6469  C  CG2 . THR C  1 57  ? 41.236  10.582  89.112  1.00 7.15   ? 144  THR C CG2 1 
ATOM   6470  N  N   . THR C  1 58  ? 37.931  9.733   87.149  1.00 8.72   ? 145  THR C N   1 
ATOM   6471  C  CA  . THR C  1 58  ? 37.882  10.002  85.709  1.00 8.87   ? 145  THR C CA  1 
ATOM   6472  C  C   . THR C  1 58  ? 38.682  11.263  85.316  1.00 9.18   ? 145  THR C C   1 
ATOM   6473  O  O   . THR C  1 58  ? 39.012  12.099  86.158  1.00 8.62   ? 145  THR C O   1 
ATOM   6474  C  CB  . THR C  1 58  ? 36.465  10.178  85.213  1.00 8.91   ? 145  THR C CB  1 
ATOM   6475  O  OG1 . THR C  1 58  ? 35.899  11.313  85.873  1.00 7.48   ? 145  THR C OG1 1 
ATOM   6476  C  CG2 . THR C  1 58  ? 35.613  8.900   85.503  1.00 9.80   ? 145  THR C CG2 1 
ATOM   6477  N  N   . LEU C  1 59  ? 38.986  11.362  84.015  1.00 8.86   ? 146  LEU C N   1 
ATOM   6478  C  CA  . LEU C  1 59  ? 39.826  12.413  83.480  1.00 9.11   ? 146  LEU C CA  1 
ATOM   6479  C  C   . LEU C  1 59  ? 39.205  13.822  83.626  1.00 9.53   ? 146  LEU C C   1 
ATOM   6480  O  O   . LEU C  1 59  ? 39.905  14.790  83.945  1.00 10.30  ? 146  LEU C O   1 
ATOM   6481  C  CB  . LEU C  1 59  ? 40.161  12.098  82.015  1.00 8.91   ? 146  LEU C CB  1 
ATOM   6482  C  CG  . LEU C  1 59  ? 41.124  13.039  81.273  1.00 8.04   ? 146  LEU C CG  1 
ATOM   6483  C  CD1 . LEU C  1 59  ? 42.519  13.135  81.918  1.00 7.23   ? 146  LEU C CD1 1 
ATOM   6484  C  CD2 . LEU C  1 59  ? 41.213  12.701  79.773  1.00 8.11   ? 146  LEU C CD2 1 
ATOM   6485  N  N   . ARG C  1 60  ? 37.898  13.914  83.384  1.00 9.53   ? 147  ARG C N   1 
ATOM   6486  C  CA  . ARG C  1 60  ? 37.133  15.149  83.541  1.00 9.23   ? 147  ARG C CA  1 
ATOM   6487  C  C   . ARG C  1 60  ? 36.628  15.356  84.985  1.00 9.35   ? 147  ARG C C   1 
ATOM   6488  O  O   . ARG C  1 60  ? 36.114  16.421  85.309  1.00 9.12   ? 147  ARG C O   1 
ATOM   6489  C  CB  . ARG C  1 60  ? 35.933  15.167  82.565  1.00 9.19   ? 147  ARG C CB  1 
ATOM   6490  C  CG  . ARG C  1 60  ? 36.269  15.572  81.117  1.00 8.85   ? 147  ARG C CG  1 
ATOM   6491  C  CD  . ARG C  1 60  ? 36.921  16.953  81.101  1.00 12.64  ? 147  ARG C CD  1 
ATOM   6492  N  NE  . ARG C  1 60  ? 36.779  17.628  79.825  1.00 11.30  ? 147  ARG C NE  1 
ATOM   6493  C  CZ  . ARG C  1 60  ? 37.113  18.896  79.620  1.00 12.50  ? 147  ARG C CZ  1 
ATOM   6494  N  NH1 . ARG C  1 60  ? 37.648  19.633  80.608  1.00 9.02   ? 147  ARG C NH1 1 
ATOM   6495  N  NH2 . ARG C  1 60  ? 36.940  19.410  78.421  1.00 10.88  ? 147  ARG C NH2 1 
ATOM   6496  N  N   . GLY C  1 61  ? 36.783  14.345  85.839  1.00 8.65   ? 148  GLY C N   1 
ATOM   6497  C  CA  . GLY C  1 61  ? 36.360  14.469  87.235  1.00 8.37   ? 148  GLY C CA  1 
ATOM   6498  C  C   . GLY C  1 61  ? 37.201  15.491  87.991  1.00 8.90   ? 148  GLY C C   1 
ATOM   6499  O  O   . GLY C  1 61  ? 38.365  15.709  87.666  1.00 8.92   ? 148  GLY C O   1 
ATOM   6500  N  N   . ARG C  1 62  ? 36.618  16.104  89.022  1.00 9.30   ? 149  ARG C N   1 
ATOM   6501  C  CA  . ARG C  1 62  ? 37.370  17.043  89.864  1.00 9.86   ? 149  ARG C CA  1 
ATOM   6502  C  C   . ARG C  1 62  ? 38.565  16.406  90.566  1.00 9.72   ? 149  ARG C C   1 
ATOM   6503  O  O   . ARG C  1 62  ? 39.552  17.077  90.842  1.00 8.87   ? 149  ARG C O   1 
ATOM   6504  C  CB  . ARG C  1 62  ? 36.446  17.766  90.853  1.00 9.76   ? 149  ARG C CB  1 
ATOM   6505  C  CG  . ARG C  1 62  ? 35.650  18.858  90.129  1.00 12.80  ? 149  ARG C CG  1 
ATOM   6506  C  CD  . ARG C  1 62  ? 34.602  19.541  90.982  1.00 16.21  ? 149  ARG C CD  1 
ATOM   6507  N  NE  . ARG C  1 62  ? 33.893  20.509  90.145  1.00 18.23  ? 149  ARG C NE  1 
ATOM   6508  C  CZ  . ARG C  1 62  ? 32.723  21.063  90.455  1.00 22.17  ? 149  ARG C CZ  1 
ATOM   6509  N  NH1 . ARG C  1 62  ? 32.117  20.769  91.601  1.00 20.96  ? 149  ARG C NH1 1 
ATOM   6510  N  NH2 . ARG C  1 62  ? 32.158  21.918  89.610  1.00 22.36  ? 149  ARG C NH2 1 
ATOM   6511  N  N   . HIS C  1 63  ? 38.481  15.104  90.838  1.00 10.06  ? 150  HIS C N   1 
ATOM   6512  C  CA  . HIS C  1 63  ? 39.598  14.368  91.468  1.00 9.96   ? 150  HIS C CA  1 
ATOM   6513  C  C   . HIS C  1 63  ? 40.794  14.082  90.534  1.00 10.26  ? 150  HIS C C   1 
ATOM   6514  O  O   . HIS C  1 63  ? 41.796  13.518  90.967  1.00 10.28  ? 150  HIS C O   1 
ATOM   6515  C  CB  . HIS C  1 63  ? 39.096  13.064  92.117  1.00 10.00  ? 150  HIS C CB  1 
ATOM   6516  C  CG  . HIS C  1 63  ? 38.038  13.281  93.158  1.00 8.43   ? 150  HIS C CG  1 
ATOM   6517  N  ND1 . HIS C  1 63  ? 38.328  13.626  94.460  1.00 10.88  ? 150  HIS C ND1 1 
ATOM   6518  C  CD2 . HIS C  1 63  ? 36.691  13.201  93.082  1.00 7.22   ? 150  HIS C CD2 1 
ATOM   6519  C  CE1 . HIS C  1 63  ? 37.205  13.747  95.143  1.00 7.09   ? 150  HIS C CE1 1 
ATOM   6520  N  NE2 . HIS C  1 63  ? 36.197  13.505  94.328  1.00 11.89  ? 150  HIS C NE2 1 
ATOM   6521  N  N   . ALA C  1 64  ? 40.689  14.465  89.261  1.00 9.84   ? 151  ALA C N   1 
ATOM   6522  C  CA  . ALA C  1 64  ? 41.851  14.399  88.369  1.00 9.99   ? 151  ALA C CA  1 
ATOM   6523  C  C   . ALA C  1 64  ? 42.908  15.436  88.804  1.00 9.56   ? 151  ALA C C   1 
ATOM   6524  O  O   . ALA C  1 64  ? 44.089  15.319  88.488  1.00 8.75   ? 151  ALA C O   1 
ATOM   6525  C  CB  . ALA C  1 64  ? 41.429  14.604  86.915  1.00 8.75   ? 151  ALA C CB  1 
ATOM   6526  N  N   . ASN C  1 65  ? 42.458  16.463  89.518  1.00 10.12  ? 152  ASN C N   1 
ATOM   6527  C  CA  . ASN C  1 65  ? 43.358  17.446  90.079  1.00 10.34  ? 152  ASN C CA  1 
ATOM   6528  C  C   . ASN C  1 65  ? 44.350  16.788  91.066  1.00 10.23  ? 152  ASN C C   1 
ATOM   6529  O  O   . ASN C  1 65  ? 43.938  16.200  92.069  1.00 10.72  ? 152  ASN C O   1 
ATOM   6530  C  CB  . ASN C  1 65  ? 42.505  18.529  90.732  1.00 10.91  ? 152  ASN C CB  1 
ATOM   6531  C  CG  . ASN C  1 65  ? 43.304  19.580  91.438  1.00 11.87  ? 152  ASN C CG  1 
ATOM   6532  O  OD1 . ASN C  1 65  ? 44.498  19.794  91.198  1.00 10.81  ? 152  ASN C OD1 1 
ATOM   6533  N  ND2 . ASN C  1 65  ? 42.624  20.257  92.355  1.00 12.73  ? 152  ASN C ND2 1 
ATOM   6534  N  N   . GLY C  1 66  ? 45.644  16.882  90.753  1.00 10.10  ? 153  GLY C N   1 
ATOM   6535  C  CA  . GLY C  1 66  ? 46.728  16.377  91.608  1.00 10.19  ? 153  GLY C CA  1 
ATOM   6536  C  C   . GLY C  1 66  ? 47.297  15.044  91.156  1.00 10.94  ? 153  GLY C C   1 
ATOM   6537  O  O   . GLY C  1 66  ? 48.178  14.482  91.831  1.00 10.02  ? 153  GLY C O   1 
ATOM   6538  N  N   . THR C  1 67  ? 46.824  14.547  89.997  1.00 10.36  ? 154  THR C N   1 
ATOM   6539  C  CA  . THR C  1 67  ? 47.218  13.208  89.534  1.00 10.61  ? 154  THR C CA  1 
ATOM   6540  C  C   . THR C  1 67  ? 48.642  13.117  88.956  1.00 11.24  ? 154  THR C C   1 
ATOM   6541  O  O   . THR C  1 67  ? 49.056  12.042  88.513  1.00 11.14  ? 154  THR C O   1 
ATOM   6542  C  CB  . THR C  1 67  ? 46.206  12.584  88.556  1.00 10.13  ? 154  THR C CB  1 
ATOM   6543  O  OG1 . THR C  1 67  ? 45.870  13.536  87.544  1.00 9.46   ? 154  THR C OG1 1 
ATOM   6544  C  CG2 . THR C  1 67  ? 44.919  12.153  89.305  1.00 8.13   ? 154  THR C CG2 1 
ATOM   6545  N  N   . ILE C  1 68  ? 49.399  14.218  88.993  1.00 10.96  ? 155  ILE C N   1 
ATOM   6546  C  CA  . ILE C  1 68  ? 50.860  14.100  88.842  1.00 11.99  ? 155  ILE C CA  1 
ATOM   6547  C  C   . ILE C  1 68  ? 51.491  13.155  89.902  1.00 12.39  ? 155  ILE C C   1 
ATOM   6548  O  O   . ILE C  1 68  ? 52.471  12.450  89.608  1.00 12.56  ? 155  ILE C O   1 
ATOM   6549  C  CB  . ILE C  1 68  ? 51.614  15.481  88.807  1.00 11.50  ? 155  ILE C CB  1 
ATOM   6550  C  CG1 . ILE C  1 68  ? 53.023  15.285  88.191  1.00 10.96  ? 155  ILE C CG1 1 
ATOM   6551  C  CG2 . ILE C  1 68  ? 51.640  16.161  90.192  1.00 12.81  ? 155  ILE C CG2 1 
ATOM   6552  C  CD1 . ILE C  1 68  ? 53.782  16.571  87.941  1.00 12.68  ? 155  ILE C CD1 1 
ATOM   6553  N  N   . HIS C  1 69  ? 50.904  13.135  91.101  1.00 12.96  ? 156  HIS C N   1 
ATOM   6554  C  CA  . HIS C  1 69  ? 51.408  12.348  92.228  1.00 13.95  ? 156  HIS C CA  1 
ATOM   6555  C  C   . HIS C  1 69  ? 51.401  10.849  91.875  1.00 13.28  ? 156  HIS C C   1 
ATOM   6556  O  O   . HIS C  1 69  ? 50.406  10.345  91.378  1.00 12.83  ? 156  HIS C O   1 
ATOM   6557  C  CB  . HIS C  1 69  ? 50.536  12.629  93.441  1.00 14.44  ? 156  HIS C CB  1 
ATOM   6558  C  CG  . HIS C  1 69  ? 51.142  12.214  94.744  1.00 18.09  ? 156  HIS C CG  1 
ATOM   6559  N  ND1 . HIS C  1 69  ? 52.271  12.808  95.264  1.00 20.25  ? 156  HIS C ND1 1 
ATOM   6560  C  CD2 . HIS C  1 69  ? 50.740  11.300  95.660  1.00 19.58  ? 156  HIS C CD2 1 
ATOM   6561  C  CE1 . HIS C  1 69  ? 52.554  12.260  96.436  1.00 21.60  ? 156  HIS C CE1 1 
ATOM   6562  N  NE2 . HIS C  1 69  ? 51.644  11.337  96.694  1.00 21.43  ? 156  HIS C NE2 1 
ATOM   6563  N  N   . ASP C  1 70  ? 52.523  10.161  92.099  1.00 13.15  ? 157  ASP C N   1 
ATOM   6564  C  CA  . ASP C  1 70  ? 52.685  8.751   91.688  1.00 12.74  ? 157  ASP C CA  1 
ATOM   6565  C  C   . ASP C  1 70  ? 52.027  7.718   92.616  1.00 12.20  ? 157  ASP C C   1 
ATOM   6566  O  O   . ASP C  1 70  ? 51.630  6.649   92.149  1.00 11.59  ? 157  ASP C O   1 
ATOM   6567  C  CB  . ASP C  1 70  ? 54.166  8.378   91.605  1.00 13.68  ? 157  ASP C CB  1 
ATOM   6568  C  CG  . ASP C  1 70  ? 54.918  9.172   90.558  1.00 16.06  ? 157  ASP C CG  1 
ATOM   6569  O  OD1 . ASP C  1 70  ? 54.406  9.348   89.435  1.00 14.52  ? 157  ASP C OD1 1 
ATOM   6570  O  OD2 . ASP C  1 70  ? 56.048  9.604   90.864  1.00 20.62  ? 157  ASP C OD2 1 
ATOM   6571  N  N   . ARG C  1 71  ? 51.994  7.987   93.926  1.00 10.78  ? 158  ARG C N   1 
ATOM   6572  C  CA  . ARG C  1 71  ? 51.593  6.948   94.889  1.00 11.37  ? 158  ARG C CA  1 
ATOM   6573  C  C   . ARG C  1 71  ? 50.483  7.456   95.793  1.00 10.97  ? 158  ARG C C   1 
ATOM   6574  O  O   . ARG C  1 71  ? 50.634  8.491   96.458  1.00 11.05  ? 158  ARG C O   1 
ATOM   6575  C  CB  . ARG C  1 71  ? 52.802  6.417   95.700  1.00 11.07  ? 158  ARG C CB  1 
ATOM   6576  C  CG  . ARG C  1 71  ? 53.903  5.740   94.836  1.00 11.77  ? 158  ARG C CG  1 
ATOM   6577  C  CD  . ARG C  1 71  ? 55.155  5.341   95.682  1.00 10.99  ? 158  ARG C CD  1 
ATOM   6578  N  NE  . ARG C  1 71  ? 55.785  6.537   96.247  1.00 12.30  ? 158  ARG C NE  1 
ATOM   6579  C  CZ  . ARG C  1 71  ? 56.572  7.380   95.576  1.00 14.86  ? 158  ARG C CZ  1 
ATOM   6580  N  NH1 . ARG C  1 71  ? 56.869  7.175   94.294  1.00 16.06  ? 158  ARG C NH1 1 
ATOM   6581  N  NH2 . ARG C  1 71  ? 57.052  8.461   96.184  1.00 16.44  ? 158  ARG C NH2 1 
ATOM   6582  N  N   . SER C  1 72  ? 49.356  6.740   95.768  1.00 10.33  ? 159  SER C N   1 
ATOM   6583  C  CA  . SER C  1 72  ? 48.211  7.025   96.638  1.00 9.05   ? 159  SER C CA  1 
ATOM   6584  C  C   . SER C  1 72  ? 47.467  5.721   96.964  1.00 9.02   ? 159  SER C C   1 
ATOM   6585  O  O   . SER C  1 72  ? 47.675  4.693   96.288  1.00 8.28   ? 159  SER C O   1 
ATOM   6586  C  CB  . SER C  1 72  ? 47.255  8.002   95.934  1.00 9.98   ? 159  SER C CB  1 
ATOM   6587  O  OG  . SER C  1 72  ? 46.348  7.285   95.100  1.00 9.70   ? 159  SER C OG  1 
ATOM   6588  N  N   . PRO C  1 73  ? 46.624  5.735   98.011  1.00 8.52   ? 160  PRO C N   1 
ATOM   6589  C  CA  . PRO C  1 73  ? 45.760  4.563   98.271  1.00 8.67   ? 160  PRO C CA  1 
ATOM   6590  C  C   . PRO C  1 73  ? 44.607  4.401   97.272  1.00 8.41   ? 160  PRO C C   1 
ATOM   6591  O  O   . PRO C  1 73  ? 43.799  3.495   97.444  1.00 9.33   ? 160  PRO C O   1 
ATOM   6592  C  CB  . PRO C  1 73  ? 45.198  4.836   99.676  1.00 8.83   ? 160  PRO C CB  1 
ATOM   6593  C  CG  . PRO C  1 73  ? 46.005  5.977   100.212 1.00 8.86   ? 160  PRO C CG  1 
ATOM   6594  C  CD  . PRO C  1 73  ? 46.442  6.781   99.037  1.00 8.12   ? 160  PRO C CD  1 
ATOM   6595  N  N   . PHE C  1 74  ? 44.547  5.240   96.235  1.00 8.36   ? 161  PHE C N   1 
ATOM   6596  C  CA  . PHE C  1 74  ? 43.413  5.235   95.291  1.00 7.83   ? 161  PHE C CA  1 
ATOM   6597  C  C   . PHE C  1 74  ? 43.802  4.650   93.947  1.00 8.44   ? 161  PHE C C   1 
ATOM   6598  O  O   . PHE C  1 74  ? 43.002  4.661   93.005  1.00 8.27   ? 161  PHE C O   1 
ATOM   6599  C  CB  . PHE C  1 74  ? 42.843  6.653   95.134  1.00 8.21   ? 161  PHE C CB  1 
ATOM   6600  C  CG  . PHE C  1 74  ? 42.880  7.447   96.417  1.00 7.41   ? 161  PHE C CG  1 
ATOM   6601  C  CD1 . PHE C  1 74  ? 43.589  8.657   96.490  1.00 6.94   ? 161  PHE C CD1 1 
ATOM   6602  C  CD2 . PHE C  1 74  ? 42.257  6.945   97.580  1.00 8.61   ? 161  PHE C CD2 1 
ATOM   6603  C  CE1 . PHE C  1 74  ? 43.656  9.386   97.703  1.00 5.77   ? 161  PHE C CE1 1 
ATOM   6604  C  CE2 . PHE C  1 74  ? 42.316  7.667   98.818  1.00 7.28   ? 161  PHE C CE2 1 
ATOM   6605  C  CZ  . PHE C  1 74  ? 43.016  8.886   98.864  1.00 8.16   ? 161  PHE C CZ  1 
ATOM   6606  N  N   . ARG C  1 75  ? 45.042  4.147   93.866  1.00 7.45   ? 162  ARG C N   1 
ATOM   6607  C  CA  . ARG C  1 75  ? 45.571  3.567   92.639  1.00 6.76   ? 162  ARG C CA  1 
ATOM   6608  C  C   . ARG C  1 75  ? 45.340  2.057   92.586  1.00 6.69   ? 162  ARG C C   1 
ATOM   6609  O  O   . ARG C  1 75  ? 45.283  1.388   93.624  1.00 6.72   ? 162  ARG C O   1 
ATOM   6610  C  CB  . ARG C  1 75  ? 47.063  3.904   92.450  1.00 5.73   ? 162  ARG C CB  1 
ATOM   6611  C  CG  . ARG C  1 75  ? 47.363  5.435   92.401  1.00 7.24   ? 162  ARG C CG  1 
ATOM   6612  C  CD  . ARG C  1 75  ? 48.641  5.753   91.610  1.00 7.61   ? 162  ARG C CD  1 
ATOM   6613  N  NE  . ARG C  1 75  ? 48.424  5.639   90.149  1.00 8.64   ? 162  ARG C NE  1 
ATOM   6614  C  CZ  . ARG C  1 75  ? 49.333  5.954   89.221  1.00 9.40   ? 162  ARG C CZ  1 
ATOM   6615  N  NH1 . ARG C  1 75  ? 50.561  6.368   89.579  1.00 7.79   ? 162  ARG C NH1 1 
ATOM   6616  N  NH2 . ARG C  1 75  ? 49.029  5.831   87.930  1.00 7.16   ? 162  ARG C NH2 1 
ATOM   6617  N  N   . ALA C  1 76  ? 45.200  1.530   91.377  1.00 6.80   ? 163  ALA C N   1 
ATOM   6618  C  CA  . ALA C  1 76  ? 45.024  0.078   91.185  1.00 7.52   ? 163  ALA C CA  1 
ATOM   6619  C  C   . ALA C  1 76  ? 45.488  -0.341  89.804  1.00 8.13   ? 163  ALA C C   1 
ATOM   6620  O  O   . ALA C  1 76  ? 45.379  0.440   88.847  1.00 7.96   ? 163  ALA C O   1 
ATOM   6621  C  CB  . ALA C  1 76  ? 43.550  -0.319  91.381  1.00 8.18   ? 163  ALA C CB  1 
ATOM   6622  N  N   . LEU C  1 77  ? 45.982  -1.578  89.689  1.00 7.30   ? 164  LEU C N   1 
ATOM   6623  C  CA  . LEU C  1 77  ? 46.228  -2.143  88.365  1.00 7.29   ? 164  LEU C CA  1 
ATOM   6624  C  C   . LEU C  1 77  ? 44.870  -2.541  87.785  1.00 7.96   ? 164  LEU C C   1 
ATOM   6625  O  O   . LEU C  1 77  ? 44.100  -3.275  88.424  1.00 7.76   ? 164  LEU C O   1 
ATOM   6626  C  CB  . LEU C  1 77  ? 47.166  -3.357  88.421  1.00 7.99   ? 164  LEU C CB  1 
ATOM   6627  C  CG  . LEU C  1 77  ? 47.438  -4.031  87.063  1.00 7.10   ? 164  LEU C CG  1 
ATOM   6628  C  CD1 . LEU C  1 77  ? 48.072  -3.056  86.041  1.00 6.86   ? 164  LEU C CD1 1 
ATOM   6629  C  CD2 . LEU C  1 77  ? 48.314  -5.295  87.209  1.00 6.96   ? 164  LEU C CD2 1 
ATOM   6630  N  N   . ILE C  1 78  ? 44.592  -2.047  86.579  1.00 6.93   ? 165  ILE C N   1 
ATOM   6631  C  CA  . ILE C  1 78  ? 43.370  -2.377  85.846  1.00 7.06   ? 165  ILE C CA  1 
ATOM   6632  C  C   . ILE C  1 78  ? 43.759  -2.903  84.475  1.00 7.10   ? 165  ILE C C   1 
ATOM   6633  O  O   . ILE C  1 78  ? 44.811  -2.530  83.935  1.00 6.40   ? 165  ILE C O   1 
ATOM   6634  C  CB  . ILE C  1 78  ? 42.430  -1.152  85.665  1.00 7.54   ? 165  ILE C CB  1 
ATOM   6635  C  CG1 . ILE C  1 78  ? 43.192  0.055   85.077  1.00 6.58   ? 165  ILE C CG1 1 
ATOM   6636  C  CG2 . ILE C  1 78  ? 41.746  -0.779  86.995  1.00 6.73   ? 165  ILE C CG2 1 
ATOM   6637  C  CD1 . ILE C  1 78  ? 42.248  1.139   84.450  1.00 8.13   ? 165  ILE C CD1 1 
ATOM   6638  N  N   . SER C  1 79  ? 42.917  -3.780  83.929  1.00 6.61   ? 166  SER C N   1 
ATOM   6639  C  CA  . SER C  1 79  ? 43.106  -4.324  82.597  1.00 6.66   ? 166  SER C CA  1 
ATOM   6640  C  C   . SER C  1 79  ? 41.794  -4.238  81.814  1.00 7.33   ? 166  SER C C   1 
ATOM   6641  O  O   . SER C  1 79  ? 40.675  -4.202  82.399  1.00 7.41   ? 166  SER C O   1 
ATOM   6642  C  CB  . SER C  1 79  ? 43.595  -5.783  82.652  1.00 6.80   ? 166  SER C CB  1 
ATOM   6643  O  OG  . SER C  1 79  ? 42.590  -6.634  83.208  1.00 9.82   ? 166  SER C OG  1 
ATOM   6644  N  N   . TRP C  1 80  ? 41.934  -4.187  80.494  1.00 6.65   ? 167  TRP C N   1 
ATOM   6645  C  CA  . TRP C  1 80  ? 40.780  -4.062  79.618  1.00 6.92   ? 167  TRP C CA  1 
ATOM   6646  C  C   . TRP C  1 80  ? 41.084  -4.604  78.230  1.00 8.12   ? 167  TRP C C   1 
ATOM   6647  O  O   . TRP C  1 80  ? 42.262  -4.794  77.870  1.00 7.77   ? 167  TRP C O   1 
ATOM   6648  C  CB  . TRP C  1 80  ? 40.242  -2.617  79.571  1.00 6.72   ? 167  TRP C CB  1 
ATOM   6649  C  CG  . TRP C  1 80  ? 41.186  -1.563  78.993  1.00 6.40   ? 167  TRP C CG  1 
ATOM   6650  C  CD1 . TRP C  1 80  ? 41.156  -1.061  77.709  1.00 6.39   ? 167  TRP C CD1 1 
ATOM   6651  C  CD2 . TRP C  1 80  ? 42.273  -0.872  79.666  1.00 6.47   ? 167  TRP C CD2 1 
ATOM   6652  N  NE1 . TRP C  1 80  ? 42.155  -0.111  77.547  1.00 5.88   ? 167  TRP C NE1 1 
ATOM   6653  C  CE2 . TRP C  1 80  ? 42.851  0.018   78.724  1.00 5.44   ? 167  TRP C CE2 1 
ATOM   6654  C  CE3 . TRP C  1 80  ? 42.826  -0.934  80.963  1.00 5.77   ? 167  TRP C CE3 1 
ATOM   6655  C  CZ2 . TRP C  1 80  ? 43.940  0.852   79.038  1.00 8.00   ? 167  TRP C CZ2 1 
ATOM   6656  C  CZ3 . TRP C  1 80  ? 43.914  -0.087  81.284  1.00 6.76   ? 167  TRP C CZ3 1 
ATOM   6657  C  CH2 . TRP C  1 80  ? 44.454  0.789   80.324  1.00 6.71   ? 167  TRP C CH2 1 
ATOM   6658  N  N   . GLU C  1 81  ? 40.018  -4.864  77.459  1.00 7.61   ? 168  GLU C N   1 
ATOM   6659  C  CA  . GLU C  1 81  ? 40.158  -5.383  76.093  1.00 10.26  ? 168  GLU C CA  1 
ATOM   6660  C  C   . GLU C  1 81  ? 40.987  -4.402  75.238  1.00 9.23   ? 168  GLU C C   1 
ATOM   6661  O  O   . GLU C  1 81  ? 40.676  -3.207  75.163  1.00 8.69   ? 168  GLU C O   1 
ATOM   6662  C  CB  . GLU C  1 81  ? 38.766  -5.560  75.457  1.00 9.84   ? 168  GLU C CB  1 
ATOM   6663  C  CG  . GLU C  1 81  ? 38.780  -6.267  74.123  1.00 12.74  ? 168  GLU C CG  1 
ATOM   6664  C  CD  . GLU C  1 81  ? 37.368  -6.511  73.604  1.00 14.92  ? 168  GLU C CD  1 
ATOM   6665  O  OE1 . GLU C  1 81  ? 36.602  -7.259  74.250  1.00 17.43  ? 168  GLU C OE1 1 
ATOM   6666  O  OE2 . GLU C  1 81  ? 37.013  -5.914  72.570  1.00 20.14  ? 168  GLU C OE2 1 
ATOM   6667  N  N   . MET C  1 82  ? 42.036  -4.925  74.605  1.00 9.45   ? 169  MET C N   1 
ATOM   6668  C  CA  . MET C  1 82  ? 42.936  -4.107  73.778  1.00 9.97   ? 169  MET C CA  1 
ATOM   6669  C  C   . MET C  1 82  ? 42.163  -3.238  72.794  1.00 9.00   ? 169  MET C C   1 
ATOM   6670  O  O   . MET C  1 82  ? 41.308  -3.749  72.055  1.00 8.77   ? 169  MET C O   1 
ATOM   6671  C  CB  . MET C  1 82  ? 43.856  -5.049  72.991  1.00 9.62   ? 169  MET C CB  1 
ATOM   6672  C  CG  . MET C  1 82  ? 44.909  -4.321  72.183  1.00 10.04  ? 169  MET C CG  1 
ATOM   6673  S  SD  . MET C  1 82  ? 46.131  -5.403  71.426  1.00 10.12  ? 169  MET C SD  1 
ATOM   6674  C  CE  . MET C  1 82  ? 45.147  -6.243  70.193  1.00 9.06   ? 169  MET C CE  1 
ATOM   6675  N  N   . GLY C  1 83  ? 42.468  -1.940  72.766  1.00 9.17   ? 170  GLY C N   1 
ATOM   6676  C  CA  . GLY C  1 83  ? 41.879  -1.025  71.779  1.00 9.12   ? 170  GLY C CA  1 
ATOM   6677  C  C   . GLY C  1 83  ? 40.840  -0.087  72.381  1.00 9.57   ? 170  GLY C C   1 
ATOM   6678  O  O   . GLY C  1 83  ? 40.734  1.086   71.990  1.00 9.18   ? 170  GLY C O   1 
ATOM   6679  N  N   . GLN C  1 84  ? 40.073  -0.604  73.340  1.00 9.85   ? 171  GLN C N   1 
ATOM   6680  C  CA  . GLN C  1 84  ? 39.160  0.238   74.121  1.00 10.65  ? 171  GLN C CA  1 
ATOM   6681  C  C   . GLN C  1 84  ? 39.941  1.221   74.985  1.00 9.52   ? 171  GLN C C   1 
ATOM   6682  O  O   . GLN C  1 84  ? 41.094  0.972   75.334  1.00 9.00   ? 171  GLN C O   1 
ATOM   6683  C  CB  . GLN C  1 84  ? 38.246  -0.622  74.999  1.00 9.86   ? 171  GLN C CB  1 
ATOM   6684  C  CG  . GLN C  1 84  ? 37.227  -1.456  74.179  1.00 12.32  ? 171  GLN C CG  1 
ATOM   6685  C  CD  . GLN C  1 84  ? 36.203  -2.163  75.050  1.00 13.56  ? 171  GLN C CD  1 
ATOM   6686  O  OE1 . GLN C  1 84  ? 36.459  -2.467  76.214  1.00 14.14  ? 171  GLN C OE1 1 
ATOM   6687  N  NE2 . GLN C  1 84  ? 35.014  -2.423  74.478  1.00 19.68  ? 171  GLN C NE2 1 
ATOM   6688  N  N   . ALA C  1 85  ? 39.315  2.358   75.298  1.00 9.38   ? 172  ALA C N   1 
ATOM   6689  C  CA  . ALA C  1 85  ? 39.837  3.237   76.332  1.00 8.82   ? 172  ALA C CA  1 
ATOM   6690  C  C   . ALA C  1 85  ? 39.357  2.719   77.713  1.00 8.60   ? 172  ALA C C   1 
ATOM   6691  O  O   . ALA C  1 85  ? 38.321  2.062   77.810  1.00 9.05   ? 172  ALA C O   1 
ATOM   6692  C  CB  . ALA C  1 85  ? 39.401  4.680   76.090  1.00 8.34   ? 172  ALA C CB  1 
ATOM   6693  N  N   . PRO C  1 86  ? 40.126  3.002   78.779  1.00 8.60   ? 173  PRO C N   1 
ATOM   6694  C  CA  . PRO C  1 86  ? 39.784  2.512   80.112  1.00 8.20   ? 173  PRO C CA  1 
ATOM   6695  C  C   . PRO C  1 86  ? 38.718  3.350   80.837  1.00 8.94   ? 173  PRO C C   1 
ATOM   6696  O  O   . PRO C  1 86  ? 38.978  4.505   81.204  1.00 8.90   ? 173  PRO C O   1 
ATOM   6697  C  CB  . PRO C  1 86  ? 41.132  2.551   80.843  1.00 7.63   ? 173  PRO C CB  1 
ATOM   6698  C  CG  . PRO C  1 86  ? 41.883  3.679   80.201  1.00 8.10   ? 173  PRO C CG  1 
ATOM   6699  C  CD  . PRO C  1 86  ? 41.362  3.810   78.785  1.00 8.49   ? 173  PRO C CD  1 
ATOM   6700  N  N   . SER C  1 87  ? 37.523  2.777   81.019  1.00 8.90   ? 174  SER C N   1 
ATOM   6701  C  CA  . SER C  1 87  ? 36.432  3.433   81.742  1.00 8.85   ? 174  SER C CA  1 
ATOM   6702  C  C   . SER C  1 87  ? 36.115  2.668   83.046  1.00 9.39   ? 174  SER C C   1 
ATOM   6703  O  O   . SER C  1 87  ? 36.536  1.526   83.205  1.00 8.73   ? 174  SER C O   1 
ATOM   6704  C  CB  . SER C  1 87  ? 35.164  3.524   80.860  1.00 8.84   ? 174  SER C CB  1 
ATOM   6705  O  OG  . SER C  1 87  ? 34.472  2.277   80.808  1.00 9.72   ? 174  SER C OG  1 
ATOM   6706  N  N   . PRO C  1 88  ? 35.322  3.276   83.953  1.00 9.81   ? 175  PRO C N   1 
ATOM   6707  C  CA  . PRO C  1 88  ? 34.864  2.535   85.140  1.00 9.99   ? 175  PRO C CA  1 
ATOM   6708  C  C   . PRO C  1 88  ? 33.965  1.338   84.767  1.00 10.09  ? 175  PRO C C   1 
ATOM   6709  O  O   . PRO C  1 88  ? 33.674  0.501   85.617  1.00 10.82  ? 175  PRO C O   1 
ATOM   6710  C  CB  . PRO C  1 88  ? 34.049  3.587   85.922  1.00 9.84   ? 175  PRO C CB  1 
ATOM   6711  C  CG  . PRO C  1 88  ? 34.483  4.932   85.373  1.00 10.91  ? 175  PRO C CG  1 
ATOM   6712  C  CD  . PRO C  1 88  ? 34.807  4.666   83.934  1.00 9.82   ? 175  PRO C CD  1 
ATOM   6713  N  N   . TYR C  1 89  ? 33.562  1.247   83.502  1.00 9.99   ? 176  TYR C N   1 
ATOM   6714  C  CA  . TYR C  1 89  ? 32.574  0.242   83.082  1.00 9.88   ? 176  TYR C CA  1 
ATOM   6715  C  C   . TYR C  1 89  ? 33.140  -0.965  82.347  1.00 9.74   ? 176  TYR C C   1 
ATOM   6716  O  O   . TYR C  1 89  ? 32.446  -1.994  82.233  1.00 10.55  ? 176  TYR C O   1 
ATOM   6717  C  CB  . TYR C  1 89  ? 31.496  0.895   82.187  1.00 8.71   ? 176  TYR C CB  1 
ATOM   6718  C  CG  . TYR C  1 89  ? 31.014  2.239   82.702  1.00 6.95   ? 176  TYR C CG  1 
ATOM   6719  C  CD1 . TYR C  1 89  ? 31.007  3.357   81.864  1.00 7.20   ? 176  TYR C CD1 1 
ATOM   6720  C  CD2 . TYR C  1 89  ? 30.586  2.398   84.042  1.00 7.32   ? 176  TYR C CD2 1 
ATOM   6721  C  CE1 . TYR C  1 89  ? 30.579  4.612   82.324  1.00 7.16   ? 176  TYR C CE1 1 
ATOM   6722  C  CE2 . TYR C  1 89  ? 30.151  3.664   84.516  1.00 9.44   ? 176  TYR C CE2 1 
ATOM   6723  C  CZ  . TYR C  1 89  ? 30.161  4.760   83.646  1.00 7.83   ? 176  TYR C CZ  1 
ATOM   6724  O  OH  . TYR C  1 89  ? 29.728  6.013   84.064  1.00 7.68   ? 176  TYR C OH  1 
ATOM   6725  N  N   . ASN C  1 90  ? 34.366  -0.854  81.829  1.00 9.04   ? 177  ASN C N   1 
ATOM   6726  C  CA  . ASN C  1 90  ? 34.945  -1.957  81.035  1.00 9.41   ? 177  ASN C CA  1 
ATOM   6727  C  C   . ASN C  1 90  ? 36.289  -2.497  81.560  1.00 9.95   ? 177  ASN C C   1 
ATOM   6728  O  O   . ASN C  1 90  ? 36.970  -3.256  80.860  1.00 10.57  ? 177  ASN C O   1 
ATOM   6729  C  CB  . ASN C  1 90  ? 35.121  -1.520  79.578  1.00 9.49   ? 177  ASN C CB  1 
ATOM   6730  C  CG  . ASN C  1 90  ? 36.272  -0.517  79.407  1.00 10.06  ? 177  ASN C CG  1 
ATOM   6731  O  OD1 . ASN C  1 90  ? 36.609  0.244   80.340  1.00 10.33  ? 177  ASN C OD1 1 
ATOM   6732  N  ND2 . ASN C  1 90  ? 36.891  -0.523  78.224  1.00 11.23  ? 177  ASN C ND2 1 
ATOM   6733  N  N   . THR C  1 91  ? 36.653  -2.122  82.785  1.00 9.30   ? 178  THR C N   1 
ATOM   6734  C  CA  . THR C  1 91  ? 37.964  -2.433  83.339  1.00 10.23  ? 178  THR C CA  1 
ATOM   6735  C  C   . THR C  1 91  ? 37.861  -3.440  84.498  1.00 10.55  ? 178  THR C C   1 
ATOM   6736  O  O   . THR C  1 91  ? 36.927  -3.358  85.330  1.00 10.75  ? 178  THR C O   1 
ATOM   6737  C  CB  . THR C  1 91  ? 38.652  -1.161  83.859  1.00 10.59  ? 178  THR C CB  1 
ATOM   6738  O  OG1 . THR C  1 91  ? 37.701  -0.386  84.608  1.00 9.22   ? 178  THR C OG1 1 
ATOM   6739  C  CG2 . THR C  1 91  ? 39.196  -0.304  82.688  1.00 9.88   ? 178  THR C CG2 1 
ATOM   6740  N  N   . ARG C  1 92  ? 38.814  -4.373  84.536  1.00 10.32  ? 179  ARG C N   1 
ATOM   6741  C  CA  . ARG C  1 92  ? 38.934  -5.379  85.599  1.00 10.69  ? 179  ARG C CA  1 
ATOM   6742  C  C   . ARG C  1 92  ? 40.043  -4.929  86.544  1.00 9.92   ? 179  ARG C C   1 
ATOM   6743  O  O   . ARG C  1 92  ? 41.136  -4.618  86.091  1.00 8.70   ? 179  ARG C O   1 
ATOM   6744  C  CB  . ARG C  1 92  ? 39.304  -6.744  84.982  1.00 10.07  ? 179  ARG C CB  1 
ATOM   6745  C  CG  . ARG C  1 92  ? 39.659  -7.839  86.006  1.00 12.04  ? 179  ARG C CG  1 
ATOM   6746  C  CD  . ARG C  1 92  ? 40.136  -9.140  85.334  1.00 14.57  ? 179  ARG C CD  1 
ATOM   6747  N  NE  . ARG C  1 92  ? 39.173  -9.615  84.332  1.00 24.90  ? 179  ARG C NE  1 
ATOM   6748  C  CZ  . ARG C  1 92  ? 39.485  -10.296 83.222  1.00 28.01  ? 179  ARG C CZ  1 
ATOM   6749  N  NH1 . ARG C  1 92  ? 40.747  -10.607 82.932  1.00 29.97  ? 179  ARG C NH1 1 
ATOM   6750  N  NH2 . ARG C  1 92  ? 38.520  -10.660 82.383  1.00 30.09  ? 179  ARG C NH2 1 
ATOM   6751  N  N   . VAL C  1 93  ? 39.766  -4.894  87.849  1.00 9.26   ? 180  VAL C N   1 
ATOM   6752  C  CA  . VAL C  1 93  ? 40.810  -4.582  88.835  1.00 8.63   ? 180  VAL C CA  1 
ATOM   6753  C  C   . VAL C  1 93  ? 41.640  -5.845  89.097  1.00 9.22   ? 180  VAL C C   1 
ATOM   6754  O  O   . VAL C  1 93  ? 41.116  -6.867  89.557  1.00 8.18   ? 180  VAL C O   1 
ATOM   6755  C  CB  . VAL C  1 93  ? 40.224  -4.003  90.156  1.00 9.32   ? 180  VAL C CB  1 
ATOM   6756  C  CG1 . VAL C  1 93  ? 41.323  -3.761  91.176  1.00 8.42   ? 180  VAL C CG1 1 
ATOM   6757  C  CG2 . VAL C  1 93  ? 39.470  -2.653  89.881  1.00 7.72   ? 180  VAL C CG2 1 
ATOM   6758  N  N   . GLU C  1 94  ? 42.932  -5.750  88.802  1.00 8.15   ? 181  GLU C N   1 
ATOM   6759  C  CA  . GLU C  1 94  ? 43.851  -6.886  88.887  1.00 8.50   ? 181  GLU C CA  1 
ATOM   6760  C  C   . GLU C  1 94  ? 44.425  -6.980  90.297  1.00 8.69   ? 181  GLU C C   1 
ATOM   6761  O  O   . GLU C  1 94  ? 44.637  -8.062  90.804  1.00 9.34   ? 181  GLU C O   1 
ATOM   6762  C  CB  . GLU C  1 94  ? 45.001  -6.741  87.850  1.00 8.59   ? 181  GLU C CB  1 
ATOM   6763  C  CG  . GLU C  1 94  ? 44.568  -6.848  86.368  1.00 9.70   ? 181  GLU C CG  1 
ATOM   6764  C  CD  . GLU C  1 94  ? 44.333  -8.297  85.891  1.00 11.58  ? 181  GLU C CD  1 
ATOM   6765  O  OE1 . GLU C  1 94  ? 44.950  -9.224  86.454  1.00 9.15   ? 181  GLU C OE1 1 
ATOM   6766  O  OE2 . GLU C  1 94  ? 43.542  -8.497  84.937  1.00 12.08  ? 181  GLU C OE2 1 
ATOM   6767  N  N   . CYS C  1 95  ? 44.672  -5.827  90.921  1.00 8.93   ? 182  CYS C N   1 
ATOM   6768  C  CA  . CYS C  1 95  ? 45.231  -5.730  92.269  1.00 8.55   ? 182  CYS C CA  1 
ATOM   6769  C  C   . CYS C  1 95  ? 45.306  -4.242  92.637  1.00 8.54   ? 182  CYS C C   1 
ATOM   6770  O  O   . CYS C  1 95  ? 45.123  -3.371  91.771  1.00 7.86   ? 182  CYS C O   1 
ATOM   6771  C  CB  . CYS C  1 95  ? 46.601  -6.440  92.412  1.00 8.20   ? 182  CYS C CB  1 
ATOM   6772  S  SG  . CYS C  1 95  ? 47.817  -6.154  91.134  1.00 10.26  ? 182  CYS C SG  1 
ATOM   6773  N  N   . ILE C  1 96  ? 45.565  -3.970  93.912  1.00 7.99   ? 183  ILE C N   1 
ATOM   6774  C  CA  . ILE C  1 96  ? 45.539  -2.607  94.444  1.00 7.46   ? 183  ILE C CA  1 
ATOM   6775  C  C   . ILE C  1 96  ? 46.975  -2.138  94.736  1.00 7.33   ? 183  ILE C C   1 
ATOM   6776  O  O   . ILE C  1 96  ? 47.747  -2.847  95.374  1.00 7.48   ? 183  ILE C O   1 
ATOM   6777  C  CB  . ILE C  1 96  ? 44.680  -2.486  95.744  1.00 7.16   ? 183  ILE C CB  1 
ATOM   6778  C  CG1 . ILE C  1 96  ? 43.295  -3.174  95.583  1.00 6.93   ? 183  ILE C CG1 1 
ATOM   6779  C  CG2 . ILE C  1 96  ? 44.531  -1.000  96.154  1.00 7.65   ? 183  ILE C CG2 1 
ATOM   6780  C  CD1 . ILE C  1 96  ? 42.437  -2.684  94.419  1.00 4.94   ? 183  ILE C CD1 1 
ATOM   6781  N  N   . GLY C  1 97  ? 47.325  -0.960  94.238  1.00 7.87   ? 184  GLY C N   1 
ATOM   6782  C  CA  . GLY C  1 97  ? 48.658  -0.393  94.468  1.00 7.12   ? 184  GLY C CA  1 
ATOM   6783  C  C   . GLY C  1 97  ? 49.141  0.522   93.359  1.00 7.58   ? 184  GLY C C   1 
ATOM   6784  O  O   . GLY C  1 97  ? 48.355  0.890   92.466  1.00 7.84   ? 184  GLY C O   1 
ATOM   6785  N  N   . TRP C  1 98  ? 50.440  0.859   93.415  1.00 7.58   ? 185  TRP C N   1 
ATOM   6786  C  CA  . TRP C  1 98  ? 51.018  1.964   92.629  1.00 8.30   ? 185  TRP C CA  1 
ATOM   6787  C  C   . TRP C  1 98  ? 52.292  1.567   91.868  1.00 7.51   ? 185  TRP C C   1 
ATOM   6788  O  O   . TRP C  1 98  ? 53.023  2.432   91.358  1.00 8.64   ? 185  TRP C O   1 
ATOM   6789  C  CB  . TRP C  1 98  ? 51.228  3.223   93.506  1.00 8.13   ? 185  TRP C CB  1 
ATOM   6790  C  CG  . TRP C  1 98  ? 51.751  2.954   94.896  1.00 8.12   ? 185  TRP C CG  1 
ATOM   6791  C  CD1 . TRP C  1 98  ? 51.105  3.242   96.079  1.00 10.26  ? 185  TRP C CD1 1 
ATOM   6792  C  CD2 . TRP C  1 98  ? 53.017  2.360   95.268  1.00 8.30   ? 185  TRP C CD2 1 
ATOM   6793  N  NE1 . TRP C  1 98  ? 51.888  2.859   97.155  1.00 9.25   ? 185  TRP C NE1 1 
ATOM   6794  C  CE2 . TRP C  1 98  ? 53.065  2.329   96.690  1.00 8.02   ? 185  TRP C CE2 1 
ATOM   6795  C  CE3 . TRP C  1 98  ? 54.116  1.865   94.543  1.00 7.64   ? 185  TRP C CE3 1 
ATOM   6796  C  CZ2 . TRP C  1 98  ? 54.175  1.800   97.411  1.00 9.10   ? 185  TRP C CZ2 1 
ATOM   6797  C  CZ3 . TRP C  1 98  ? 55.225  1.332   95.251  1.00 8.94   ? 185  TRP C CZ3 1 
ATOM   6798  C  CH2 . TRP C  1 98  ? 55.238  1.304   96.677  1.00 9.66   ? 185  TRP C CH2 1 
ATOM   6799  N  N   . SER C  1 99  ? 52.547  0.258   91.797  1.00 7.97   ? 186  SER C N   1 
ATOM   6800  C  CA  . SER C  1 99  ? 53.599  -0.302  90.946  1.00 8.16   ? 186  SER C CA  1 
ATOM   6801  C  C   . SER C  1 99  ? 53.165  -1.726  90.640  1.00 8.45   ? 186  SER C C   1 
ATOM   6802  O  O   . SER C  1 99  ? 52.609  -2.405  91.513  1.00 8.30   ? 186  SER C O   1 
ATOM   6803  C  CB  . SER C  1 99  ? 54.962  -0.290  91.651  1.00 8.57   ? 186  SER C CB  1 
ATOM   6804  O  OG  . SER C  1 99  ? 55.951  -0.832  90.785  1.00 8.34   ? 186  SER C OG  1 
ATOM   6805  N  N   . SER C  1 100 ? 53.344  -2.176  89.404  1.00 8.55   ? 187  SER C N   1 
ATOM   6806  C  CA  . SER C  1 100 ? 52.815  -3.497  89.061  1.00 7.55   ? 187  SER C CA  1 
ATOM   6807  C  C   . SER C  1 100 ? 53.600  -4.248  87.994  1.00 7.47   ? 187  SER C C   1 
ATOM   6808  O  O   . SER C  1 100 ? 54.431  -3.687  87.284  1.00 7.11   ? 187  SER C O   1 
ATOM   6809  C  CB  . SER C  1 100 ? 51.327  -3.405  88.599  1.00 7.26   ? 187  SER C CB  1 
ATOM   6810  O  OG  . SER C  1 100 ? 51.243  -3.074  87.204  1.00 8.60   ? 187  SER C OG  1 
ATOM   6811  N  N   . THR C  1 101 ? 53.271  -5.531  87.889  1.00 6.63   ? 188  THR C N   1 
ATOM   6812  C  CA  . THR C  1 101 ? 53.583  -6.357  86.722  1.00 6.93   ? 188  THR C CA  1 
ATOM   6813  C  C   . THR C  1 101 ? 52.483  -7.422  86.563  1.00 7.47   ? 188  THR C C   1 
ATOM   6814  O  O   . THR C  1 101 ? 51.644  -7.633  87.452  1.00 6.78   ? 188  THR C O   1 
ATOM   6815  C  CB  . THR C  1 101 ? 55.009  -7.012  86.805  1.00 7.00   ? 188  THR C CB  1 
ATOM   6816  O  OG1 . THR C  1 101 ? 55.299  -7.695  85.562  1.00 7.63   ? 188  THR C OG1 1 
ATOM   6817  C  CG2 . THR C  1 101 ? 55.086  -8.020  87.974  1.00 8.58   ? 188  THR C CG2 1 
ATOM   6818  N  N   . SER C  1 102 ? 52.455  -8.066  85.403  1.00 7.83   ? 189  SER C N   1 
ATOM   6819  C  CA  . SER C  1 102 ? 51.466  -9.086  85.146  1.00 7.96   ? 189  SER C CA  1 
ATOM   6820  C  C   . SER C  1 102 ? 51.950  -9.960  83.981  1.00 7.80   ? 189  SER C C   1 
ATOM   6821  O  O   . SER C  1 102 ? 52.570  -9.452  83.052  1.00 8.15   ? 189  SER C O   1 
ATOM   6822  C  CB  . SER C  1 102 ? 50.116  -8.449  84.781  1.00 6.78   ? 189  SER C CB  1 
ATOM   6823  O  OG  . SER C  1 102 ? 49.091  -9.420  84.736  1.00 8.35   ? 189  SER C OG  1 
ATOM   6824  N  N   . CYS C  1 103 ? 51.643  -11.254 84.041  1.00 7.61   ? 190  CYS C N   1 
ATOM   6825  C  CA  . CYS C  1 103 ? 51.902  -12.179 82.927  1.00 8.29   ? 190  CYS C CA  1 
ATOM   6826  C  C   . CYS C  1 103 ? 51.047  -13.438 83.003  1.00 8.40   ? 190  CYS C C   1 
ATOM   6827  O  O   . CYS C  1 103 ? 50.613  -13.835 84.088  1.00 8.64   ? 190  CYS C O   1 
ATOM   6828  C  CB  . CYS C  1 103 ? 53.396  -12.556 82.813  1.00 7.60   ? 190  CYS C CB  1 
ATOM   6829  S  SG  . CYS C  1 103 ? 54.245  -13.037 84.368  1.00 9.14   ? 190  CYS C SG  1 
ATOM   6830  N  N   . HIS C  1 104 ? 50.787  -14.033 81.840  1.00 9.11   ? 191  HIS C N   1 
ATOM   6831  C  CA  . HIS C  1 104 ? 50.081  -15.307 81.751  1.00 10.11  ? 191  HIS C CA  1 
ATOM   6832  C  C   . HIS C  1 104 ? 51.071  -16.452 81.511  1.00 10.50  ? 191  HIS C C   1 
ATOM   6833  O  O   . HIS C  1 104 ? 51.952  -16.345 80.657  1.00 11.25  ? 191  HIS C O   1 
ATOM   6834  C  CB  . HIS C  1 104 ? 49.043  -15.249 80.623  1.00 10.34  ? 191  HIS C CB  1 
ATOM   6835  C  CG  . HIS C  1 104 ? 47.893  -16.199 80.799  1.00 9.16   ? 191  HIS C CG  1 
ATOM   6836  N  ND1 . HIS C  1 104 ? 47.988  -17.544 80.521  1.00 11.29  ? 191  HIS C ND1 1 
ATOM   6837  C  CD2 . HIS C  1 104 ? 46.608  -15.983 81.182  1.00 8.85   ? 191  HIS C CD2 1 
ATOM   6838  C  CE1 . HIS C  1 104 ? 46.816  -18.124 80.733  1.00 9.92   ? 191  HIS C CE1 1 
ATOM   6839  N  NE2 . HIS C  1 104 ? 45.958  -17.198 81.134  1.00 11.12  ? 191  HIS C NE2 1 
ATOM   6840  N  N   . ASP C  1 105 ? 50.927  -17.540 82.264  1.00 10.71  ? 192  ASP C N   1 
ATOM   6841  C  CA  . ASP C  1 105 ? 51.850  -18.663 82.144  1.00 11.44  ? 192  ASP C CA  1 
ATOM   6842  C  C   . ASP C  1 105 ? 51.350  -19.742 81.170  1.00 11.30  ? 192  ASP C C   1 
ATOM   6843  O  O   . ASP C  1 105 ? 51.952  -20.809 81.046  1.00 11.41  ? 192  ASP C O   1 
ATOM   6844  C  CB  . ASP C  1 105 ? 52.173  -19.238 83.537  1.00 11.53  ? 192  ASP C CB  1 
ATOM   6845  C  CG  . ASP C  1 105 ? 50.956  -19.870 84.244  1.00 10.91  ? 192  ASP C CG  1 
ATOM   6846  O  OD1 . ASP C  1 105 ? 49.871  -20.065 83.649  1.00 12.45  ? 192  ASP C OD1 1 
ATOM   6847  O  OD2 . ASP C  1 105 ? 51.104  -20.202 85.429  1.00 14.00  ? 192  ASP C OD2 1 
ATOM   6848  N  N   . GLY C  1 106 ? 50.242  -19.457 80.486  1.00 11.51  ? 193  GLY C N   1 
ATOM   6849  C  CA  . GLY C  1 106 ? 49.578  -20.465 79.652  1.00 12.09  ? 193  GLY C CA  1 
ATOM   6850  C  C   . GLY C  1 106 ? 48.343  -21.078 80.301  1.00 12.44  ? 193  GLY C C   1 
ATOM   6851  O  O   . GLY C  1 106 ? 47.412  -21.515 79.589  1.00 12.68  ? 193  GLY C O   1 
ATOM   6852  N  N   . MET C  1 107 ? 48.335  -21.128 81.638  1.00 11.98  ? 194  MET C N   1 
ATOM   6853  C  CA  . MET C  1 107 ? 47.182  -21.608 82.421  1.00 12.19  ? 194  MET C CA  1 
ATOM   6854  C  C   . MET C  1 107 ? 46.325  -20.481 83.028  1.00 12.32  ? 194  MET C C   1 
ATOM   6855  O  O   . MET C  1 107 ? 45.095  -20.410 82.787  1.00 12.19  ? 194  MET C O   1 
ATOM   6856  C  CB  . MET C  1 107 ? 47.651  -22.548 83.537  1.00 12.72  ? 194  MET C CB  1 
ATOM   6857  C  CG  . MET C  1 107 ? 48.428  -23.787 83.033  1.00 15.59  ? 194  MET C CG  1 
ATOM   6858  S  SD  . MET C  1 107 ? 47.374  -24.914 82.108  1.00 23.00  ? 194  MET C SD  1 
ATOM   6859  C  CE  . MET C  1 107 ? 46.372  -25.607 83.408  1.00 20.61  ? 194  MET C CE  1 
ATOM   6860  N  N   . SER C  1 108 ? 46.967  -19.622 83.831  1.00 11.34  ? 195  SER C N   1 
ATOM   6861  C  CA  . SER C  1 108 ? 46.323  -18.455 84.426  1.00 11.13  ? 195  SER C CA  1 
ATOM   6862  C  C   . SER C  1 108 ? 47.269  -17.260 84.467  1.00 10.51  ? 195  SER C C   1 
ATOM   6863  O  O   . SER C  1 108 ? 48.487  -17.398 84.280  1.00 10.37  ? 195  SER C O   1 
ATOM   6864  C  CB  . SER C  1 108 ? 45.866  -18.748 85.869  1.00 11.39  ? 195  SER C CB  1 
ATOM   6865  O  OG  . SER C  1 108 ? 45.023  -19.886 85.923  1.00 11.69  ? 195  SER C OG  1 
ATOM   6866  N  N   . ARG C  1 109 ? 46.689  -16.110 84.805  1.00 10.07  ? 196  ARG C N   1 
ATOM   6867  C  CA  . ARG C  1 109 ? 47.404  -14.845 84.867  1.00 9.18   ? 196  ARG C CA  1 
ATOM   6868  C  C   . ARG C  1 109 ? 47.891  -14.537 86.290  1.00 9.29   ? 196  ARG C C   1 
ATOM   6869  O  O   . ARG C  1 109 ? 47.125  -14.631 87.253  1.00 9.19   ? 196  ARG C O   1 
ATOM   6870  C  CB  . ARG C  1 109 ? 46.524  -13.712 84.329  1.00 9.43   ? 196  ARG C CB  1 
ATOM   6871  C  CG  . ARG C  1 109 ? 47.167  -12.299 84.513  1.00 8.58   ? 196  ARG C CG  1 
ATOM   6872  C  CD  . ARG C  1 109 ? 46.477  -11.251 83.634  1.00 8.54   ? 196  ARG C CD  1 
ATOM   6873  N  NE  . ARG C  1 109 ? 46.693  -11.500 82.188  1.00 7.58   ? 196  ARG C NE  1 
ATOM   6874  C  CZ  . ARG C  1 109 ? 47.837  -11.261 81.540  1.00 8.70   ? 196  ARG C CZ  1 
ATOM   6875  N  NH1 . ARG C  1 109 ? 47.945  -11.520 80.238  1.00 8.08   ? 196  ARG C NH1 1 
ATOM   6876  N  NH2 . ARG C  1 109 ? 48.889  -10.758 82.186  1.00 8.47   ? 196  ARG C NH2 1 
ATOM   6877  N  N   . MET C  1 110 ? 49.192  -14.241 86.410  1.00 8.37   ? 197  MET C N   1 
ATOM   6878  C  CA  . MET C  1 110 ? 49.769  -13.735 87.648  1.00 8.00   ? 197  MET C CA  1 
ATOM   6879  C  C   . MET C  1 110 ? 49.785  -12.203 87.581  1.00 8.31   ? 197  MET C C   1 
ATOM   6880  O  O   . MET C  1 110 ? 50.243  -11.623 86.593  1.00 8.17   ? 197  MET C O   1 
ATOM   6881  C  CB  . MET C  1 110 ? 51.200  -14.247 87.846  1.00 7.97   ? 197  MET C CB  1 
ATOM   6882  C  CG  . MET C  1 110 ? 51.783  -13.804 89.177  1.00 8.39   ? 197  MET C CG  1 
ATOM   6883  S  SD  . MET C  1 110 ? 53.489  -14.269 89.522  1.00 9.91   ? 197  MET C SD  1 
ATOM   6884  C  CE  . MET C  1 110 ? 54.351  -13.488 88.132  1.00 12.23  ? 197  MET C CE  1 
ATOM   6885  N  N   . SER C  1 111 ? 49.286  -11.547 88.626  1.00 8.08   ? 198  SER C N   1 
ATOM   6886  C  CA  . SER C  1 111 ? 49.404  -10.075 88.701  1.00 8.09   ? 198  SER C CA  1 
ATOM   6887  C  C   . SER C  1 111 ? 49.942  -9.679  90.053  1.00 8.61   ? 198  SER C C   1 
ATOM   6888  O  O   . SER C  1 111 ? 49.532  -10.246 91.087  1.00 9.71   ? 198  SER C O   1 
ATOM   6889  C  CB  . SER C  1 111 ? 48.048  -9.403  88.474  1.00 8.66   ? 198  SER C CB  1 
ATOM   6890  O  OG  . SER C  1 111 ? 47.594  -9.579  87.142  1.00 8.30   ? 198  SER C OG  1 
ATOM   6891  N  N   . ILE C  1 112 ? 50.822  -8.679  90.060  1.00 8.23   ? 199  ILE C N   1 
ATOM   6892  C  CA  . ILE C  1 112 ? 51.487  -8.225  91.279  1.00 8.12   ? 199  ILE C CA  1 
ATOM   6893  C  C   . ILE C  1 112 ? 51.387  -6.701  91.407  1.00 8.17   ? 199  ILE C C   1 
ATOM   6894  O  O   . ILE C  1 112 ? 51.663  -5.983  90.447  1.00 7.39   ? 199  ILE C O   1 
ATOM   6895  C  CB  . ILE C  1 112 ? 52.996  -8.642  91.314  1.00 8.00   ? 199  ILE C CB  1 
ATOM   6896  C  CG1 . ILE C  1 112 ? 53.162  -10.173 91.181  1.00 9.72   ? 199  ILE C CG1 1 
ATOM   6897  C  CG2 . ILE C  1 112 ? 53.717  -8.039  92.561  1.00 8.75   ? 199  ILE C CG2 1 
ATOM   6898  C  CD1 . ILE C  1 112 ? 54.633  -10.620 90.946  1.00 8.44   ? 199  ILE C CD1 1 
ATOM   6899  N  N   . CYS C  1 113 ? 50.958  -6.224  92.578  1.00 8.54   ? 200  CYS C N   1 
ATOM   6900  C  CA  . CYS C  1 113 ? 50.868  -4.785  92.879  1.00 9.66   ? 200  CYS C CA  1 
ATOM   6901  C  C   . CYS C  1 113 ? 51.551  -4.490  94.203  1.00 9.48   ? 200  CYS C C   1 
ATOM   6902  O  O   . CYS C  1 113 ? 51.323  -5.204  95.202  1.00 9.91   ? 200  CYS C O   1 
ATOM   6903  C  CB  . CYS C  1 113 ? 49.408  -4.335  93.025  1.00 9.42   ? 200  CYS C CB  1 
ATOM   6904  S  SG  . CYS C  1 113 ? 48.477  -4.230  91.496  1.00 13.90  ? 200  CYS C SG  1 
ATOM   6905  N  N   . MET C  1 114 ? 52.359  -3.433  94.225  1.00 9.24   ? 201  MET C N   1 
ATOM   6906  C  CA  . MET C  1 114 ? 52.912  -2.939  95.479  1.00 9.81   ? 201  MET C CA  1 
ATOM   6907  C  C   . MET C  1 114 ? 52.019  -1.818  95.983  1.00 9.95   ? 201  MET C C   1 
ATOM   6908  O  O   . MET C  1 114 ? 51.567  -0.980  95.209  1.00 10.77  ? 201  MET C O   1 
ATOM   6909  C  CB  . MET C  1 114 ? 54.342  -2.405  95.308  1.00 9.70   ? 201  MET C CB  1 
ATOM   6910  C  CG  . MET C  1 114 ? 55.432  -3.477  95.219  1.00 10.00  ? 201  MET C CG  1 
ATOM   6911  S  SD  . MET C  1 114 ? 55.287  -4.508  93.772  1.00 10.89  ? 201  MET C SD  1 
ATOM   6912  C  CE  . MET C  1 114 ? 56.879  -5.400  93.906  1.00 10.94  ? 201  MET C CE  1 
ATOM   6913  N  N   . SER C  1 115 ? 51.801  -1.756  97.290  1.00 9.94   ? 202  SER C N   1 
ATOM   6914  C  CA  . SER C  1 115 ? 51.136  -0.574  97.845  1.00 10.02  ? 202  SER C CA  1 
ATOM   6915  C  C   . SER C  1 115 ? 51.701  -0.249  99.221  1.00 10.54  ? 202  SER C C   1 
ATOM   6916  O  O   . SER C  1 115 ? 52.515  -0.994  99.735  1.00 10.37  ? 202  SER C O   1 
ATOM   6917  C  CB  . SER C  1 115 ? 49.625  -0.824  97.966  1.00 10.49  ? 202  SER C CB  1 
ATOM   6918  O  OG  . SER C  1 115 ? 49.368  -1.674  99.087  1.00 11.65  ? 202  SER C OG  1 
ATOM   6919  N  N   . GLY C  1 116 ? 51.219  0.836   99.827  1.00 10.51  ? 203  GLY C N   1 
ATOM   6920  C  CA  . GLY C  1 116 ? 51.622  1.204   101.179 1.00 10.64  ? 203  GLY C CA  1 
ATOM   6921  C  C   . GLY C  1 116 ? 52.443  2.468   101.178 1.00 10.60  ? 203  GLY C C   1 
ATOM   6922  O  O   . GLY C  1 116 ? 52.679  3.048   100.105 1.00 10.30  ? 203  GLY C O   1 
ATOM   6923  N  N   . PRO C  1 117 ? 52.920  2.891   102.378 1.00 10.81  ? 204  PRO C N   1 
ATOM   6924  C  CA  . PRO C  1 117 ? 53.738  4.102   102.456 1.00 10.82  ? 204  PRO C CA  1 
ATOM   6925  C  C   . PRO C  1 117 ? 55.164  3.781   102.013 1.00 11.01  ? 204  PRO C C   1 
ATOM   6926  O  O   . PRO C  1 117 ? 55.542  2.611   101.973 1.00 9.53   ? 204  PRO C O   1 
ATOM   6927  C  CB  . PRO C  1 117 ? 53.714  4.446   103.946 1.00 10.87  ? 204  PRO C CB  1 
ATOM   6928  C  CG  . PRO C  1 117 ? 53.579  3.135   104.641 1.00 10.70  ? 204  PRO C CG  1 
ATOM   6929  C  CD  . PRO C  1 117 ? 52.767  2.237   103.693 1.00 11.22  ? 204  PRO C CD  1 
ATOM   6930  N  N   . ASN C  1 118 ? 55.931  4.821   101.690 1.00 10.87  ? 205  ASN C N   1 
ATOM   6931  C  CA  . ASN C  1 118 ? 57.272  4.667   101.135 1.00 11.91  ? 205  ASN C CA  1 
ATOM   6932  C  C   . ASN C  1 118 ? 58.182  3.795   102.002 1.00 11.39  ? 205  ASN C C   1 
ATOM   6933  O  O   . ASN C  1 118 ? 58.972  3.017   101.488 1.00 12.30  ? 205  ASN C O   1 
ATOM   6934  C  CB  . ASN C  1 118 ? 57.922  6.043   100.966 1.00 11.49  ? 205  ASN C CB  1 
ATOM   6935  C  CG  . ASN C  1 118 ? 57.210  6.916   99.940  1.00 13.89  ? 205  ASN C CG  1 
ATOM   6936  O  OD1 . ASN C  1 118 ? 56.351  6.457   99.170  1.00 13.37  ? 205  ASN C OD1 1 
ATOM   6937  N  ND2 . ASN C  1 118 ? 57.585  8.193   99.917  1.00 14.34  ? 205  ASN C ND2 1 
ATOM   6938  N  N   . ASN C  1 119 ? 58.066  3.938   103.316 1.00 11.79  ? 206  ASN C N   1 
ATOM   6939  C  CA  . ASN C  1 119 ? 58.981  3.231   104.221 1.00 12.09  ? 206  ASN C CA  1 
ATOM   6940  C  C   . ASN C  1 119 ? 58.452  1.857   104.640 1.00 11.89  ? 206  ASN C C   1 
ATOM   6941  O  O   . ASN C  1 119 ? 59.041  1.178   105.486 1.00 11.99  ? 206  ASN C O   1 
ATOM   6942  C  CB  . ASN C  1 119 ? 59.322  4.109   105.434 1.00 12.91  ? 206  ASN C CB  1 
ATOM   6943  C  CG  . ASN C  1 119 ? 58.147  4.263   106.408 1.00 15.15  ? 206  ASN C CG  1 
ATOM   6944  O  OD1 . ASN C  1 119 ? 57.022  3.851   106.133 1.00 16.07  ? 206  ASN C OD1 1 
ATOM   6945  N  ND2 . ASN C  1 119 ? 58.427  4.829   107.564 1.00 18.63  ? 206  ASN C ND2 1 
ATOM   6946  N  N   . ASN C  1 120 ? 57.332  1.444   104.054 1.00 11.30  ? 207  ASN C N   1 
ATOM   6947  C  CA  . ASN C  1 120 ? 56.678  0.240   104.542 1.00 11.50  ? 207  ASN C CA  1 
ATOM   6948  C  C   . ASN C  1 120 ? 55.731  -0.392  103.524 1.00 11.40  ? 207  ASN C C   1 
ATOM   6949  O  O   . ASN C  1 120 ? 54.631  -0.847  103.882 1.00 10.96  ? 207  ASN C O   1 
ATOM   6950  C  CB  . ASN C  1 120 ? 55.910  0.616   105.786 1.00 12.25  ? 207  ASN C CB  1 
ATOM   6951  C  CG  . ASN C  1 120 ? 56.071  -0.372  106.903 1.00 15.21  ? 207  ASN C CG  1 
ATOM   6952  O  OD1 . ASN C  1 120 ? 56.776  -1.380  106.813 1.00 18.01  ? 207  ASN C OD1 1 
ATOM   6953  N  ND2 . ASN C  1 120 ? 55.364  -0.094  107.978 1.00 19.81  ? 207  ASN C ND2 1 
ATOM   6954  N  N   . ALA C  1 121 ? 56.169  -0.422  102.265 1.00 10.37  ? 208  ALA C N   1 
ATOM   6955  C  CA  . ALA C  1 121 ? 55.364  -0.977  101.180 1.00 9.88   ? 208  ALA C CA  1 
ATOM   6956  C  C   . ALA C  1 121 ? 55.350  -2.509  101.234 1.00 9.17   ? 208  ALA C C   1 
ATOM   6957  O  O   . ALA C  1 121 ? 56.178  -3.125  101.910 1.00 9.05   ? 208  ALA C O   1 
ATOM   6958  C  CB  . ALA C  1 121 ? 55.890  -0.490  99.826  1.00 9.77   ? 208  ALA C CB  1 
ATOM   6959  N  N   . SER C  1 122 ? 54.411  -3.109  100.509 1.00 8.65   ? 209  SER C N   1 
ATOM   6960  C  CA  . SER C  1 122 ? 54.306  -4.558  100.416 1.00 8.64   ? 209  SER C CA  1 
ATOM   6961  C  C   . SER C  1 122 ? 53.742  -4.935  99.044  1.00 8.91   ? 209  SER C C   1 
ATOM   6962  O  O   . SER C  1 122 ? 52.933  -4.193  98.467  1.00 8.87   ? 209  SER C O   1 
ATOM   6963  C  CB  . SER C  1 122 ? 53.436  -5.119  101.553 1.00 8.61   ? 209  SER C CB  1 
ATOM   6964  O  OG  . SER C  1 122 ? 52.098  -4.661  101.432 1.00 10.59  ? 209  SER C OG  1 
ATOM   6965  N  N   . ALA C  1 123 ? 54.184  -6.077  98.519  1.00 8.78   ? 210  ALA C N   1 
ATOM   6966  C  CA  . ALA C  1 123 ? 53.651  -6.596  97.258  1.00 8.70   ? 210  ALA C CA  1 
ATOM   6967  C  C   . ALA C  1 123 ? 52.584  -7.638  97.594  1.00 9.04   ? 210  ALA C C   1 
ATOM   6968  O  O   . ALA C  1 123 ? 52.728  -8.400  98.560  1.00 10.08  ? 210  ALA C O   1 
ATOM   6969  C  CB  . ALA C  1 123 ? 54.764  -7.222  96.397  1.00 8.84   ? 210  ALA C CB  1 
ATOM   6970  N  N   . VAL C  1 124 ? 51.484  -7.629  96.844  1.00 8.93   ? 211  VAL C N   1 
ATOM   6971  C  CA  . VAL C  1 124 ? 50.551  -8.773  96.852  1.00 8.44   ? 211  VAL C CA  1 
ATOM   6972  C  C   . VAL C  1 124 ? 50.575  -9.443  95.474  1.00 8.67   ? 211  VAL C C   1 
ATOM   6973  O  O   . VAL C  1 124 ? 50.420  -8.771  94.436  1.00 7.85   ? 211  VAL C O   1 
ATOM   6974  C  CB  . VAL C  1 124 ? 49.094  -8.370  97.251  1.00 8.18   ? 211  VAL C CB  1 
ATOM   6975  C  CG1 . VAL C  1 124 ? 48.197  -9.610  97.314  1.00 8.50   ? 211  VAL C CG1 1 
ATOM   6976  C  CG2 . VAL C  1 124 ? 49.098  -7.650  98.610  1.00 8.56   ? 211  VAL C CG2 1 
ATOM   6977  N  N   . VAL C  1 125 ? 50.761  -10.762 95.494  1.00 8.17   ? 212  VAL C N   1 
ATOM   6978  C  CA  . VAL C  1 125 ? 50.918  -11.586 94.289  1.00 8.85   ? 212  VAL C CA  1 
ATOM   6979  C  C   . VAL C  1 125 ? 49.636  -12.383 94.081  1.00 8.34   ? 212  VAL C C   1 
ATOM   6980  O  O   . VAL C  1 125 ? 49.251  -13.194 94.942  1.00 9.17   ? 212  VAL C O   1 
ATOM   6981  C  CB  . VAL C  1 125 ? 52.114  -12.562 94.403  1.00 9.05   ? 212  VAL C CB  1 
ATOM   6982  C  CG1 . VAL C  1 125 ? 52.302  -13.361 93.093  1.00 8.90   ? 212  VAL C CG1 1 
ATOM   6983  C  CG2 . VAL C  1 125 ? 53.410  -11.800 94.768  1.00 8.82   ? 212  VAL C CG2 1 
ATOM   6984  N  N   . TRP C  1 126 ? 48.976  -12.106 92.960  1.00 8.27   ? 213  TRP C N   1 
ATOM   6985  C  CA  . TRP C  1 126 ? 47.706  -12.749 92.582  1.00 8.98   ? 213  TRP C CA  1 
ATOM   6986  C  C   . TRP C  1 126 ? 47.923  -13.783 91.478  1.00 9.89   ? 213  TRP C C   1 
ATOM   6987  O  O   . TRP C  1 126 ? 48.788  -13.590 90.612  1.00 9.73   ? 213  TRP C O   1 
ATOM   6988  C  CB  . TRP C  1 126 ? 46.698  -11.698 92.084  1.00 9.24   ? 213  TRP C CB  1 
ATOM   6989  C  CG  . TRP C  1 126 ? 46.299  -10.645 93.106  1.00 9.60   ? 213  TRP C CG  1 
ATOM   6990  C  CD1 . TRP C  1 126 ? 47.108  -9.706  93.697  1.00 10.28  ? 213  TRP C CD1 1 
ATOM   6991  C  CD2 . TRP C  1 126 ? 44.980  -10.438 93.649  1.00 11.15  ? 213  TRP C CD2 1 
ATOM   6992  N  NE1 . TRP C  1 126 ? 46.365  -8.913  94.574  1.00 10.16  ? 213  TRP C NE1 1 
ATOM   6993  C  CE2 . TRP C  1 126 ? 45.059  -9.345  94.552  1.00 11.16  ? 213  TRP C CE2 1 
ATOM   6994  C  CE3 . TRP C  1 126 ? 43.732  -11.065 93.446  1.00 11.49  ? 213  TRP C CE3 1 
ATOM   6995  C  CZ2 . TRP C  1 126 ? 43.938  -8.863  95.255  1.00 11.38  ? 213  TRP C CZ2 1 
ATOM   6996  C  CZ3 . TRP C  1 126 ? 42.604  -10.573 94.147  1.00 10.23  ? 213  TRP C CZ3 1 
ATOM   6997  C  CH2 . TRP C  1 126 ? 42.724  -9.489  95.040  1.00 10.26  ? 213  TRP C CH2 1 
ATOM   6998  N  N   . TYR C  1 127 ? 47.120  -14.853 91.493  1.00 10.26  ? 214  TYR C N   1 
ATOM   6999  C  CA  . TYR C  1 127 ? 47.143  -15.889 90.448  1.00 10.55  ? 214  TYR C CA  1 
ATOM   7000  C  C   . TYR C  1 127 ? 45.721  -16.398 90.193  1.00 10.74  ? 214  TYR C C   1 
ATOM   7001  O  O   . TYR C  1 127 ? 45.009  -16.796 91.134  1.00 11.33  ? 214  TYR C O   1 
ATOM   7002  C  CB  . TYR C  1 127 ? 48.076  -17.051 90.831  1.00 10.77  ? 214  TYR C CB  1 
ATOM   7003  C  CG  . TYR C  1 127 ? 48.300  -18.071 89.739  1.00 10.56  ? 214  TYR C CG  1 
ATOM   7004  C  CD1 . TYR C  1 127 ? 47.723  -19.336 89.814  1.00 10.52  ? 214  TYR C CD1 1 
ATOM   7005  C  CD2 . TYR C  1 127 ? 49.090  -17.769 88.623  1.00 10.22  ? 214  TYR C CD2 1 
ATOM   7006  C  CE1 . TYR C  1 127 ? 47.925  -20.282 88.808  1.00 9.76   ? 214  TYR C CE1 1 
ATOM   7007  C  CE2 . TYR C  1 127 ? 49.308  -18.702 87.612  1.00 11.37  ? 214  TYR C CE2 1 
ATOM   7008  C  CZ  . TYR C  1 127 ? 48.711  -19.966 87.714  1.00 9.78   ? 214  TYR C CZ  1 
ATOM   7009  O  OH  . TYR C  1 127 ? 48.914  -20.907 86.734  1.00 9.97   ? 214  TYR C OH  1 
ATOM   7010  N  N   . GLY C  1 128 ? 45.302  -16.371 88.934  1.00 10.08  ? 215  GLY C N   1 
ATOM   7011  C  CA  . GLY C  1 128 ? 43.934  -16.751 88.571  1.00 10.54  ? 215  GLY C CA  1 
ATOM   7012  C  C   . GLY C  1 128 ? 42.871  -15.930 89.292  1.00 10.53  ? 215  GLY C C   1 
ATOM   7013  O  O   . GLY C  1 128 ? 41.782  -16.440 89.589  1.00 10.21  ? 215  GLY C O   1 
ATOM   7014  N  N   . GLY C  1 129 ? 43.197  -14.660 89.574  1.00 9.57   ? 216  GLY C N   1 
ATOM   7015  C  CA  . GLY C  1 129 ? 42.293  -13.715 90.220  1.00 10.74  ? 216  GLY C CA  1 
ATOM   7016  C  C   . GLY C  1 129 ? 42.158  -13.831 91.748  1.00 10.74  ? 216  GLY C C   1 
ATOM   7017  O  O   . GLY C  1 129 ? 41.266  -13.226 92.331  1.00 10.28  ? 216  GLY C O   1 
ATOM   7018  N  N   . ARG C  1 130 ? 43.032  -14.616 92.385  1.00 10.72  ? 217  ARG C N   1 
ATOM   7019  C  CA  . ARG C  1 130 ? 43.045  -14.795 93.844  1.00 11.55  ? 217  ARG C CA  1 
ATOM   7020  C  C   . ARG C  1 130 ? 44.415  -14.403 94.398  1.00 11.42  ? 217  ARG C C   1 
ATOM   7021  O  O   . ARG C  1 130 ? 45.436  -14.655 93.725  1.00 10.71  ? 217  ARG C O   1 
ATOM   7022  C  CB  . ARG C  1 130 ? 42.737  -16.256 94.212  1.00 11.91  ? 217  ARG C CB  1 
ATOM   7023  C  CG  . ARG C  1 130 ? 41.272  -16.698 93.909  1.00 12.49  ? 217  ARG C CG  1 
ATOM   7024  C  CD  . ARG C  1 130 ? 40.945  -18.166 94.283  1.00 13.53  ? 217  ARG C CD  1 
ATOM   7025  N  NE  . ARG C  1 130 ? 39.569  -18.214 94.789  1.00 15.76  ? 217  ARG C NE  1 
ATOM   7026  C  CZ  . ARG C  1 130 ? 38.475  -18.579 94.109  1.00 18.18  ? 217  ARG C CZ  1 
ATOM   7027  N  NH1 . ARG C  1 130 ? 37.269  -18.507 94.702  1.00 14.41  ? 217  ARG C NH1 1 
ATOM   7028  N  NH2 . ARG C  1 130 ? 38.560  -19.026 92.865  1.00 16.48  ? 217  ARG C NH2 1 
ATOM   7029  N  N   . PRO C  1 131 ? 44.456  -13.799 95.616  1.00 11.29  ? 218  PRO C N   1 
ATOM   7030  C  CA  . PRO C  1 131 ? 45.740  -13.487 96.247  1.00 11.73  ? 218  PRO C CA  1 
ATOM   7031  C  C   . PRO C  1 131 ? 46.440  -14.761 96.780  1.00 11.58  ? 218  PRO C C   1 
ATOM   7032  O  O   . PRO C  1 131 ? 45.800  -15.607 97.422  1.00 11.63  ? 218  PRO C O   1 
ATOM   7033  C  CB  . PRO C  1 131 ? 45.340  -12.541 97.384  1.00 11.52  ? 218  PRO C CB  1 
ATOM   7034  C  CG  . PRO C  1 131 ? 43.975  -13.032 97.793  1.00 11.44  ? 218  PRO C CG  1 
ATOM   7035  C  CD  . PRO C  1 131 ? 43.319  -13.378 96.472  1.00 12.36  ? 218  PRO C CD  1 
ATOM   7036  N  N   . ILE C  1 132 ? 47.732  -14.902 96.484  1.00 11.64  ? 219  ILE C N   1 
ATOM   7037  C  CA  . ILE C  1 132 ? 48.492  -16.109 96.825  1.00 11.16  ? 219  ILE C CA  1 
ATOM   7038  C  C   . ILE C  1 132 ? 49.593  -15.849 97.850  1.00 12.15  ? 219  ILE C C   1 
ATOM   7039  O  O   . ILE C  1 132 ? 49.736  -16.618 98.814  1.00 12.49  ? 219  ILE C O   1 
ATOM   7040  C  CB  . ILE C  1 132 ? 49.136  -16.802 95.558  1.00 11.03  ? 219  ILE C CB  1 
ATOM   7041  C  CG1 . ILE C  1 132 ? 48.096  -16.933 94.419  1.00 9.11   ? 219  ILE C CG1 1 
ATOM   7042  C  CG2 . ILE C  1 132 ? 49.787  -18.193 95.924  1.00 10.87  ? 219  ILE C CG2 1 
ATOM   7043  C  CD1 . ILE C  1 132 ? 46.886  -17.810 94.743  1.00 10.34  ? 219  ILE C CD1 1 
ATOM   7044  N  N   . THR C  1 133 ? 50.377  -14.798 97.612  1.00 11.93  ? 220  THR C N   1 
ATOM   7045  C  CA  . THR C  1 133 ? 51.570  -14.475 98.385  1.00 12.69  ? 220  THR C CA  1 
ATOM   7046  C  C   . THR C  1 133 ? 51.658  -12.974 98.694  1.00 12.64  ? 220  THR C C   1 
ATOM   7047  O  O   . THR C  1 133 ? 51.230  -12.137 97.887  1.00 12.28  ? 220  THR C O   1 
ATOM   7048  C  CB  . THR C  1 133 ? 52.846  -14.892 97.586  1.00 12.77  ? 220  THR C CB  1 
ATOM   7049  O  OG1 . THR C  1 133 ? 52.762  -16.293 97.292  1.00 13.36  ? 220  THR C OG1 1 
ATOM   7050  C  CG2 . THR C  1 133 ? 54.117  -14.632 98.389  1.00 13.88  ? 220  THR C CG2 1 
ATOM   7051  N  N   . GLU C  1 134 ? 52.254  -12.638 99.839  1.00 12.02  ? 221  GLU C N   1 
ATOM   7052  C  CA  . GLU C  1 134 ? 52.541  -11.243 100.200 1.00 12.16  ? 221  GLU C CA  1 
ATOM   7053  C  C   . GLU C  1 134 ? 54.033  -11.115 100.474 1.00 12.45  ? 221  GLU C C   1 
ATOM   7054  O  O   . GLU C  1 134 ? 54.646  -12.044 101.031 1.00 12.92  ? 221  GLU C O   1 
ATOM   7055  C  CB  . GLU C  1 134 ? 51.754  -10.811 101.440 1.00 11.95  ? 221  GLU C CB  1 
ATOM   7056  C  CG  . GLU C  1 134 ? 50.251  -11.141 101.394 1.00 12.91  ? 221  GLU C CG  1 
ATOM   7057  C  CD  . GLU C  1 134 ? 49.974  -12.585 101.812 1.00 15.18  ? 221  GLU C CD  1 
ATOM   7058  O  OE1 . GLU C  1 134 ? 49.193  -13.247 101.130 1.00 17.10  ? 221  GLU C OE1 1 
ATOM   7059  O  OE2 . GLU C  1 134 ? 50.576  -13.073 102.799 1.00 16.16  ? 221  GLU C OE2 1 
ATOM   7060  N  N   . ILE C  1 135 ? 54.622  -10.000 100.054 1.00 11.63  ? 222  ILE C N   1 
ATOM   7061  C  CA  . ILE C  1 135 ? 56.054  -9.799  100.212 1.00 11.65  ? 222  ILE C CA  1 
ATOM   7062  C  C   . ILE C  1 135 ? 56.296  -8.428  100.833 1.00 11.87  ? 222  ILE C C   1 
ATOM   7063  O  O   . ILE C  1 135 ? 55.984  -7.410  100.218 1.00 10.89  ? 222  ILE C O   1 
ATOM   7064  C  CB  . ILE C  1 135 ? 56.828  -9.897  98.871  1.00 11.31  ? 222  ILE C CB  1 
ATOM   7065  C  CG1 . ILE C  1 135 ? 56.594  -11.264 98.180  1.00 11.42  ? 222  ILE C CG1 1 
ATOM   7066  C  CG2 . ILE C  1 135 ? 58.326  -9.554  99.106  1.00 13.03  ? 222  ILE C CG2 1 
ATOM   7067  C  CD1 . ILE C  1 135 ? 56.943  -11.262 96.674  1.00 12.32  ? 222  ILE C CD1 1 
ATOM   7068  N  N   . PRO C  1 136 ? 56.836  -8.408  102.069 1.00 11.91  ? 223  PRO C N   1 
ATOM   7069  C  CA  . PRO C  1 136 ? 57.121  -7.128  102.698 1.00 11.47  ? 223  PRO C CA  1 
ATOM   7070  C  C   . PRO C  1 136 ? 58.382  -6.474  102.112 1.00 11.39  ? 223  PRO C C   1 
ATOM   7071  O  O   . PRO C  1 136 ? 59.298  -7.174  101.686 1.00 11.12  ? 223  PRO C O   1 
ATOM   7072  C  CB  . PRO C  1 136 ? 57.328  -7.488  104.186 1.00 11.67  ? 223  PRO C CB  1 
ATOM   7073  C  CG  . PRO C  1 136 ? 57.660  -8.943  104.223 1.00 12.01  ? 223  PRO C CG  1 
ATOM   7074  C  CD  . PRO C  1 136 ? 57.181  -9.573  102.924 1.00 12.15  ? 223  PRO C CD  1 
ATOM   7075  N  N   . SER C  1 137 ? 58.404  -5.140  102.101 1.00 11.41  ? 224  SER C N   1 
ATOM   7076  C  CA  . SER C  1 137 ? 59.578  -4.346  101.744 1.00 11.20  ? 224  SER C CA  1 
ATOM   7077  C  C   . SER C  1 137 ? 60.809  -4.842  102.506 1.00 11.81  ? 224  SER C C   1 
ATOM   7078  O  O   . SER C  1 137 ? 60.746  -5.031  103.727 1.00 11.77  ? 224  SER C O   1 
ATOM   7079  C  CB  . SER C  1 137 ? 59.335  -2.873  102.109 1.00 11.33  ? 224  SER C CB  1 
ATOM   7080  O  OG  . SER C  1 137 ? 60.507  -2.089  101.956 1.00 10.59  ? 224  SER C OG  1 
ATOM   7081  N  N   . TRP C  1 138 ? 61.907  -5.069  101.789 1.00 12.05  ? 225  TRP C N   1 
ATOM   7082  C  CA  . TRP C  1 138 ? 63.174  -5.500  102.421 1.00 12.31  ? 225  TRP C CA  1 
ATOM   7083  C  C   . TRP C  1 138 ? 64.187  -4.370  102.690 1.00 12.99  ? 225  TRP C C   1 
ATOM   7084  O  O   . TRP C  1 138 ? 65.152  -4.568  103.436 1.00 13.48  ? 225  TRP C O   1 
ATOM   7085  C  CB  . TRP C  1 138 ? 63.841  -6.625  101.623 1.00 11.76  ? 225  TRP C CB  1 
ATOM   7086  C  CG  . TRP C  1 138 ? 64.073  -6.306  100.152 1.00 12.13  ? 225  TRP C CG  1 
ATOM   7087  C  CD1 . TRP C  1 138 ? 65.068  -5.522  99.602  1.00 12.69  ? 225  TRP C CD1 1 
ATOM   7088  C  CD2 . TRP C  1 138 ? 63.280  -6.776  99.057  1.00 11.60  ? 225  TRP C CD2 1 
ATOM   7089  N  NE1 . TRP C  1 138 ? 64.945  -5.507  98.218  1.00 11.51  ? 225  TRP C NE1 1 
ATOM   7090  C  CE2 . TRP C  1 138 ? 63.852  -6.258  97.863  1.00 10.85  ? 225  TRP C CE2 1 
ATOM   7091  C  CE3 . TRP C  1 138 ? 62.143  -7.595  98.969  1.00 12.08  ? 225  TRP C CE3 1 
ATOM   7092  C  CZ2 . TRP C  1 138 ? 63.318  -6.535  96.590  1.00 11.43  ? 225  TRP C CZ2 1 
ATOM   7093  C  CZ3 . TRP C  1 138 ? 61.608  -7.876  97.702  1.00 12.46  ? 225  TRP C CZ3 1 
ATOM   7094  C  CH2 . TRP C  1 138 ? 62.196  -7.334  96.529  1.00 11.90  ? 225  TRP C CH2 1 
ATOM   7095  N  N   . ALA C  1 139 ? 63.984  -3.189  102.111 1.00 12.03  ? 226  ALA C N   1 
ATOM   7096  C  CA  . ALA C  1 139 ? 64.941  -2.096  102.287 1.00 12.38  ? 226  ALA C CA  1 
ATOM   7097  C  C   . ALA C  1 139 ? 64.249  -0.823  102.801 1.00 12.28  ? 226  ALA C C   1 
ATOM   7098  O  O   . ALA C  1 139 ? 64.885  0.223   102.983 1.00 12.08  ? 226  ALA C O   1 
ATOM   7099  C  CB  . ALA C  1 139 ? 65.712  -1.822  100.969 1.00 12.35  ? 226  ALA C CB  1 
ATOM   7100  N  N   . GLY C  1 140 ? 62.936  -0.912  102.985 1.00 11.87  ? 227  GLY C N   1 
ATOM   7101  C  CA  . GLY C  1 140 ? 62.141  0.211   103.509 1.00 11.89  ? 227  GLY C CA  1 
ATOM   7102  C  C   . GLY C  1 140 ? 62.146  1.482   102.669 1.00 12.06  ? 227  GLY C C   1 
ATOM   7103  O  O   . GLY C  1 140 ? 62.085  2.587   103.207 1.00 11.96  ? 227  GLY C O   1 
ATOM   7104  N  N   . ASN C  1 141 ? 62.200  1.339   101.345 1.00 12.23  ? 228  ASN C N   1 
ATOM   7105  C  CA  . ASN C  1 141 ? 62.201  2.510   100.463 1.00 11.74  ? 228  ASN C CA  1 
ATOM   7106  C  C   . ASN C  1 141 ? 61.537  2.238   99.104  1.00 10.97  ? 228  ASN C C   1 
ATOM   7107  O  O   . ASN C  1 141 ? 62.212  1.955   98.112  1.00 10.55  ? 228  ASN C O   1 
ATOM   7108  C  CB  . ASN C  1 141 ? 63.639  3.050   100.294 1.00 12.27  ? 228  ASN C CB  1 
ATOM   7109  C  CG  . ASN C  1 141 ? 63.693  4.438   99.648  1.00 14.87  ? 228  ASN C CG  1 
ATOM   7110  O  OD1 . ASN C  1 141 ? 62.697  4.961   99.126  1.00 14.88  ? 228  ASN C OD1 1 
ATOM   7111  N  ND2 . ASN C  1 141 ? 64.896  5.043   99.669  1.00 16.49  ? 228  ASN C ND2 1 
ATOM   7112  N  N   . ILE C  1 142 ? 60.205  2.303   99.092  1.00 10.73  ? 229  ILE C N   1 
ATOM   7113  C  CA  . ILE C  1 142 ? 59.382  2.124   97.876  1.00 10.44  ? 229  ILE C CA  1 
ATOM   7114  C  C   . ILE C  1 142 ? 59.657  0.814   97.127  1.00 9.63   ? 229  ILE C C   1 
ATOM   7115  O  O   . ILE C  1 142 ? 60.141  0.833   95.986  1.00 9.36   ? 229  ILE C O   1 
ATOM   7116  C  CB  . ILE C  1 142 ? 59.466  3.374   96.896  1.00 10.98  ? 229  ILE C CB  1 
ATOM   7117  C  CG1 . ILE C  1 142 ? 59.337  4.692   97.682  1.00 10.61  ? 229  ILE C CG1 1 
ATOM   7118  C  CG2 . ILE C  1 142 ? 58.388  3.268   95.742  1.00 9.77   ? 229  ILE C CG2 1 
ATOM   7119  C  CD1 . ILE C  1 142 ? 59.625  5.994   96.870  1.00 10.63  ? 229  ILE C CD1 1 
ATOM   7120  N  N   . LEU C  1 143 ? 59.353  -0.322  97.763  1.00 8.77   ? 230  LEU C N   1 
ATOM   7121  C  CA  . LEU C  1 143 ? 59.357  -1.608  97.060  1.00 8.89   ? 230  LEU C CA  1 
ATOM   7122  C  C   . LEU C  1 143 ? 58.540  -1.468  95.768  1.00 8.32   ? 230  LEU C C   1 
ATOM   7123  O  O   . LEU C  1 143 ? 57.419  -0.935  95.809  1.00 8.39   ? 230  LEU C O   1 
ATOM   7124  C  CB  . LEU C  1 143 ? 58.743  -2.690  97.953  1.00 8.22   ? 230  LEU C CB  1 
ATOM   7125  C  CG  . LEU C  1 143 ? 58.627  -4.066  97.296  1.00 9.13   ? 230  LEU C CG  1 
ATOM   7126  C  CD1 . LEU C  1 143 ? 60.048  -4.614  96.927  1.00 7.76   ? 230  LEU C CD1 1 
ATOM   7127  C  CD2 . LEU C  1 143 ? 57.821  -5.066  98.170  1.00 9.55   ? 230  LEU C CD2 1 
ATOM   7128  N  N   . ARG C  1 144 ? 59.102  -1.887  94.632  1.00 8.17   ? 231  ARG C N   1 
ATOM   7129  C  CA  . ARG C  1 144 ? 58.545  -1.522  93.318  1.00 7.63   ? 231  ARG C CA  1 
ATOM   7130  C  C   . ARG C  1 144 ? 58.982  -2.483  92.210  1.00 7.87   ? 231  ARG C C   1 
ATOM   7131  O  O   . ARG C  1 144 ? 59.933  -3.249  92.392  1.00 8.36   ? 231  ARG C O   1 
ATOM   7132  C  CB  . ARG C  1 144 ? 58.945  -0.078  92.954  1.00 7.21   ? 231  ARG C CB  1 
ATOM   7133  C  CG  . ARG C  1 144 ? 60.464  0.143   92.846  1.00 7.97   ? 231  ARG C CG  1 
ATOM   7134  C  CD  . ARG C  1 144 ? 60.792  1.653   92.850  1.00 7.46   ? 231  ARG C CD  1 
ATOM   7135  N  NE  . ARG C  1 144 ? 62.217  1.957   92.743  1.00 9.80   ? 231  ARG C NE  1 
ATOM   7136  C  CZ  . ARG C  1 144 ? 63.038  2.150   93.781  1.00 13.34  ? 231  ARG C CZ  1 
ATOM   7137  N  NH1 . ARG C  1 144 ? 62.603  2.020   95.039  1.00 13.92  ? 231  ARG C NH1 1 
ATOM   7138  N  NH2 . ARG C  1 144 ? 64.314  2.458   93.561  1.00 11.30  ? 231  ARG C NH2 1 
ATOM   7139  N  N   . THR C  1 145 ? 58.293  -2.458  91.066  1.00 7.77   ? 232  THR C N   1 
ATOM   7140  C  CA  . THR C  1 145 ? 58.578  -3.460  90.030  1.00 8.43   ? 232  THR C CA  1 
ATOM   7141  C  C   . THR C  1 145 ? 58.513  -2.908  88.591  1.00 8.61   ? 232  THR C C   1 
ATOM   7142  O  O   . THR C  1 145 ? 58.710  -1.687  88.373  1.00 8.59   ? 232  THR C O   1 
ATOM   7143  C  CB  . THR C  1 145 ? 57.772  -4.821  90.295  1.00 8.40   ? 232  THR C CB  1 
ATOM   7144  O  OG1 . THR C  1 145 ? 58.215  -5.854  89.399  1.00 8.39   ? 232  THR C OG1 1 
ATOM   7145  C  CG2 . THR C  1 145 ? 56.236  -4.621  90.176  1.00 8.47   ? 232  THR C CG2 1 
ATOM   7146  N  N   . GLN C  1 146 ? 58.208  -3.788  87.637  1.00 8.69   ? 233  GLN C N   1 
ATOM   7147  C  CA  . GLN C  1 146 ? 58.516  -3.581  86.217  1.00 8.94   ? 233  GLN C CA  1 
ATOM   7148  C  C   . GLN C  1 146 ? 57.712  -2.479  85.500  1.00 8.79   ? 233  GLN C C   1 
ATOM   7149  O  O   . GLN C  1 146 ? 58.283  -1.697  84.717  1.00 8.96   ? 233  GLN C O   1 
ATOM   7150  C  CB  . GLN C  1 146 ? 58.432  -4.909  85.452  1.00 8.87   ? 233  GLN C CB  1 
ATOM   7151  C  CG  . GLN C  1 146 ? 59.522  -5.895  85.856  1.00 9.01   ? 233  GLN C CG  1 
ATOM   7152  C  CD  . GLN C  1 146 ? 59.400  -7.265  85.212  1.00 9.92   ? 233  GLN C CD  1 
ATOM   7153  O  OE1 . GLN C  1 146 ? 58.696  -7.463  84.203  1.00 11.12  ? 233  GLN C OE1 1 
ATOM   7154  N  NE2 . GLN C  1 146 ? 60.090  -8.211  85.786  1.00 8.52   ? 233  GLN C NE2 1 
ATOM   7155  N  N   . GLU C  1 147 ? 56.401  -2.408  85.763  1.00 8.16   ? 234  GLU C N   1 
ATOM   7156  C  CA  . GLU C  1 147 ? 55.492  -1.522  85.011  1.00 8.62   ? 234  GLU C CA  1 
ATOM   7157  C  C   . GLU C  1 147 ? 55.308  -1.975  83.553  1.00 8.88   ? 234  GLU C C   1 
ATOM   7158  O  O   . GLU C  1 147 ? 54.870  -1.202  82.713  1.00 9.16   ? 234  GLU C O   1 
ATOM   7159  C  CB  . GLU C  1 147 ? 55.870  -0.010  85.099  1.00 8.38   ? 234  GLU C CB  1 
ATOM   7160  C  CG  . GLU C  1 147 ? 56.479  0.495   86.429  1.00 8.35   ? 234  GLU C CG  1 
ATOM   7161  C  CD  . GLU C  1 147 ? 55.587  0.289   87.672  1.00 7.09   ? 234  GLU C CD  1 
ATOM   7162  O  OE1 . GLU C  1 147 ? 56.047  0.697   88.766  1.00 9.73   ? 234  GLU C OE1 1 
ATOM   7163  O  OE2 . GLU C  1 147 ? 54.449  -0.255  87.583  1.00 7.81   ? 234  GLU C OE2 1 
ATOM   7164  N  N   . SER C  1 148 ? 55.637  -3.244  83.278  1.00 9.06   ? 235  SER C N   1 
ATOM   7165  C  CA  . SER C  1 148 ? 55.233  -3.942  82.057  1.00 9.23   ? 235  SER C CA  1 
ATOM   7166  C  C   . SER C  1 148 ? 55.254  -5.436  82.353  1.00 9.03   ? 235  SER C C   1 
ATOM   7167  O  O   . SER C  1 148 ? 55.564  -5.838  83.485  1.00 9.46   ? 235  SER C O   1 
ATOM   7168  C  CB  . SER C  1 148 ? 56.113  -3.596  80.844  1.00 8.74   ? 235  SER C CB  1 
ATOM   7169  O  OG  . SER C  1 148 ? 57.461  -4.017  81.038  1.00 8.25   ? 235  SER C OG  1 
ATOM   7170  N  N   . GLU C  1 149 ? 54.936  -6.259  81.349  1.00 8.14   ? 236  GLU C N   1 
ATOM   7171  C  CA  . GLU C  1 149 ? 54.696  -7.673  81.606  1.00 7.74   ? 236  GLU C CA  1 
ATOM   7172  C  C   . GLU C  1 149 ? 55.946  -8.463  82.003  1.00 8.31   ? 236  GLU C C   1 
ATOM   7173  O  O   . GLU C  1 149 ? 57.080  -8.173  81.571  1.00 8.03   ? 236  GLU C O   1 
ATOM   7174  C  CB  . GLU C  1 149 ? 53.957  -8.351  80.426  1.00 7.29   ? 236  GLU C CB  1 
ATOM   7175  C  CG  . GLU C  1 149 ? 54.852  -8.761  79.257  1.00 7.28   ? 236  GLU C CG  1 
ATOM   7176  C  CD  . GLU C  1 149 ? 54.115  -9.623  78.211  1.00 7.33   ? 236  GLU C CD  1 
ATOM   7177  O  OE1 . GLU C  1 149 ? 52.877  -9.817  78.321  1.00 6.29   ? 236  GLU C OE1 1 
ATOM   7178  O  OE2 . GLU C  1 149 ? 54.785  -10.111 77.283  1.00 9.23   ? 236  GLU C OE2 1 
ATOM   7179  N  N   . CYS C  1 150 ? 55.717  -9.433  82.873  1.00 8.54   ? 237  CYS C N   1 
ATOM   7180  C  CA  . CYS C  1 150 ? 56.689  -10.478 83.130  1.00 8.93   ? 237  CYS C CA  1 
ATOM   7181  C  C   . CYS C  1 150 ? 56.565  -11.580 82.053  1.00 9.46   ? 237  CYS C C   1 
ATOM   7182  O  O   . CYS C  1 150 ? 55.770  -11.459 81.102  1.00 9.91   ? 237  CYS C O   1 
ATOM   7183  C  CB  . CYS C  1 150 ? 56.547  -11.009 84.567  1.00 8.70   ? 237  CYS C CB  1 
ATOM   7184  S  SG  . CYS C  1 150 ? 54.811  -11.254 85.161  1.00 9.95   ? 237  CYS C SG  1 
ATOM   7185  N  N   . VAL C  1 151 ? 57.396  -12.620 82.152  1.00 9.69   ? 238  VAL C N   1 
ATOM   7186  C  CA  . VAL C  1 151 ? 57.444  -13.653 81.113  1.00 9.91   ? 238  VAL C CA  1 
ATOM   7187  C  C   . VAL C  1 151 ? 57.559  -14.982 81.856  1.00 10.20  ? 238  VAL C C   1 
ATOM   7188  O  O   . VAL C  1 151 ? 58.250  -15.053 82.888  1.00 10.27  ? 238  VAL C O   1 
ATOM   7189  C  CB  . VAL C  1 151 ? 58.679  -13.474 80.157  1.00 10.10  ? 238  VAL C CB  1 
ATOM   7190  C  CG1 . VAL C  1 151 ? 58.629  -14.464 78.969  1.00 9.69   ? 238  VAL C CG1 1 
ATOM   7191  C  CG2 . VAL C  1 151 ? 58.808  -12.018 79.641  1.00 11.06  ? 238  VAL C CG2 1 
ATOM   7192  N  N   . CYS C  1 152 ? 56.885  -16.012 81.348  1.00 10.01  ? 239  CYS C N   1 
ATOM   7193  C  CA  . CYS C  1 152 ? 56.869  -17.331 81.973  1.00 10.35  ? 239  CYS C CA  1 
ATOM   7194  C  C   . CYS C  1 152 ? 57.396  -18.430 81.052  1.00 10.74  ? 239  CYS C C   1 
ATOM   7195  O  O   . CYS C  1 152 ? 57.252  -18.345 79.821  1.00 11.50  ? 239  CYS C O   1 
ATOM   7196  C  CB  . CYS C  1 152 ? 55.448  -17.709 82.405  1.00 10.23  ? 239  CYS C CB  1 
ATOM   7197  S  SG  . CYS C  1 152 ? 54.632  -16.449 83.413  1.00 11.58  ? 239  CYS C SG  1 
ATOM   7198  N  N   . HIS C  1 153 ? 57.977  -19.459 81.671  1.00 10.46  ? 240  HIS C N   1 
ATOM   7199  C  CA  . HIS C  1 153 ? 58.521  -20.637 80.973  1.00 10.64  ? 240  HIS C CA  1 
ATOM   7200  C  C   . HIS C  1 153 ? 58.334  -21.875 81.861  1.00 10.95  ? 240  HIS C C   1 
ATOM   7201  O  O   . HIS C  1 153 ? 58.840  -21.916 82.997  1.00 10.30  ? 240  HIS C O   1 
ATOM   7202  C  CB  . HIS C  1 153 ? 60.017  -20.434 80.638  1.00 11.32  ? 240  HIS C CB  1 
ATOM   7203  C  CG  . HIS C  1 153 ? 60.638  -21.588 79.901  1.00 13.00  ? 240  HIS C CG  1 
ATOM   7204  N  ND1 . HIS C  1 153 ? 61.498  -22.484 80.501  1.00 14.84  ? 240  HIS C ND1 1 
ATOM   7205  C  CD2 . HIS C  1 153 ? 60.510  -21.995 78.615  1.00 11.03  ? 240  HIS C CD2 1 
ATOM   7206  C  CE1 . HIS C  1 153 ? 61.884  -23.385 79.612  1.00 11.57  ? 240  HIS C CE1 1 
ATOM   7207  N  NE2 . HIS C  1 153 ? 61.289  -23.119 78.464  1.00 15.56  ? 240  HIS C NE2 1 
ATOM   7208  N  N   . LYS C  1 154 ? 57.611  -22.865 81.333  1.00 10.79  ? 241  LYS C N   1 
ATOM   7209  C  CA  . LYS C  1 154 ? 57.322  -24.114 82.055  1.00 12.42  ? 241  LYS C CA  1 
ATOM   7210  C  C   . LYS C  1 154 ? 56.704  -23.829 83.424  1.00 11.74  ? 241  LYS C C   1 
ATOM   7211  O  O   . LYS C  1 154 ? 56.937  -24.575 84.387  1.00 12.75  ? 241  LYS C O   1 
ATOM   7212  C  CB  . LYS C  1 154 ? 58.591  -24.994 82.175  1.00 11.59  ? 241  LYS C CB  1 
ATOM   7213  C  CG  . LYS C  1 154 ? 59.161  -25.459 80.823  1.00 13.59  ? 241  LYS C CG  1 
ATOM   7214  C  CD  . LYS C  1 154 ? 60.423  -26.362 80.975  1.00 14.63  ? 241  LYS C CD  1 
ATOM   7215  C  CE  . LYS C  1 154 ? 60.860  -26.881 79.585  1.00 15.65  ? 241  LYS C CE  1 
ATOM   7216  N  NZ  . LYS C  1 154 ? 62.173  -27.613 79.627  1.00 20.16  ? 241  LYS C NZ  1 
ATOM   7217  N  N   . GLY C  1 155 ? 55.915  -22.748 83.497  1.00 11.87  ? 242  GLY C N   1 
ATOM   7218  C  CA  . GLY C  1 155 ? 55.243  -22.345 84.726  1.00 11.53  ? 242  GLY C CA  1 
ATOM   7219  C  C   . GLY C  1 155 ? 56.015  -21.423 85.646  1.00 11.93  ? 242  GLY C C   1 
ATOM   7220  O  O   . GLY C  1 155 ? 55.453  -20.928 86.634  1.00 11.79  ? 242  GLY C O   1 
ATOM   7221  N  N   . VAL C  1 156 ? 57.297  -21.185 85.344  1.00 11.19  ? 243  VAL C N   1 
ATOM   7222  C  CA  . VAL C  1 156 ? 58.136  -20.329 86.186  1.00 11.12  ? 243  VAL C CA  1 
ATOM   7223  C  C   . VAL C  1 156 ? 58.175  -18.925 85.585  1.00 10.57  ? 243  VAL C C   1 
ATOM   7224  O  O   . VAL C  1 156 ? 58.571  -18.772 84.429  1.00 11.17  ? 243  VAL C O   1 
ATOM   7225  C  CB  . VAL C  1 156 ? 59.597  -20.888 86.319  1.00 11.01  ? 243  VAL C CB  1 
ATOM   7226  C  CG1 . VAL C  1 156 ? 60.477  -19.922 87.110  1.00 11.02  ? 243  VAL C CG1 1 
ATOM   7227  C  CG2 . VAL C  1 156 ? 59.609  -22.266 86.970  1.00 11.65  ? 243  VAL C CG2 1 
ATOM   7228  N  N   . CYS C  1 157 ? 57.750  -17.918 86.363  1.00 10.47  ? 244  CYS C N   1 
ATOM   7229  C  CA  . CYS C  1 157 ? 57.686  -16.514 85.899  1.00 10.11  ? 244  CYS C CA  1 
ATOM   7230  C  C   . CYS C  1 157 ? 58.590  -15.629 86.736  1.00 10.31  ? 244  CYS C C   1 
ATOM   7231  O  O   . CYS C  1 157 ? 58.249  -15.270 87.875  1.00 10.53  ? 244  CYS C O   1 
ATOM   7232  C  CB  . CYS C  1 157 ? 56.246  -15.961 85.944  1.00 10.44  ? 244  CYS C CB  1 
ATOM   7233  S  SG  . CYS C  1 157 ? 54.971  -17.066 85.314  1.00 11.16  ? 244  CYS C SG  1 
ATOM   7234  N  N   . PRO C  1 158 ? 59.784  -15.295 86.203  1.00 10.11  ? 245  PRO C N   1 
ATOM   7235  C  CA  . PRO C  1 158 ? 60.647  -14.406 86.958  1.00 9.93   ? 245  PRO C CA  1 
ATOM   7236  C  C   . PRO C  1 158 ? 60.128  -12.959 86.932  1.00 8.97   ? 245  PRO C C   1 
ATOM   7237  O  O   . PRO C  1 158 ? 59.593  -12.508 85.917  1.00 9.12   ? 245  PRO C O   1 
ATOM   7238  C  CB  . PRO C  1 158 ? 61.992  -14.489 86.211  1.00 10.54  ? 245  PRO C CB  1 
ATOM   7239  C  CG  . PRO C  1 158 ? 61.890  -15.689 85.292  1.00 11.72  ? 245  PRO C CG  1 
ATOM   7240  C  CD  . PRO C  1 158 ? 60.413  -15.730 84.944  1.00 9.41   ? 245  PRO C CD  1 
ATOM   7241  N  N   . VAL C  1 159 ? 60.278  -12.266 88.055  1.00 8.91   ? 246  VAL C N   1 
ATOM   7242  C  CA  . VAL C  1 159 ? 59.942  -10.836 88.193  1.00 8.88   ? 246  VAL C CA  1 
ATOM   7243  C  C   . VAL C  1 159 ? 61.109  -10.067 88.826  1.00 9.56   ? 246  VAL C C   1 
ATOM   7244  O  O   . VAL C  1 159 ? 61.666  -10.494 89.858  1.00 9.82   ? 246  VAL C O   1 
ATOM   7245  C  CB  . VAL C  1 159 ? 58.666  -10.655 89.085  1.00 8.83   ? 246  VAL C CB  1 
ATOM   7246  C  CG1 . VAL C  1 159 ? 58.322  -9.185  89.295  1.00 8.38   ? 246  VAL C CG1 1 
ATOM   7247  C  CG2 . VAL C  1 159 ? 57.466  -11.382 88.450  1.00 7.97   ? 246  VAL C CG2 1 
ATOM   7248  N  N   . VAL C  1 160 ? 61.462  -8.921  88.234  1.00 9.51   ? 247  VAL C N   1 
ATOM   7249  C  CA  . VAL C  1 160 ? 62.545  -8.089  88.768  1.00 9.66   ? 247  VAL C CA  1 
ATOM   7250  C  C   . VAL C  1 160 ? 61.917  -7.032  89.678  1.00 9.69   ? 247  VAL C C   1 
ATOM   7251  O  O   . VAL C  1 160 ? 60.969  -6.353  89.281  1.00 9.07   ? 247  VAL C O   1 
ATOM   7252  C  CB  . VAL C  1 160 ? 63.363  -7.400  87.667  1.00 9.17   ? 247  VAL C CB  1 
ATOM   7253  C  CG1 . VAL C  1 160 ? 64.556  -6.623  88.281  1.00 9.47   ? 247  VAL C CG1 1 
ATOM   7254  C  CG2 . VAL C  1 160 ? 63.844  -8.427  86.605  1.00 10.65  ? 247  VAL C CG2 1 
ATOM   7255  N  N   . MET C  1 161 ? 62.424  -6.924  90.901  1.00 9.60   ? 248  MET C N   1 
ATOM   7256  C  CA  . MET C  1 161 ? 61.941  -5.913  91.853  1.00 9.62   ? 248  MET C CA  1 
ATOM   7257  C  C   . MET C  1 161 ? 63.085  -5.134  92.491  1.00 9.75   ? 248  MET C C   1 
ATOM   7258  O  O   . MET C  1 161 ? 64.202  -5.639  92.639  1.00 10.61  ? 248  MET C O   1 
ATOM   7259  C  CB  . MET C  1 161 ? 61.104  -6.542  92.984  1.00 9.89   ? 248  MET C CB  1 
ATOM   7260  C  CG  . MET C  1 161 ? 59.906  -7.380  92.554  1.00 9.14   ? 248  MET C CG  1 
ATOM   7261  S  SD  . MET C  1 161 ? 59.154  -8.152  94.004  1.00 9.52   ? 248  MET C SD  1 
ATOM   7262  C  CE  . MET C  1 161 ? 57.846  -9.087  93.208  1.00 11.30  ? 248  MET C CE  1 
ATOM   7263  N  N   . THR C  1 162 ? 62.798  -3.896  92.874  1.00 9.42   ? 249  THR C N   1 
ATOM   7264  C  CA  . THR C  1 162 ? 63.789  -3.034  93.495  1.00 8.75   ? 249  THR C CA  1 
ATOM   7265  C  C   . THR C  1 162 ? 63.192  -2.411  94.767  1.00 8.75   ? 249  THR C C   1 
ATOM   7266  O  O   . THR C  1 162 ? 62.002  -2.134  94.822  1.00 8.03   ? 249  THR C O   1 
ATOM   7267  C  CB  . THR C  1 162 ? 64.289  -1.965  92.482  1.00 8.94   ? 249  THR C CB  1 
ATOM   7268  O  OG1 . THR C  1 162 ? 64.893  -2.631  91.370  1.00 9.95   ? 249  THR C OG1 1 
ATOM   7269  C  CG2 . THR C  1 162 ? 65.317  -0.986  93.114  1.00 8.97   ? 249  THR C CG2 1 
ATOM   7270  N  N   . ASP C  1 163 ? 64.028  -2.243  95.789  1.00 8.36   ? 250  ASP C N   1 
ATOM   7271  C  CA  . ASP C  1 163 ? 63.666  -1.573  97.031  1.00 9.30   ? 250  ASP C CA  1 
ATOM   7272  C  C   . ASP C  1 163 ? 64.920  -0.780  97.438  1.00 10.13  ? 250  ASP C C   1 
ATOM   7273  O  O   . ASP C  1 163 ? 65.997  -1.333  97.464  1.00 10.25  ? 250  ASP C O   1 
ATOM   7274  C  CB  . ASP C  1 163 ? 63.294  -2.611  98.094  1.00 8.76   ? 250  ASP C CB  1 
ATOM   7275  C  CG  . ASP C  1 163 ? 62.522  -2.026  99.279  1.00 8.89   ? 250  ASP C CG  1 
ATOM   7276  O  OD1 . ASP C  1 163 ? 61.926  -2.822  100.033 1.00 9.16   ? 250  ASP C OD1 1 
ATOM   7277  O  OD2 . ASP C  1 163 ? 62.527  -0.795  99.489  1.00 8.58   ? 250  ASP C OD2 1 
ATOM   7278  N  N   . GLY C  1 164 ? 64.770  0.503   97.744  1.00 11.01  ? 251  GLY C N   1 
ATOM   7279  C  CA  . GLY C  1 164 ? 65.905  1.359   98.132  1.00 11.83  ? 251  GLY C CA  1 
ATOM   7280  C  C   . GLY C  1 164 ? 65.906  2.636   97.302  1.00 12.69  ? 251  GLY C C   1 
ATOM   7281  O  O   . GLY C  1 164 ? 64.940  2.896   96.566  1.00 12.77  ? 251  GLY C O   1 
ATOM   7282  N  N   . PRO C  1 165 ? 66.982  3.446   97.409  1.00 13.39  ? 252  PRO C N   1 
ATOM   7283  C  CA  . PRO C  1 165 ? 67.011  4.773   96.779  1.00 14.14  ? 252  PRO C CA  1 
ATOM   7284  C  C   . PRO C  1 165 ? 66.887  4.711   95.260  1.00 14.35  ? 252  PRO C C   1 
ATOM   7285  O  O   . PRO C  1 165 ? 67.320  3.749   94.635  1.00 14.64  ? 252  PRO C O   1 
ATOM   7286  C  CB  . PRO C  1 165 ? 68.408  5.312   97.134  1.00 13.91  ? 252  PRO C CB  1 
ATOM   7287  C  CG  . PRO C  1 165 ? 68.900  4.472   98.260  1.00 14.39  ? 252  PRO C CG  1 
ATOM   7288  C  CD  . PRO C  1 165 ? 68.232  3.146   98.137  1.00 13.78  ? 252  PRO C CD  1 
ATOM   7289  N  N   . ALA C  1 166 ? 66.304  5.755   94.682  1.00 15.29  ? 253  ALA C N   1 
ATOM   7290  C  CA  . ALA C  1 166 ? 66.263  5.928   93.225  1.00 15.86  ? 253  ALA C CA  1 
ATOM   7291  C  C   . ALA C  1 166 ? 67.557  6.551   92.686  1.00 16.48  ? 253  ALA C C   1 
ATOM   7292  O  O   . ALA C  1 166 ? 67.789  6.541   91.474  1.00 16.20  ? 253  ALA C O   1 
ATOM   7293  C  CB  . ALA C  1 166 ? 65.070  6.791   92.842  1.00 16.01  ? 253  ALA C CB  1 
ATOM   7294  N  N   . ASN C  1 167 ? 68.391  7.077   93.589  1.00 17.30  ? 254  ASN C N   1 
ATOM   7295  C  CA  . ASN C  1 167 ? 69.551  7.902   93.212  1.00 17.89  ? 254  ASN C CA  1 
ATOM   7296  C  C   . ASN C  1 167 ? 70.885  7.399   93.784  1.00 18.15  ? 254  ASN C C   1 
ATOM   7297  O  O   . ASN C  1 167 ? 71.837  8.178   93.951  1.00 18.45  ? 254  ASN C O   1 
ATOM   7298  C  CB  . ASN C  1 167 ? 69.315  9.366   93.640  1.00 18.52  ? 254  ASN C CB  1 
ATOM   7299  C  CG  . ASN C  1 167 ? 69.210  9.529   95.168  1.00 19.23  ? 254  ASN C CG  1 
ATOM   7300  O  OD1 . ASN C  1 167 ? 69.106  8.549   95.912  1.00 20.48  ? 254  ASN C OD1 1 
ATOM   7301  N  ND2 . ASN C  1 167 ? 69.241  10.768  95.631  1.00 22.30  ? 254  ASN C ND2 1 
ATOM   7302  N  N   . ASN C  1 168 ? 70.945  6.105   94.095  1.00 17.93  ? 255  ASN C N   1 
ATOM   7303  C  CA  . ASN C  1 168 ? 72.103  5.498   94.749  1.00 18.46  ? 255  ASN C CA  1 
ATOM   7304  C  C   . ASN C  1 168 ? 71.956  3.992   94.639  1.00 18.53  ? 255  ASN C C   1 
ATOM   7305  O  O   . ASN C  1 168 ? 70.992  3.508   94.026  1.00 18.25  ? 255  ASN C O   1 
ATOM   7306  C  CB  . ASN C  1 168 ? 72.154  5.901   96.230  1.00 18.47  ? 255  ASN C CB  1 
ATOM   7307  C  CG  . ASN C  1 168 ? 73.577  5.981   96.786  1.00 20.84  ? 255  ASN C CG  1 
ATOM   7308  O  OD1 . ASN C  1 168 ? 74.517  5.330   96.291  1.00 22.58  ? 255  ASN C OD1 1 
ATOM   7309  N  ND2 . ASN C  1 168 ? 73.742  6.797   97.830  1.00 22.72  ? 255  ASN C ND2 1 
ATOM   7310  N  N   . ARG C  1 169 ? 72.895  3.248   95.227  1.00 18.30  ? 256  ARG C N   1 
ATOM   7311  C  CA  . ARG C  1 169 ? 72.772  1.799   95.267  1.00 19.18  ? 256  ARG C CA  1 
ATOM   7312  C  C   . ARG C  1 169 ? 71.476  1.367   95.997  1.00 17.72  ? 256  ARG C C   1 
ATOM   7313  O  O   . ARG C  1 169 ? 71.144  1.873   97.084  1.00 17.12  ? 256  ARG C O   1 
ATOM   7314  C  CB  . ARG C  1 169 ? 74.015  1.136   95.875  1.00 18.78  ? 256  ARG C CB  1 
ATOM   7315  C  CG  . ARG C  1 169 ? 74.125  -0.332  95.501  1.00 22.21  ? 256  ARG C CG  1 
ATOM   7316  C  CD  . ARG C  1 169 ? 75.526  -0.951  95.735  1.00 22.89  ? 256  ARG C CD  1 
ATOM   7317  N  NE  . ARG C  1 169 ? 76.647  -0.399  94.945  1.00 29.38  ? 256  ARG C NE  1 
ATOM   7318  C  CZ  . ARG C  1 169 ? 76.793  -0.437  93.610  1.00 30.34  ? 256  ARG C CZ  1 
ATOM   7319  N  NH1 . ARG C  1 169 ? 75.854  -0.948  92.803  1.00 28.39  ? 256  ARG C NH1 1 
ATOM   7320  N  NH2 . ARG C  1 169 ? 77.900  0.082   93.067  1.00 29.67  ? 256  ARG C NH2 1 
ATOM   7321  N  N   . ALA C  1 170 ? 70.762  0.437   95.366  1.00 16.41  ? 257  ALA C N   1 
ATOM   7322  C  CA  . ALA C  1 170 ? 69.507  -0.094  95.877  1.00 14.96  ? 257  ALA C CA  1 
ATOM   7323  C  C   . ALA C  1 170 ? 69.609  -1.611  95.964  1.00 14.41  ? 257  ALA C C   1 
ATOM   7324  O  O   . ALA C  1 170 ? 70.630  -2.190  95.572  1.00 14.71  ? 257  ALA C O   1 
ATOM   7325  C  CB  . ALA C  1 170 ? 68.360  0.311   94.967  1.00 13.73  ? 257  ALA C CB  1 
ATOM   7326  N  N   . ALA C  1 171 ? 68.549  -2.255  96.461  1.00 12.73  ? 258  ALA C N   1 
ATOM   7327  C  CA  . ALA C  1 171 ? 68.537  -3.701  96.643  1.00 12.12  ? 258  ALA C CA  1 
ATOM   7328  C  C   . ALA C  1 171 ? 67.545  -4.313  95.663  1.00 11.64  ? 258  ALA C C   1 
ATOM   7329  O  O   . ALA C  1 171 ? 66.324  -4.295  95.895  1.00 11.93  ? 258  ALA C O   1 
ATOM   7330  C  CB  . ALA C  1 171 ? 68.173  -4.072  98.082  1.00 11.91  ? 258  ALA C CB  1 
ATOM   7331  N  N   . THR C  1 172 ? 68.076  -4.811  94.554  1.00 10.64  ? 259  THR C N   1 
ATOM   7332  C  CA  . THR C  1 172 ? 67.258  -5.432  93.512  1.00 10.50  ? 259  THR C CA  1 
ATOM   7333  C  C   . THR C  1 172 ? 67.262  -6.943  93.691  1.00 10.50  ? 259  THR C C   1 
ATOM   7334  O  O   . THR C  1 172 ? 68.280  -7.526  94.078  1.00 10.34  ? 259  THR C O   1 
ATOM   7335  C  CB  . THR C  1 172 ? 67.728  -4.991  92.095  1.00 9.49   ? 259  THR C CB  1 
ATOM   7336  O  OG1 . THR C  1 172 ? 67.419  -3.600  91.919  1.00 10.84  ? 259  THR C OG1 1 
ATOM   7337  C  CG2 . THR C  1 172 ? 67.077  -5.819  90.965  1.00 9.22   ? 259  THR C CG2 1 
ATOM   7338  N  N   . LYS C  1 173 ? 66.102  -7.556  93.467  1.00 10.91  ? 260  LYS C N   1 
ATOM   7339  C  CA  . LYS C  1 173 ? 65.966  -9.008  93.522  1.00 11.60  ? 260  LYS C CA  1 
ATOM   7340  C  C   . LYS C  1 173 ? 65.213  -9.550  92.316  1.00 11.98  ? 260  LYS C C   1 
ATOM   7341  O  O   . LYS C  1 173 ? 64.370  -8.861  91.720  1.00 12.01  ? 260  LYS C O   1 
ATOM   7342  C  CB  . LYS C  1 173 ? 65.297  -9.481  94.827  1.00 11.17  ? 260  LYS C CB  1 
ATOM   7343  C  CG  . LYS C  1 173 ? 66.096  -9.150  96.060  1.00 13.79  ? 260  LYS C CG  1 
ATOM   7344  C  CD  . LYS C  1 173 ? 65.354  -9.498  97.316  1.00 15.25  ? 260  LYS C CD  1 
ATOM   7345  C  CE  . LYS C  1 173 ? 66.114  -9.006  98.520  1.00 16.98  ? 260  LYS C CE  1 
ATOM   7346  N  NZ  . LYS C  1 173 ? 65.501  -9.644  99.706  1.00 21.09  ? 260  LYS C NZ  1 
ATOM   7347  N  N   . ILE C  1 174 ? 65.564  -10.779 91.950  1.00 11.91  ? 261  ILE C N   1 
ATOM   7348  C  CA  . ILE C  1 174 ? 64.809  -11.556 90.972  1.00 13.05  ? 261  ILE C CA  1 
ATOM   7349  C  C   . ILE C  1 174 ? 64.061  -12.625 91.747  1.00 12.80  ? 261  ILE C C   1 
ATOM   7350  O  O   . ILE C  1 174 ? 64.669  -13.449 92.455  1.00 12.62  ? 261  ILE C O   1 
ATOM   7351  C  CB  . ILE C  1 174 ? 65.706  -12.230 89.880  1.00 13.24  ? 261  ILE C CB  1 
ATOM   7352  C  CG1 . ILE C  1 174 ? 66.812  -11.285 89.355  1.00 15.60  ? 261  ILE C CG1 1 
ATOM   7353  C  CG2 . ILE C  1 174 ? 64.838  -12.834 88.758  1.00 13.30  ? 261  ILE C CG2 1 
ATOM   7354  C  CD1 . ILE C  1 174 ? 66.340  -9.943  88.854  1.00 20.01  ? 261  ILE C CD1 1 
ATOM   7355  N  N   . ILE C  1 175 ? 62.735  -12.591 91.643  1.00 12.23  ? 262  ILE C N   1 
ATOM   7356  C  CA  . ILE C  1 175 ? 61.897  -13.546 92.366  1.00 12.20  ? 262  ILE C CA  1 
ATOM   7357  C  C   . ILE C  1 175 ? 61.196  -14.412 91.343  1.00 11.92  ? 262  ILE C C   1 
ATOM   7358  O  O   . ILE C  1 175 ? 60.581  -13.918 90.396  1.00 11.96  ? 262  ILE C O   1 
ATOM   7359  C  CB  . ILE C  1 175 ? 60.896  -12.856 93.341  1.00 12.19  ? 262  ILE C CB  1 
ATOM   7360  C  CG1 . ILE C  1 175 ? 61.640  -11.868 94.260  1.00 13.27  ? 262  ILE C CG1 1 
ATOM   7361  C  CG2 . ILE C  1 175 ? 60.076  -13.926 94.156  1.00 11.76  ? 262  ILE C CG2 1 
ATOM   7362  C  CD1 . ILE C  1 175 ? 60.803  -11.294 95.390  1.00 12.84  ? 262  ILE C CD1 1 
ATOM   7363  N  N   . TYR C  1 176 ? 61.354  -15.714 91.506  1.00 11.46  ? 263  TYR C N   1 
ATOM   7364  C  CA  . TYR C  1 176 ? 60.853  -16.677 90.537  1.00 11.70  ? 263  TYR C CA  1 
ATOM   7365  C  C   . TYR C  1 176 ? 59.576  -17.283 91.089  1.00 11.59  ? 263  TYR C C   1 
ATOM   7366  O  O   . TYR C  1 176 ? 59.608  -17.935 92.139  1.00 12.20  ? 263  TYR C O   1 
ATOM   7367  C  CB  . TYR C  1 176 ? 61.900  -17.771 90.318  1.00 11.73  ? 263  TYR C CB  1 
ATOM   7368  C  CG  . TYR C  1 176 ? 63.213  -17.257 89.750  1.00 12.15  ? 263  TYR C CG  1 
ATOM   7369  C  CD1 . TYR C  1 176 ? 64.180  -16.682 90.583  1.00 11.86  ? 263  TYR C CD1 1 
ATOM   7370  C  CD2 . TYR C  1 176 ? 63.491  -17.363 88.380  1.00 10.24  ? 263  TYR C CD2 1 
ATOM   7371  C  CE1 . TYR C  1 176 ? 65.389  -16.227 90.070  1.00 12.06  ? 263  TYR C CE1 1 
ATOM   7372  C  CE2 . TYR C  1 176 ? 64.686  -16.905 87.853  1.00 11.18  ? 263  TYR C CE2 1 
ATOM   7373  C  CZ  . TYR C  1 176 ? 65.630  -16.328 88.700  1.00 11.70  ? 263  TYR C CZ  1 
ATOM   7374  O  OH  . TYR C  1 176 ? 66.838  -15.887 88.211  1.00 13.18  ? 263  TYR C OH  1 
ATOM   7375  N  N   . PHE C  1 177 ? 58.467  -17.056 90.386  1.00 11.62  ? 264  PHE C N   1 
ATOM   7376  C  CA  . PHE C  1 177 ? 57.140  -17.532 90.816  1.00 11.12  ? 264  PHE C CA  1 
ATOM   7377  C  C   . PHE C  1 177 ? 56.631  -18.714 90.019  1.00 11.27  ? 264  PHE C C   1 
ATOM   7378  O  O   . PHE C  1 177 ? 56.937  -18.853 88.839  1.00 11.72  ? 264  PHE C O   1 
ATOM   7379  C  CB  . PHE C  1 177 ? 56.107  -16.406 90.685  1.00 10.32  ? 264  PHE C CB  1 
ATOM   7380  C  CG  . PHE C  1 177 ? 56.367  -15.228 91.573  1.00 10.16  ? 264  PHE C CG  1 
ATOM   7381  C  CD1 . PHE C  1 177 ? 57.022  -14.089 91.074  1.00 9.69   ? 264  PHE C CD1 1 
ATOM   7382  C  CD2 . PHE C  1 177 ? 55.945  -15.239 92.908  1.00 10.47  ? 264  PHE C CD2 1 
ATOM   7383  C  CE1 . PHE C  1 177 ? 57.270  -12.973 91.915  1.00 11.36  ? 264  PHE C CE1 1 
ATOM   7384  C  CE2 . PHE C  1 177 ? 56.176  -14.137 93.752  1.00 10.28  ? 264  PHE C CE2 1 
ATOM   7385  C  CZ  . PHE C  1 177 ? 56.832  -13.002 93.257  1.00 10.41  ? 264  PHE C CZ  1 
ATOM   7386  N  N   . LYS C  1 178 ? 55.825  -19.546 90.668  1.00 11.81  ? 265  LYS C N   1 
ATOM   7387  C  CA  . LYS C  1 178 ? 55.040  -20.580 90.002  1.00 12.14  ? 265  LYS C CA  1 
ATOM   7388  C  C   . LYS C  1 178 ? 53.698  -20.665 90.701  1.00 11.69  ? 265  LYS C C   1 
ATOM   7389  O  O   . LYS C  1 178 ? 53.635  -20.891 91.919  1.00 10.00  ? 265  LYS C O   1 
ATOM   7390  C  CB  . LYS C  1 178 ? 55.742  -21.941 90.005  1.00 12.22  ? 265  LYS C CB  1 
ATOM   7391  C  CG  . LYS C  1 178 ? 55.004  -22.982 89.201  1.00 14.69  ? 265  LYS C CG  1 
ATOM   7392  C  CD  . LYS C  1 178 ? 55.722  -24.316 89.167  1.00 19.20  ? 265  LYS C CD  1 
ATOM   7393  C  CE  . LYS C  1 178 ? 54.885  -25.351 88.434  1.00 21.92  ? 265  LYS C CE  1 
ATOM   7394  N  NZ  . LYS C  1 178 ? 55.496  -26.706 88.533  1.00 26.93  ? 265  LYS C NZ  1 
ATOM   7395  N  N   . GLU C  1 179 ? 52.643  -20.433 89.916  1.00 11.87  ? 266  GLU C N   1 
ATOM   7396  C  CA  . GLU C  1 179 ? 51.251  -20.375 90.398  1.00 12.34  ? 266  GLU C CA  1 
ATOM   7397  C  C   . GLU C  1 179 ? 51.109  -19.365 91.557  1.00 11.25  ? 266  GLU C C   1 
ATOM   7398  O  O   . GLU C  1 179 ? 50.368  -19.585 92.520  1.00 10.42  ? 266  GLU C O   1 
ATOM   7399  C  CB  . GLU C  1 179 ? 50.730  -21.790 90.742  1.00 12.37  ? 266  GLU C CB  1 
ATOM   7400  C  CG  . GLU C  1 179 ? 50.735  -22.680 89.498  1.00 13.52  ? 266  GLU C CG  1 
ATOM   7401  C  CD  . GLU C  1 179 ? 50.290  -24.118 89.722  1.00 16.89  ? 266  GLU C CD  1 
ATOM   7402  O  OE1 . GLU C  1 179 ? 50.357  -24.630 90.857  1.00 21.81  ? 266  GLU C OE1 1 
ATOM   7403  O  OE2 . GLU C  1 179 ? 49.893  -24.744 88.723  1.00 21.54  ? 266  GLU C OE2 1 
ATOM   7404  N  N   . GLY C  1 180 ? 51.885  -18.280 91.461  1.00 11.17  ? 267  GLY C N   1 
ATOM   7405  C  CA  . GLY C  1 180 ? 51.895  -17.211 92.464  1.00 10.89  ? 267  GLY C CA  1 
ATOM   7406  C  C   . GLY C  1 180 ? 52.740  -17.474 93.695  1.00 11.36  ? 267  GLY C C   1 
ATOM   7407  O  O   . GLY C  1 180 ? 52.823  -16.620 94.585  1.00 11.26  ? 267  GLY C O   1 
ATOM   7408  N  N   . LYS C  1 181 ? 53.372  -18.648 93.753  1.00 11.44  ? 268  LYS C N   1 
ATOM   7409  C  CA  . LYS C  1 181 ? 54.203  -19.032 94.911  1.00 12.76  ? 268  LYS C CA  1 
ATOM   7410  C  C   . LYS C  1 181 ? 55.679  -18.859 94.621  1.00 11.69  ? 268  LYS C C   1 
ATOM   7411  O  O   . LYS C  1 181 ? 56.122  -19.148 93.511  1.00 12.57  ? 268  LYS C O   1 
ATOM   7412  C  CB  . LYS C  1 181 ? 53.948  -20.478 95.338  1.00 11.70  ? 268  LYS C CB  1 
ATOM   7413  C  CG  . LYS C  1 181 ? 52.489  -20.807 95.695  1.00 15.40  ? 268  LYS C CG  1 
ATOM   7414  C  CD  . LYS C  1 181 ? 52.385  -22.200 96.305  1.00 16.39  ? 268  LYS C CD  1 
ATOM   7415  C  CE  . LYS C  1 181 ? 51.073  -22.369 97.074  1.00 23.57  ? 268  LYS C CE  1 
ATOM   7416  N  NZ  . LYS C  1 181 ? 50.858  -23.802 97.523  1.00 27.35  ? 268  LYS C NZ  1 
ATOM   7417  N  N   . ILE C  1 182 ? 56.434  -18.421 95.628  1.00 11.45  ? 269  ILE C N   1 
ATOM   7418  C  CA  . ILE C  1 182 ? 57.864  -18.126 95.442  1.00 11.53  ? 269  ILE C CA  1 
ATOM   7419  C  C   . ILE C  1 182 ? 58.627  -19.450 95.378  1.00 11.66  ? 269  ILE C C   1 
ATOM   7420  O  O   . ILE C  1 182 ? 58.523  -20.275 96.291  1.00 11.23  ? 269  ILE C O   1 
ATOM   7421  C  CB  . ILE C  1 182 ? 58.429  -17.220 96.567  1.00 10.79  ? 269  ILE C CB  1 
ATOM   7422  C  CG1 . ILE C  1 182 ? 57.780  -15.817 96.513  1.00 12.07  ? 269  ILE C CG1 1 
ATOM   7423  C  CG2 . ILE C  1 182 ? 59.995  -17.128 96.474  1.00 9.62   ? 269  ILE C CG2 1 
ATOM   7424  C  CD1 . ILE C  1 182 ? 58.099  -14.902 97.716  1.00 12.17  ? 269  ILE C CD1 1 
ATOM   7425  N  N   . GLN C  1 183 ? 59.359  -19.639 94.281  1.00 12.07  ? 270  GLN C N   1 
ATOM   7426  C  CA  . GLN C  1 183 ? 60.212  -20.813 94.076  1.00 11.98  ? 270  GLN C CA  1 
ATOM   7427  C  C   . GLN C  1 183 ? 61.649  -20.557 94.512  1.00 12.41  ? 270  GLN C C   1 
ATOM   7428  O  O   . GLN C  1 183 ? 62.337  -21.485 94.942  1.00 12.45  ? 270  GLN C O   1 
ATOM   7429  C  CB  . GLN C  1 183 ? 60.204  -21.242 92.601  1.00 12.18  ? 270  GLN C CB  1 
ATOM   7430  C  CG  . GLN C  1 183 ? 58.820  -21.509 92.018  1.00 12.24  ? 270  GLN C CG  1 
ATOM   7431  C  CD  . GLN C  1 183 ? 58.036  -22.520 92.836  1.00 17.12  ? 270  GLN C CD  1 
ATOM   7432  O  OE1 . GLN C  1 183 ? 56.997  -22.193 93.448  1.00 18.22  ? 270  GLN C OE1 1 
ATOM   7433  N  NE2 . GLN C  1 183 ? 58.537  -23.755 92.877  1.00 14.67  ? 270  GLN C NE2 1 
ATOM   7434  N  N   . LYS C  1 184 ? 62.099  -19.308 94.377  1.00 11.96  ? 271  LYS C N   1 
ATOM   7435  C  CA  . LYS C  1 184 ? 63.499  -18.920 94.612  1.00 11.80  ? 271  LYS C CA  1 
ATOM   7436  C  C   . LYS C  1 184 ? 63.582  -17.396 94.585  1.00 12.35  ? 271  LYS C C   1 
ATOM   7437  O  O   . LYS C  1 184 ? 62.826  -16.752 93.841  1.00 11.59  ? 271  LYS C O   1 
ATOM   7438  C  CB  . LYS C  1 184 ? 64.418  -19.490 93.521  1.00 11.58  ? 271  LYS C CB  1 
ATOM   7439  C  CG  . LYS C  1 184 ? 65.939  -19.347 93.796  1.00 12.28  ? 271  LYS C CG  1 
ATOM   7440  C  CD  . LYS C  1 184 ? 66.767  -19.891 92.635  1.00 11.75  ? 271  LYS C CD  1 
ATOM   7441  C  CE  . LYS C  1 184 ? 68.261  -19.779 92.953  1.00 14.00  ? 271  LYS C CE  1 
ATOM   7442  N  NZ  . LYS C  1 184 ? 69.060  -20.368 91.834  1.00 14.14  ? 271  LYS C NZ  1 
ATOM   7443  N  N   . ILE C  1 185 ? 64.494  -16.848 95.390  1.00 12.36  ? 272  ILE C N   1 
ATOM   7444  C  CA  . ILE C  1 185 ? 64.825  -15.417 95.404  1.00 13.50  ? 272  ILE C CA  1 
ATOM   7445  C  C   . ILE C  1 185 ? 66.348  -15.247 95.231  1.00 14.62  ? 272  ILE C C   1 
ATOM   7446  O  O   . ILE C  1 185 ? 67.126  -15.858 95.968  1.00 15.07  ? 272  ILE C O   1 
ATOM   7447  C  CB  . ILE C  1 185 ? 64.390  -14.745 96.736  1.00 13.65  ? 272  ILE C CB  1 
ATOM   7448  C  CG1 . ILE C  1 185 ? 62.877  -14.841 96.953  1.00 14.52  ? 272  ILE C CG1 1 
ATOM   7449  C  CG2 . ILE C  1 185 ? 64.834  -13.289 96.788  1.00 14.51  ? 272  ILE C CG2 1 
ATOM   7450  C  CD1 . ILE C  1 185 ? 62.444  -14.622 98.391  1.00 14.11  ? 272  ILE C CD1 1 
ATOM   7451  N  N   . GLU C  1 186 ? 66.772  -14.445 94.252  1.00 14.51  ? 273  GLU C N   1 
ATOM   7452  C  CA  . GLU C  1 186 ? 68.188  -14.130 94.082  1.00 14.30  ? 273  GLU C CA  1 
ATOM   7453  C  C   . GLU C  1 186 ? 68.425  -12.642 94.261  1.00 14.82  ? 273  GLU C C   1 
ATOM   7454  O  O   . GLU C  1 186 ? 67.627  -11.837 93.788  1.00 14.49  ? 273  GLU C O   1 
ATOM   7455  C  CB  . GLU C  1 186 ? 68.658  -14.491 92.673  1.00 14.42  ? 273  GLU C CB  1 
ATOM   7456  C  CG  . GLU C  1 186 ? 68.684  -15.960 92.326  1.00 15.05  ? 273  GLU C CG  1 
ATOM   7457  C  CD  . GLU C  1 186 ? 69.384  -16.171 91.014  1.00 16.61  ? 273  GLU C CD  1 
ATOM   7458  O  OE1 . GLU C  1 186 ? 68.864  -15.653 90.004  1.00 13.86  ? 273  GLU C OE1 1 
ATOM   7459  O  OE2 . GLU C  1 186 ? 70.465  -16.820 91.000  1.00 16.91  ? 273  GLU C OE2 1 
ATOM   7460  N  N   . GLU C  1 187 ? 69.531  -12.275 94.910  1.00 13.84  ? 274  GLU C N   1 
ATOM   7461  C  CA  . GLU C  1 187 ? 69.972  -10.894 94.880  1.00 15.77  ? 274  GLU C CA  1 
ATOM   7462  C  C   . GLU C  1 187 ? 70.551  -10.624 93.489  1.00 14.24  ? 274  GLU C C   1 
ATOM   7463  O  O   . GLU C  1 187 ? 71.111  -11.527 92.858  1.00 13.44  ? 274  GLU C O   1 
ATOM   7464  C  CB  . GLU C  1 187 ? 71.002  -10.596 95.982  1.00 15.50  ? 274  GLU C CB  1 
ATOM   7465  C  CG  . GLU C  1 187 ? 70.398  -10.685 97.391  1.00 19.63  ? 274  GLU C CG  1 
ATOM   7466  C  CD  . GLU C  1 187 ? 71.438  -10.591 98.501  1.00 20.36  ? 274  GLU C CD  1 
ATOM   7467  O  OE1 . GLU C  1 187 ? 72.650  -10.427 98.206  1.00 25.09  ? 274  GLU C OE1 1 
ATOM   7468  O  OE2 . GLU C  1 187 ? 71.032  -10.686 99.682  1.00 27.18  ? 274  GLU C OE2 1 
ATOM   7469  N  N   . LEU C  1 188 ? 70.364  -9.403  93.003  1.00 13.82  ? 275  LEU C N   1 
ATOM   7470  C  CA  . LEU C  1 188 ? 70.957  -8.987  91.735  1.00 13.78  ? 275  LEU C CA  1 
ATOM   7471  C  C   . LEU C  1 188 ? 72.473  -9.224  91.746  1.00 13.71  ? 275  LEU C C   1 
ATOM   7472  O  O   . LEU C  1 188 ? 73.167  -8.810  92.684  1.00 14.22  ? 275  LEU C O   1 
ATOM   7473  C  CB  . LEU C  1 188 ? 70.679  -7.503  91.468  1.00 13.50  ? 275  LEU C CB  1 
ATOM   7474  C  CG  . LEU C  1 188 ? 71.296  -6.917  90.187  1.00 14.51  ? 275  LEU C CG  1 
ATOM   7475  C  CD1 . LEU C  1 188 ? 70.643  -7.500  88.911  1.00 15.55  ? 275  LEU C CD1 1 
ATOM   7476  C  CD2 . LEU C  1 188 ? 71.263  -5.372  90.221  1.00 13.50  ? 275  LEU C CD2 1 
ATOM   7477  N  N   . ALA C  1 189 ? 72.968  -9.851  90.688  1.00 13.82  ? 276  ALA C N   1 
ATOM   7478  C  CA  . ALA C  1 189 ? 74.398  -10.090 90.507  1.00 13.81  ? 276  ALA C CA  1 
ATOM   7479  C  C   . ALA C  1 189 ? 74.858  -9.434  89.207  1.00 14.09  ? 276  ALA C C   1 
ATOM   7480  O  O   . ALA C  1 189 ? 74.026  -8.938  88.409  1.00 14.24  ? 276  ALA C O   1 
ATOM   7481  C  CB  . ALA C  1 189 ? 74.682  -11.605 90.504  1.00 14.57  ? 276  ALA C CB  1 
ATOM   7482  N  N   . GLY C  1 190 ? 76.169  -9.399  88.986  1.00 13.33  ? 277  GLY C N   1 
ATOM   7483  C  CA  . GLY C  1 190 ? 76.692  -8.850  87.745  1.00 12.96  ? 277  GLY C CA  1 
ATOM   7484  C  C   . GLY C  1 190 ? 77.041  -7.373  87.784  1.00 12.72  ? 277  GLY C C   1 
ATOM   7485  O  O   . GLY C  1 190 ? 77.168  -6.753  88.860  1.00 12.82  ? 277  GLY C O   1 
ATOM   7486  N  N   . ASN C  1 191 ? 77.204  -6.806  86.598  1.00 12.37  ? 278  ASN C N   1 
ATOM   7487  C  CA  . ASN C  1 191 ? 77.735  -5.462  86.462  1.00 12.10  ? 278  ASN C CA  1 
ATOM   7488  C  C   . ASN C  1 191 ? 76.728  -4.313  86.322  1.00 12.01  ? 278  ASN C C   1 
ATOM   7489  O  O   . ASN C  1 191 ? 77.131  -3.157  86.253  1.00 12.61  ? 278  ASN C O   1 
ATOM   7490  C  CB  . ASN C  1 191 ? 78.794  -5.410  85.346  1.00 11.95  ? 278  ASN C CB  1 
ATOM   7491  C  CG  . ASN C  1 191 ? 80.094  -6.046  85.765  1.00 12.51  ? 278  ASN C CG  1 
ATOM   7492  O  OD1 . ASN C  1 191 ? 80.337  -6.241  86.959  1.00 9.90   ? 278  ASN C OD1 1 
ATOM   7493  N  ND2 . ASN C  1 191 ? 80.931  -6.392  84.789  1.00 11.40  ? 278  ASN C ND2 1 
ATOM   7494  N  N   . ALA C  1 192 ? 75.429  -4.611  86.261  1.00 12.32  ? 279  ALA C N   1 
ATOM   7495  C  CA  . ALA C  1 192 ? 74.427  -3.536  86.293  1.00 12.00  ? 279  ALA C CA  1 
ATOM   7496  C  C   . ALA C  1 192 ? 74.453  -2.873  87.693  1.00 12.35  ? 279  ALA C C   1 
ATOM   7497  O  O   . ALA C  1 192 ? 74.402  -3.570  88.695  1.00 12.93  ? 279  ALA C O   1 
ATOM   7498  C  CB  . ALA C  1 192 ? 73.032  -4.090  85.964  1.00 11.20  ? 279  ALA C CB  1 
ATOM   7499  N  N   . GLN C  1 193 ? 74.583  -1.543  87.755  1.00 12.50  ? 280  GLN C N   1 
ATOM   7500  C  CA  . GLN C  1 193 ? 74.806  -0.868  89.046  1.00 13.03  ? 280  GLN C CA  1 
ATOM   7501  C  C   . GLN C  1 193 ? 73.528  -0.392  89.739  1.00 12.46  ? 280  GLN C C   1 
ATOM   7502  O  O   . GLN C  1 193 ? 73.535  -0.147  90.960  1.00 12.44  ? 280  GLN C O   1 
ATOM   7503  C  CB  . GLN C  1 193 ? 75.800  0.283   88.901  1.00 12.73  ? 280  GLN C CB  1 
ATOM   7504  C  CG  . GLN C  1 193 ? 77.236  -0.190  88.558  1.00 14.14  ? 280  GLN C CG  1 
ATOM   7505  C  CD  . GLN C  1 193 ? 78.243  0.936   88.548  1.00 15.52  ? 280  GLN C CD  1 
ATOM   7506  O  OE1 . GLN C  1 193 ? 77.943  2.049   88.985  1.00 18.29  ? 280  GLN C OE1 1 
ATOM   7507  N  NE2 . GLN C  1 193 ? 79.461  0.648   88.061  1.00 15.64  ? 280  GLN C NE2 1 
ATOM   7508  N  N   . HIS C  1 194 ? 72.456  -0.260  88.951  1.00 11.90  ? 281  HIS C N   1 
ATOM   7509  C  CA  . HIS C  1 194 ? 71.137  0.192   89.422  1.00 11.37  ? 281  HIS C CA  1 
ATOM   7510  C  C   . HIS C  1 194 ? 70.055  -0.317  88.464  1.00 11.23  ? 281  HIS C C   1 
ATOM   7511  O  O   . HIS C  1 194 ? 70.255  -0.278  87.242  1.00 10.48  ? 281  HIS C O   1 
ATOM   7512  C  CB  . HIS C  1 194 ? 71.066  1.722   89.502  1.00 11.79  ? 281  HIS C CB  1 
ATOM   7513  C  CG  . HIS C  1 194 ? 69.861  2.225   90.236  1.00 12.97  ? 281  HIS C CG  1 
ATOM   7514  N  ND1 . HIS C  1 194 ? 69.796  2.282   91.613  1.00 14.39  ? 281  HIS C ND1 1 
ATOM   7515  C  CD2 . HIS C  1 194 ? 68.662  2.669   89.784  1.00 13.34  ? 281  HIS C CD2 1 
ATOM   7516  C  CE1 . HIS C  1 194 ? 68.613  2.751   91.977  1.00 12.10  ? 281  HIS C CE1 1 
ATOM   7517  N  NE2 . HIS C  1 194 ? 67.900  2.976   90.888  1.00 14.60  ? 281  HIS C NE2 1 
ATOM   7518  N  N   . ILE C  1 195 ? 68.922  -0.774  89.019  1.00 10.68  ? 282  ILE C N   1 
ATOM   7519  C  CA  . ILE C  1 195 ? 67.868  -1.408  88.226  1.00 10.36  ? 282  ILE C CA  1 
ATOM   7520  C  C   . ILE C  1 195 ? 66.487  -0.851  88.563  1.00 10.51  ? 282  ILE C C   1 
ATOM   7521  O  O   . ILE C  1 195 ? 66.074  -0.881  89.728  1.00 11.41  ? 282  ILE C O   1 
ATOM   7522  C  CB  . ILE C  1 195 ? 67.869  -2.964  88.410  1.00 10.42  ? 282  ILE C CB  1 
ATOM   7523  C  CG1 . ILE C  1 195 ? 69.155  -3.595  87.858  1.00 10.32  ? 282  ILE C CG1 1 
ATOM   7524  C  CG2 . ILE C  1 195 ? 66.617  -3.596  87.753  1.00 10.77  ? 282  ILE C CG2 1 
ATOM   7525  C  CD1 . ILE C  1 195 ? 69.286  -3.556  86.312  1.00 12.09  ? 282  ILE C CD1 1 
ATOM   7526  N  N   . GLU C  1 196 ? 65.780  -0.348  87.549  1.00 9.75   ? 283  GLU C N   1 
ATOM   7527  C  CA  . GLU C  1 196 ? 64.352  0.017   87.692  1.00 10.07  ? 283  GLU C CA  1 
ATOM   7528  C  C   . GLU C  1 196 ? 63.570  -0.473  86.486  1.00 9.35   ? 283  GLU C C   1 
ATOM   7529  O  O   . GLU C  1 196 ? 64.116  -0.514  85.390  1.00 9.66   ? 283  GLU C O   1 
ATOM   7530  C  CB  . GLU C  1 196 ? 64.138  1.529   87.730  1.00 10.29  ? 283  GLU C CB  1 
ATOM   7531  C  CG  . GLU C  1 196 ? 64.932  2.314   88.742  1.00 12.92  ? 283  GLU C CG  1 
ATOM   7532  C  CD  . GLU C  1 196 ? 64.332  2.302   90.123  1.00 16.70  ? 283  GLU C CD  1 
ATOM   7533  O  OE1 . GLU C  1 196 ? 63.265  1.675   90.331  1.00 18.07  ? 283  GLU C OE1 1 
ATOM   7534  O  OE2 . GLU C  1 196 ? 64.939  2.934   91.015  1.00 19.58  ? 283  GLU C OE2 1 
ATOM   7535  N  N   . GLU C  1 197 ? 62.282  -0.765  86.691  1.00 8.65   ? 284  GLU C N   1 
ATOM   7536  C  CA  . GLU C  1 197 ? 61.280  -0.835  85.605  1.00 8.73   ? 284  GLU C CA  1 
ATOM   7537  C  C   . GLU C  1 197 ? 61.713  -1.674  84.390  1.00 8.43   ? 284  GLU C C   1 
ATOM   7538  O  O   . GLU C  1 197 ? 61.651  -1.203  83.242  1.00 8.81   ? 284  GLU C O   1 
ATOM   7539  C  CB  . GLU C  1 197 ? 60.872  0.586   85.155  1.00 8.75   ? 284  GLU C CB  1 
ATOM   7540  C  CG  . GLU C  1 197 ? 60.293  1.440   86.276  1.00 8.12   ? 284  GLU C CG  1 
ATOM   7541  C  CD  . GLU C  1 197 ? 60.170  2.956   85.958  1.00 9.40   ? 284  GLU C CD  1 
ATOM   7542  O  OE1 . GLU C  1 197 ? 60.798  3.476   85.004  1.00 9.86   ? 284  GLU C OE1 1 
ATOM   7543  O  OE2 . GLU C  1 197 ? 59.412  3.638   86.683  1.00 11.06  ? 284  GLU C OE2 1 
ATOM   7544  N  N   . CYS C  1 198 ? 62.117  -2.916  84.640  1.00 8.08   ? 285  CYS C N   1 
ATOM   7545  C  CA  . CYS C  1 198 ? 62.565  -3.824  83.575  1.00 8.73   ? 285  CYS C CA  1 
ATOM   7546  C  C   . CYS C  1 198 ? 61.478  -4.138  82.556  1.00 8.72   ? 285  CYS C C   1 
ATOM   7547  O  O   . CYS C  1 198 ? 60.315  -4.367  82.923  1.00 9.16   ? 285  CYS C O   1 
ATOM   7548  C  CB  . CYS C  1 198 ? 63.124  -5.118  84.157  1.00 7.89   ? 285  CYS C CB  1 
ATOM   7549  S  SG  . CYS C  1 198 ? 64.642  -4.789  85.053  1.00 10.98  ? 285  CYS C SG  1 
ATOM   7550  N  N   . SER C  1 199 ? 61.852  -4.090  81.276  1.00 9.22   ? 286  SER C N   1 
ATOM   7551  C  CA  . SER C  1 199 ? 60.977  -4.557  80.177  1.00 9.27   ? 286  SER C CA  1 
ATOM   7552  C  C   . SER C  1 199 ? 61.585  -5.861  79.667  1.00 9.89   ? 286  SER C C   1 
ATOM   7553  O  O   . SER C  1 199 ? 62.746  -5.882  79.242  1.00 9.79   ? 286  SER C O   1 
ATOM   7554  C  CB  . SER C  1 199 ? 60.903  -3.521  79.035  1.00 9.75   ? 286  SER C CB  1 
ATOM   7555  O  OG  . SER C  1 199 ? 60.388  -2.256  79.492  1.00 8.99   ? 286  SER C OG  1 
ATOM   7556  N  N   . CYS C  1 200 ? 60.788  -6.929  79.696  1.00 9.73   ? 287  CYS C N   1 
ATOM   7557  C  CA  . CYS C  1 200 ? 61.277  -8.294  79.524  1.00 10.36  ? 287  CYS C CA  1 
ATOM   7558  C  C   . CYS C  1 200 ? 60.521  -9.052  78.432  1.00 10.50  ? 287  CYS C C   1 
ATOM   7559  O  O   . CYS C  1 200 ? 59.335  -8.832  78.225  1.00 11.03  ? 287  CYS C O   1 
ATOM   7560  C  CB  . CYS C  1 200 ? 61.174  -9.081  80.842  1.00 10.17  ? 287  CYS C CB  1 
ATOM   7561  S  SG  . CYS C  1 200 ? 61.829  -8.288  82.344  1.00 10.75  ? 287  CYS C SG  1 
ATOM   7562  N  N   . TYR C  1 201 ? 61.226  -9.958  77.750  1.00 10.72  ? 288  TYR C N   1 
ATOM   7563  C  CA  . TYR C  1 201 ? 60.615  -10.841 76.754  1.00 10.74  ? 288  TYR C CA  1 
ATOM   7564  C  C   . TYR C  1 201 ? 61.425  -12.135 76.721  1.00 11.08  ? 288  TYR C C   1 
ATOM   7565  O  O   . TYR C  1 201 ? 62.583  -12.169 77.179  1.00 11.48  ? 288  TYR C O   1 
ATOM   7566  C  CB  . TYR C  1 201 ? 60.569  -10.186 75.358  1.00 10.12  ? 288  TYR C CB  1 
ATOM   7567  C  CG  . TYR C  1 201 ? 61.955  -10.063 74.756  1.00 9.99   ? 288  TYR C CG  1 
ATOM   7568  C  CD1 . TYR C  1 201 ? 62.742  -8.935  75.002  1.00 8.04   ? 288  TYR C CD1 1 
ATOM   7569  C  CD2 . TYR C  1 201 ? 62.500  -11.114 73.998  1.00 10.11  ? 288  TYR C CD2 1 
ATOM   7570  C  CE1 . TYR C  1 201 ? 64.059  -8.848  74.478  1.00 12.55  ? 288  TYR C CE1 1 
ATOM   7571  C  CE2 . TYR C  1 201 ? 63.801  -11.037 73.473  1.00 8.55   ? 288  TYR C CE2 1 
ATOM   7572  C  CZ  . TYR C  1 201 ? 64.573  -9.909  73.719  1.00 11.22  ? 288  TYR C CZ  1 
ATOM   7573  O  OH  . TYR C  1 201 ? 65.852  -9.857  73.177  1.00 9.67   ? 288  TYR C OH  1 
ATOM   7574  N  N   . GLY C  1 202 ? 60.830  -13.182 76.165  1.00 10.91  ? 289  GLY C N   1 
ATOM   7575  C  CA  . GLY C  1 202 ? 61.500  -14.467 76.064  1.00 11.44  ? 289  GLY C CA  1 
ATOM   7576  C  C   . GLY C  1 202 ? 61.639  -14.997 74.647  1.00 11.49  ? 289  GLY C C   1 
ATOM   7577  O  O   . GLY C  1 202 ? 60.786  -14.747 73.788  1.00 11.36  ? 289  GLY C O   1 
ATOM   7578  N  N   . ALA C  1 203 ? 62.699  -15.767 74.423  1.00 12.21  ? 290  ALA C N   1 
ATOM   7579  C  CA  . ALA C  1 203 ? 62.975  -16.420 73.134  1.00 12.39  ? 290  ALA C CA  1 
ATOM   7580  C  C   . ALA C  1 203 ? 64.030  -17.489 73.368  1.00 12.39  ? 290  ALA C C   1 
ATOM   7581  O  O   . ALA C  1 203 ? 64.975  -17.265 74.119  1.00 12.65  ? 290  ALA C O   1 
ATOM   7582  C  CB  . ALA C  1 203 ? 63.486  -15.387 72.091  1.00 11.91  ? 290  ALA C CB  1 
ATOM   7583  N  N   . GLY C  1 204 ? 63.875  -18.652 72.739  1.00 12.72  ? 291  GLY C N   1 
ATOM   7584  C  CA  . GLY C  1 204 ? 64.865  -19.721 72.873  1.00 13.60  ? 291  GLY C CA  1 
ATOM   7585  C  C   . GLY C  1 204 ? 65.288  -20.025 74.299  1.00 13.70  ? 291  GLY C C   1 
ATOM   7586  O  O   . GLY C  1 204 ? 66.484  -20.191 74.581  1.00 13.93  ? 291  GLY C O   1 
ATOM   7587  N  N   . GLY C  1 205 ? 64.306  -20.091 75.191  1.00 14.11  ? 292  GLY C N   1 
ATOM   7588  C  CA  . GLY C  1 205 ? 64.501  -20.485 76.578  1.00 14.71  ? 292  GLY C CA  1 
ATOM   7589  C  C   . GLY C  1 205 ? 65.249  -19.491 77.440  1.00 14.92  ? 292  GLY C C   1 
ATOM   7590  O  O   . GLY C  1 205 ? 65.684  -19.831 78.549  1.00 16.08  ? 292  GLY C O   1 
ATOM   7591  N  N   . VAL C  1 206 ? 65.394  -18.268 76.933  1.00 14.42  ? 293  VAL C N   1 
ATOM   7592  C  CA  . VAL C  1 206 ? 66.120  -17.197 77.610  1.00 14.35  ? 293  VAL C CA  1 
ATOM   7593  C  C   . VAL C  1 206 ? 65.190  -15.992 77.749  1.00 13.73  ? 293  VAL C C   1 
ATOM   7594  O  O   . VAL C  1 206 ? 64.465  -15.645 76.808  1.00 13.56  ? 293  VAL C O   1 
ATOM   7595  C  CB  . VAL C  1 206 ? 67.408  -16.792 76.813  1.00 14.68  ? 293  VAL C CB  1 
ATOM   7596  C  CG1 . VAL C  1 206 ? 68.155  -15.666 77.490  1.00 14.32  ? 293  VAL C CG1 1 
ATOM   7597  C  CG2 . VAL C  1 206 ? 68.332  -17.995 76.634  1.00 14.93  ? 293  VAL C CG2 1 
ATOM   7598  N  N   . ILE C  1 207 ? 65.186  -15.396 78.934  1.00 13.36  ? 294  ILE C N   1 
ATOM   7599  C  CA  . ILE C  1 207 ? 64.467  -14.145 79.185  1.00 12.78  ? 294  ILE C CA  1 
ATOM   7600  C  C   . ILE C  1 207 ? 65.441  -12.983 79.302  1.00 12.89  ? 294  ILE C C   1 
ATOM   7601  O  O   . ILE C  1 207 ? 66.390  -13.042 80.098  1.00 12.64  ? 294  ILE C O   1 
ATOM   7602  C  CB  . ILE C  1 207 ? 63.560  -14.248 80.458  1.00 12.83  ? 294  ILE C CB  1 
ATOM   7603  C  CG1 . ILE C  1 207 ? 62.437  -15.265 80.227  1.00 12.01  ? 294  ILE C CG1 1 
ATOM   7604  C  CG2 . ILE C  1 207 ? 62.991  -12.847 80.880  1.00 13.13  ? 294  ILE C CG2 1 
ATOM   7605  C  CD1 . ILE C  1 207 ? 61.708  -15.668 81.527  1.00 12.80  ? 294  ILE C CD1 1 
ATOM   7606  N  N   . LYS C  1 208 ? 65.204  -11.936 78.526  1.00 11.02  ? 295  LYS C N   1 
ATOM   7607  C  CA  . LYS C  1 208 ? 66.012  -10.737 78.628  1.00 10.23  ? 295  LYS C CA  1 
ATOM   7608  C  C   . LYS C  1 208 ? 65.191  -9.553  79.102  1.00 10.40  ? 295  LYS C C   1 
ATOM   7609  O  O   . LYS C  1 208 ? 64.121  -9.271  78.583  1.00 10.63  ? 295  LYS C O   1 
ATOM   7610  C  CB  . LYS C  1 208 ? 66.717  -10.414 77.308  1.00 11.28  ? 295  LYS C CB  1 
ATOM   7611  C  CG  . LYS C  1 208 ? 67.663  -11.506 76.829  1.00 12.01  ? 295  LYS C CG  1 
ATOM   7612  C  CD  . LYS C  1 208 ? 68.451  -11.053 75.604  1.00 12.20  ? 295  LYS C CD  1 
ATOM   7613  C  CE  . LYS C  1 208 ? 68.896  -12.200 74.732  1.00 12.34  ? 295  LYS C CE  1 
ATOM   7614  N  NZ  . LYS C  1 208 ? 69.755  -11.831 73.589  1.00 11.21  ? 295  LYS C NZ  1 
ATOM   7615  N  N   . CYS C  1 209 ? 65.739  -8.885  80.104  1.00 10.82  ? 296  CYS C N   1 
ATOM   7616  C  CA  . CYS C  1 209 ? 65.110  -7.696  80.683  1.00 10.57  ? 296  CYS C CA  1 
ATOM   7617  C  C   . CYS C  1 209 ? 65.990  -6.491  80.432  1.00 10.12  ? 296  CYS C C   1 
ATOM   7618  O  O   . CYS C  1 209 ? 67.172  -6.496  80.797  1.00 9.22   ? 296  CYS C O   1 
ATOM   7619  C  CB  . CYS C  1 209 ? 64.876  -7.863  82.182  1.00 9.97   ? 296  CYS C CB  1 
ATOM   7620  S  SG  . CYS C  1 209 ? 63.686  -9.151  82.593  1.00 11.58  ? 296  CYS C SG  1 
ATOM   7621  N  N   . ILE C  1 210 ? 65.398  -5.461  79.820  1.00 9.67   ? 297  ILE C N   1 
ATOM   7622  C  CA  . ILE C  1 210 ? 66.111  -4.236  79.480  1.00 9.27   ? 297  ILE C CA  1 
ATOM   7623  C  C   . ILE C  1 210 ? 65.524  -3.154  80.380  1.00 9.57   ? 297  ILE C C   1 
ATOM   7624  O  O   . ILE C  1 210 ? 64.309  -2.914  80.369  1.00 9.36   ? 297  ILE C O   1 
ATOM   7625  C  CB  . ILE C  1 210 ? 65.955  -3.874  77.973  1.00 9.43   ? 297  ILE C CB  1 
ATOM   7626  C  CG1 . ILE C  1 210 ? 66.809  -4.787  77.085  1.00 10.07  ? 297  ILE C CG1 1 
ATOM   7627  C  CG2 . ILE C  1 210 ? 66.412  -2.419  77.721  1.00 6.89   ? 297  ILE C CG2 1 
ATOM   7628  C  CD1 . ILE C  1 210 ? 66.340  -6.253  76.982  1.00 9.17   ? 297  ILE C CD1 1 
ATOM   7629  N  N   . CYS C  1 211 ? 66.382  -2.543  81.192  1.00 9.41   ? 298  CYS C N   1 
ATOM   7630  C  CA  . CYS C  1 211 ? 65.914  -1.799  82.361  1.00 9.68   ? 298  CYS C CA  1 
ATOM   7631  C  C   . CYS C  1 211 ? 66.339  -0.323  82.348  1.00 9.86   ? 298  CYS C C   1 
ATOM   7632  O  O   . CYS C  1 211 ? 66.823  0.202   81.325  1.00 9.83   ? 298  CYS C O   1 
ATOM   7633  C  CB  . CYS C  1 211 ? 66.337  -2.550  83.658  1.00 10.21  ? 298  CYS C CB  1 
ATOM   7634  S  SG  . CYS C  1 211 ? 66.054  -4.390  83.592  1.00 11.18  ? 298  CYS C SG  1 
ATOM   7635  N  N   . ARG C  1 212 ? 66.148  0.340   83.477  1.00 9.13   ? 299  ARG C N   1 
ATOM   7636  C  CA  . ARG C  1 212 ? 66.424  1.766   83.628  1.00 10.16  ? 299  ARG C CA  1 
ATOM   7637  C  C   . ARG C  1 212 ? 67.407  1.928   84.796  1.00 10.36  ? 299  ARG C C   1 
ATOM   7638  O  O   . ARG C  1 212 ? 67.099  1.576   85.929  1.00 9.21   ? 299  ARG C O   1 
ATOM   7639  C  CB  . ARG C  1 212 ? 65.100  2.497   83.904  1.00 10.27  ? 299  ARG C CB  1 
ATOM   7640  C  CG  . ARG C  1 212 ? 65.217  3.945   84.393  1.00 9.45   ? 299  ARG C CG  1 
ATOM   7641  C  CD  . ARG C  1 212 ? 63.858  4.403   84.893  1.00 10.77  ? 299  ARG C CD  1 
ATOM   7642  N  NE  . ARG C  1 212 ? 63.920  5.689   85.579  1.00 9.59   ? 299  ARG C NE  1 
ATOM   7643  C  CZ  . ARG C  1 212 ? 62.875  6.494   85.798  1.00 10.41  ? 299  ARG C CZ  1 
ATOM   7644  N  NH1 . ARG C  1 212 ? 61.659  6.175   85.357  1.00 10.11  ? 299  ARG C NH1 1 
ATOM   7645  N  NH2 . ARG C  1 212 ? 63.053  7.635   86.446  1.00 11.77  ? 299  ARG C NH2 1 
ATOM   7646  N  N   . ASP C  1 213 ? 68.618  2.403   84.499  1.00 10.32  ? 300  ASP C N   1 
ATOM   7647  C  CA  . ASP C  1 213 ? 69.560  2.768   85.548  1.00 10.66  ? 300  ASP C CA  1 
ATOM   7648  C  C   . ASP C  1 213 ? 69.257  4.219   85.928  1.00 11.22  ? 300  ASP C C   1 
ATOM   7649  O  O   . ASP C  1 213 ? 69.550  5.150   85.162  1.00 11.43  ? 300  ASP C O   1 
ATOM   7650  C  CB  . ASP C  1 213 ? 71.026  2.591   85.071  1.00 10.68  ? 300  ASP C CB  1 
ATOM   7651  C  CG  . ASP C  1 213 ? 72.050  3.087   86.098  1.00 11.52  ? 300  ASP C CG  1 
ATOM   7652  O  OD1 . ASP C  1 213 ? 73.251  2.813   85.935  1.00 12.56  ? 300  ASP C OD1 1 
ATOM   7653  O  OD2 . ASP C  1 213 ? 71.659  3.763   87.059  1.00 14.31  ? 300  ASP C OD2 1 
ATOM   7654  N  N   . ASN C  1 214 ? 68.627  4.414   87.083  1.00 11.89  ? 301  ASN C N   1 
ATOM   7655  C  CA  . ASN C  1 214 ? 68.208  5.754   87.492  1.00 12.82  ? 301  ASN C CA  1 
ATOM   7656  C  C   . ASN C  1 214 ? 69.300  6.505   88.227  1.00 13.74  ? 301  ASN C C   1 
ATOM   7657  O  O   . ASN C  1 214 ? 69.168  7.700   88.513  1.00 13.88  ? 301  ASN C O   1 
ATOM   7658  C  CB  . ASN C  1 214 ? 66.946  5.697   88.370  1.00 13.10  ? 301  ASN C CB  1 
ATOM   7659  C  CG  . ASN C  1 214 ? 66.128  6.959   88.264  1.00 13.71  ? 301  ASN C CG  1 
ATOM   7660  O  OD1 . ASN C  1 214 ? 65.687  7.328   87.182  1.00 14.74  ? 301  ASN C OD1 1 
ATOM   7661  N  ND2 . ASN C  1 214 ? 65.933  7.644   89.391  1.00 16.84  ? 301  ASN C ND2 1 
ATOM   7662  N  N   . TRP C  1 215 ? 70.363  5.780   88.553  1.00 14.81  ? 302  TRP C N   1 
ATOM   7663  C  CA  . TRP C  1 215 ? 71.492  6.319   89.326  1.00 16.02  ? 302  TRP C CA  1 
ATOM   7664  C  C   . TRP C  1 215 ? 72.545  7.031   88.452  1.00 16.70  ? 302  TRP C C   1 
ATOM   7665  O  O   . TRP C  1 215 ? 72.720  8.229   88.568  1.00 17.52  ? 302  TRP C O   1 
ATOM   7666  C  CB  . TRP C  1 215 ? 72.108  5.191   90.168  1.00 15.98  ? 302  TRP C CB  1 
ATOM   7667  C  CG  . TRP C  1 215 ? 73.206  5.624   91.108  1.00 17.00  ? 302  TRP C CG  1 
ATOM   7668  C  CD1 . TRP C  1 215 ? 73.503  6.900   91.506  1.00 16.35  ? 302  TRP C CD1 1 
ATOM   7669  C  CD2 . TRP C  1 215 ? 74.128  4.766   91.790  1.00 17.89  ? 302  TRP C CD2 1 
ATOM   7670  N  NE1 . TRP C  1 215 ? 74.575  6.889   92.377  1.00 18.00  ? 302  TRP C NE1 1 
ATOM   7671  C  CE2 . TRP C  1 215 ? 74.977  5.595   92.569  1.00 16.85  ? 302  TRP C CE2 1 
ATOM   7672  C  CE3 . TRP C  1 215 ? 74.322  3.377   91.820  1.00 18.82  ? 302  TRP C CE3 1 
ATOM   7673  C  CZ2 . TRP C  1 215 ? 76.007  5.078   93.373  1.00 18.62  ? 302  TRP C CZ2 1 
ATOM   7674  C  CZ3 . TRP C  1 215 ? 75.358  2.864   92.620  1.00 17.99  ? 302  TRP C CZ3 1 
ATOM   7675  C  CH2 . TRP C  1 215 ? 76.182  3.726   93.384  1.00 16.39  ? 302  TRP C CH2 1 
ATOM   7676  N  N   . LYS C  1 216 ? 73.227  6.307   87.569  1.00 16.96  ? 303  LYS C N   1 
ATOM   7677  C  CA  . LYS C  1 216 ? 74.307  6.910   86.788  1.00 17.28  ? 303  LYS C CA  1 
ATOM   7678  C  C   . LYS C  1 216 ? 74.119  6.821   85.272  1.00 16.57  ? 303  LYS C C   1 
ATOM   7679  O  O   . LYS C  1 216 ? 74.434  7.752   84.554  1.00 15.99  ? 303  LYS C O   1 
ATOM   7680  C  CB  . LYS C  1 216 ? 75.659  6.278   87.152  1.00 17.98  ? 303  LYS C CB  1 
ATOM   7681  C  CG  . LYS C  1 216 ? 76.130  6.489   88.594  1.00 21.41  ? 303  LYS C CG  1 
ATOM   7682  C  CD  . LYS C  1 216 ? 77.195  5.444   88.918  1.00 24.18  ? 303  LYS C CD  1 
ATOM   7683  C  CE  . LYS C  1 216 ? 77.786  5.623   90.290  1.00 27.43  ? 303  LYS C CE  1 
ATOM   7684  N  NZ  . LYS C  1 216 ? 78.684  4.454   90.604  1.00 28.33  ? 303  LYS C NZ  1 
ATOM   7685  N  N   . GLY C  1 217 ? 73.633  5.686   84.789  1.00 15.60  ? 304  GLY C N   1 
ATOM   7686  C  CA  . GLY C  1 217 ? 73.763  5.353   83.370  1.00 14.89  ? 304  GLY C CA  1 
ATOM   7687  C  C   . GLY C  1 217 ? 72.694  5.871   82.425  1.00 13.89  ? 304  GLY C C   1 
ATOM   7688  O  O   . GLY C  1 217 ? 71.501  5.776   82.708  1.00 13.24  ? 304  GLY C O   1 
ATOM   7689  N  N   . ALA C  1 218 ? 73.139  6.404   81.295  1.00 13.02  ? 305  ALA C N   1 
ATOM   7690  C  CA  . ALA C  1 218 ? 72.261  6.745   80.166  1.00 13.11  ? 305  ALA C CA  1 
ATOM   7691  C  C   . ALA C  1 218 ? 72.199  5.593   79.176  1.00 13.02  ? 305  ALA C C   1 
ATOM   7692  O  O   . ALA C  1 218 ? 71.362  5.591   78.263  1.00 13.48  ? 305  ALA C O   1 
ATOM   7693  C  CB  . ALA C  1 218 ? 72.744  8.001   79.476  1.00 13.54  ? 305  ALA C CB  1 
ATOM   7694  N  N   . ASN C  1 219 ? 73.113  4.636   79.338  1.00 12.23  ? 306  ASN C N   1 
ATOM   7695  C  CA  . ASN C  1 219 ? 72.980  3.306   78.728  1.00 11.80  ? 306  ASN C CA  1 
ATOM   7696  C  C   . ASN C  1 219 ? 72.130  2.391   79.631  1.00 10.97  ? 306  ASN C C   1 
ATOM   7697  O  O   . ASN C  1 219 ? 72.167  2.530   80.858  1.00 10.62  ? 306  ASN C O   1 
ATOM   7698  C  CB  . ASN C  1 219 ? 74.354  2.671   78.402  1.00 12.58  ? 306  ASN C CB  1 
ATOM   7699  C  CG  . ASN C  1 219 ? 75.313  2.621   79.616  1.00 13.51  ? 306  ASN C CG  1 
ATOM   7700  O  OD1 . ASN C  1 219 ? 75.149  3.355   80.593  1.00 14.11  ? 306  ASN C OD1 1 
ATOM   7701  N  ND2 . ASN C  1 219 ? 76.324  1.739   79.536  1.00 11.94  ? 306  ASN C ND2 1 
ATOM   7702  N  N   . ARG C  1 220 ? 71.339  1.498   79.029  1.00 10.43  ? 307  ARG C N   1 
ATOM   7703  C  CA  . ARG C  1 220 ? 70.399  0.654   79.807  1.00 10.06  ? 307  ARG C CA  1 
ATOM   7704  C  C   . ARG C  1 220 ? 70.976  -0.669  80.292  1.00 10.33  ? 307  ARG C C   1 
ATOM   7705  O  O   . ARG C  1 220 ? 71.616  -1.416  79.516  1.00 10.97  ? 307  ARG C O   1 
ATOM   7706  C  CB  . ARG C  1 220 ? 69.119  0.359   79.011  1.00 10.34  ? 307  ARG C CB  1 
ATOM   7707  C  CG  . ARG C  1 220 ? 68.298  1.598   78.682  1.00 8.42   ? 307  ARG C CG  1 
ATOM   7708  C  CD  . ARG C  1 220 ? 66.925  1.204   78.070  1.00 9.42   ? 307  ARG C CD  1 
ATOM   7709  N  NE  . ARG C  1 220 ? 66.086  2.394   77.865  1.00 10.06  ? 307  ARG C NE  1 
ATOM   7710  C  CZ  . ARG C  1 220 ? 65.488  3.074   78.850  1.00 9.90   ? 307  ARG C CZ  1 
ATOM   7711  N  NH1 . ARG C  1 220 ? 65.600  2.684   80.133  1.00 8.31   ? 307  ARG C NH1 1 
ATOM   7712  N  NH2 . ARG C  1 220 ? 64.762  4.135   78.561  1.00 6.76   ? 307  ARG C NH2 1 
ATOM   7713  N  N   . PRO C  1 221 ? 70.733  -0.993  81.569  1.00 10.35  ? 308  PRO C N   1 
ATOM   7714  C  CA  . PRO C  1 221 ? 71.116  -2.312  82.066  1.00 10.61  ? 308  PRO C CA  1 
ATOM   7715  C  C   . PRO C  1 221 ? 70.379  -3.415  81.320  1.00 11.16  ? 308  PRO C C   1 
ATOM   7716  O  O   . PRO C  1 221 ? 69.222  -3.214  80.890  1.00 12.02  ? 308  PRO C O   1 
ATOM   7717  C  CB  . PRO C  1 221 ? 70.678  -2.276  83.538  1.00 10.32  ? 308  PRO C CB  1 
ATOM   7718  C  CG  . PRO C  1 221 ? 70.586  -0.855  83.864  1.00 9.96   ? 308  PRO C CG  1 
ATOM   7719  C  CD  . PRO C  1 221 ? 70.156  -0.148  82.635  1.00 9.79   ? 308  PRO C CD  1 
ATOM   7720  N  N   . VAL C  1 222 ? 71.048  -4.548  81.140  1.00 11.32  ? 309  VAL C N   1 
ATOM   7721  C  CA  . VAL C  1 222 ? 70.423  -5.747  80.592  1.00 11.84  ? 309  VAL C CA  1 
ATOM   7722  C  C   . VAL C  1 222 ? 70.611  -6.929  81.552  1.00 12.10  ? 309  VAL C C   1 
ATOM   7723  O  O   . VAL C  1 222 ? 71.753  -7.288  81.906  1.00 12.34  ? 309  VAL C O   1 
ATOM   7724  C  CB  . VAL C  1 222 ? 70.998  -6.090  79.195  1.00 11.89  ? 309  VAL C CB  1 
ATOM   7725  C  CG1 . VAL C  1 222 ? 70.296  -7.322  78.609  1.00 12.96  ? 309  VAL C CG1 1 
ATOM   7726  C  CG2 . VAL C  1 222 ? 70.893  -4.859  78.262  1.00 12.28  ? 309  VAL C CG2 1 
ATOM   7727  N  N   . ILE C  1 223 ? 69.496  -7.517  81.990  1.00 11.13  ? 310  ILE C N   1 
ATOM   7728  C  CA  . ILE C  1 223 ? 69.515  -8.720  82.844  1.00 11.35  ? 310  ILE C CA  1 
ATOM   7729  C  C   . ILE C  1 223 ? 69.132  -9.928  81.996  1.00 11.38  ? 310  ILE C C   1 
ATOM   7730  O  O   . ILE C  1 223 ? 68.064  -9.925  81.361  1.00 12.16  ? 310  ILE C O   1 
ATOM   7731  C  CB  . ILE C  1 223 ? 68.520  -8.616  84.058  1.00 11.70  ? 310  ILE C CB  1 
ATOM   7732  C  CG1 . ILE C  1 223 ? 68.792  -7.364  84.919  1.00 12.28  ? 310  ILE C CG1 1 
ATOM   7733  C  CG2 . ILE C  1 223 ? 68.514  -9.921  84.878  1.00 10.89  ? 310  ILE C CG2 1 
ATOM   7734  C  CD1 . ILE C  1 223 ? 67.871  -7.190  86.159  1.00 10.36  ? 310  ILE C CD1 1 
ATOM   7735  N  N   . THR C  1 224 ? 69.985  -10.956 81.980  1.00 10.73  ? 311  THR C N   1 
ATOM   7736  C  CA  . THR C  1 224 ? 69.707  -12.190 81.229  1.00 11.04  ? 311  THR C CA  1 
ATOM   7737  C  C   . THR C  1 224 ? 69.365  -13.314 82.189  1.00 11.19  ? 311  THR C C   1 
ATOM   7738  O  O   . THR C  1 224 ? 70.169  -13.655 83.052  1.00 11.14  ? 311  THR C O   1 
ATOM   7739  C  CB  . THR C  1 224 ? 70.901  -12.588 80.296  1.00 10.58  ? 311  THR C CB  1 
ATOM   7740  O  OG1 . THR C  1 224 ? 71.150  -11.524 79.375  1.00 11.38  ? 311  THR C OG1 1 
ATOM   7741  C  CG2 . THR C  1 224 ? 70.597  -13.866 79.486  1.00 9.94   ? 311  THR C CG2 1 
ATOM   7742  N  N   . ILE C  1 225 ? 68.158  -13.871 82.043  1.00 10.85  ? 312  ILE C N   1 
ATOM   7743  C  CA  . ILE C  1 225 ? 67.619  -14.828 83.005  1.00 11.21  ? 312  ILE C CA  1 
ATOM   7744  C  C   . ILE C  1 225 ? 67.369  -16.190 82.356  1.00 11.83  ? 312  ILE C C   1 
ATOM   7745  O  O   . ILE C  1 225 ? 66.754  -16.287 81.281  1.00 11.99  ? 312  ILE C O   1 
ATOM   7746  C  CB  . ILE C  1 225 ? 66.275  -14.335 83.663  1.00 10.75  ? 312  ILE C CB  1 
ATOM   7747  C  CG1 . ILE C  1 225 ? 66.455  -12.960 84.318  1.00 10.61  ? 312  ILE C CG1 1 
ATOM   7748  C  CG2 . ILE C  1 225 ? 65.736  -15.375 84.679  1.00 11.30  ? 312  ILE C CG2 1 
ATOM   7749  C  CD1 . ILE C  1 225 ? 65.134  -12.250 84.621  1.00 11.88  ? 312  ILE C CD1 1 
ATOM   7750  N  N   . ASP C  1 226 ? 67.881  -17.216 83.023  1.00 12.23  ? 313  ASP C N   1 
ATOM   7751  C  CA  . ASP C  1 226 ? 67.582  -18.620 82.737  1.00 13.39  ? 313  ASP C CA  1 
ATOM   7752  C  C   . ASP C  1 226 ? 66.446  -19.067 83.680  1.00 13.41  ? 313  ASP C C   1 
ATOM   7753  O  O   . ASP C  1 226 ? 66.677  -19.312 84.875  1.00 13.50  ? 313  ASP C O   1 
ATOM   7754  C  CB  . ASP C  1 226 ? 68.869  -19.455 82.935  1.00 13.70  ? 313  ASP C CB  1 
ATOM   7755  C  CG  . ASP C  1 226 ? 68.680  -20.941 82.620  1.00 15.97  ? 313  ASP C CG  1 
ATOM   7756  O  OD1 . ASP C  1 226 ? 69.707  -21.614 82.395  1.00 18.36  ? 313  ASP C OD1 1 
ATOM   7757  O  OD2 . ASP C  1 226 ? 67.534  -21.442 82.588  1.00 15.30  ? 313  ASP C OD2 1 
ATOM   7758  N  N   . PRO C  1 227 ? 65.204  -19.173 83.154  1.00 13.22  ? 314  PRO C N   1 
ATOM   7759  C  CA  . PRO C  1 227 ? 64.058  -19.523 84.006  1.00 13.70  ? 314  PRO C CA  1 
ATOM   7760  C  C   . PRO C  1 227 ? 63.990  -21.015 84.416  1.00 13.93  ? 314  PRO C C   1 
ATOM   7761  O  O   . PRO C  1 227 ? 63.186  -21.383 85.291  1.00 14.55  ? 314  PRO C O   1 
ATOM   7762  C  CB  . PRO C  1 227 ? 62.850  -19.131 83.140  1.00 13.26  ? 314  PRO C CB  1 
ATOM   7763  C  CG  . PRO C  1 227 ? 63.310  -19.344 81.745  1.00 13.03  ? 314  PRO C CG  1 
ATOM   7764  C  CD  . PRO C  1 227 ? 64.805  -19.010 81.741  1.00 13.59  ? 314  PRO C CD  1 
ATOM   7765  N  N   . GLU C  1 228 ? 64.818  -21.859 83.799  1.00 14.61  ? 315  GLU C N   1 
ATOM   7766  C  CA  . GLU C  1 228 ? 64.897  -23.278 84.174  1.00 15.54  ? 315  GLU C CA  1 
ATOM   7767  C  C   . GLU C  1 228 ? 65.854  -23.462 85.352  1.00 15.58  ? 315  GLU C C   1 
ATOM   7768  O  O   . GLU C  1 228 ? 65.466  -24.022 86.385  1.00 15.27  ? 315  GLU C O   1 
ATOM   7769  C  CB  . GLU C  1 228 ? 65.316  -24.158 82.982  1.00 15.23  ? 315  GLU C CB  1 
ATOM   7770  C  CG  . GLU C  1 228 ? 64.247  -24.284 81.894  1.00 16.01  ? 315  GLU C CG  1 
ATOM   7771  C  CD  . GLU C  1 228 ? 64.577  -25.329 80.827  1.00 16.86  ? 315  GLU C CD  1 
ATOM   7772  O  OE1 . GLU C  1 228 ? 63.759  -25.505 79.907  1.00 16.95  ? 315  GLU C OE1 1 
ATOM   7773  O  OE2 . GLU C  1 228 ? 65.656  -25.965 80.894  1.00 17.28  ? 315  GLU C OE2 1 
ATOM   7774  N  N   . MET C  1 229 ? 67.090  -22.970 85.201  1.00 16.31  ? 316  MET C N   1 
ATOM   7775  C  CA  . MET C  1 229 ? 68.090  -22.963 86.287  1.00 16.54  ? 316  MET C CA  1 
ATOM   7776  C  C   . MET C  1 229 ? 67.767  -21.932 87.378  1.00 15.96  ? 316  MET C C   1 
ATOM   7777  O  O   . MET C  1 229 ? 68.263  -22.039 88.502  1.00 15.08  ? 316  MET C O   1 
ATOM   7778  C  CB  . MET C  1 229 ? 69.494  -22.674 85.741  1.00 17.39  ? 316  MET C CB  1 
ATOM   7779  C  CG  . MET C  1 229 ? 70.080  -23.768 84.858  1.00 20.91  ? 316  MET C CG  1 
ATOM   7780  S  SD  . MET C  1 229 ? 70.224  -25.339 85.722  1.00 29.94  ? 316  MET C SD  1 
ATOM   7781  C  CE  . MET C  1 229 ? 71.544  -25.021 86.889  1.00 27.33  ? 316  MET C CE  1 
ATOM   7782  N  N   . MET C  1 230 ? 66.937  -20.940 87.034  1.00 14.91  ? 317  MET C N   1 
ATOM   7783  C  CA  . MET C  1 230 ? 66.601  -19.812 87.931  1.00 14.32  ? 317  MET C CA  1 
ATOM   7784  C  C   . MET C  1 230 ? 67.846  -19.052 88.378  1.00 13.18  ? 317  MET C C   1 
ATOM   7785  O  O   . MET C  1 230 ? 68.077  -18.801 89.568  1.00 12.57  ? 317  MET C O   1 
ATOM   7786  C  CB  . MET C  1 230 ? 65.718  -20.243 89.109  1.00 14.33  ? 317  MET C CB  1 
ATOM   7787  C  CG  . MET C  1 230 ? 64.403  -20.905 88.670  1.00 15.01  ? 317  MET C CG  1 
ATOM   7788  S  SD  . MET C  1 230 ? 63.260  -21.278 90.021  1.00 16.22  ? 317  MET C SD  1 
ATOM   7789  C  CE  . MET C  1 230 ? 64.193  -22.489 90.936  1.00 17.93  ? 317  MET C CE  1 
ATOM   7790  N  N   . THR C  1 231 ? 68.650  -18.692 87.386  1.00 12.83  ? 318  THR C N   1 
ATOM   7791  C  CA  . THR C  1 231 ? 69.867  -17.948 87.603  1.00 12.38  ? 318  THR C CA  1 
ATOM   7792  C  C   . THR C  1 231 ? 69.855  -16.784 86.626  1.00 12.61  ? 318  THR C C   1 
ATOM   7793  O  O   . THR C  1 231 ? 69.055  -16.778 85.676  1.00 11.96  ? 318  THR C O   1 
ATOM   7794  C  CB  . THR C  1 231 ? 71.111  -18.865 87.407  1.00 13.09  ? 318  THR C CB  1 
ATOM   7795  O  OG1 . THR C  1 231 ? 71.027  -19.523 86.138  1.00 12.35  ? 318  THR C OG1 1 
ATOM   7796  C  CG2 . THR C  1 231 ? 71.130  -19.935 88.489  1.00 11.88  ? 318  THR C CG2 1 
ATOM   7797  N  N   . HIS C  1 232 ? 70.712  -15.793 86.868  1.00 12.55  ? 319  HIS C N   1 
ATOM   7798  C  CA  . HIS C  1 232 ? 70.797  -14.630 85.992  1.00 13.04  ? 319  HIS C CA  1 
ATOM   7799  C  C   . HIS C  1 232 ? 72.204  -14.057 85.962  1.00 13.27  ? 319  HIS C C   1 
ATOM   7800  O  O   . HIS C  1 232 ? 73.058  -14.384 86.814  1.00 13.02  ? 319  HIS C O   1 
ATOM   7801  C  CB  . HIS C  1 232 ? 69.809  -13.523 86.432  1.00 12.91  ? 319  HIS C CB  1 
ATOM   7802  C  CG  . HIS C  1 232 ? 70.260  -12.771 87.645  1.00 13.22  ? 319  HIS C CG  1 
ATOM   7803  N  ND1 . HIS C  1 232 ? 70.167  -13.295 88.917  1.00 13.71  ? 319  HIS C ND1 1 
ATOM   7804  C  CD2 . HIS C  1 232 ? 70.826  -11.548 87.783  1.00 14.27  ? 319  HIS C CD2 1 
ATOM   7805  C  CE1 . HIS C  1 232 ? 70.656  -12.428 89.786  1.00 12.78  ? 319  HIS C CE1 1 
ATOM   7806  N  NE2 . HIS C  1 232 ? 71.058  -11.357 89.125  1.00 14.41  ? 319  HIS C NE2 1 
ATOM   7807  N  N   . THR C  1 233 ? 72.427  -13.201 84.970  1.00 13.41  ? 320  THR C N   1 
ATOM   7808  C  CA  . THR C  1 233 ? 73.633  -12.385 84.869  1.00 14.02  ? 320  THR C CA  1 
ATOM   7809  C  C   . THR C  1 233 ? 73.172  -10.974 84.511  1.00 13.69  ? 320  THR C C   1 
ATOM   7810  O  O   . THR C  1 233 ? 72.035  -10.794 84.064  1.00 14.86  ? 320  THR C O   1 
ATOM   7811  C  CB  . THR C  1 233 ? 74.591  -12.936 83.772  1.00 13.57  ? 320  THR C CB  1 
ATOM   7812  O  OG1 . THR C  1 233 ? 73.905  -12.980 82.512  1.00 14.59  ? 320  THR C OG1 1 
ATOM   7813  C  CG2 . THR C  1 233 ? 75.069  -14.346 84.129  1.00 15.31  ? 320  THR C CG2 1 
ATOM   7814  N  N   . SER C  1 234 ? 74.024  -9.971  84.724  1.00 13.60  ? 321  SER C N   1 
ATOM   7815  C  CA  . SER C  1 234 ? 73.677  -8.589  84.345  1.00 12.77  ? 321  SER C CA  1 
ATOM   7816  C  C   . SER C  1 234 ? 74.871  -7.792  83.835  1.00 12.62  ? 321  SER C C   1 
ATOM   7817  O  O   . SER C  1 234 ? 76.016  -8.057  84.199  1.00 12.20  ? 321  SER C O   1 
ATOM   7818  C  CB  . SER C  1 234 ? 73.000  -7.839  85.513  1.00 13.18  ? 321  SER C CB  1 
ATOM   7819  O  OG  . SER C  1 234 ? 73.947  -7.247  86.398  1.00 12.26  ? 321  SER C OG  1 
ATOM   7820  N  N   . LYS C  1 235 ? 74.579  -6.803  82.993  1.00 12.60  ? 322  LYS C N   1 
ATOM   7821  C  CA  . LYS C  1 235 ? 75.580  -5.873  82.460  1.00 12.84  ? 322  LYS C CA  1 
ATOM   7822  C  C   . LYS C  1 235 ? 74.815  -4.700  81.837  1.00 12.21  ? 322  LYS C C   1 
ATOM   7823  O  O   . LYS C  1 235 ? 73.657  -4.469  82.204  1.00 12.39  ? 322  LYS C O   1 
ATOM   7824  C  CB  . LYS C  1 235 ? 76.506  -6.582  81.459  1.00 12.33  ? 322  LYS C CB  1 
ATOM   7825  C  CG  . LYS C  1 235 ? 75.842  -7.034  80.165  1.00 12.63  ? 322  LYS C CG  1 
ATOM   7826  C  CD  . LYS C  1 235 ? 76.725  -8.035  79.406  1.00 13.57  ? 322  LYS C CD  1 
ATOM   7827  C  CE  . LYS C  1 235 ? 77.987  -7.401  78.830  1.00 15.42  ? 322  LYS C CE  1 
ATOM   7828  N  NZ  . LYS C  1 235 ? 78.836  -8.485  78.172  1.00 15.80  ? 322  LYS C NZ  1 
ATOM   7829  N  N   . TYR C  1 236 ? 75.445  -3.963  80.923  1.00 11.41  ? 323  TYR C N   1 
ATOM   7830  C  CA  . TYR C  1 236 ? 74.780  -2.879  80.194  1.00 12.14  ? 323  TYR C CA  1 
ATOM   7831  C  C   . TYR C  1 236 ? 74.713  -3.203  78.717  1.00 11.89  ? 323  TYR C C   1 
ATOM   7832  O  O   . TYR C  1 236 ? 75.549  -3.930  78.189  1.00 11.83  ? 323  TYR C O   1 
ATOM   7833  C  CB  . TYR C  1 236 ? 75.501  -1.542  80.393  1.00 12.33  ? 323  TYR C CB  1 
ATOM   7834  C  CG  . TYR C  1 236 ? 75.320  -0.947  81.775  1.00 12.63  ? 323  TYR C CG  1 
ATOM   7835  C  CD1 . TYR C  1 236 ? 76.118  -1.379  82.856  1.00 13.50  ? 323  TYR C CD1 1 
ATOM   7836  C  CD2 . TYR C  1 236 ? 74.358  0.041   82.007  1.00 11.80  ? 323  TYR C CD2 1 
ATOM   7837  C  CE1 . TYR C  1 236 ? 75.942  -0.852  84.134  1.00 13.06  ? 323  TYR C CE1 1 
ATOM   7838  C  CE2 . TYR C  1 236 ? 74.181  0.590   83.276  1.00 12.35  ? 323  TYR C CE2 1 
ATOM   7839  C  CZ  . TYR C  1 236 ? 74.984  0.142   84.331  1.00 13.43  ? 323  TYR C CZ  1 
ATOM   7840  O  OH  . TYR C  1 236 ? 74.816  0.678   85.589  1.00 14.74  ? 323  TYR C OH  1 
ATOM   7841  N  N   . LEU C  1 237 ? 73.693  -2.678  78.050  1.00 12.27  ? 324  LEU C N   1 
ATOM   7842  C  CA  . LEU C  1 237 ? 73.663  -2.693  76.600  1.00 13.13  ? 324  LEU C CA  1 
ATOM   7843  C  C   . LEU C  1 237 ? 75.008  -2.116  76.089  1.00 12.52  ? 324  LEU C C   1 
ATOM   7844  O  O   . LEU C  1 237 ? 75.432  -1.036  76.544  1.00 12.83  ? 324  LEU C O   1 
ATOM   7845  C  CB  . LEU C  1 237 ? 72.497  -1.814  76.131  1.00 13.60  ? 324  LEU C CB  1 
ATOM   7846  C  CG  . LEU C  1 237 ? 71.439  -2.364  75.195  1.00 17.15  ? 324  LEU C CG  1 
ATOM   7847  C  CD1 . LEU C  1 237 ? 70.431  -1.251  74.873  1.00 17.60  ? 324  LEU C CD1 1 
ATOM   7848  C  CD2 . LEU C  1 237 ? 72.069  -2.907  73.922  1.00 19.84  ? 324  LEU C CD2 1 
ATOM   7849  N  N   . CYS C  1 238 ? 75.677  -2.837  75.177  1.00 12.71  ? 325  CYS C N   1 
ATOM   7850  C  CA  . CYS C  1 238 ? 77.036  -2.453  74.719  1.00 13.09  ? 325  CYS C CA  1 
ATOM   7851  C  C   . CYS C  1 238 ? 77.059  -1.257  73.766  1.00 12.66  ? 325  CYS C C   1 
ATOM   7852  O  O   . CYS C  1 238 ? 78.055  -0.536  73.691  1.00 13.16  ? 325  CYS C O   1 
ATOM   7853  C  CB  . CYS C  1 238 ? 77.735  -3.612  74.003  1.00 12.98  ? 325  CYS C CB  1 
ATOM   7854  S  SG  . CYS C  1 238 ? 78.241  -4.959  75.039  1.00 14.02  ? 325  CYS C SG  1 
ATOM   7855  N  N   . SER C  1 239 ? 75.976  -1.079  73.012  1.00 12.18  ? 326  SER C N   1 
ATOM   7856  C  CA  . SER C  1 239 ? 75.939  -0.106  71.925  1.00 12.15  ? 326  SER C CA  1 
ATOM   7857  C  C   . SER C  1 239 ? 76.201  1.324   72.368  1.00 11.86  ? 326  SER C C   1 
ATOM   7858  O  O   . SER C  1 239 ? 75.768  1.751   73.437  1.00 11.33  ? 326  SER C O   1 
ATOM   7859  C  CB  . SER C  1 239 ? 74.591  -0.168  71.194  1.00 12.04  ? 326  SER C CB  1 
ATOM   7860  O  OG  . SER C  1 239 ? 74.555  0.828   70.192  1.00 10.15  ? 326  SER C OG  1 
ATOM   7861  N  N   . LYS C  1 240 ? 76.904  2.060   71.506  1.00 12.52  ? 327  LYS C N   1 
ATOM   7862  C  CA  . LYS C  1 240 ? 77.073  3.489   71.634  1.00 12.62  ? 327  LYS C CA  1 
ATOM   7863  C  C   . LYS C  1 240 ? 75.753  4.264   71.466  1.00 12.25  ? 327  LYS C C   1 
ATOM   7864  O  O   . LYS C  1 240 ? 75.676  5.433   71.817  1.00 11.80  ? 327  LYS C O   1 
ATOM   7865  C  CB  . LYS C  1 240 ? 78.090  3.986   70.595  1.00 13.40  ? 327  LYS C CB  1 
ATOM   7866  C  CG  . LYS C  1 240 ? 77.604  3.868   69.156  1.00 15.03  ? 327  LYS C CG  1 
ATOM   7867  C  CD  . LYS C  1 240 ? 78.731  4.030   68.160  1.00 17.46  ? 327  LYS C CD  1 
ATOM   7868  C  CE  . LYS C  1 240 ? 78.218  3.882   66.741  1.00 19.72  ? 327  LYS C CE  1 
ATOM   7869  N  NZ  . LYS C  1 240 ? 79.357  3.672   65.795  1.00 22.18  ? 327  LYS C NZ  1 
ATOM   7870  N  N   . VAL C  1 241 ? 74.729  3.621   70.909  1.00 12.31  ? 328  VAL C N   1 
ATOM   7871  C  CA  . VAL C  1 241 ? 73.406  4.266   70.740  1.00 11.51  ? 328  VAL C CA  1 
ATOM   7872  C  C   . VAL C  1 241 ? 72.688  4.235   72.106  1.00 11.70  ? 328  VAL C C   1 
ATOM   7873  O  O   . VAL C  1 241 ? 72.148  3.206   72.522  1.00 12.32  ? 328  VAL C O   1 
ATOM   7874  C  CB  . VAL C  1 241 ? 72.554  3.549   69.657  1.00 11.74  ? 328  VAL C CB  1 
ATOM   7875  C  CG1 . VAL C  1 241 ? 71.157  4.205   69.539  1.00 11.19  ? 328  VAL C CG1 1 
ATOM   7876  C  CG2 . VAL C  1 241 ? 73.294  3.547   68.310  1.00 10.62  ? 328  VAL C CG2 1 
ATOM   7877  N  N   . LEU C  1 242 ? 72.729  5.366   72.803  1.00 11.36  ? 329  LEU C N   1 
ATOM   7878  C  CA  . LEU C  1 242 ? 72.296  5.430   74.205  1.00 11.39  ? 329  LEU C CA  1 
ATOM   7879  C  C   . LEU C  1 242 ? 70.777  5.565   74.248  1.00 11.15  ? 329  LEU C C   1 
ATOM   7880  O  O   . LEU C  1 242 ? 70.195  6.340   73.460  1.00 10.95  ? 329  LEU C O   1 
ATOM   7881  C  CB  . LEU C  1 242 ? 72.964  6.621   74.912  1.00 11.50  ? 329  LEU C CB  1 
ATOM   7882  C  CG  . LEU C  1 242 ? 74.491  6.646   75.017  1.00 10.76  ? 329  LEU C CG  1 
ATOM   7883  C  CD1 . LEU C  1 242 ? 74.894  7.894   75.798  1.00 13.69  ? 329  LEU C CD1 1 
ATOM   7884  C  CD2 . LEU C  1 242 ? 75.057  5.390   75.672  1.00 12.32  ? 329  LEU C CD2 1 
ATOM   7885  N  N   . THR C  1 243 ? 70.126  4.807   75.131  1.00 10.57  ? 330  THR C N   1 
ATOM   7886  C  CA  . THR C  1 243 ? 68.648  4.735   75.043  1.00 10.50  ? 330  THR C CA  1 
ATOM   7887  C  C   . THR C  1 243 ? 67.804  5.161   76.245  1.00 10.41  ? 330  THR C C   1 
ATOM   7888  O  O   . THR C  1 243 ? 66.569  5.130   76.156  1.00 11.62  ? 330  THR C O   1 
ATOM   7889  C  CB  . THR C  1 243 ? 68.116  3.404   74.486  1.00 9.33   ? 330  THR C CB  1 
ATOM   7890  O  OG1 . THR C  1 243 ? 68.396  2.326   75.387  1.00 11.02  ? 330  THR C OG1 1 
ATOM   7891  C  CG2 . THR C  1 243 ? 68.655  3.108   73.074  1.00 8.72   ? 330  THR C CG2 1 
ATOM   7892  N  N   . ASP C  1 244 ? 68.440  5.580   77.336  1.00 10.82  ? 331  ASP C N   1 
ATOM   7893  C  CA  . ASP C  1 244 ? 67.693  6.204   78.431  1.00 10.60  ? 331  ASP C CA  1 
ATOM   7894  C  C   . ASP C  1 244 ? 67.406  7.663   78.104  1.00 11.08  ? 331  ASP C C   1 
ATOM   7895  O  O   . ASP C  1 244 ? 67.892  8.196   77.089  1.00 10.93  ? 331  ASP C O   1 
ATOM   7896  C  CB  . ASP C  1 244 ? 68.433  6.069   79.780  1.00 10.53  ? 331  ASP C CB  1 
ATOM   7897  C  CG  . ASP C  1 244 ? 67.471  6.013   80.981  1.00 11.15  ? 331  ASP C CG  1 
ATOM   7898  O  OD1 . ASP C  1 244 ? 66.254  6.272   80.803  1.00 9.22   ? 331  ASP C OD1 1 
ATOM   7899  O  OD2 . ASP C  1 244 ? 67.926  5.704   82.105  1.00 12.53  ? 331  ASP C OD2 1 
ATOM   7900  N  N   . THR C  1 245 ? 66.623  8.310   78.965  1.00 11.25  ? 332  THR C N   1 
ATOM   7901  C  CA  . THR C  1 245 ? 66.352  9.759   78.883  1.00 11.61  ? 332  THR C CA  1 
ATOM   7902  C  C   . THR C  1 245 ? 66.328  10.297  80.312  1.00 12.39  ? 332  THR C C   1 
ATOM   7903  O  O   . THR C  1 245 ? 65.568  9.779   81.116  1.00 12.64  ? 332  THR C O   1 
ATOM   7904  C  CB  . THR C  1 245 ? 64.988  10.063  78.213  1.00 11.59  ? 332  THR C CB  1 
ATOM   7905  O  OG1 . THR C  1 245 ? 64.925  9.408   76.937  1.00 13.01  ? 332  THR C OG1 1 
ATOM   7906  C  CG2 . THR C  1 245 ? 64.740  11.616  78.065  1.00 11.02  ? 332  THR C CG2 1 
ATOM   7907  N  N   . SER C  1 246 ? 67.110  11.337  80.647  1.00 12.65  ? 333  SER C N   1 
ATOM   7908  C  CA  . SER C  1 246 ? 67.952  12.095  79.719  1.00 13.00  ? 333  SER C CA  1 
ATOM   7909  C  C   . SER C  1 246 ? 69.256  11.373  79.400  1.00 13.09  ? 333  SER C C   1 
ATOM   7910  O  O   . SER C  1 246 ? 69.670  10.438  80.116  1.00 13.27  ? 333  SER C O   1 
ATOM   7911  C  CB  . SER C  1 246 ? 68.281  13.478  80.299  1.00 12.87  ? 333  SER C CB  1 
ATOM   7912  O  OG  . SER C  1 246 ? 67.112  14.124  80.764  1.00 13.24  ? 333  SER C OG  1 
ATOM   7913  N  N   . ARG C  1 247 ? 69.896  11.800  78.315  1.00 12.50  ? 334  ARG C N   1 
ATOM   7914  C  CA  . ARG C  1 247 ? 71.176  11.222  77.916  1.00 12.88  ? 334  ARG C CA  1 
ATOM   7915  C  C   . ARG C  1 247 ? 72.035  12.288  77.228  1.00 12.73  ? 334  ARG C C   1 
ATOM   7916  O  O   . ARG C  1 247 ? 71.507  13.290  76.766  1.00 13.43  ? 334  ARG C O   1 
ATOM   7917  C  CB  . ARG C  1 247 ? 70.954  10.026  76.975  1.00 12.45  ? 334  ARG C CB  1 
ATOM   7918  C  CG  . ARG C  1 247 ? 70.285  10.406  75.651  1.00 13.61  ? 334  ARG C CG  1 
ATOM   7919  C  CD  . ARG C  1 247 ? 69.885  9.182   74.818  1.00 12.39  ? 334  ARG C CD  1 
ATOM   7920  N  NE  . ARG C  1 247 ? 69.230  9.601   73.577  1.00 12.26  ? 334  ARG C NE  1 
ATOM   7921  C  CZ  . ARG C  1 247 ? 67.908  9.684   73.393  1.00 11.79  ? 334  ARG C CZ  1 
ATOM   7922  N  NH1 . ARG C  1 247 ? 67.058  9.384   74.378  1.00 9.62   ? 334  ARG C NH1 1 
ATOM   7923  N  NH2 . ARG C  1 247 ? 67.435  10.093  72.214  1.00 10.38  ? 334  ARG C NH2 1 
ATOM   7924  N  N   . PRO C  1 248 ? 73.368  12.089  77.172  1.00 13.95  ? 335  PRO C N   1 
ATOM   7925  C  CA  . PRO C  1 248 ? 74.173  12.982  76.317  1.00 14.34  ? 335  PRO C CA  1 
ATOM   7926  C  C   . PRO C  1 248 ? 74.097  12.502  74.855  1.00 14.94  ? 335  PRO C C   1 
ATOM   7927  O  O   . PRO C  1 248 ? 73.405  11.508  74.551  1.00 14.60  ? 335  PRO C O   1 
ATOM   7928  C  CB  . PRO C  1 248 ? 75.593  12.762  76.850  1.00 14.92  ? 335  PRO C CB  1 
ATOM   7929  C  CG  . PRO C  1 248 ? 75.596  11.313  77.257  1.00 13.65  ? 335  PRO C CG  1 
ATOM   7930  C  CD  . PRO C  1 248 ? 74.200  11.075  77.839  1.00 13.36  ? 335  PRO C CD  1 
ATOM   7931  N  N   . ASN C  1 249 ? 74.792  13.197  73.950  1.00 15.47  ? 336  ASN C N   1 
ATOM   7932  C  CA  . ASN C  1 249 ? 74.996  12.674  72.589  1.00 15.70  ? 336  ASN C CA  1 
ATOM   7933  C  C   . ASN C  1 249 ? 75.628  11.297  72.634  1.00 15.18  ? 336  ASN C C   1 
ATOM   7934  O  O   . ASN C  1 249 ? 76.429  10.995  73.544  1.00 15.31  ? 336  ASN C O   1 
ATOM   7935  C  CB  . ASN C  1 249 ? 75.912  13.592  71.762  1.00 16.61  ? 336  ASN C CB  1 
ATOM   7936  C  CG  . ASN C  1 249 ? 75.320  14.984  71.521  1.00 18.57  ? 336  ASN C CG  1 
ATOM   7937  O  OD1 . ASN C  1 249 ? 74.111  15.160  71.380  1.00 21.10  ? 336  ASN C OD1 1 
ATOM   7938  N  ND2 . ASN C  1 249 ? 76.203  15.977  71.425  1.00 22.58  ? 336  ASN C ND2 1 
ATOM   7939  N  N   . ASP C  1 250 ? 75.264  10.454  71.667  1.00 14.12  ? 337  ASP C N   1 
ATOM   7940  C  CA  . ASP C  1 250 ? 75.880  9.145   71.522  1.00 14.20  ? 337  ASP C CA  1 
ATOM   7941  C  C   . ASP C  1 250 ? 77.391  9.290   71.379  1.00 14.47  ? 337  ASP C C   1 
ATOM   7942  O  O   . ASP C  1 250 ? 77.854  10.064  70.537  1.00 14.42  ? 337  ASP C O   1 
ATOM   7943  C  CB  . ASP C  1 250 ? 75.317  8.410   70.317  1.00 14.03  ? 337  ASP C CB  1 
ATOM   7944  C  CG  . ASP C  1 250 ? 73.832  8.075   70.481  1.00 14.50  ? 337  ASP C CG  1 
ATOM   7945  O  OD1 . ASP C  1 250 ? 73.150  7.877   69.459  1.00 15.28  ? 337  ASP C OD1 1 
ATOM   7946  O  OD2 . ASP C  1 250 ? 73.363  8.020   71.636  1.00 13.05  ? 337  ASP C OD2 1 
ATOM   7947  N  N   . PRO C  1 251 ? 78.159  8.571   72.228  1.00 14.64  ? 338  PRO C N   1 
ATOM   7948  C  CA  . PRO C  1 251 ? 79.628  8.632   72.147  1.00 14.66  ? 338  PRO C CA  1 
ATOM   7949  C  C   . PRO C  1 251 ? 80.176  7.786   70.993  1.00 15.07  ? 338  PRO C C   1 
ATOM   7950  O  O   . PRO C  1 251 ? 79.413  7.135   70.284  1.00 14.10  ? 338  PRO C O   1 
ATOM   7951  C  CB  . PRO C  1 251 ? 80.080  8.070   73.495  1.00 14.40  ? 338  PRO C CB  1 
ATOM   7952  C  CG  . PRO C  1 251 ? 78.976  7.139   73.920  1.00 14.74  ? 338  PRO C CG  1 
ATOM   7953  C  CD  . PRO C  1 251 ? 77.688  7.722   73.344  1.00 14.38  ? 338  PRO C CD  1 
ATOM   7954  N  N   . THR C  1 252 ? 81.495  7.817   70.806  1.00 16.08  ? 339  THR C N   1 
ATOM   7955  C  CA  . THR C  1 252 ? 82.155  6.970   69.808  1.00 17.06  ? 339  THR C CA  1 
ATOM   7956  C  C   . THR C  1 252 ? 81.995  5.481   70.123  1.00 16.19  ? 339  THR C C   1 
ATOM   7957  O  O   . THR C  1 252 ? 81.909  4.652   69.222  1.00 16.72  ? 339  THR C O   1 
ATOM   7958  C  CB  . THR C  1 252 ? 83.658  7.347   69.686  1.00 16.83  ? 339  THR C CB  1 
ATOM   7959  O  OG1 . THR C  1 252 ? 83.740  8.718   69.284  1.00 21.01  ? 339  THR C OG1 1 
ATOM   7960  C  CG2 . THR C  1 252 ? 84.342  6.508   68.643  1.00 19.76  ? 339  THR C CG2 1 
ATOM   7961  N  N   . ASN C  1 253 ? 81.980  5.147   71.406  1.00 15.59  ? 340  ASN C N   1 
ATOM   7962  C  CA  . ASN C  1 253 ? 81.827  3.767   71.847  1.00 15.48  ? 340  ASN C CA  1 
ATOM   7963  C  C   . ASN C  1 253 ? 80.913  3.709   73.047  1.00 14.56  ? 340  ASN C C   1 
ATOM   7964  O  O   . ASN C  1 253 ? 80.944  4.605   73.895  1.00 14.34  ? 340  ASN C O   1 
ATOM   7965  C  CB  . ASN C  1 253 ? 83.185  3.155   72.229  1.00 15.84  ? 340  ASN C CB  1 
ATOM   7966  C  CG  . ASN C  1 253 ? 84.207  3.239   71.097  1.00 18.44  ? 340  ASN C CG  1 
ATOM   7967  O  OD1 . ASN C  1 253 ? 85.101  4.108   71.104  1.00 20.45  ? 340  ASN C OD1 1 
ATOM   7968  N  ND2 . ASN C  1 253 ? 84.067  2.365   70.117  1.00 17.73  ? 340  ASN C ND2 1 
ATOM   7969  N  N   . GLY C  1 254 ? 80.108  2.651   73.110  1.00 14.00  ? 341  GLY C N   1 
ATOM   7970  C  CA  . GLY C  1 254 ? 79.331  2.337   74.304  1.00 14.01  ? 341  GLY C CA  1 
ATOM   7971  C  C   . GLY C  1 254 ? 80.193  1.661   75.356  1.00 13.93  ? 341  GLY C C   1 
ATOM   7972  O  O   . GLY C  1 254 ? 81.437  1.646   75.265  1.00 12.52  ? 341  GLY C O   1 
ATOM   7973  N  N   . ASN C  1 255 ? 79.531  1.117   76.374  1.00 13.22  ? 342  ASN C N   1 
ATOM   7974  C  CA  . ASN C  1 255 ? 80.217  0.485   77.485  1.00 13.36  ? 342  ASN C CA  1 
ATOM   7975  C  C   . ASN C  1 255 ? 79.348  -0.629  78.023  1.00 13.30  ? 342  ASN C C   1 
ATOM   7976  O  O   . ASN C  1 255 ? 78.292  -0.364  78.586  1.00 12.81  ? 342  ASN C O   1 
ATOM   7977  C  CB  . ASN C  1 255 ? 80.525  1.495   78.604  1.00 12.46  ? 342  ASN C CB  1 
ATOM   7978  C  CG  . ASN C  1 255 ? 81.533  0.956   79.630  1.00 14.02  ? 342  ASN C CG  1 
ATOM   7979  O  OD1 . ASN C  1 255 ? 81.467  -0.208  80.036  1.00 15.08  ? 342  ASN C OD1 1 
ATOM   7980  N  ND2 . ASN C  1 255 ? 82.475  1.816   80.053  1.00 14.18  ? 342  ASN C ND2 1 
ATOM   7981  N  N   . CYS C  1 256 ? 79.805  -1.868  77.846  1.00 13.75  ? 343  CYS C N   1 
ATOM   7982  C  CA  . CYS C  1 256 ? 79.061  -3.057  78.230  1.00 14.16  ? 343  CYS C CA  1 
ATOM   7983  C  C   . CYS C  1 256 ? 78.984  -3.274  79.749  1.00 14.82  ? 343  CYS C C   1 
ATOM   7984  O  O   . CYS C  1 256 ? 78.151  -4.052  80.217  1.00 15.10  ? 343  CYS C O   1 
ATOM   7985  C  CB  . CYS C  1 256 ? 79.715  -4.319  77.623  1.00 14.42  ? 343  CYS C CB  1 
ATOM   7986  S  SG  . CYS C  1 256 ? 80.013  -4.324  75.827  1.00 15.62  ? 343  CYS C SG  1 
ATOM   7987  N  N   . ASP C  1 257 ? 79.884  -2.643  80.508  1.00 14.64  ? 344  ASP C N   1 
ATOM   7988  C  CA  . ASP C  1 257 ? 80.132  -3.066  81.894  1.00 15.06  ? 344  ASP C CA  1 
ATOM   7989  C  C   . ASP C  1 257 ? 80.158  -1.967  82.945  1.00 14.65  ? 344  ASP C C   1 
ATOM   7990  O  O   . ASP C  1 257 ? 80.542  -2.204  84.101  1.00 14.35  ? 344  ASP C O   1 
ATOM   7991  C  CB  . ASP C  1 257 ? 81.406  -3.942  81.966  1.00 15.44  ? 344  ASP C CB  1 
ATOM   7992  C  CG  . ASP C  1 257 ? 81.189  -5.317  81.386  1.00 17.09  ? 344  ASP C CG  1 
ATOM   7993  O  OD1 . ASP C  1 257 ? 81.631  -5.558  80.234  1.00 16.82  ? 344  ASP C OD1 1 
ATOM   7994  O  OD2 . ASP C  1 257 ? 80.559  -6.162  82.072  1.00 15.91  ? 344  ASP C OD2 1 
ATOM   7995  N  N   . ALA C  1 258 ? 79.685  -0.788  82.552  1.00 14.60  ? 345  ALA C N   1 
ATOM   7996  C  CA  . ALA C  1 258 ? 79.673  0.412   83.390  1.00 14.68  ? 345  ALA C CA  1 
ATOM   7997  C  C   . ALA C  1 258 ? 78.681  1.426   82.828  1.00 14.48  ? 345  ALA C C   1 
ATOM   7998  O  O   . ALA C  1 258 ? 78.493  1.498   81.609  1.00 14.33  ? 345  ALA C O   1 
ATOM   7999  C  CB  . ALA C  1 258 ? 81.079  1.032   83.448  1.00 14.94  ? 345  ALA C CB  1 
ATOM   8000  N  N   . PRO C  1 259 ? 78.057  2.229   83.705  1.00 14.42  ? 346  PRO C N   1 
ATOM   8001  C  CA  . PRO C  1 259 ? 77.158  3.264   83.229  1.00 14.56  ? 346  PRO C CA  1 
ATOM   8002  C  C   . PRO C  1 259 ? 77.938  4.401   82.549  1.00 15.16  ? 346  PRO C C   1 
ATOM   8003  O  O   . PRO C  1 259 ? 79.058  4.731   82.962  1.00 14.95  ? 346  PRO C O   1 
ATOM   8004  C  CB  . PRO C  1 259 ? 76.487  3.750   84.520  1.00 14.38  ? 346  PRO C CB  1 
ATOM   8005  C  CG  . PRO C  1 259 ? 77.519  3.486   85.583  1.00 14.86  ? 346  PRO C CG  1 
ATOM   8006  C  CD  . PRO C  1 259 ? 78.154  2.223   85.183  1.00 14.47  ? 346  PRO C CD  1 
ATOM   8007  N  N   . ILE C  1 260 ? 77.360  4.933   81.480  1.00 15.68  ? 347  ILE C N   1 
ATOM   8008  C  CA  . ILE C  1 260 ? 77.836  6.139   80.823  1.00 16.47  ? 347  ILE C CA  1 
ATOM   8009  C  C   . ILE C  1 260 ? 76.988  7.281   81.380  1.00 17.83  ? 347  ILE C C   1 
ATOM   8010  O  O   . ILE C  1 260 ? 75.750  7.289   81.230  1.00 17.20  ? 347  ILE C O   1 
ATOM   8011  C  CB  . ILE C  1 260 ? 77.702  6.005   79.273  1.00 16.53  ? 347  ILE C CB  1 
ATOM   8012  C  CG1 . ILE C  1 260 ? 78.726  4.990   78.756  1.00 15.73  ? 347  ILE C CG1 1 
ATOM   8013  C  CG2 . ILE C  1 260 ? 77.827  7.369   78.572  1.00 15.01  ? 347  ILE C CG2 1 
ATOM   8014  C  CD1 . ILE C  1 260 ? 78.491  4.481   77.335  1.00 15.27  ? 347  ILE C CD1 1 
ATOM   8015  N  N   . THR C  1 261 ? 77.641  8.235   82.034  1.00 19.33  ? 348  THR C N   1 
ATOM   8016  C  CA  . THR C  1 261 ? 76.901  9.227   82.818  1.00 21.96  ? 348  THR C CA  1 
ATOM   8017  C  C   . THR C  1 261 ? 76.090  10.198  81.960  1.00 23.46  ? 348  THR C C   1 
ATOM   8018  O  O   . THR C  1 261 ? 76.577  10.712  80.953  1.00 23.29  ? 348  THR C O   1 
ATOM   8019  C  CB  . THR C  1 261 ? 77.772  9.937   83.866  1.00 22.28  ? 348  THR C CB  1 
ATOM   8020  O  OG1 . THR C  1 261 ? 79.021  10.316  83.284  1.00 23.38  ? 348  THR C OG1 1 
ATOM   8021  C  CG2 . THR C  1 261 ? 78.037  8.993   85.031  1.00 23.22  ? 348  THR C CG2 1 
ATOM   8022  N  N   . GLY C  1 262 ? 74.848  10.420  82.401  1.00 25.65  ? 349  GLY C N   1 
ATOM   8023  C  CA  . GLY C  1 262 ? 73.732  10.905  81.565  1.00 27.24  ? 349  GLY C CA  1 
ATOM   8024  C  C   . GLY C  1 262 ? 73.689  12.362  81.157  1.00 28.25  ? 349  GLY C C   1 
ATOM   8025  O  O   . GLY C  1 262 ? 74.714  13.061  81.145  1.00 29.62  ? 349  GLY C O   1 
ATOM   8026  N  N   . GLY C  1 263 ? 72.490  12.811  80.797  1.00 29.04  ? 350  GLY C N   1 
ATOM   8027  C  CA  . GLY C  1 263 ? 72.261  14.166  80.315  1.00 28.50  ? 350  GLY C CA  1 
ATOM   8028  C  C   . GLY C  1 263 ? 71.526  15.013  81.333  1.00 28.38  ? 350  GLY C C   1 
ATOM   8029  O  O   . GLY C  1 263 ? 71.876  15.008  82.512  1.00 29.27  ? 350  GLY C O   1 
ATOM   8030  N  N   . SER C  1 264 ? 70.496  15.724  80.880  1.00 27.21  ? 351  SER C N   1 
ATOM   8031  C  CA  . SER C  1 264 ? 69.838  16.753  81.658  1.00 26.48  ? 351  SER C CA  1 
ATOM   8032  C  C   . SER C  1 264 ? 68.433  17.007  81.087  1.00 24.92  ? 351  SER C C   1 
ATOM   8033  O  O   . SER C  1 264 ? 68.283  17.148  79.882  1.00 25.69  ? 351  SER C O   1 
ATOM   8034  C  CB  . SER C  1 264 ? 70.683  18.031  81.554  1.00 27.03  ? 351  SER C CB  1 
ATOM   8035  O  OG  . SER C  1 264 ? 70.227  19.040  82.426  1.00 29.65  ? 351  SER C OG  1 
ATOM   8036  N  N   . PRO C  1 265 ? 67.403  17.120  81.936  1.00 23.15  ? 352  PRO C N   1 
ATOM   8037  C  CA  . PRO C  1 265 ? 67.351  17.118  83.388  1.00 21.38  ? 352  PRO C CA  1 
ATOM   8038  C  C   . PRO C  1 265 ? 66.791  15.869  84.086  1.00 19.49  ? 352  PRO C C   1 
ATOM   8039  O  O   . PRO C  1 265 ? 66.664  15.901  85.310  1.00 19.16  ? 352  PRO C O   1 
ATOM   8040  C  CB  . PRO C  1 265 ? 66.398  18.283  83.646  1.00 21.33  ? 352  PRO C CB  1 
ATOM   8041  C  CG  . PRO C  1 265 ? 65.399  18.199  82.521  1.00 22.36  ? 352  PRO C CG  1 
ATOM   8042  C  CD  . PRO C  1 265 ? 66.075  17.438  81.383  1.00 22.95  ? 352  PRO C CD  1 
ATOM   8043  N  N   . ASP C  1 266 ? 66.460  14.804  83.338  1.00 17.40  ? 353  ASP C N   1 
ATOM   8044  C  CA  . ASP C  1 266 ? 65.786  13.589  83.888  1.00 16.19  ? 353  ASP C CA  1 
ATOM   8045  C  C   . ASP C  1 266 ? 66.783  12.455  84.191  1.00 14.49  ? 353  ASP C C   1 
ATOM   8046  O  O   . ASP C  1 266 ? 67.639  12.152  83.352  1.00 13.29  ? 353  ASP C O   1 
ATOM   8047  C  CB  . ASP C  1 266 ? 64.749  13.021  82.894  1.00 15.97  ? 353  ASP C CB  1 
ATOM   8048  C  CG  . ASP C  1 266 ? 63.632  14.000  82.505  1.00 17.57  ? 353  ASP C CG  1 
ATOM   8049  O  OD1 . ASP C  1 266 ? 63.444  15.073  83.138  1.00 17.64  ? 353  ASP C OD1 1 
ATOM   8050  O  OD2 . ASP C  1 266 ? 62.906  13.665  81.528  1.00 17.13  ? 353  ASP C OD2 1 
ATOM   8051  N  N   . PRO C  1 267 ? 66.683  11.809  85.378  1.00 14.13  ? 354  PRO C N   1 
ATOM   8052  C  CA  . PRO C  1 267 ? 67.558  10.655  85.651  1.00 13.61  ? 354  PRO C CA  1 
ATOM   8053  C  C   . PRO C  1 267 ? 67.270  9.373   84.861  1.00 12.78  ? 354  PRO C C   1 
ATOM   8054  O  O   . PRO C  1 267 ? 68.132  8.493   84.789  1.00 12.30  ? 354  PRO C O   1 
ATOM   8055  C  CB  . PRO C  1 267 ? 67.351  10.397  87.159  1.00 13.28  ? 354  PRO C CB  1 
ATOM   8056  C  CG  . PRO C  1 267 ? 66.027  10.912  87.446  1.00 14.12  ? 354  PRO C CG  1 
ATOM   8057  C  CD  . PRO C  1 267 ? 65.846  12.130  86.551  1.00 14.30  ? 354  PRO C CD  1 
ATOM   8058  N  N   . GLY C  1 268 ? 66.060  9.238   84.324  1.00 12.00  ? 355  GLY C N   1 
ATOM   8059  C  CA  . GLY C  1 268 ? 65.732  8.047   83.562  1.00 10.89  ? 355  GLY C CA  1 
ATOM   8060  C  C   . GLY C  1 268 ? 64.281  7.976   83.128  1.00 10.23  ? 355  GLY C C   1 
ATOM   8061  O  O   . GLY C  1 268 ? 63.456  8.823   83.516  1.00 10.24  ? 355  GLY C O   1 
ATOM   8062  N  N   . VAL C  1 269 ? 63.998  6.974   82.297  1.00 9.06   ? 356  VAL C N   1 
ATOM   8063  C  CA  . VAL C  1 269 ? 62.649  6.645   81.854  1.00 8.39   ? 356  VAL C CA  1 
ATOM   8064  C  C   . VAL C  1 269 ? 62.588  5.153   81.560  1.00 7.69   ? 356  VAL C C   1 
ATOM   8065  O  O   . VAL C  1 269 ? 63.602  4.546   81.161  1.00 7.46   ? 356  VAL C O   1 
ATOM   8066  C  CB  . VAL C  1 269 ? 62.212  7.477   80.583  1.00 8.13   ? 356  VAL C CB  1 
ATOM   8067  C  CG1 . VAL C  1 269 ? 63.022  7.088   79.313  1.00 8.07   ? 356  VAL C CG1 1 
ATOM   8068  C  CG2 . VAL C  1 269 ? 60.708  7.326   80.325  1.00 6.66   ? 356  VAL C CG2 1 
ATOM   8069  N  N   . LYS C  1 270 ? 61.421  4.542   81.775  1.00 7.09   ? 357  LYS C N   1 
ATOM   8070  C  CA  . LYS C  1 270 ? 61.290  3.118   81.456  1.00 6.74   ? 357  LYS C CA  1 
ATOM   8071  C  C   . LYS C  1 270 ? 61.391  2.923   79.925  1.00 6.89   ? 357  LYS C C   1 
ATOM   8072  O  O   . LYS C  1 270 ? 60.828  3.702   79.165  1.00 7.59   ? 357  LYS C O   1 
ATOM   8073  C  CB  . LYS C  1 270 ? 59.986  2.552   82.023  1.00 6.60   ? 357  LYS C CB  1 
ATOM   8074  C  CG  . LYS C  1 270 ? 59.682  1.161   81.562  1.00 6.88   ? 357  LYS C CG  1 
ATOM   8075  C  CD  . LYS C  1 270 ? 58.340  0.648   82.102  1.00 6.04   ? 357  LYS C CD  1 
ATOM   8076  C  CE  . LYS C  1 270 ? 58.086  -0.727  81.493  1.00 5.51   ? 357  LYS C CE  1 
ATOM   8077  N  NZ  . LYS C  1 270 ? 59.035  -1.779  82.013  1.00 6.82   ? 357  LYS C NZ  1 
ATOM   8078  N  N   . GLY C  1 271 ? 62.139  1.908   79.496  1.00 7.46   ? 358  GLY C N   1 
ATOM   8079  C  CA  . GLY C  1 271 ? 62.368  1.656   78.070  1.00 7.35   ? 358  GLY C CA  1 
ATOM   8080  C  C   . GLY C  1 271 ? 62.586  0.181   77.789  1.00 8.28   ? 358  GLY C C   1 
ATOM   8081  O  O   . GLY C  1 271 ? 62.406  -0.655  78.658  1.00 7.76   ? 358  GLY C O   1 
ATOM   8082  N  N   . PHE C  1 272 ? 62.975  -0.141  76.560  1.00 8.28   ? 359  PHE C N   1 
ATOM   8083  C  CA  . PHE C  1 272 ? 63.052  -1.538  76.151  1.00 8.87   ? 359  PHE C CA  1 
ATOM   8084  C  C   . PHE C  1 272 ? 63.958  -1.699  74.925  1.00 8.72   ? 359  PHE C C   1 
ATOM   8085  O  O   . PHE C  1 272 ? 64.299  -0.729  74.232  1.00 8.45   ? 359  PHE C O   1 
ATOM   8086  C  CB  . PHE C  1 272 ? 61.620  -2.062  75.802  1.00 8.13   ? 359  PHE C CB  1 
ATOM   8087  C  CG  . PHE C  1 272 ? 61.178  -1.669  74.419  1.00 8.90   ? 359  PHE C CG  1 
ATOM   8088  C  CD1 . PHE C  1 272 ? 60.634  -0.401  74.181  1.00 8.45   ? 359  PHE C CD1 1 
ATOM   8089  C  CD2 . PHE C  1 272 ? 61.333  -2.553  73.348  1.00 10.67  ? 359  PHE C CD2 1 
ATOM   8090  C  CE1 . PHE C  1 272 ? 60.261  -0.007  72.885  1.00 8.07   ? 359  PHE C CE1 1 
ATOM   8091  C  CE2 . PHE C  1 272 ? 60.963  -2.173  72.043  1.00 10.94  ? 359  PHE C CE2 1 
ATOM   8092  C  CZ  . PHE C  1 272 ? 60.422  -0.896  71.822  1.00 8.04   ? 359  PHE C CZ  1 
ATOM   8093  N  N   . ALA C  1 273 ? 64.313  -2.949  74.634  1.00 9.22   ? 360  ALA C N   1 
ATOM   8094  C  CA  . ALA C  1 273 ? 64.990  -3.284  73.387  1.00 9.06   ? 360  ALA C CA  1 
ATOM   8095  C  C   . ALA C  1 273 ? 64.758  -4.783  73.116  1.00 9.56   ? 360  ALA C C   1 
ATOM   8096  O  O   . ALA C  1 273 ? 64.461  -5.545  74.035  1.00 9.97   ? 360  ALA C O   1 
ATOM   8097  C  CB  . ALA C  1 273 ? 66.471  -2.985  73.508  1.00 8.85   ? 360  ALA C CB  1 
ATOM   8098  N  N   . PHE C  1 274 ? 64.847  -5.177  71.850  1.00 9.20   ? 361  PHE C N   1 
ATOM   8099  C  CA  . PHE C  1 274 ? 64.879  -6.579  71.480  1.00 9.76   ? 361  PHE C CA  1 
ATOM   8100  C  C   . PHE C  1 274 ? 66.304  -6.873  71.007  1.00 10.21  ? 361  PHE C C   1 
ATOM   8101  O  O   . PHE C  1 274 ? 66.806  -6.223  70.106  1.00 10.72  ? 361  PHE C O   1 
ATOM   8102  C  CB  . PHE C  1 274 ? 63.822  -6.866  70.404  1.00 9.72   ? 361  PHE C CB  1 
ATOM   8103  C  CG  . PHE C  1 274 ? 62.411  -6.816  70.942  1.00 8.84   ? 361  PHE C CG  1 
ATOM   8104  C  CD1 . PHE C  1 274 ? 61.879  -7.915  71.619  1.00 9.06   ? 361  PHE C CD1 1 
ATOM   8105  C  CD2 . PHE C  1 274 ? 61.648  -5.659  70.845  1.00 9.52   ? 361  PHE C CD2 1 
ATOM   8106  C  CE1 . PHE C  1 274 ? 60.589  -7.882  72.153  1.00 7.72   ? 361  PHE C CE1 1 
ATOM   8107  C  CE2 . PHE C  1 274 ? 60.358  -5.622  71.385  1.00 8.87   ? 361  PHE C CE2 1 
ATOM   8108  C  CZ  . PHE C  1 274 ? 59.828  -6.742  72.035  1.00 10.09  ? 361  PHE C CZ  1 
ATOM   8109  N  N   . LEU C  1 275 ? 66.958  -7.830  71.657  1.00 10.96  ? 362  LEU C N   1 
ATOM   8110  C  CA  . LEU C  1 275 ? 68.360  -8.096  71.397  1.00 10.92  ? 362  LEU C CA  1 
ATOM   8111  C  C   . LEU C  1 275 ? 68.527  -9.496  70.800  1.00 11.04  ? 362  LEU C C   1 
ATOM   8112  O  O   . LEU C  1 275 ? 68.370  -10.497 71.502  1.00 10.67  ? 362  LEU C O   1 
ATOM   8113  C  CB  . LEU C  1 275 ? 69.175  -7.926  72.688  1.00 11.17  ? 362  LEU C CB  1 
ATOM   8114  C  CG  . LEU C  1 275 ? 69.023  -6.598  73.431  1.00 12.68  ? 362  LEU C CG  1 
ATOM   8115  C  CD1 . LEU C  1 275 ? 69.725  -6.691  74.809  1.00 13.38  ? 362  LEU C CD1 1 
ATOM   8116  C  CD2 . LEU C  1 275 ? 69.552  -5.399  72.599  1.00 10.90  ? 362  LEU C CD2 1 
ATOM   8117  N  N   . ASP C  1 276 ? 68.846  -9.545  69.500  1.00 11.95  ? 363  ASP C N   1 
ATOM   8118  C  CA  . ASP C  1 276 ? 68.928  -10.807 68.758  1.00 12.92  ? 363  ASP C CA  1 
ATOM   8119  C  C   . ASP C  1 276 ? 69.967  -10.762 67.615  1.00 13.08  ? 363  ASP C C   1 
ATOM   8120  O  O   . ASP C  1 276 ? 69.613  -10.928 66.440  1.00 12.88  ? 363  ASP C O   1 
ATOM   8121  C  CB  . ASP C  1 276 ? 67.530  -11.147 68.211  1.00 13.25  ? 363  ASP C CB  1 
ATOM   8122  C  CG  . ASP C  1 276 ? 67.477  -12.490 67.504  1.00 14.43  ? 363  ASP C CG  1 
ATOM   8123  O  OD1 . ASP C  1 276 ? 66.698  -12.628 66.547  1.00 13.71  ? 363  ASP C OD1 1 
ATOM   8124  O  OD2 . ASP C  1 276 ? 68.229  -13.400 67.880  1.00 17.01  ? 363  ASP C OD2 1 
ATOM   8125  N  N   . GLY C  1 277 ? 71.246  -10.559 67.967  1.00 13.60  ? 364  GLY C N   1 
ATOM   8126  C  CA  . GLY C  1 277 ? 72.319  -10.407 66.972  1.00 13.15  ? 364  GLY C CA  1 
ATOM   8127  C  C   . GLY C  1 277 ? 72.043  -9.304  65.955  1.00 13.38  ? 364  GLY C C   1 
ATOM   8128  O  O   . GLY C  1 277 ? 71.811  -8.151  66.323  1.00 13.02  ? 364  GLY C O   1 
ATOM   8129  N  N   . GLU C  1 278 ? 72.067  -9.664  64.675  1.00 13.38  ? 365  GLU C N   1 
ATOM   8130  C  CA  . GLU C  1 278 ? 71.740  -8.741  63.585  1.00 14.73  ? 365  GLU C CA  1 
ATOM   8131  C  C   . GLU C  1 278 ? 70.315  -8.168  63.718  1.00 13.54  ? 365  GLU C C   1 
ATOM   8132  O  O   . GLU C  1 278 ? 70.062  -7.015  63.385  1.00 13.83  ? 365  GLU C O   1 
ATOM   8133  C  CB  . GLU C  1 278 ? 71.894  -9.439  62.230  1.00 14.94  ? 365  GLU C CB  1 
ATOM   8134  C  CG  . GLU C  1 278 ? 73.262  -10.125 62.035  1.00 21.69  ? 365  GLU C CG  1 
ATOM   8135  C  CD  . GLU C  1 278 ? 74.411  -9.159  61.786  1.00 26.74  ? 365  GLU C CD  1 
ATOM   8136  O  OE1 . GLU C  1 278 ? 74.170  -7.968  61.482  1.00 29.83  ? 365  GLU C OE1 1 
ATOM   8137  O  OE2 . GLU C  1 278 ? 75.577  -9.604  61.877  1.00 32.52  ? 365  GLU C OE2 1 
ATOM   8138  N  N   . ASN C  1 279 ? 69.417  -8.996  64.241  1.00 13.22  ? 366  ASN C N   1 
ATOM   8139  C  CA  . ASN C  1 279 ? 67.988  -8.683  64.370  1.00 12.01  ? 366  ASN C CA  1 
ATOM   8140  C  C   . ASN C  1 279 ? 67.694  -7.967  65.707  1.00 12.44  ? 366  ASN C C   1 
ATOM   8141  O  O   . ASN C  1 279 ? 66.844  -8.422  66.494  1.00 12.68  ? 366  ASN C O   1 
ATOM   8142  C  CB  . ASN C  1 279 ? 67.218  -10.012 64.297  1.00 12.70  ? 366  ASN C CB  1 
ATOM   8143  C  CG  . ASN C  1 279 ? 65.722  -9.830  64.230  1.00 11.08  ? 366  ASN C CG  1 
ATOM   8144  O  OD1 . ASN C  1 279 ? 65.214  -9.043  63.423  1.00 13.32  ? 366  ASN C OD1 1 
ATOM   8145  N  ND2 . ASN C  1 279 ? 65.003  -10.596 65.045  1.00 11.77  ? 366  ASN C ND2 1 
ATOM   8146  N  N   . SER C  1 280 ? 68.409  -6.869  65.968  1.00 10.96  ? 367  SER C N   1 
ATOM   8147  C  CA  . SER C  1 280 ? 68.274  -6.113  67.224  1.00 10.20  ? 367  SER C CA  1 
ATOM   8148  C  C   . SER C  1 280 ? 67.703  -4.728  66.972  1.00 10.38  ? 367  SER C C   1 
ATOM   8149  O  O   . SER C  1 280 ? 68.120  -4.028  66.029  1.00 9.45   ? 367  SER C O   1 
ATOM   8150  C  CB  . SER C  1 280 ? 69.607  -5.974  67.965  1.00 9.87   ? 367  SER C CB  1 
ATOM   8151  O  OG  . SER C  1 280 ? 70.131  -7.244  68.277  1.00 9.70   ? 367  SER C OG  1 
ATOM   8152  N  N   . TRP C  1 281 ? 66.756  -4.344  67.835  1.00 9.89   ? 368  TRP C N   1 
ATOM   8153  C  CA  . TRP C  1 281 ? 66.040  -3.078  67.722  1.00 10.48  ? 368  TRP C CA  1 
ATOM   8154  C  C   . TRP C  1 281 ? 65.979  -2.368  69.076  1.00 10.92  ? 368  TRP C C   1 
ATOM   8155  O  O   . TRP C  1 281 ? 65.629  -2.981  70.080  1.00 11.74  ? 368  TRP C O   1 
ATOM   8156  C  CB  . TRP C  1 281 ? 64.615  -3.313  67.243  1.00 10.00  ? 368  TRP C CB  1 
ATOM   8157  C  CG  . TRP C  1 281 ? 64.453  -3.585  65.771  1.00 10.22  ? 368  TRP C CG  1 
ATOM   8158  C  CD1 . TRP C  1 281 ? 64.484  -4.809  65.143  1.00 11.27  ? 368  TRP C CD1 1 
ATOM   8159  C  CD2 . TRP C  1 281 ? 64.191  -2.612  64.751  1.00 9.95   ? 368  TRP C CD2 1 
ATOM   8160  N  NE1 . TRP C  1 281 ? 64.274  -4.641  63.781  1.00 10.59  ? 368  TRP C NE1 1 
ATOM   8161  C  CE2 . TRP C  1 281 ? 64.064  -3.308  63.526  1.00 9.89   ? 368  TRP C CE2 1 
ATOM   8162  C  CE3 . TRP C  1 281 ? 64.045  -1.215  64.756  1.00 6.58   ? 368  TRP C CE3 1 
ATOM   8163  C  CZ2 . TRP C  1 281 ? 63.811  -2.645  62.312  1.00 10.55  ? 368  TRP C CZ2 1 
ATOM   8164  C  CZ3 . TRP C  1 281 ? 63.773  -0.558  63.551  1.00 10.01  ? 368  TRP C CZ3 1 
ATOM   8165  C  CH2 . TRP C  1 281 ? 63.660  -1.277  62.348  1.00 10.04  ? 368  TRP C CH2 1 
ATOM   8166  N  N   . LEU C  1 282 ? 66.326  -1.086  69.080  1.00 10.91  ? 369  LEU C N   1 
ATOM   8167  C  CA  . LEU C  1 282 ? 66.370  -0.284  70.289  1.00 12.06  ? 369  LEU C CA  1 
ATOM   8168  C  C   . LEU C  1 282 ? 65.322  0.811   70.159  1.00 11.56  ? 369  LEU C C   1 
ATOM   8169  O  O   . LEU C  1 282 ? 65.263  1.512   69.142  1.00 11.23  ? 369  LEU C O   1 
ATOM   8170  C  CB  . LEU C  1 282 ? 67.752  0.371   70.485  1.00 12.22  ? 369  LEU C CB  1 
ATOM   8171  C  CG  . LEU C  1 282 ? 69.041  -0.458  70.380  1.00 15.53  ? 369  LEU C CG  1 
ATOM   8172  C  CD1 . LEU C  1 282 ? 70.291  0.301   70.902  1.00 14.45  ? 369  LEU C CD1 1 
ATOM   8173  C  CD2 . LEU C  1 282 ? 68.936  -1.869  70.962  1.00 13.70  ? 369  LEU C CD2 1 
ATOM   8174  N  N   . GLY C  1 283 ? 64.502  0.950   71.195  1.00 11.43  ? 370  GLY C N   1 
ATOM   8175  C  CA  . GLY C  1 283 ? 63.591  2.086   71.304  1.00 10.86  ? 370  GLY C CA  1 
ATOM   8176  C  C   . GLY C  1 283 ? 64.224  3.203   72.109  1.00 11.14  ? 370  GLY C C   1 
ATOM   8177  O  O   . GLY C  1 283 ? 65.010  2.951   73.032  1.00 11.41  ? 370  GLY C O   1 
ATOM   8178  N  N   . ARG C  1 284 ? 63.890  4.442   71.767  1.00 10.41  ? 371  ARG C N   1 
ATOM   8179  C  CA  . ARG C  1 284 ? 64.224  5.581   72.634  1.00 10.19  ? 371  ARG C CA  1 
ATOM   8180  C  C   . ARG C  1 284 ? 63.377  6.794   72.281  1.00 10.04  ? 371  ARG C C   1 
ATOM   8181  O  O   . ARG C  1 284 ? 62.797  6.857   71.184  1.00 10.53  ? 371  ARG C O   1 
ATOM   8182  C  CB  . ARG C  1 284 ? 65.739  5.899   72.585  1.00 10.16  ? 371  ARG C CB  1 
ATOM   8183  C  CG  . ARG C  1 284 ? 66.231  6.433   71.244  1.00 11.13  ? 371  ARG C CG  1 
ATOM   8184  C  CD  . ARG C  1 284 ? 67.755  6.703   71.297  1.00 10.05  ? 371  ARG C CD  1 
ATOM   8185  N  NE  . ARG C  1 284 ? 68.222  7.387   70.086  1.00 12.29  ? 371  ARG C NE  1 
ATOM   8186  C  CZ  . ARG C  1 284 ? 69.495  7.724   69.869  1.00 13.83  ? 371  ARG C CZ  1 
ATOM   8187  N  NH1 . ARG C  1 284 ? 70.417  7.470   70.797  1.00 12.91  ? 371  ARG C NH1 1 
ATOM   8188  N  NH2 . ARG C  1 284 ? 69.843  8.348   68.736  1.00 13.63  ? 371  ARG C NH2 1 
ATOM   8189  N  N   . THR C  1 285 ? 63.277  7.745   73.209  1.00 10.04  ? 372  THR C N   1 
ATOM   8190  C  CA  . THR C  1 285 ? 62.657  9.051   72.912  1.00 10.09  ? 372  THR C CA  1 
ATOM   8191  C  C   . THR C  1 285 ? 63.542  9.752   71.867  1.00 10.30  ? 372  THR C C   1 
ATOM   8192  O  O   . THR C  1 285 ? 64.760  9.532   71.823  1.00 10.10  ? 372  THR C O   1 
ATOM   8193  C  CB  . THR C  1 285 ? 62.511  9.941   74.172  1.00 9.98   ? 372  THR C CB  1 
ATOM   8194  O  OG1 . THR C  1 285 ? 63.820  10.268  74.681  1.00 9.41   ? 372  THR C OG1 1 
ATOM   8195  C  CG2 . THR C  1 285 ? 61.706  9.214   75.283  1.00 9.07   ? 372  THR C CG2 1 
ATOM   8196  N  N   . ILE C  1 286 ? 62.932  10.526  70.979  1.00 10.41  ? 373  ILE C N   1 
ATOM   8197  C  CA  . ILE C  1 286 ? 63.740  11.311  70.003  1.00 10.74  ? 373  ILE C CA  1 
ATOM   8198  C  C   . ILE C  1 286 ? 64.567  12.383  70.721  1.00 11.48  ? 373  ILE C C   1 
ATOM   8199  O  O   . ILE C  1 286 ? 65.773  12.484  70.497  1.00 11.52  ? 373  ILE C O   1 
ATOM   8200  C  CB  . ILE C  1 286 ? 62.879  11.892  68.858  1.00 10.06  ? 373  ILE C CB  1 
ATOM   8201  C  CG1 . ILE C  1 286 ? 62.233  10.741  68.064  1.00 9.49   ? 373  ILE C CG1 1 
ATOM   8202  C  CG2 . ILE C  1 286 ? 63.743  12.832  67.933  1.00 10.33  ? 373  ILE C CG2 1 
ATOM   8203  C  CD1 . ILE C  1 286 ? 61.193  11.167  67.029  1.00 10.24  ? 373  ILE C CD1 1 
ATOM   8204  N  N   . SER C  1 287 ? 63.921  13.175  71.575  1.00 12.41  ? 374  SER C N   1 
ATOM   8205  C  CA  . SER C  1 287 ? 64.645  14.111  72.474  1.00 13.43  ? 374  SER C CA  1 
ATOM   8206  C  C   . SER C  1 287 ? 65.638  13.347  73.358  1.00 14.18  ? 374  SER C C   1 
ATOM   8207  O  O   . SER C  1 287 ? 65.317  12.265  73.884  1.00 13.75  ? 374  SER C O   1 
ATOM   8208  C  CB  . SER C  1 287 ? 63.654  14.870  73.352  1.00 13.32  ? 374  SER C CB  1 
ATOM   8209  O  OG  . SER C  1 287 ? 64.299  15.776  74.253  1.00 13.91  ? 374  SER C OG  1 
ATOM   8210  N  N   . LYS C  1 288 ? 66.843  13.899  73.507  1.00 13.85  ? 375  LYS C N   1 
ATOM   8211  C  CA  . LYS C  1 288 ? 67.788  13.377  74.478  1.00 15.55  ? 375  LYS C CA  1 
ATOM   8212  C  C   . LYS C  1 288 ? 67.526  13.932  75.891  1.00 14.83  ? 375  LYS C C   1 
ATOM   8213  O  O   . LYS C  1 288 ? 68.010  13.357  76.861  1.00 15.09  ? 375  LYS C O   1 
ATOM   8214  C  CB  . LYS C  1 288 ? 69.247  13.612  74.039  1.00 14.99  ? 375  LYS C CB  1 
ATOM   8215  C  CG  . LYS C  1 288 ? 69.723  15.018  74.221  1.00 17.00  ? 375  LYS C CG  1 
ATOM   8216  C  CD  . LYS C  1 288 ? 71.240  15.160  73.881  1.00 18.72  ? 375  LYS C CD  1 
ATOM   8217  C  CE  . LYS C  1 288 ? 71.636  16.620  73.663  1.00 24.70  ? 375  LYS C CE  1 
ATOM   8218  N  NZ  . LYS C  1 288 ? 70.822  17.576  74.482  1.00 24.90  ? 375  LYS C NZ  1 
ATOM   8219  N  N   . ASP C  1 289 ? 66.764  15.030  75.990  1.00 15.19  ? 376  ASP C N   1 
ATOM   8220  C  CA  . ASP C  1 289 ? 66.483  15.695  77.277  1.00 16.28  ? 376  ASP C CA  1 
ATOM   8221  C  C   . ASP C  1 289 ? 65.198  15.191  77.923  1.00 15.51  ? 376  ASP C C   1 
ATOM   8222  O  O   . ASP C  1 289 ? 65.141  14.973  79.134  1.00 15.53  ? 376  ASP C O   1 
ATOM   8223  C  CB  . ASP C  1 289 ? 66.335  17.211  77.117  1.00 17.14  ? 376  ASP C CB  1 
ATOM   8224  C  CG  . ASP C  1 289 ? 67.606  17.877  76.615  1.00 21.38  ? 376  ASP C CG  1 
ATOM   8225  O  OD1 . ASP C  1 289 ? 68.717  17.430  76.964  1.00 21.21  ? 376  ASP C OD1 1 
ATOM   8226  O  OD2 . ASP C  1 289 ? 67.474  18.842  75.841  1.00 26.95  ? 376  ASP C OD2 1 
ATOM   8227  N  N   . SER C  1 290 ? 64.176  15.022  77.101  1.00 15.10  ? 377  SER C N   1 
ATOM   8228  C  CA  . SER C  1 290 ? 62.815  14.900  77.607  1.00 15.29  ? 377  SER C CA  1 
ATOM   8229  C  C   . SER C  1 290 ? 62.019  13.795  76.966  1.00 14.07  ? 377  SER C C   1 
ATOM   8230  O  O   . SER C  1 290 ? 62.391  13.248  75.924  1.00 13.45  ? 377  SER C O   1 
ATOM   8231  C  CB  . SER C  1 290 ? 62.082  16.233  77.467  1.00 16.06  ? 377  SER C CB  1 
ATOM   8232  O  OG  . SER C  1 290 ? 62.780  17.221  78.207  1.00 20.18  ? 377  SER C OG  1 
ATOM   8233  N  N   . ARG C  1 291 ? 60.918  13.472  77.628  1.00 12.69  ? 378  ARG C N   1 
ATOM   8234  C  CA  . ARG C  1 291 ? 59.982  12.467  77.158  1.00 11.92  ? 378  ARG C CA  1 
ATOM   8235  C  C   . ARG C  1 291 ? 59.153  12.969  75.964  1.00 11.56  ? 378  ARG C C   1 
ATOM   8236  O  O   . ARG C  1 291 ? 57.937  13.125  76.035  1.00 11.88  ? 378  ARG C O   1 
ATOM   8237  C  CB  . ARG C  1 291 ? 59.122  12.003  78.337  1.00 11.56  ? 378  ARG C CB  1 
ATOM   8238  C  CG  . ARG C  1 291 ? 59.934  11.134  79.299  1.00 10.21  ? 378  ARG C CG  1 
ATOM   8239  C  CD  . ARG C  1 291 ? 59.309  11.097  80.690  1.00 11.44  ? 378  ARG C CD  1 
ATOM   8240  N  NE  . ARG C  1 291 ? 60.162  10.384  81.641  1.00 9.11   ? 378  ARG C NE  1 
ATOM   8241  C  CZ  . ARG C  1 291 ? 59.772  9.986   82.844  1.00 10.28  ? 378  ARG C CZ  1 
ATOM   8242  N  NH1 . ARG C  1 291 ? 58.526  10.225  83.262  1.00 8.76   ? 378  ARG C NH1 1 
ATOM   8243  N  NH2 . ARG C  1 291 ? 60.624  9.326   83.629  1.00 9.79   ? 378  ARG C NH2 1 
ATOM   8244  N  N   . SER C  1 292 ? 59.831  13.204  74.849  1.00 12.42  ? 379  SER C N   1 
ATOM   8245  C  CA  . SER C  1 292 ? 59.139  13.581  73.622  1.00 12.90  ? 379  SER C CA  1 
ATOM   8246  C  C   . SER C  1 292 ? 59.682  12.833  72.433  1.00 12.27  ? 379  SER C C   1 
ATOM   8247  O  O   . SER C  1 292 ? 60.895  12.533  72.336  1.00 11.54  ? 379  SER C O   1 
ATOM   8248  C  CB  . SER C  1 292 ? 59.116  15.102  73.340  1.00 14.42  ? 379  SER C CB  1 
ATOM   8249  O  OG  . SER C  1 292 ? 60.391  15.675  73.371  1.00 18.94  ? 379  SER C OG  1 
ATOM   8250  N  N   . GLY C  1 293 ? 58.756  12.545  71.527  1.00 11.01  ? 380  GLY C N   1 
ATOM   8251  C  CA  . GLY C  1 293 ? 59.033  11.711  70.377  1.00 10.60  ? 380  GLY C CA  1 
ATOM   8252  C  C   . GLY C  1 293 ? 59.319  10.279  70.766  1.00 10.52  ? 380  GLY C C   1 
ATOM   8253  O  O   . GLY C  1 293 ? 59.496  9.953   71.945  1.00 10.48  ? 380  GLY C O   1 
ATOM   8254  N  N   . TYR C  1 294 ? 59.324  9.412   69.764  1.00 10.46  ? 381  TYR C N   1 
ATOM   8255  C  CA  . TYR C  1 294 ? 59.699  8.023   69.945  1.00 10.61  ? 381  TYR C CA  1 
ATOM   8256  C  C   . TYR C  1 294 ? 60.181  7.426   68.632  1.00 10.61  ? 381  TYR C C   1 
ATOM   8257  O  O   . TYR C  1 294 ? 59.527  7.562   67.616  1.00 11.12  ? 381  TYR C O   1 
ATOM   8258  C  CB  . TYR C  1 294 ? 58.572  7.151   70.550  1.00 10.40  ? 381  TYR C CB  1 
ATOM   8259  C  CG  . TYR C  1 294 ? 59.219  6.023   71.310  1.00 10.98  ? 381  TYR C CG  1 
ATOM   8260  C  CD1 . TYR C  1 294 ? 59.519  4.810   70.681  1.00 11.50  ? 381  TYR C CD1 1 
ATOM   8261  C  CD2 . TYR C  1 294 ? 59.639  6.215   72.630  1.00 12.19  ? 381  TYR C CD2 1 
ATOM   8262  C  CE1 . TYR C  1 294 ? 60.182  3.770   71.379  1.00 10.10  ? 381  TYR C CE1 1 
ATOM   8263  C  CE2 . TYR C  1 294 ? 60.283  5.190   73.341  1.00 10.65  ? 381  TYR C CE2 1 
ATOM   8264  C  CZ  . TYR C  1 294 ? 60.560  3.982   72.701  1.00 10.07  ? 381  TYR C CZ  1 
ATOM   8265  O  OH  . TYR C  1 294 ? 61.220  3.008   73.380  1.00 10.95  ? 381  TYR C OH  1 
ATOM   8266  N  N   . GLU C  1 295 ? 61.325  6.759   68.675  1.00 10.71  ? 382  GLU C N   1 
ATOM   8267  C  CA  . GLU C  1 295 ? 61.909  6.157   67.472  1.00 11.54  ? 382  GLU C CA  1 
ATOM   8268  C  C   . GLU C  1 295 ? 62.363  4.734   67.718  1.00 10.56  ? 382  GLU C C   1 
ATOM   8269  O  O   . GLU C  1 295 ? 62.813  4.405   68.824  1.00 12.32  ? 382  GLU C O   1 
ATOM   8270  C  CB  . GLU C  1 295 ? 63.091  7.008   66.959  1.00 11.84  ? 382  GLU C CB  1 
ATOM   8271  C  CG  . GLU C  1 295 ? 64.293  7.089   67.924  1.00 12.76  ? 382  GLU C CG  1 
ATOM   8272  C  CD  . GLU C  1 295 ? 65.362  8.125   67.513  1.00 13.97  ? 382  GLU C CD  1 
ATOM   8273  O  OE1 . GLU C  1 295 ? 65.366  8.579   66.340  1.00 14.05  ? 382  GLU C OE1 1 
ATOM   8274  O  OE2 . GLU C  1 295 ? 66.199  8.462   68.377  1.00 12.84  ? 382  GLU C OE2 1 
ATOM   8275  N  N   . MET C  1 296 ? 62.276  3.896   66.688  1.00 9.94   ? 383  MET C N   1 
ATOM   8276  C  CA  . MET C  1 296 ? 62.820  2.541   66.717  1.00 9.63   ? 383  MET C CA  1 
ATOM   8277  C  C   . MET C  1 296 ? 64.058  2.535   65.839  1.00 9.84   ? 383  MET C C   1 
ATOM   8278  O  O   . MET C  1 296 ? 63.997  2.989   64.693  1.00 9.45   ? 383  MET C O   1 
ATOM   8279  C  CB  . MET C  1 296 ? 61.807  1.514   66.201  1.00 9.91   ? 383  MET C CB  1 
ATOM   8280  C  CG  . MET C  1 296 ? 60.631  1.229   67.171  1.00 9.52   ? 383  MET C CG  1 
ATOM   8281  S  SD  . MET C  1 296 ? 61.148  0.815   68.874  1.00 8.62   ? 383  MET C SD  1 
ATOM   8282  C  CE  . MET C  1 296 ? 61.999  -0.730  68.610  1.00 9.80   ? 383  MET C CE  1 
ATOM   8283  N  N   . LEU C  1 297 ? 65.165  2.032   66.383  1.00 9.54   ? 384  LEU C N   1 
ATOM   8284  C  CA  . LEU C  1 297 ? 66.436  1.934   65.642  1.00 10.29  ? 384  LEU C CA  1 
ATOM   8285  C  C   . LEU C  1 297 ? 66.917  0.482   65.529  1.00 10.74  ? 384  LEU C C   1 
ATOM   8286  O  O   . LEU C  1 297 ? 67.008  -0.232  66.535  1.00 10.17  ? 384  LEU C O   1 
ATOM   8287  C  CB  . LEU C  1 297 ? 67.509  2.811   66.302  1.00 10.95  ? 384  LEU C CB  1 
ATOM   8288  C  CG  . LEU C  1 297 ? 67.099  4.246   66.643  1.00 11.73  ? 384  LEU C CG  1 
ATOM   8289  C  CD1 . LEU C  1 297 ? 68.092  4.886   67.627  1.00 14.34  ? 384  LEU C CD1 1 
ATOM   8290  C  CD2 . LEU C  1 297 ? 66.952  5.111   65.382  1.00 15.19  ? 384  LEU C CD2 1 
ATOM   8291  N  N   . LYS C  1 298 ? 67.194  0.039   64.305  1.00 10.45  ? 385  LYS C N   1 
ATOM   8292  C  CA  . LYS C  1 298 ? 67.759  -1.302  64.110  1.00 11.60  ? 385  LYS C CA  1 
ATOM   8293  C  C   . LYS C  1 298 ? 69.284  -1.192  64.247  1.00 11.39  ? 385  LYS C C   1 
ATOM   8294  O  O   . LYS C  1 298 ? 69.927  -0.526  63.432  1.00 10.74  ? 385  LYS C O   1 
ATOM   8295  C  CB  . LYS C  1 298 ? 67.377  -1.892  62.743  1.00 11.34  ? 385  LYS C CB  1 
ATOM   8296  C  CG  . LYS C  1 298 ? 67.725  -3.389  62.618  1.00 12.08  ? 385  LYS C CG  1 
ATOM   8297  C  CD  . LYS C  1 298 ? 67.075  -4.017  61.377  1.00 13.14  ? 385  LYS C CD  1 
ATOM   8298  C  CE  . LYS C  1 298 ? 67.037  -5.529  61.539  1.00 15.75  ? 385  LYS C CE  1 
ATOM   8299  N  NZ  . LYS C  1 298 ? 66.617  -6.230  60.284  1.00 16.09  ? 385  LYS C NZ  1 
ATOM   8300  N  N   . VAL C  1 299 ? 69.825  -1.837  65.286  1.00 11.12  ? 386  VAL C N   1 
ATOM   8301  C  CA  . VAL C  1 299 ? 71.245  -1.698  65.673  1.00 11.06  ? 386  VAL C CA  1 
ATOM   8302  C  C   . VAL C  1 299 ? 71.831  -3.096  65.787  1.00 11.18  ? 386  VAL C C   1 
ATOM   8303  O  O   . VAL C  1 299 ? 71.829  -3.705  66.869  1.00 11.09  ? 386  VAL C O   1 
ATOM   8304  C  CB  . VAL C  1 299 ? 71.429  -0.928  67.007  1.00 10.40  ? 386  VAL C CB  1 
ATOM   8305  C  CG1 . VAL C  1 299 ? 72.932  -0.788  67.368  1.00 10.66  ? 386  VAL C CG1 1 
ATOM   8306  C  CG2 . VAL C  1 299 ? 70.771  0.432   66.949  1.00 9.90   ? 386  VAL C CG2 1 
ATOM   8307  N  N   . PRO C  1 300 ? 72.297  -3.638  64.653  1.00 11.61  ? 387  PRO C N   1 
ATOM   8308  C  CA  . PRO C  1 300 ? 72.813  -5.008  64.661  1.00 12.02  ? 387  PRO C CA  1 
ATOM   8309  C  C   . PRO C  1 300 ? 73.884  -5.164  65.747  1.00 12.14  ? 387  PRO C C   1 
ATOM   8310  O  O   . PRO C  1 300 ? 74.740  -4.289  65.887  1.00 12.54  ? 387  PRO C O   1 
ATOM   8311  C  CB  . PRO C  1 300 ? 73.413  -5.152  63.259  1.00 11.71  ? 387  PRO C CB  1 
ATOM   8312  C  CG  . PRO C  1 300 ? 72.536  -4.236  62.398  1.00 12.81  ? 387  PRO C CG  1 
ATOM   8313  C  CD  . PRO C  1 300 ? 72.337  -3.038  63.301  1.00 12.01  ? 387  PRO C CD  1 
ATOM   8314  N  N   . ASN C  1 301 ? 73.785  -6.239  66.534  1.00 12.61  ? 388  ASN C N   1 
ATOM   8315  C  CA  . ASN C  1 301 ? 74.773  -6.560  67.595  1.00 13.08  ? 388  ASN C CA  1 
ATOM   8316  C  C   . ASN C  1 301 ? 74.910  -5.518  68.713  1.00 13.44  ? 388  ASN C C   1 
ATOM   8317  O  O   . ASN C  1 301 ? 75.974  -5.405  69.341  1.00 13.61  ? 388  ASN C O   1 
ATOM   8318  C  CB  . ASN C  1 301 ? 76.143  -6.885  66.964  1.00 13.24  ? 388  ASN C CB  1 
ATOM   8319  C  CG  . ASN C  1 301 ? 76.050  -8.041  65.987  1.00 14.28  ? 388  ASN C CG  1 
ATOM   8320  O  OD1 . ASN C  1 301 ? 75.565  -9.115  66.343  1.00 15.50  ? 388  ASN C OD1 1 
ATOM   8321  N  ND2 . ASN C  1 301 ? 76.480  -7.820  64.745  1.00 16.87  ? 388  ASN C ND2 1 
ATOM   8322  N  N   . ALA C  1 302 ? 73.828  -4.777  68.961  1.00 13.18  ? 389  ALA C N   1 
ATOM   8323  C  CA  . ALA C  1 302 ? 73.765  -3.782  70.047  1.00 13.02  ? 389  ALA C CA  1 
ATOM   8324  C  C   . ALA C  1 302 ? 74.156  -4.384  71.405  1.00 12.69  ? 389  ALA C C   1 
ATOM   8325  O  O   . ALA C  1 302 ? 74.706  -3.676  72.263  1.00 12.73  ? 389  ALA C O   1 
ATOM   8326  C  CB  . ALA C  1 302 ? 72.365  -3.170  70.117  1.00 12.85  ? 389  ALA C CB  1 
ATOM   8327  N  N   . GLU C  1 303 ? 73.876  -5.675  71.589  1.00 11.62  ? 390  GLU C N   1 
ATOM   8328  C  CA  . GLU C  1 303 ? 74.090  -6.347  72.869  1.00 12.42  ? 390  GLU C CA  1 
ATOM   8329  C  C   . GLU C  1 303 ? 75.570  -6.685  73.118  1.00 12.98  ? 390  GLU C C   1 
ATOM   8330  O  O   . GLU C  1 303 ? 75.977  -6.871  74.262  1.00 13.28  ? 390  GLU C O   1 
ATOM   8331  C  CB  . GLU C  1 303 ? 73.243  -7.628  72.968  1.00 12.22  ? 390  GLU C CB  1 
ATOM   8332  C  CG  . GLU C  1 303 ? 73.254  -8.247  74.386  1.00 12.53  ? 390  GLU C CG  1 
ATOM   8333  C  CD  . GLU C  1 303 ? 72.315  -9.413  74.555  1.00 13.15  ? 390  GLU C CD  1 
ATOM   8334  O  OE1 . GLU C  1 303 ? 72.034  -9.766  75.730  1.00 14.80  ? 390  GLU C OE1 1 
ATOM   8335  O  OE2 . GLU C  1 303 ? 71.850  -9.968  73.534  1.00 12.24  ? 390  GLU C OE2 1 
ATOM   8336  N  N   . THR C  1 304 ? 76.364  -6.769  72.050  1.00 13.40  ? 391  THR C N   1 
ATOM   8337  C  CA  . THR C  1 304 ? 77.757  -7.221  72.177  1.00 13.86  ? 391  THR C CA  1 
ATOM   8338  C  C   . THR C  1 304 ? 78.816  -6.274  71.612  1.00 14.09  ? 391  THR C C   1 
ATOM   8339  O  O   . THR C  1 304 ? 79.999  -6.446  71.898  1.00 14.68  ? 391  THR C O   1 
ATOM   8340  C  CB  . THR C  1 304 ? 77.952  -8.568  71.490  1.00 14.27  ? 391  THR C CB  1 
ATOM   8341  O  OG1 . THR C  1 304 ? 77.614  -8.416  70.108  1.00 14.89  ? 391  THR C OG1 1 
ATOM   8342  C  CG2 . THR C  1 304 ? 77.071  -9.638  72.124  1.00 15.13  ? 391  THR C CG2 1 
ATOM   8343  N  N   . ASP C  1 305 ? 78.414  -5.285  70.818  1.00 13.38  ? 392  ASP C N   1 
ATOM   8344  C  CA  . ASP C  1 305 ? 79.385  -4.466  70.060  1.00 13.27  ? 392  ASP C CA  1 
ATOM   8345  C  C   . ASP C  1 305 ? 79.283  -2.998  70.478  1.00 12.96  ? 392  ASP C C   1 
ATOM   8346  O  O   . ASP C  1 305 ? 78.259  -2.365  70.237  1.00 13.03  ? 392  ASP C O   1 
ATOM   8347  C  CB  . ASP C  1 305 ? 79.141  -4.643  68.552  1.00 13.52  ? 392  ASP C CB  1 
ATOM   8348  C  CG  . ASP C  1 305 ? 80.233  -4.010  67.683  1.00 15.10  ? 392  ASP C CG  1 
ATOM   8349  O  OD1 . ASP C  1 305 ? 81.097  -3.283  68.207  1.00 15.42  ? 392  ASP C OD1 1 
ATOM   8350  O  OD2 . ASP C  1 305 ? 80.221  -4.244  66.449  1.00 17.36  ? 392  ASP C OD2 1 
ATOM   8351  N  N   . ILE C  1 306 ? 80.334  -2.475  71.127  1.00 12.01  ? 393  ILE C N   1 
ATOM   8352  C  CA  . ILE C  1 306 ? 80.344  -1.071  71.599  1.00 12.45  ? 393  ILE C CA  1 
ATOM   8353  C  C   . ILE C  1 306 ? 80.337  -0.053  70.463  1.00 12.10  ? 393  ILE C C   1 
ATOM   8354  O  O   . ILE C  1 306 ? 80.014  1.127   70.676  1.00 12.86  ? 393  ILE C O   1 
ATOM   8355  C  CB  . ILE C  1 306 ? 81.532  -0.752  72.588  1.00 13.06  ? 393  ILE C CB  1 
ATOM   8356  C  CG1 . ILE C  1 306 ? 82.905  -0.770  71.863  1.00 13.21  ? 393  ILE C CG1 1 
ATOM   8357  C  CG2 . ILE C  1 306 ? 81.495  -1.700  73.772  1.00 13.67  ? 393  ILE C CG2 1 
ATOM   8358  C  CD1 . ILE C  1 306 ? 84.126  -0.575  72.817  1.00 13.18  ? 393  ILE C CD1 1 
ATOM   8359  N  N   . GLN C  1 307 ? 80.680  -0.512  69.259  1.00 12.72  ? 394  GLN C N   1 
ATOM   8360  C  CA  . GLN C  1 307 ? 80.705  0.351   68.068  1.00 13.35  ? 394  GLN C CA  1 
ATOM   8361  C  C   . GLN C  1 307 ? 79.434  0.271   67.226  1.00 13.04  ? 394  GLN C C   1 
ATOM   8362  O  O   . GLN C  1 307 ? 79.308  1.008   66.249  1.00 12.49  ? 394  GLN C O   1 
ATOM   8363  C  CB  . GLN C  1 307 ? 81.888  0.003   67.166  1.00 13.84  ? 394  GLN C CB  1 
ATOM   8364  C  CG  . GLN C  1 307 ? 83.243  0.111   67.819  1.00 17.76  ? 394  GLN C CG  1 
ATOM   8365  C  CD  . GLN C  1 307 ? 84.340  -0.043  66.788  1.00 20.89  ? 394  GLN C CD  1 
ATOM   8366  O  OE1 . GLN C  1 307 ? 84.642  -1.160  66.327  1.00 24.31  ? 394  GLN C OE1 1 
ATOM   8367  N  NE2 . GLN C  1 307 ? 84.902  1.079   66.377  1.00 22.47  ? 394  GLN C NE2 1 
ATOM   8368  N  N   . SER C  1 308 ? 78.514  -0.632  67.584  1.00 12.61  ? 395  SER C N   1 
ATOM   8369  C  CA  . SER C  1 308 ? 77.255  -0.788  66.832  1.00 13.12  ? 395  SER C CA  1 
ATOM   8370  C  C   . SER C  1 308 ? 76.414  0.498   66.742  1.00 13.58  ? 395  SER C C   1 
ATOM   8371  O  O   . SER C  1 308 ? 76.121  1.152   67.758  1.00 13.70  ? 395  SER C O   1 
ATOM   8372  C  CB  . SER C  1 308 ? 76.415  -1.938  67.399  1.00 12.89  ? 395  SER C CB  1 
ATOM   8373  O  OG  . SER C  1 308 ? 76.123  -1.762  68.777  1.00 11.52  ? 395  SER C OG  1 
ATOM   8374  N  N   . GLY C  1 309 ? 76.009  0.832   65.514  1.00 14.05  ? 396  GLY C N   1 
ATOM   8375  C  CA  . GLY C  1 309 ? 75.125  1.972   65.235  1.00 13.95  ? 396  GLY C CA  1 
ATOM   8376  C  C   . GLY C  1 309 ? 73.916  1.564   64.393  1.00 13.53  ? 396  GLY C C   1 
ATOM   8377  O  O   . GLY C  1 309 ? 73.818  0.406   63.963  1.00 13.54  ? 396  GLY C O   1 
ATOM   8378  N  N   . PRO C  1 310 ? 72.974  2.500   64.168  1.00 13.47  ? 397  PRO C N   1 
ATOM   8379  C  CA  . PRO C  1 310 ? 71.740  2.152   63.444  1.00 13.95  ? 397  PRO C CA  1 
ATOM   8380  C  C   . PRO C  1 310 ? 71.958  1.875   61.953  1.00 14.55  ? 397  PRO C C   1 
ATOM   8381  O  O   . PRO C  1 310 ? 72.805  2.527   61.314  1.00 13.47  ? 397  PRO C O   1 
ATOM   8382  C  CB  . PRO C  1 310 ? 70.850  3.407   63.623  1.00 13.72  ? 397  PRO C CB  1 
ATOM   8383  C  CG  . PRO C  1 310 ? 71.462  4.177   64.762  1.00 14.29  ? 397  PRO C CG  1 
ATOM   8384  C  CD  . PRO C  1 310 ? 72.961  3.914   64.585  1.00 13.77  ? 397  PRO C CD  1 
ATOM   8385  N  N   . ILE C  1 311 ? 71.212  0.907   61.416  1.00 14.51  ? 398  ILE C N   1 
ATOM   8386  C  CA  . ILE C  1 311 ? 71.169  0.661   59.965  1.00 15.19  ? 398  ILE C CA  1 
ATOM   8387  C  C   . ILE C  1 311 ? 69.791  0.992   59.355  1.00 15.64  ? 398  ILE C C   1 
ATOM   8388  O  O   . ILE C  1 311 ? 69.646  1.094   58.130  1.00 15.34  ? 398  ILE C O   1 
ATOM   8389  C  CB  . ILE C  1 311 ? 71.595  -0.789  59.597  1.00 15.11  ? 398  ILE C CB  1 
ATOM   8390  C  CG1 . ILE C  1 311 ? 70.549  -1.828  60.073  1.00 14.97  ? 398  ILE C CG1 1 
ATOM   8391  C  CG2 . ILE C  1 311 ? 73.039  -1.068  60.104  1.00 15.90  ? 398  ILE C CG2 1 
ATOM   8392  C  CD1 . ILE C  1 311 ? 70.710  -3.230  59.401  1.00 15.64  ? 398  ILE C CD1 1 
ATOM   8393  N  N   . SER C  1 312 ? 68.783  1.128   60.215  1.00 15.04  ? 399  SER C N   1 
ATOM   8394  C  CA  . SER C  1 312 ? 67.475  1.642   59.793  1.00 15.00  ? 399  SER C CA  1 
ATOM   8395  C  C   . SER C  1 312 ? 66.732  2.275   60.966  1.00 13.94  ? 399  SER C C   1 
ATOM   8396  O  O   . SER C  1 312 ? 67.130  2.121   62.132  1.00 13.70  ? 399  SER C O   1 
ATOM   8397  C  CB  . SER C  1 312 ? 66.637  0.568   59.098  1.00 14.30  ? 399  SER C CB  1 
ATOM   8398  O  OG  . SER C  1 312 ? 66.499  -0.539  59.924  1.00 18.44  ? 399  SER C OG  1 
ATOM   8399  N  N   . ASN C  1 313 ? 65.683  3.025   60.650  1.00 13.44  ? 400  ASN C N   1 
ATOM   8400  C  CA  . ASN C  1 313 ? 64.942  3.758   61.656  1.00 13.21  ? 400  ASN C CA  1 
ATOM   8401  C  C   . ASN C  1 313 ? 63.470  3.825   61.296  1.00 13.07  ? 400  ASN C C   1 
ATOM   8402  O  O   . ASN C  1 313 ? 63.094  3.763   60.113  1.00 12.69  ? 400  ASN C O   1 
ATOM   8403  C  CB  . ASN C  1 313 ? 65.507  5.165   61.850  1.00 13.68  ? 400  ASN C CB  1 
ATOM   8404  C  CG  . ASN C  1 313 ? 65.042  6.143   60.765  1.00 16.52  ? 400  ASN C CG  1 
ATOM   8405  O  OD1 . ASN C  1 313 ? 63.967  6.739   60.877  1.00 18.18  ? 400  ASN C OD1 1 
ATOM   8406  N  ND2 . ASN C  1 313 ? 65.851  6.304   59.710  1.00 16.38  ? 400  ASN C ND2 1 
ATOM   8407  N  N   . GLN C  1 314 ? 62.651  3.936   62.331  1.00 12.06  ? 401  GLN C N   1 
ATOM   8408  C  CA  . GLN C  1 314 ? 61.228  4.199   62.165  1.00 11.43  ? 401  GLN C CA  1 
ATOM   8409  C  C   . GLN C  1 314 ? 60.769  5.136   63.269  1.00 11.10  ? 401  GLN C C   1 
ATOM   8410  O  O   . GLN C  1 314 ? 60.915  4.829   64.477  1.00 11.67  ? 401  GLN C O   1 
ATOM   8411  C  CB  . GLN C  1 314 ? 60.409  2.913   62.155  1.00 11.11  ? 401  GLN C CB  1 
ATOM   8412  C  CG  . GLN C  1 314 ? 58.943  3.196   61.734  1.00 11.30  ? 401  GLN C CG  1 
ATOM   8413  C  CD  . GLN C  1 314 ? 58.118  1.945   61.631  1.00 11.00  ? 401  GLN C CD  1 
ATOM   8414  O  OE1 . GLN C  1 314 ? 58.638  0.870   61.322  1.00 11.91  ? 401  GLN C OE1 1 
ATOM   8415  N  NE2 . GLN C  1 314 ? 56.824  2.068   61.932  1.00 9.15   ? 401  GLN C NE2 1 
ATOM   8416  N  N   . VAL C  1 315 ? 60.266  6.297   62.854  1.00 10.89  ? 402  VAL C N   1 
ATOM   8417  C  CA  . VAL C  1 315 ? 59.637  7.238   63.767  1.00 10.35  ? 402  VAL C CA  1 
ATOM   8418  C  C   . VAL C  1 315 ? 58.241  6.735   64.184  1.00 10.44  ? 402  VAL C C   1 
ATOM   8419  O  O   . VAL C  1 315 ? 57.375  6.497   63.344  1.00 9.90   ? 402  VAL C O   1 
ATOM   8420  C  CB  . VAL C  1 315 ? 59.572  8.658   63.151  1.00 10.94  ? 402  VAL C CB  1 
ATOM   8421  C  CG1 . VAL C  1 315 ? 58.648  9.603   63.965  1.00 11.74  ? 402  VAL C CG1 1 
ATOM   8422  C  CG2 . VAL C  1 315 ? 61.000  9.239   63.027  1.00 9.75   ? 402  VAL C CG2 1 
ATOM   8423  N  N   . ILE C  1 316 ? 58.058  6.572   65.496  1.00 10.29  ? 403  ILE C N   1 
ATOM   8424  C  CA  . ILE C  1 316 ? 56.802  6.045   66.067  1.00 10.38  ? 403  ILE C CA  1 
ATOM   8425  C  C   . ILE C  1 316 ? 55.910  7.213   66.486  1.00 10.56  ? 403  ILE C C   1 
ATOM   8426  O  O   . ILE C  1 316 ? 54.692  7.206   66.234  1.00 10.14  ? 403  ILE C O   1 
ATOM   8427  C  CB  . ILE C  1 316 ? 57.077  5.096   67.276  1.00 9.85   ? 403  ILE C CB  1 
ATOM   8428  C  CG1 . ILE C  1 316 ? 58.011  3.929   66.885  1.00 10.71  ? 403  ILE C CG1 1 
ATOM   8429  C  CG2 . ILE C  1 316 ? 55.730  4.565   67.891  1.00 10.54  ? 403  ILE C CG2 1 
ATOM   8430  C  CD1 . ILE C  1 316 ? 57.600  3.167   65.605  1.00 9.46   ? 403  ILE C CD1 1 
ATOM   8431  N  N   . VAL C  1 317 ? 56.526  8.209   67.134  1.00 11.06  ? 404  VAL C N   1 
ATOM   8432  C  CA  . VAL C  1 317 ? 55.844  9.436   67.556  1.00 11.33  ? 404  VAL C CA  1 
ATOM   8433  C  C   . VAL C  1 317 ? 56.786  10.597  67.218  1.00 11.73  ? 404  VAL C C   1 
ATOM   8434  O  O   . VAL C  1 317 ? 57.993  10.579  67.571  1.00 10.87  ? 404  VAL C O   1 
ATOM   8435  C  CB  . VAL C  1 317 ? 55.544  9.442   69.086  1.00 11.67  ? 404  VAL C CB  1 
ATOM   8436  C  CG1 . VAL C  1 317 ? 54.801  10.707  69.507  1.00 11.75  ? 404  VAL C CG1 1 
ATOM   8437  C  CG2 . VAL C  1 317 ? 54.772  8.181   69.491  1.00 10.02  ? 404  VAL C CG2 1 
ATOM   8438  N  N   . ASN C  1 318 ? 56.277  11.600  66.517  1.00 12.60  ? 405  ASN C N   1 
ATOM   8439  C  CA  . ASN C  1 318 ? 57.204  12.675  66.151  1.00 14.30  ? 405  ASN C CA  1 
ATOM   8440  C  C   . ASN C  1 318 ? 57.631  13.479  67.387  1.00 14.16  ? 405  ASN C C   1 
ATOM   8441  O  O   . ASN C  1 318 ? 56.972  13.405  68.452  1.00 13.77  ? 405  ASN C O   1 
ATOM   8442  C  CB  . ASN C  1 318 ? 56.719  13.532  64.960  1.00 15.51  ? 405  ASN C CB  1 
ATOM   8443  C  CG  . ASN C  1 318 ? 55.485  14.329  65.259  1.00 16.22  ? 405  ASN C CG  1 
ATOM   8444  O  OD1 . ASN C  1 318 ? 55.364  14.951  66.316  1.00 19.80  ? 405  ASN C OD1 1 
ATOM   8445  N  ND2 . ASN C  1 318 ? 54.551  14.333  64.308  1.00 17.64  ? 405  ASN C ND2 1 
ATOM   8446  N  N   . ASN C  1 319 ? 58.748  14.197  67.251  1.00 14.37  ? 406  ASN C N   1 
ATOM   8447  C  CA  . ASN C  1 319 ? 59.366  14.930  68.367  1.00 14.61  ? 406  ASN C CA  1 
ATOM   8448  C  C   . ASN C  1 319 ? 58.643  16.242  68.689  1.00 14.73  ? 406  ASN C C   1 
ATOM   8449  O  O   . ASN C  1 319 ? 59.117  17.015  69.516  1.00 15.16  ? 406  ASN C O   1 
ATOM   8450  C  CB  . ASN C  1 319 ? 60.875  15.174  68.105  1.00 14.33  ? 406  ASN C CB  1 
ATOM   8451  C  CG  . ASN C  1 319 ? 61.650  15.628  69.362  1.00 15.67  ? 406  ASN C CG  1 
ATOM   8452  O  OD1 . ASN C  1 319 ? 62.585  16.457  69.281  1.00 16.57  ? 406  ASN C OD1 1 
ATOM   8453  N  ND2 . ASN C  1 319 ? 61.304  15.054  70.519  1.00 11.92  ? 406  ASN C ND2 1 
ATOM   8454  N  N   . GLN C  1 320 ? 57.494  16.475  68.049  1.00 14.47  ? 407  GLN C N   1 
ATOM   8455  C  CA  . GLN C  1 320 ? 56.599  17.586  68.415  1.00 14.37  ? 407  GLN C CA  1 
ATOM   8456  C  C   . GLN C  1 320 ? 55.477  17.121  69.352  1.00 14.38  ? 407  GLN C C   1 
ATOM   8457  O  O   . GLN C  1 320 ? 54.570  17.911  69.709  1.00 14.78  ? 407  GLN C O   1 
ATOM   8458  C  CB  . GLN C  1 320 ? 55.970  18.207  67.164  1.00 15.62  ? 407  GLN C CB  1 
ATOM   8459  C  CG  . GLN C  1 320 ? 56.970  18.919  66.258  1.00 19.22  ? 407  GLN C CG  1 
ATOM   8460  C  CD  . GLN C  1 320 ? 56.286  19.700  65.155  1.00 21.99  ? 407  GLN C CD  1 
ATOM   8461  O  OE1 . GLN C  1 320 ? 56.231  19.258  64.006  1.00 25.20  ? 407  GLN C OE1 1 
ATOM   8462  N  NE2 . GLN C  1 320 ? 55.769  20.869  65.496  1.00 24.34  ? 407  GLN C NE2 1 
ATOM   8463  N  N   . ASN C  1 321 ? 55.518  15.834  69.703  1.00 12.36  ? 408  ASN C N   1 
ATOM   8464  C  CA  . ASN C  1 321 ? 54.508  15.227  70.566  1.00 12.31  ? 408  ASN C CA  1 
ATOM   8465  C  C   . ASN C  1 321 ? 55.123  14.490  71.740  1.00 12.11  ? 408  ASN C C   1 
ATOM   8466  O  O   . ASN C  1 321 ? 56.235  13.967  71.620  1.00 11.79  ? 408  ASN C O   1 
ATOM   8467  C  CB  . ASN C  1 321 ? 53.639  14.292  69.730  1.00 11.80  ? 408  ASN C CB  1 
ATOM   8468  C  CG  . ASN C  1 321 ? 52.690  15.061  68.827  1.00 13.53  ? 408  ASN C CG  1 
ATOM   8469  O  OD1 . ASN C  1 321 ? 52.929  15.199  67.618  1.00 16.29  ? 408  ASN C OD1 1 
ATOM   8470  N  ND2 . ASN C  1 321 ? 51.613  15.570  69.407  1.00 11.13  ? 408  ASN C ND2 1 
ATOM   8471  N  N   . TRP C  1 322 ? 54.392  14.437  72.856  1.00 11.69  ? 409  TRP C N   1 
ATOM   8472  C  CA  . TRP C  1 322 ? 54.871  13.814  74.098  1.00 11.60  ? 409  TRP C CA  1 
ATOM   8473  C  C   . TRP C  1 322 ? 54.779  12.286  74.055  1.00 11.29  ? 409  TRP C C   1 
ATOM   8474  O  O   . TRP C  1 322 ? 53.797  11.714  73.561  1.00 10.33  ? 409  TRP C O   1 
ATOM   8475  C  CB  . TRP C  1 322 ? 54.107  14.378  75.321  1.00 12.78  ? 409  TRP C CB  1 
ATOM   8476  C  CG  . TRP C  1 322 ? 54.196  15.904  75.423  1.00 13.57  ? 409  TRP C CG  1 
ATOM   8477  C  CD1 . TRP C  1 322 ? 53.177  16.803  75.286  1.00 14.29  ? 409  TRP C CD1 1 
ATOM   8478  C  CD2 . TRP C  1 322 ? 55.383  16.674  75.660  1.00 12.65  ? 409  TRP C CD2 1 
ATOM   8479  N  NE1 . TRP C  1 322 ? 53.660  18.092  75.416  1.00 15.23  ? 409  TRP C NE1 1 
ATOM   8480  C  CE2 . TRP C  1 322 ? 55.008  18.036  75.653  1.00 13.71  ? 409  TRP C CE2 1 
ATOM   8481  C  CE3 . TRP C  1 322 ? 56.732  16.338  75.880  1.00 13.56  ? 409  TRP C CE3 1 
ATOM   8482  C  CZ2 . TRP C  1 322 ? 55.935  19.078  75.867  1.00 16.05  ? 409  TRP C CZ2 1 
ATOM   8483  C  CZ3 . TRP C  1 322 ? 57.662  17.364  76.082  1.00 12.88  ? 409  TRP C CZ3 1 
ATOM   8484  C  CH2 . TRP C  1 322 ? 57.255  18.725  76.070  1.00 14.64  ? 409  TRP C CH2 1 
ATOM   8485  N  N   . SER C  1 323 ? 55.806  11.629  74.586  1.00 9.89   ? 410  SER C N   1 
ATOM   8486  C  CA  . SER C  1 323 ? 55.781  10.178  74.718  1.00 9.75   ? 410  SER C CA  1 
ATOM   8487  C  C   . SER C  1 323 ? 55.767  9.896   76.228  1.00 9.33   ? 410  SER C C   1 
ATOM   8488  O  O   . SER C  1 323 ? 55.010  10.542  76.966  1.00 9.49   ? 410  SER C O   1 
ATOM   8489  C  CB  . SER C  1 323 ? 56.958  9.522   73.963  1.00 9.47   ? 410  SER C CB  1 
ATOM   8490  O  OG  . SER C  1 323 ? 58.232  10.062  74.358  1.00 8.64   ? 410  SER C OG  1 
ATOM   8491  N  N   . GLY C  1 324 ? 56.579  8.948   76.681  1.00 9.72   ? 411  GLY C N   1 
ATOM   8492  C  CA  . GLY C  1 324 ? 56.544  8.501   78.093  1.00 9.21   ? 411  GLY C CA  1 
ATOM   8493  C  C   . GLY C  1 324 ? 57.251  7.170   78.225  1.00 9.33   ? 411  GLY C C   1 
ATOM   8494  O  O   . GLY C  1 324 ? 58.203  6.898   77.492  1.00 9.35   ? 411  GLY C O   1 
ATOM   8495  N  N   . TYR C  1 325 ? 56.783  6.325   79.149  1.00 8.88   ? 412  TYR C N   1 
ATOM   8496  C  CA  . TYR C  1 325 ? 57.334  4.960   79.302  1.00 8.67   ? 412  TYR C CA  1 
ATOM   8497  C  C   . TYR C  1 325 ? 57.107  4.156   78.028  1.00 8.41   ? 412  TYR C C   1 
ATOM   8498  O  O   . TYR C  1 325 ? 56.144  4.411   77.270  1.00 9.92   ? 412  TYR C O   1 
ATOM   8499  C  CB  . TYR C  1 325 ? 56.680  4.232   80.490  1.00 8.82   ? 412  TYR C CB  1 
ATOM   8500  C  CG  . TYR C  1 325 ? 57.172  4.677   81.850  1.00 9.59   ? 412  TYR C CG  1 
ATOM   8501  C  CD1 . TYR C  1 325 ? 58.027  5.777   81.986  1.00 10.18  ? 412  TYR C CD1 1 
ATOM   8502  C  CD2 . TYR C  1 325 ? 56.816  3.967   83.006  1.00 11.27  ? 412  TYR C CD2 1 
ATOM   8503  C  CE1 . TYR C  1 325 ? 58.513  6.175   83.245  1.00 10.02  ? 412  TYR C CE1 1 
ATOM   8504  C  CE2 . TYR C  1 325 ? 57.280  4.372   84.268  1.00 9.76   ? 412  TYR C CE2 1 
ATOM   8505  C  CZ  . TYR C  1 325 ? 58.127  5.466   84.366  1.00 9.07   ? 412  TYR C CZ  1 
ATOM   8506  O  OH  . TYR C  1 325 ? 58.588  5.856   85.599  1.00 8.48   ? 412  TYR C OH  1 
ATOM   8507  N  N   . SER C  1 326 ? 57.986  3.193   77.787  1.00 7.82   ? 413  SER C N   1 
ATOM   8508  C  CA  . SER C  1 326 ? 57.780  2.230   76.715  1.00 7.74   ? 413  SER C CA  1 
ATOM   8509  C  C   . SER C  1 326 ? 58.220  0.858   77.213  1.00 7.45   ? 413  SER C C   1 
ATOM   8510  O  O   . SER C  1 326 ? 59.078  0.759   78.098  1.00 7.98   ? 413  SER C O   1 
ATOM   8511  C  CB  . SER C  1 326 ? 58.543  2.619   75.450  1.00 7.45   ? 413  SER C CB  1 
ATOM   8512  O  OG  . SER C  1 326 ? 59.957  2.729   75.709  1.00 8.49   ? 413  SER C OG  1 
ATOM   8513  N  N   . GLY C  1 327 ? 57.654  -0.196  76.643  1.00 7.48   ? 414  GLY C N   1 
ATOM   8514  C  CA  . GLY C  1 327 ? 57.983  -1.549  77.108  1.00 7.29   ? 414  GLY C CA  1 
ATOM   8515  C  C   . GLY C  1 327 ? 57.677  -2.631  76.101  1.00 7.92   ? 414  GLY C C   1 
ATOM   8516  O  O   . GLY C  1 327 ? 56.978  -2.415  75.099  1.00 8.11   ? 414  GLY C O   1 
ATOM   8517  N  N   . ALA C  1 328 ? 58.181  -3.819  76.391  1.00 7.81   ? 415  ALA C N   1 
ATOM   8518  C  CA  . ALA C  1 328 ? 58.018  -4.957  75.515  1.00 8.21   ? 415  ALA C CA  1 
ATOM   8519  C  C   . ALA C  1 328 ? 56.875  -5.886  75.938  1.00 7.80   ? 415  ALA C C   1 
ATOM   8520  O  O   . ALA C  1 328 ? 56.596  -6.071  77.138  1.00 8.40   ? 415  ALA C O   1 
ATOM   8521  C  CB  . ALA C  1 328 ? 59.348  -5.748  75.459  1.00 8.05   ? 415  ALA C CB  1 
ATOM   8522  N  N   . PHE C  1 329 ? 56.254  -6.507  74.944  1.00 7.55   ? 416  PHE C N   1 
ATOM   8523  C  CA  . PHE C  1 329 ? 55.405  -7.666  75.160  1.00 7.84   ? 416  PHE C CA  1 
ATOM   8524  C  C   . PHE C  1 329 ? 55.400  -8.485  73.879  1.00 8.45   ? 416  PHE C C   1 
ATOM   8525  O  O   . PHE C  1 329 ? 55.787  -7.983  72.810  1.00 8.33   ? 416  PHE C O   1 
ATOM   8526  C  CB  . PHE C  1 329 ? 53.955  -7.274  75.538  1.00 7.48   ? 416  PHE C CB  1 
ATOM   8527  C  CG  . PHE C  1 329 ? 53.204  -6.537  74.437  1.00 8.00   ? 416  PHE C CG  1 
ATOM   8528  C  CD1 . PHE C  1 329 ? 53.463  -5.188  74.169  1.00 9.42   ? 416  PHE C CD1 1 
ATOM   8529  C  CD2 . PHE C  1 329 ? 52.194  -7.181  73.714  1.00 6.46   ? 416  PHE C CD2 1 
ATOM   8530  C  CE1 . PHE C  1 329 ? 52.766  -4.509  73.161  1.00 8.93   ? 416  PHE C CE1 1 
ATOM   8531  C  CE2 . PHE C  1 329 ? 51.491  -6.511  72.702  1.00 8.00   ? 416  PHE C CE2 1 
ATOM   8532  C  CZ  . PHE C  1 329 ? 51.760  -5.185  72.429  1.00 7.48   ? 416  PHE C CZ  1 
ATOM   8533  N  N   . ILE C  1 330 ? 54.975  -9.735  74.006  1.00 8.51   ? 417  ILE C N   1 
ATOM   8534  C  CA  . ILE C  1 330 ? 54.858  -10.639 72.850  1.00 9.32   ? 417  ILE C CA  1 
ATOM   8535  C  C   . ILE C  1 330 ? 53.561  -11.438 72.981  1.00 9.22   ? 417  ILE C C   1 
ATOM   8536  O  O   . ILE C  1 330 ? 53.189  -11.875 74.078  1.00 9.78   ? 417  ILE C O   1 
ATOM   8537  C  CB  . ILE C  1 330 ? 56.093  -11.598 72.688  1.00 9.45   ? 417  ILE C CB  1 
ATOM   8538  C  CG1 . ILE C  1 330 ? 57.393  -10.799 72.428  1.00 9.92   ? 417  ILE C CG1 1 
ATOM   8539  C  CG2 . ILE C  1 330 ? 55.848  -12.619 71.552  1.00 10.55  ? 417  ILE C CG2 1 
ATOM   8540  C  CD1 . ILE C  1 330 ? 58.659  -11.635 72.261  1.00 9.11   ? 417  ILE C CD1 1 
ATOM   8541  N  N   . ASP C  1 331 ? 52.868  -11.630 71.859  1.00 9.89   ? 418  ASP C N   1 
ATOM   8542  C  CA  . ASP C  1 331 ? 51.781  -12.594 71.831  1.00 9.73   ? 418  ASP C CA  1 
ATOM   8543  C  C   . ASP C  1 331 ? 52.385  -14.004 71.687  1.00 9.69   ? 418  ASP C C   1 
ATOM   8544  O  O   . ASP C  1 331 ? 52.519  -14.532 70.581  1.00 9.13   ? 418  ASP C O   1 
ATOM   8545  C  CB  . ASP C  1 331 ? 50.751  -12.310 70.729  1.00 9.09   ? 418  ASP C CB  1 
ATOM   8546  C  CG  . ASP C  1 331 ? 49.615  -13.350 70.715  1.00 11.07  ? 418  ASP C CG  1 
ATOM   8547  O  OD1 . ASP C  1 331 ? 49.530  -14.192 71.649  1.00 10.07  ? 418  ASP C OD1 1 
ATOM   8548  O  OD2 . ASP C  1 331 ? 48.795  -13.328 69.774  1.00 12.84  ? 418  ASP C OD2 1 
ATOM   8549  N  N   . TYR C  1 332 ? 52.749  -14.599 72.824  1.00 10.33  ? 419  TYR C N   1 
ATOM   8550  C  CA  . TYR C  1 332 ? 53.381  -15.924 72.824  1.00 10.81  ? 419  TYR C CA  1 
ATOM   8551  C  C   . TYR C  1 332 ? 52.493  -17.045 72.282  1.00 10.90  ? 419  TYR C C   1 
ATOM   8552  O  O   . TYR C  1 332 ? 52.976  -18.149 72.022  1.00 11.49  ? 419  TYR C O   1 
ATOM   8553  C  CB  . TYR C  1 332 ? 53.923  -16.280 74.215  1.00 10.72  ? 419  TYR C CB  1 
ATOM   8554  C  CG  . TYR C  1 332 ? 55.029  -15.337 74.646  1.00 10.84  ? 419  TYR C CG  1 
ATOM   8555  C  CD1 . TYR C  1 332 ? 56.328  -15.469 74.137  1.00 11.50  ? 419  TYR C CD1 1 
ATOM   8556  C  CD2 . TYR C  1 332 ? 54.768  -14.291 75.534  1.00 10.32  ? 419  TYR C CD2 1 
ATOM   8557  C  CE1 . TYR C  1 332 ? 57.332  -14.591 74.511  1.00 10.51  ? 419  TYR C CE1 1 
ATOM   8558  C  CE2 . TYR C  1 332 ? 55.763  -13.402 75.919  1.00 8.35   ? 419  TYR C CE2 1 
ATOM   8559  C  CZ  . TYR C  1 332 ? 57.041  -13.552 75.413  1.00 12.47  ? 419  TYR C CZ  1 
ATOM   8560  O  OH  . TYR C  1 332 ? 58.029  -12.655 75.798  1.00 10.64  ? 419  TYR C OH  1 
ATOM   8561  N  N   . TRP C  1 333 ? 51.205  -16.761 72.102  1.00 11.16  ? 420  TRP C N   1 
ATOM   8562  C  CA  . TRP C  1 333 ? 50.247  -17.795 71.698  1.00 11.94  ? 420  TRP C CA  1 
ATOM   8563  C  C   . TRP C  1 333 ? 49.788  -17.625 70.243  1.00 12.97  ? 420  TRP C C   1 
ATOM   8564  O  O   . TRP C  1 333 ? 48.829  -18.269 69.793  1.00 12.88  ? 420  TRP C O   1 
ATOM   8565  C  CB  . TRP C  1 333 ? 49.068  -17.823 72.670  1.00 10.98  ? 420  TRP C CB  1 
ATOM   8566  C  CG  . TRP C  1 333 ? 49.531  -18.150 74.056  1.00 11.82  ? 420  TRP C CG  1 
ATOM   8567  C  CD1 . TRP C  1 333 ? 49.607  -19.397 74.627  1.00 11.09  ? 420  TRP C CD1 1 
ATOM   8568  C  CD2 . TRP C  1 333 ? 50.029  -17.224 75.040  1.00 10.77  ? 420  TRP C CD2 1 
ATOM   8569  N  NE1 . TRP C  1 333 ? 50.096  -19.293 75.911  1.00 11.65  ? 420  TRP C NE1 1 
ATOM   8570  C  CE2 . TRP C  1 333 ? 50.376  -17.976 76.185  1.00 10.61  ? 420  TRP C CE2 1 
ATOM   8571  C  CE3 . TRP C  1 333 ? 50.216  -15.827 75.061  1.00 10.13  ? 420  TRP C CE3 1 
ATOM   8572  C  CZ2 . TRP C  1 333 ? 50.888  -17.377 77.358  1.00 10.39  ? 420  TRP C CZ2 1 
ATOM   8573  C  CZ3 . TRP C  1 333 ? 50.747  -15.232 76.224  1.00 10.23  ? 420  TRP C CZ3 1 
ATOM   8574  C  CH2 . TRP C  1 333 ? 51.071  -16.009 77.351  1.00 9.96   ? 420  TRP C CH2 1 
ATOM   8575  N  N   . ALA C  1 334 ? 50.493  -16.762 69.512  1.00 13.62  ? 421  ALA C N   1 
ATOM   8576  C  CA  . ALA C  1 334 ? 50.237  -16.578 68.079  1.00 14.51  ? 421  ALA C CA  1 
ATOM   8577  C  C   . ALA C  1 334 ? 50.513  -17.869 67.306  1.00 14.82  ? 421  ALA C C   1 
ATOM   8578  O  O   . ALA C  1 334 ? 51.327  -18.692 67.740  1.00 13.68  ? 421  ALA C O   1 
ATOM   8579  C  CB  . ALA C  1 334 ? 51.068  -15.405 67.518  1.00 14.28  ? 421  ALA C CB  1 
ATOM   8580  N  N   . ASN C  1 335 ? 49.803  -18.030 66.182  1.00 15.99  ? 422  ASN C N   1 
ATOM   8581  C  CA  . ASN C  1 335 ? 49.943  -19.167 65.262  1.00 18.06  ? 422  ASN C CA  1 
ATOM   8582  C  C   . ASN C  1 335 ? 51.077  -18.877 64.277  1.00 19.07  ? 422  ASN C C   1 
ATOM   8583  O  O   . ASN C  1 335 ? 50.843  -18.607 63.090  1.00 20.15  ? 422  ASN C O   1 
ATOM   8584  C  CB  . ASN C  1 335 ? 48.602  -19.397 64.540  1.00 18.41  ? 422  ASN C CB  1 
ATOM   8585  C  CG  . ASN C  1 335 ? 48.583  -20.663 63.688  1.00 20.51  ? 422  ASN C CG  1 
ATOM   8586  O  OD1 . ASN C  1 335 ? 47.791  -20.769 62.741  1.00 23.53  ? 422  ASN C OD1 1 
ATOM   8587  N  ND2 . ASN C  1 335 ? 49.445  -21.626 64.015  1.00 21.13  ? 422  ASN C ND2 1 
ATOM   8588  N  N   . LYS C  1 336 ? 52.299  -18.884 64.805  1.00 19.63  ? 423  LYS C N   1 
ATOM   8589  C  CA  . LYS C  1 336 ? 53.523  -18.496 64.094  1.00 20.84  ? 423  LYS C CA  1 
ATOM   8590  C  C   . LYS C  1 336 ? 54.694  -19.339 64.610  1.00 19.73  ? 423  LYS C C   1 
ATOM   8591  O  O   . LYS C  1 336 ? 54.713  -19.705 65.781  1.00 19.05  ? 423  LYS C O   1 
ATOM   8592  C  CB  . LYS C  1 336 ? 53.827  -17.012 64.336  1.00 20.48  ? 423  LYS C CB  1 
ATOM   8593  C  CG  . LYS C  1 336 ? 53.813  -16.137 63.095  1.00 23.25  ? 423  LYS C CG  1 
ATOM   8594  C  CD  . LYS C  1 336 ? 53.874  -14.635 63.417  1.00 23.79  ? 423  LYS C CD  1 
ATOM   8595  C  CE  . LYS C  1 336 ? 52.477  -13.999 63.276  1.00 28.47  ? 423  LYS C CE  1 
ATOM   8596  N  NZ  . LYS C  1 336 ? 52.467  -12.520 63.492  1.00 32.79  ? 423  LYS C NZ  1 
ATOM   8597  N  N   . GLU C  1 337 ? 55.678  -19.627 63.748  1.00 18.91  ? 424  GLU C N   1 
ATOM   8598  C  CA  . GLU C  1 337 ? 56.839  -20.419 64.163  1.00 18.97  ? 424  GLU C CA  1 
ATOM   8599  C  C   . GLU C  1 337 ? 57.878  -19.630 64.948  1.00 17.50  ? 424  GLU C C   1 
ATOM   8600  O  O   . GLU C  1 337 ? 58.819  -20.204 65.485  1.00 16.74  ? 424  GLU C O   1 
ATOM   8601  C  CB  . GLU C  1 337 ? 57.514  -21.110 62.966  1.00 20.11  ? 424  GLU C CB  1 
ATOM   8602  C  CG  . GLU C  1 337 ? 56.815  -22.397 62.485  1.00 24.29  ? 424  GLU C CG  1 
ATOM   8603  C  CD  . GLU C  1 337 ? 56.094  -23.182 63.595  1.00 30.87  ? 424  GLU C CD  1 
ATOM   8604  O  OE1 . GLU C  1 337 ? 54.912  -23.536 63.374  1.00 34.74  ? 424  GLU C OE1 1 
ATOM   8605  O  OE2 . GLU C  1 337 ? 56.678  -23.450 64.679  1.00 34.21  ? 424  GLU C OE2 1 
ATOM   8606  N  N   . CYS C  1 338 ? 57.703  -18.312 65.013  1.00 15.95  ? 425  CYS C N   1 
ATOM   8607  C  CA  . CYS C  1 338 ? 58.608  -17.459 65.790  1.00 13.82  ? 425  CYS C CA  1 
ATOM   8608  C  C   . CYS C  1 338 ? 57.785  -16.543 66.692  1.00 12.96  ? 425  CYS C C   1 
ATOM   8609  O  O   . CYS C  1 338 ? 56.601  -16.336 66.439  1.00 12.06  ? 425  CYS C O   1 
ATOM   8610  C  CB  . CYS C  1 338 ? 59.507  -16.638 64.854  1.00 14.12  ? 425  CYS C CB  1 
ATOM   8611  S  SG  . CYS C  1 338 ? 58.583  -15.701 63.592  1.00 15.65  ? 425  CYS C SG  1 
ATOM   8612  N  N   . PHE C  1 339 ? 58.424  -16.022 67.741  1.00 12.01  ? 426  PHE C N   1 
ATOM   8613  C  CA  . PHE C  1 339 ? 57.800  -15.070 68.655  1.00 11.62  ? 426  PHE C CA  1 
ATOM   8614  C  C   . PHE C  1 339 ? 58.047  -13.670 68.072  1.00 10.90  ? 426  PHE C C   1 
ATOM   8615  O  O   . PHE C  1 339 ? 59.201  -13.272 67.896  1.00 10.63  ? 426  PHE C O   1 
ATOM   8616  C  CB  . PHE C  1 339 ? 58.475  -15.155 70.032  1.00 11.32  ? 426  PHE C CB  1 
ATOM   8617  C  CG  . PHE C  1 339 ? 58.161  -16.408 70.818  1.00 11.92  ? 426  PHE C CG  1 
ATOM   8618  C  CD1 . PHE C  1 339 ? 56.911  -17.047 70.721  1.00 10.68  ? 426  PHE C CD1 1 
ATOM   8619  C  CD2 . PHE C  1 339 ? 59.109  -16.913 71.720  1.00 12.42  ? 426  PHE C CD2 1 
ATOM   8620  C  CE1 . PHE C  1 339 ? 56.618  -18.200 71.488  1.00 11.04  ? 426  PHE C CE1 1 
ATOM   8621  C  CE2 . PHE C  1 339 ? 58.834  -18.071 72.477  1.00 11.96  ? 426  PHE C CE2 1 
ATOM   8622  C  CZ  . PHE C  1 339 ? 57.583  -18.706 72.370  1.00 11.65  ? 426  PHE C CZ  1 
ATOM   8623  N  N   . ASN C  1 340 ? 56.983  -12.934 67.759  1.00 10.75  ? 427  ASN C N   1 
ATOM   8624  C  CA  . ASN C  1 340 ? 57.129  -11.637 67.088  1.00 10.06  ? 427  ASN C CA  1 
ATOM   8625  C  C   . ASN C  1 340 ? 57.163  -10.478 68.091  1.00 9.59   ? 427  ASN C C   1 
ATOM   8626  O  O   . ASN C  1 340 ? 56.190  -10.279 68.827  1.00 8.51   ? 427  ASN C O   1 
ATOM   8627  C  CB  . ASN C  1 340 ? 56.001  -11.444 66.051  1.00 9.54   ? 427  ASN C CB  1 
ATOM   8628  C  CG  . ASN C  1 340 ? 56.204  -10.218 65.150  1.00 10.46  ? 427  ASN C CG  1 
ATOM   8629  O  OD1 . ASN C  1 340 ? 55.243  -9.504  64.838  1.00 10.17  ? 427  ASN C OD1 1 
ATOM   8630  N  ND2 . ASN C  1 340 ? 57.422  -10.006 64.697  1.00 8.52   ? 427  ASN C ND2 1 
ATOM   8631  N  N   . PRO C  1 341 ? 58.292  -9.729  68.151  1.00 9.80   ? 428  PRO C N   1 
ATOM   8632  C  CA  . PRO C  1 341 ? 58.379  -8.581  69.060  1.00 9.09   ? 428  PRO C CA  1 
ATOM   8633  C  C   . PRO C  1 341 ? 57.212  -7.587  68.930  1.00 9.07   ? 428  PRO C C   1 
ATOM   8634  O  O   . PRO C  1 341 ? 56.819  -7.227  67.811  1.00 9.03   ? 428  PRO C O   1 
ATOM   8635  C  CB  . PRO C  1 341 ? 59.688  -7.895  68.625  1.00 9.01   ? 428  PRO C CB  1 
ATOM   8636  C  CG  . PRO C  1 341 ? 60.524  -8.999  68.109  1.00 10.10  ? 428  PRO C CG  1 
ATOM   8637  C  CD  . PRO C  1 341 ? 59.560  -9.932  67.413  1.00 10.06  ? 428  PRO C CD  1 
ATOM   8638  N  N   . CYS C  1 342 ? 56.658  -7.163  70.069  1.00 8.74   ? 429  CYS C N   1 
ATOM   8639  C  CA  . CYS C  1 342 ? 55.754  -5.986  70.114  1.00 8.54   ? 429  CYS C CA  1 
ATOM   8640  C  C   . CYS C  1 342 ? 56.229  -5.010  71.177  1.00 8.01   ? 429  CYS C C   1 
ATOM   8641  O  O   . CYS C  1 342 ? 56.993  -5.379  72.068  1.00 8.32   ? 429  CYS C O   1 
ATOM   8642  C  CB  . CYS C  1 342 ? 54.299  -6.397  70.419  1.00 7.86   ? 429  CYS C CB  1 
ATOM   8643  S  SG  . CYS C  1 342 ? 53.589  -7.609  69.289  1.00 10.48  ? 429  CYS C SG  1 
ATOM   8644  N  N   . PHE C  1 343 ? 55.796  -3.756  71.074  1.00 7.82   ? 430  PHE C N   1 
ATOM   8645  C  CA  . PHE C  1 343 ? 56.063  -2.783  72.129  1.00 8.25   ? 430  PHE C CA  1 
ATOM   8646  C  C   . PHE C  1 343 ? 54.906  -1.793  72.247  1.00 8.58   ? 430  PHE C C   1 
ATOM   8647  O  O   . PHE C  1 343 ? 54.071  -1.701  71.344  1.00 8.39   ? 430  PHE C O   1 
ATOM   8648  C  CB  . PHE C  1 343 ? 57.399  -2.067  71.888  1.00 7.86   ? 430  PHE C CB  1 
ATOM   8649  C  CG  . PHE C  1 343 ? 57.386  -1.109  70.715  1.00 8.21   ? 430  PHE C CG  1 
ATOM   8650  C  CD1 . PHE C  1 343 ? 57.166  0.265   70.918  1.00 6.85   ? 430  PHE C CD1 1 
ATOM   8651  C  CD2 . PHE C  1 343 ? 57.587  -1.582  69.419  1.00 8.48   ? 430  PHE C CD2 1 
ATOM   8652  C  CE1 . PHE C  1 343 ? 57.166  1.144   69.825  1.00 7.69   ? 430  PHE C CE1 1 
ATOM   8653  C  CE2 . PHE C  1 343 ? 57.594  -0.714  68.341  1.00 9.32   ? 430  PHE C CE2 1 
ATOM   8654  C  CZ  . PHE C  1 343 ? 57.377  0.644   68.540  1.00 7.01   ? 430  PHE C CZ  1 
ATOM   8655  N  N   . TYR C  1 344 ? 54.845  -1.072  73.367  1.00 8.38   ? 431  TYR C N   1 
ATOM   8656  C  CA  . TYR C  1 344 ? 53.912  0.049   73.483  1.00 8.30   ? 431  TYR C CA  1 
ATOM   8657  C  C   . TYR C  1 344 ? 54.710  1.310   73.821  1.00 8.53   ? 431  TYR C C   1 
ATOM   8658  O  O   . TYR C  1 344 ? 55.847  1.246   74.345  1.00 8.52   ? 431  TYR C O   1 
ATOM   8659  C  CB  . TYR C  1 344 ? 52.825  -0.208  74.573  1.00 8.03   ? 431  TYR C CB  1 
ATOM   8660  C  CG  . TYR C  1 344 ? 53.469  -0.283  75.923  1.00 7.66   ? 431  TYR C CG  1 
ATOM   8661  C  CD1 . TYR C  1 344 ? 53.966  -1.496  76.403  1.00 8.57   ? 431  TYR C CD1 1 
ATOM   8662  C  CD2 . TYR C  1 344 ? 53.679  0.873   76.680  1.00 8.66   ? 431  TYR C CD2 1 
ATOM   8663  C  CE1 . TYR C  1 344 ? 54.634  -1.559  77.632  1.00 8.76   ? 431  TYR C CE1 1 
ATOM   8664  C  CE2 . TYR C  1 344 ? 54.349  0.826   77.875  1.00 8.50   ? 431  TYR C CE2 1 
ATOM   8665  C  CZ  . TYR C  1 344 ? 54.805  -0.396  78.363  1.00 8.40   ? 431  TYR C CZ  1 
ATOM   8666  O  OH  . TYR C  1 344 ? 55.481  -0.447  79.565  1.00 7.82   ? 431  TYR C OH  1 
ATOM   8667  N  N   . VAL C  1 345 ? 54.090  2.451   73.560  1.00 7.77   ? 432  VAL C N   1 
ATOM   8668  C  CA  . VAL C  1 345 ? 54.572  3.717   74.057  1.00 8.68   ? 432  VAL C CA  1 
ATOM   8669  C  C   . VAL C  1 345 ? 53.406  4.358   74.793  1.00 8.47   ? 432  VAL C C   1 
ATOM   8670  O  O   . VAL C  1 345 ? 52.278  4.400   74.259  1.00 8.88   ? 432  VAL C O   1 
ATOM   8671  C  CB  . VAL C  1 345 ? 54.993  4.680   72.904  1.00 8.41   ? 432  VAL C CB  1 
ATOM   8672  C  CG1 . VAL C  1 345 ? 55.604  5.964   73.490  1.00 9.22   ? 432  VAL C CG1 1 
ATOM   8673  C  CG2 . VAL C  1 345 ? 55.981  3.989   71.950  1.00 8.38   ? 432  VAL C CG2 1 
ATOM   8674  N  N   . GLU C  1 346 ? 53.683  4.810   76.020  1.00 7.01   ? 433  GLU C N   1 
ATOM   8675  C  CA  . GLU C  1 346 ? 52.776  5.604   76.830  1.00 7.78   ? 433  GLU C CA  1 
ATOM   8676  C  C   . GLU C  1 346 ? 52.829  7.043   76.331  1.00 7.50   ? 433  GLU C C   1 
ATOM   8677  O  O   . GLU C  1 346 ? 53.915  7.614   76.206  1.00 8.01   ? 433  GLU C O   1 
ATOM   8678  C  CB  . GLU C  1 346 ? 53.212  5.552   78.304  1.00 7.62   ? 433  GLU C CB  1 
ATOM   8679  C  CG  . GLU C  1 346 ? 52.420  6.462   79.236  1.00 7.32   ? 433  GLU C CG  1 
ATOM   8680  C  CD  . GLU C  1 346 ? 53.047  6.623   80.618  1.00 9.39   ? 433  GLU C CD  1 
ATOM   8681  O  OE1 . GLU C  1 346 ? 52.264  6.729   81.599  1.00 8.24   ? 433  GLU C OE1 1 
ATOM   8682  O  OE2 . GLU C  1 346 ? 54.297  6.627   80.736  1.00 9.41   ? 433  GLU C OE2 1 
ATOM   8683  N  N   . LEU C  1 347 ? 51.674  7.610   76.005  1.00 6.35   ? 434  LEU C N   1 
ATOM   8684  C  CA  . LEU C  1 347 ? 51.653  8.969   75.478  1.00 7.83   ? 434  LEU C CA  1 
ATOM   8685  C  C   . LEU C  1 347 ? 51.124  9.893   76.571  1.00 7.72   ? 434  LEU C C   1 
ATOM   8686  O  O   . LEU C  1 347 ? 49.906  10.024  76.771  1.00 7.27   ? 434  LEU C O   1 
ATOM   8687  C  CB  . LEU C  1 347 ? 50.828  9.058   74.184  1.00 8.01   ? 434  LEU C CB  1 
ATOM   8688  C  CG  . LEU C  1 347 ? 51.147  7.956   73.156  1.00 6.60   ? 434  LEU C CG  1 
ATOM   8689  C  CD1 . LEU C  1 347 ? 50.077  7.900   72.073  1.00 6.74   ? 434  LEU C CD1 1 
ATOM   8690  C  CD2 . LEU C  1 347 ? 52.508  8.203   72.521  1.00 5.75   ? 434  LEU C CD2 1 
ATOM   8691  N  N   . ILE C  1 348 ? 52.051  10.494  77.306  1.00 7.72   ? 435  ILE C N   1 
ATOM   8692  C  CA  . ILE C  1 348 ? 51.688  11.289  78.492  1.00 8.44   ? 435  ILE C CA  1 
ATOM   8693  C  C   . ILE C  1 348 ? 51.162  12.680  78.141  1.00 8.59   ? 435  ILE C C   1 
ATOM   8694  O  O   . ILE C  1 348 ? 51.800  13.425  77.390  1.00 8.57   ? 435  ILE C O   1 
ATOM   8695  C  CB  . ILE C  1 348 ? 52.871  11.427  79.522  1.00 8.42   ? 435  ILE C CB  1 
ATOM   8696  C  CG1 . ILE C  1 348 ? 53.379  10.044  79.967  1.00 9.01   ? 435  ILE C CG1 1 
ATOM   8697  C  CG2 . ILE C  1 348 ? 52.435  12.282  80.763  1.00 8.03   ? 435  ILE C CG2 1 
ATOM   8698  C  CD1 . ILE C  1 348 ? 54.670  10.119  80.817  1.00 9.78   ? 435  ILE C CD1 1 
ATOM   8699  N  N   . ARG C  1 349 ? 50.010  13.030  78.726  1.00 8.50   ? 436  ARG C N   1 
ATOM   8700  C  CA  . ARG C  1 349 ? 49.401  14.343  78.539  1.00 8.86   ? 436  ARG C CA  1 
ATOM   8701  C  C   . ARG C  1 349 ? 49.181  14.999  79.901  1.00 9.82   ? 436  ARG C C   1 
ATOM   8702  O  O   . ARG C  1 349 ? 49.009  14.287  80.900  1.00 9.78   ? 436  ARG C O   1 
ATOM   8703  C  CB  . ARG C  1 349 ? 48.065  14.226  77.795  1.00 8.24   ? 436  ARG C CB  1 
ATOM   8704  C  CG  . ARG C  1 349 ? 48.139  13.596  76.380  1.00 8.92   ? 436  ARG C CG  1 
ATOM   8705  C  CD  . ARG C  1 349 ? 49.169  14.273  75.413  1.00 8.50   ? 436  ARG C CD  1 
ATOM   8706  N  NE  . ARG C  1 349 ? 48.925  15.712  75.272  1.00 10.41  ? 436  ARG C NE  1 
ATOM   8707  C  CZ  . ARG C  1 349 ? 48.149  16.249  74.330  1.00 10.18  ? 436  ARG C CZ  1 
ATOM   8708  N  NH1 . ARG C  1 349 ? 47.524  15.466  73.437  1.00 9.49   ? 436  ARG C NH1 1 
ATOM   8709  N  NH2 . ARG C  1 349 ? 47.989  17.578  74.292  1.00 10.53  ? 436  ARG C NH2 1 
ATOM   8710  N  N   . GLY C  1 350 ? 49.178  16.337  79.928  1.00 9.61   ? 437  GLY C N   1 
ATOM   8711  C  CA  . GLY C  1 350 ? 49.019  17.097  81.169  1.00 10.70  ? 437  GLY C CA  1 
ATOM   8712  C  C   . GLY C  1 350 ? 50.359  17.325  81.850  1.00 10.96  ? 437  GLY C C   1 
ATOM   8713  O  O   . GLY C  1 350 ? 51.392  17.451  81.179  1.00 10.72  ? 437  GLY C O   1 
ATOM   8714  N  N   . ARG C  1 351 ? 50.357  17.318  83.179  1.00 11.80  ? 438  ARG C N   1 
ATOM   8715  C  CA  . ARG C  1 351 ? 51.531  17.769  83.964  1.00 11.87  ? 438  ARG C CA  1 
ATOM   8716  C  C   . ARG C  1 351 ? 52.680  16.750  83.968  1.00 12.08  ? 438  ARG C C   1 
ATOM   8717  O  O   . ARG C  1 351 ? 52.433  15.558  83.906  1.00 11.55  ? 438  ARG C O   1 
ATOM   8718  C  CB  . ARG C  1 351 ? 51.113  18.110  85.404  1.00 11.90  ? 438  ARG C CB  1 
ATOM   8719  C  CG  . ARG C  1 351 ? 49.984  19.126  85.484  1.00 15.72  ? 438  ARG C CG  1 
ATOM   8720  C  CD  . ARG C  1 351 ? 50.009  19.959  86.768  1.00 20.42  ? 438  ARG C CD  1 
ATOM   8721  N  NE  . ARG C  1 351 ? 49.345  21.239  86.539  1.00 25.64  ? 438  ARG C NE  1 
ATOM   8722  C  CZ  . ARG C  1 351 ? 49.631  22.365  87.177  1.00 27.84  ? 438  ARG C CZ  1 
ATOM   8723  N  NH1 . ARG C  1 351 ? 50.594  22.387  88.096  1.00 30.28  ? 438  ARG C NH1 1 
ATOM   8724  N  NH2 . ARG C  1 351 ? 48.950  23.470  86.894  1.00 28.06  ? 438  ARG C NH2 1 
ATOM   8725  N  N   . PRO C  1 352 ? 53.944  17.216  84.072  1.00 11.96  ? 439  PRO C N   1 
ATOM   8726  C  CA  . PRO C  1 352 ? 54.409  18.607  84.198  1.00 12.74  ? 439  PRO C CA  1 
ATOM   8727  C  C   . PRO C  1 352 ? 54.570  19.374  82.877  1.00 13.69  ? 439  PRO C C   1 
ATOM   8728  O  O   . PRO C  1 352 ? 54.657  20.614  82.899  1.00 14.28  ? 439  PRO C O   1 
ATOM   8729  C  CB  . PRO C  1 352 ? 55.785  18.442  84.860  1.00 12.65  ? 439  PRO C CB  1 
ATOM   8730  C  CG  . PRO C  1 352 ? 56.317  17.130  84.278  1.00 10.63  ? 439  PRO C CG  1 
ATOM   8731  C  CD  . PRO C  1 352 ? 55.066  16.252  84.124  1.00 12.67  ? 439  PRO C CD  1 
ATOM   8732  N  N   . LYS C  1 353 ? 54.599  18.672  81.747  1.00 13.25  ? 440  LYS C N   1 
ATOM   8733  C  CA  . LYS C  1 353 ? 54.958  19.318  80.468  1.00 13.95  ? 440  LYS C CA  1 
ATOM   8734  C  C   . LYS C  1 353 ? 53.874  20.260  79.925  1.00 14.13  ? 440  LYS C C   1 
ATOM   8735  O  O   . LYS C  1 353 ? 54.176  21.199  79.185  1.00 14.78  ? 440  LYS C O   1 
ATOM   8736  C  CB  . LYS C  1 353 ? 55.369  18.271  79.419  1.00 14.00  ? 440  LYS C CB  1 
ATOM   8737  C  CG  . LYS C  1 353 ? 56.695  17.525  79.749  1.00 15.30  ? 440  LYS C CG  1 
ATOM   8738  C  CD  . LYS C  1 353 ? 57.903  18.468  79.576  1.00 16.73  ? 440  LYS C CD  1 
ATOM   8739  C  CE  . LYS C  1 353 ? 59.250  17.778  79.785  1.00 16.52  ? 440  LYS C CE  1 
ATOM   8740  N  NZ  . LYS C  1 353 ? 59.485  17.498  81.238  1.00 18.30  ? 440  LYS C NZ  1 
ATOM   8741  N  N   . GLU C  1 354 ? 52.623  19.990  80.301  1.00 13.69  ? 441  GLU C N   1 
ATOM   8742  C  CA  . GLU C  1 354 ? 51.459  20.775  79.889  1.00 13.84  ? 441  GLU C CA  1 
ATOM   8743  C  C   . GLU C  1 354 ? 50.753  21.221  81.156  1.00 14.94  ? 441  GLU C C   1 
ATOM   8744  O  O   . GLU C  1 354 ? 49.854  20.534  81.681  1.00 15.46  ? 441  GLU C O   1 
ATOM   8745  C  CB  . GLU C  1 354 ? 50.526  19.951  78.981  1.00 13.46  ? 441  GLU C CB  1 
ATOM   8746  C  CG  . GLU C  1 354 ? 51.190  19.484  77.669  1.00 13.29  ? 441  GLU C CG  1 
ATOM   8747  C  CD  . GLU C  1 354 ? 50.321  18.535  76.848  1.00 13.28  ? 441  GLU C CD  1 
ATOM   8748  O  OE1 . GLU C  1 354 ? 50.012  18.859  75.684  1.00 12.27  ? 441  GLU C OE1 1 
ATOM   8749  O  OE2 . GLU C  1 354 ? 49.968  17.454  77.356  1.00 12.02  ? 441  GLU C OE2 1 
ATOM   8750  N  N   . SER C  1 355 ? 51.162  22.373  81.676  1.00 15.35  ? 442  SER C N   1 
ATOM   8751  C  CA  . SER C  1 355 ? 50.657  22.805  82.992  1.00 16.03  ? 442  SER C CA  1 
ATOM   8752  C  C   . SER C  1 355 ? 49.382  23.668  82.927  1.00 15.75  ? 442  SER C C   1 
ATOM   8753  O  O   . SER C  1 355 ? 48.931  24.193  83.943  1.00 15.36  ? 442  SER C O   1 
ATOM   8754  C  CB  . SER C  1 355 ? 51.768  23.507  83.767  1.00 17.25  ? 442  SER C CB  1 
ATOM   8755  O  OG  . SER C  1 355 ? 52.258  24.579  82.996  1.00 19.10  ? 442  SER C OG  1 
ATOM   8756  N  N   . SER C  1 356 ? 48.770  23.777  81.748  1.00 14.85  ? 443  SER C N   1 
ATOM   8757  C  CA  . SER C  1 356 ? 47.482  24.475  81.652  1.00 14.78  ? 443  SER C CA  1 
ATOM   8758  C  C   . SER C  1 356 ? 46.311  23.628  82.181  1.00 14.61  ? 443  SER C C   1 
ATOM   8759  O  O   . SER C  1 356 ? 45.196  24.132  82.326  1.00 14.99  ? 443  SER C O   1 
ATOM   8760  C  CB  . SER C  1 356 ? 47.201  24.942  80.228  1.00 15.02  ? 443  SER C CB  1 
ATOM   8761  O  OG  . SER C  1 356 ? 46.976  23.838  79.384  1.00 15.85  ? 443  SER C OG  1 
ATOM   8762  N  N   . VAL C  1 357 ? 46.573  22.346  82.453  1.00 13.26  ? 444  VAL C N   1 
ATOM   8763  C  CA  . VAL C  1 357 ? 45.604  21.468  83.124  1.00 12.33  ? 444  VAL C CA  1 
ATOM   8764  C  C   . VAL C  1 357 ? 46.148  21.034  84.486  1.00 12.05  ? 444  VAL C C   1 
ATOM   8765  O  O   . VAL C  1 357 ? 47.364  21.120  84.733  1.00 12.69  ? 444  VAL C O   1 
ATOM   8766  C  CB  . VAL C  1 357 ? 45.247  20.222  82.263  1.00 11.73  ? 444  VAL C CB  1 
ATOM   8767  C  CG1 . VAL C  1 357 ? 44.596  20.649  80.928  1.00 11.98  ? 444  VAL C CG1 1 
ATOM   8768  C  CG2 . VAL C  1 357 ? 46.485  19.357  81.991  1.00 10.94  ? 444  VAL C CG2 1 
ATOM   8769  N  N   . LEU C  1 358 ? 45.258  20.552  85.355  1.00 11.73  ? 445  LEU C N   1 
ATOM   8770  C  CA  . LEU C  1 358 ? 45.612  20.184  86.732  1.00 12.46  ? 445  LEU C CA  1 
ATOM   8771  C  C   . LEU C  1 358 ? 46.005  18.691  86.894  1.00 11.70  ? 445  LEU C C   1 
ATOM   8772  O  O   . LEU C  1 358 ? 46.386  18.257  87.992  1.00 12.19  ? 445  LEU C O   1 
ATOM   8773  C  CB  . LEU C  1 358 ? 44.418  20.481  87.644  1.00 11.86  ? 445  LEU C CB  1 
ATOM   8774  C  CG  . LEU C  1 358 ? 44.189  21.802  88.396  1.00 15.69  ? 445  LEU C CG  1 
ATOM   8775  C  CD1 . LEU C  1 358 ? 45.211  22.927  88.137  1.00 15.41  ? 445  LEU C CD1 1 
ATOM   8776  C  CD2 . LEU C  1 358 ? 42.749  22.261  88.281  1.00 17.03  ? 445  LEU C CD2 1 
ATOM   8777  N  N   . TRP C  1 359 ? 45.886  17.933  85.801  1.00 11.29  ? 446  TRP C N   1 
ATOM   8778  C  CA  . TRP C  1 359 ? 45.988  16.471  85.814  1.00 9.89   ? 446  TRP C CA  1 
ATOM   8779  C  C   . TRP C  1 359 ? 47.160  15.927  84.981  1.00 9.92   ? 446  TRP C C   1 
ATOM   8780  O  O   . TRP C  1 359 ? 47.761  16.643  84.189  1.00 9.42   ? 446  TRP C O   1 
ATOM   8781  C  CB  . TRP C  1 359 ? 44.664  15.835  85.329  1.00 9.63   ? 446  TRP C CB  1 
ATOM   8782  C  CG  . TRP C  1 359 ? 44.136  16.338  83.998  1.00 9.53   ? 446  TRP C CG  1 
ATOM   8783  C  CD1 . TRP C  1 359 ? 43.125  17.252  83.822  1.00 9.36   ? 446  TRP C CD1 1 
ATOM   8784  C  CD2 . TRP C  1 359 ? 44.581  15.979  82.670  1.00 9.74   ? 446  TRP C CD2 1 
ATOM   8785  N  NE1 . TRP C  1 359 ? 42.916  17.474  82.485  1.00 11.15  ? 446  TRP C NE1 1 
ATOM   8786  C  CE2 . TRP C  1 359 ? 43.782  16.706  81.754  1.00 9.86   ? 446  TRP C CE2 1 
ATOM   8787  C  CE3 . TRP C  1 359 ? 45.572  15.112  82.168  1.00 7.36   ? 446  TRP C CE3 1 
ATOM   8788  C  CZ2 . TRP C  1 359 ? 43.943  16.609  80.362  1.00 9.25   ? 446  TRP C CZ2 1 
ATOM   8789  C  CZ3 . TRP C  1 359 ? 45.734  15.011  80.779  1.00 9.26   ? 446  TRP C CZ3 1 
ATOM   8790  C  CH2 . TRP C  1 359 ? 44.916  15.756  79.893  1.00 9.46   ? 446  TRP C CH2 1 
ATOM   8791  N  N   . THR C  1 360 ? 47.452  14.640  85.171  1.00 9.39   ? 447  THR C N   1 
ATOM   8792  C  CA  . THR C  1 360 ? 48.422  13.905  84.356  1.00 9.25   ? 447  THR C CA  1 
ATOM   8793  C  C   . THR C  1 360 ? 47.757  12.594  84.017  1.00 9.50   ? 447  THR C C   1 
ATOM   8794  O  O   . THR C  1 360 ? 47.251  11.903  84.908  1.00 8.54   ? 447  THR C O   1 
ATOM   8795  C  CB  . THR C  1 360 ? 49.736  13.580  85.124  1.00 9.31   ? 447  THR C CB  1 
ATOM   8796  O  OG1 . THR C  1 360 ? 50.405  14.789  85.472  1.00 10.57  ? 447  THR C OG1 1 
ATOM   8797  C  CG2 . THR C  1 360 ? 50.685  12.696  84.275  1.00 9.01   ? 447  THR C CG2 1 
ATOM   8798  N  N   . SER C  1 361 ? 47.739  12.269  82.729  1.00 9.67   ? 448  SER C N   1 
ATOM   8799  C  CA  . SER C  1 361 ? 47.254  10.979  82.308  1.00 9.51   ? 448  SER C CA  1 
ATOM   8800  C  C   . SER C  1 361 ? 48.002  10.556  81.057  1.00 9.35   ? 448  SER C C   1 
ATOM   8801  O  O   . SER C  1 361 ? 49.081  11.098  80.764  1.00 8.20   ? 448  SER C O   1 
ATOM   8802  C  CB  . SER C  1 361 ? 45.730  11.026  82.106  1.00 10.01  ? 448  SER C CB  1 
ATOM   8803  O  OG  . SER C  1 361 ? 45.210  9.700   82.077  1.00 8.25   ? 448  SER C OG  1 
ATOM   8804  N  N   . ASN C  1 362 ? 47.475  9.556   80.348  1.00 8.29   ? 449  ASN C N   1 
ATOM   8805  C  CA  . ASN C  1 362 ? 48.134  9.061   79.158  1.00 8.44   ? 449  ASN C CA  1 
ATOM   8806  C  C   . ASN C  1 362 ? 47.129  8.359   78.247  1.00 7.87   ? 449  ASN C C   1 
ATOM   8807  O  O   . ASN C  1 362 ? 46.005  8.024   78.664  1.00 8.56   ? 449  ASN C O   1 
ATOM   8808  C  CB  . ASN C  1 362 ? 49.262  8.067   79.502  1.00 8.09   ? 449  ASN C CB  1 
ATOM   8809  C  CG  . ASN C  1 362 ? 48.722  6.721   79.964  1.00 8.88   ? 449  ASN C CG  1 
ATOM   8810  O  OD1 . ASN C  1 362 ? 48.688  5.739   79.195  1.00 9.68   ? 449  ASN C OD1 1 
ATOM   8811  N  ND2 . ASN C  1 362 ? 48.218  6.691   81.181  1.00 5.30   ? 449  ASN C ND2 1 
ATOM   8812  N  N   . SER C  1 363 ? 47.537  8.172   76.999  1.00 8.02   ? 450  SER C N   1 
ATOM   8813  C  CA  . SER C  1 363 ? 46.932  7.144   76.167  1.00 7.43   ? 450  SER C CA  1 
ATOM   8814  C  C   . SER C  1 363 ? 48.007  6.119   75.760  1.00 8.71   ? 450  SER C C   1 
ATOM   8815  O  O   . SER C  1 363 ? 49.186  6.202   76.180  1.00 7.57   ? 450  SER C O   1 
ATOM   8816  C  CB  . SER C  1 363 ? 46.201  7.764   74.968  1.00 8.46   ? 450  SER C CB  1 
ATOM   8817  O  OG  . SER C  1 363 ? 47.117  8.248   73.996  1.00 7.21   ? 450  SER C OG  1 
ATOM   8818  N  N   . ILE C  1 364 ? 47.606  5.146   74.948  1.00 8.19   ? 451  ILE C N   1 
ATOM   8819  C  CA  . ILE C  1 364 ? 48.492  4.038   74.603  1.00 8.34   ? 451  ILE C CA  1 
ATOM   8820  C  C   . ILE C  1 364 ? 48.552  3.873   73.080  1.00 8.60   ? 451  ILE C C   1 
ATOM   8821  O  O   . ILE C  1 364 ? 47.535  3.988   72.412  1.00 8.94   ? 451  ILE C O   1 
ATOM   8822  C  CB  . ILE C  1 364 ? 48.032  2.697   75.248  1.00 8.19   ? 451  ILE C CB  1 
ATOM   8823  C  CG1 . ILE C  1 364 ? 48.007  2.797   76.793  1.00 9.12   ? 451  ILE C CG1 1 
ATOM   8824  C  CG2 . ILE C  1 364 ? 48.975  1.562   74.847  1.00 8.80   ? 451  ILE C CG2 1 
ATOM   8825  C  CD1 . ILE C  1 364 ? 47.300  1.608   77.486  1.00 8.44   ? 451  ILE C CD1 1 
ATOM   8826  N  N   . VAL C  1 365 ? 49.744  3.613   72.550  1.00 8.01   ? 452  VAL C N   1 
ATOM   8827  C  CA  . VAL C  1 365 ? 49.878  3.062   71.210  1.00 8.20   ? 452  VAL C CA  1 
ATOM   8828  C  C   . VAL C  1 365 ? 50.766  1.817   71.275  1.00 8.23   ? 452  VAL C C   1 
ATOM   8829  O  O   . VAL C  1 365 ? 51.711  1.767   72.068  1.00 9.02   ? 452  VAL C O   1 
ATOM   8830  C  CB  . VAL C  1 365 ? 50.429  4.096   70.172  1.00 7.01   ? 452  VAL C CB  1 
ATOM   8831  C  CG1 . VAL C  1 365 ? 51.867  4.501   70.498  1.00 7.26   ? 452  VAL C CG1 1 
ATOM   8832  C  CG2 . VAL C  1 365 ? 50.371  3.498   68.770  1.00 7.66   ? 452  VAL C CG2 1 
ATOM   8833  N  N   . ALA C  1 366 ? 50.450  0.824   70.452  1.00 8.55   ? 453  ALA C N   1 
ATOM   8834  C  CA  . ALA C  1 366 ? 51.194  -0.443  70.425  1.00 8.28   ? 453  ALA C CA  1 
ATOM   8835  C  C   . ALA C  1 366 ? 51.462  -0.887  68.984  1.00 8.55   ? 453  ALA C C   1 
ATOM   8836  O  O   . ALA C  1 366 ? 50.591  -0.727  68.109  1.00 7.92   ? 453  ALA C O   1 
ATOM   8837  C  CB  . ALA C  1 366 ? 50.433  -1.514  71.191  1.00 8.36   ? 453  ALA C CB  1 
ATOM   8838  N  N   . LEU C  1 367 ? 52.666  -1.436  68.747  1.00 8.24   ? 454  LEU C N   1 
ATOM   8839  C  CA  . LEU C  1 367 ? 53.084  -1.882  67.420  1.00 8.10   ? 454  LEU C CA  1 
ATOM   8840  C  C   . LEU C  1 367 ? 53.808  -3.231  67.526  1.00 8.26   ? 454  LEU C C   1 
ATOM   8841  O  O   . LEU C  1 367 ? 54.324  -3.570  68.589  1.00 8.90   ? 454  LEU C O   1 
ATOM   8842  C  CB  . LEU C  1 367 ? 53.990  -0.831  66.724  1.00 7.92   ? 454  LEU C CB  1 
ATOM   8843  C  CG  . LEU C  1 367 ? 53.390  0.541   66.345  1.00 8.53   ? 454  LEU C CG  1 
ATOM   8844  C  CD1 . LEU C  1 367 ? 53.541  1.531   67.501  1.00 6.20   ? 454  LEU C CD1 1 
ATOM   8845  C  CD2 . LEU C  1 367 ? 54.014  1.111   65.067  1.00 8.33   ? 454  LEU C CD2 1 
ATOM   8846  N  N   . CYS C  1 368 ? 53.837  -3.998  66.441  1.00 8.02   ? 455  CYS C N   1 
ATOM   8847  C  CA  . CYS C  1 368 ? 54.581  -5.249  66.405  1.00 8.57   ? 455  CYS C CA  1 
ATOM   8848  C  C   . CYS C  1 368 ? 55.419  -5.334  65.137  1.00 8.99   ? 455  CYS C C   1 
ATOM   8849  O  O   . CYS C  1 368 ? 55.163  -4.631  64.166  1.00 8.64   ? 455  CYS C O   1 
ATOM   8850  C  CB  . CYS C  1 368 ? 53.639  -6.457  66.453  1.00 8.64   ? 455  CYS C CB  1 
ATOM   8851  S  SG  . CYS C  1 368 ? 52.541  -6.544  67.901  1.00 11.47  ? 455  CYS C SG  1 
ATOM   8852  N  N   . GLY C  1 369 ? 56.393  -6.242  65.151  1.00 10.67  ? 456  GLY C N   1 
ATOM   8853  C  CA  . GLY C  1 369 ? 57.306  -6.418  64.024  1.00 10.35  ? 456  GLY C CA  1 
ATOM   8854  C  C   . GLY C  1 369 ? 56.617  -6.813  62.728  1.00 11.53  ? 456  GLY C C   1 
ATOM   8855  O  O   . GLY C  1 369 ? 55.593  -7.505  62.735  1.00 11.98  ? 456  GLY C O   1 
ATOM   8856  N  N   . SER C  1 370 ? 57.184  -6.345  61.617  1.00 11.93  ? 457  SER C N   1 
ATOM   8857  C  CA  . SER C  1 370 ? 56.908  -6.900  60.301  1.00 12.59  ? 457  SER C CA  1 
ATOM   8858  C  C   . SER C  1 370 ? 58.227  -7.280  59.600  1.00 13.06  ? 457  SER C C   1 
ATOM   8859  O  O   . SER C  1 370 ? 59.271  -6.621  59.778  1.00 13.31  ? 457  SER C O   1 
ATOM   8860  C  CB  . SER C  1 370 ? 56.128  -5.894  59.433  1.00 12.68  ? 457  SER C CB  1 
ATOM   8861  O  OG  . SER C  1 370 ? 55.902  -6.417  58.120  1.00 12.53  ? 457  SER C OG  1 
ATOM   8862  N  N   . LYS C  1 371 ? 58.166  -8.316  58.780  1.00 13.03  ? 458  LYS C N   1 
ATOM   8863  C  CA  . LYS C  1 371 ? 59.287  -8.617  57.860  1.00 15.06  ? 458  LYS C CA  1 
ATOM   8864  C  C   . LYS C  1 371 ? 59.295  -7.753  56.611  1.00 15.30  ? 458  LYS C C   1 
ATOM   8865  O  O   . LYS C  1 371 ? 60.322  -7.649  55.924  1.00 15.83  ? 458  LYS C O   1 
ATOM   8866  C  CB  . LYS C  1 371 ? 59.270  -10.080 57.446  1.00 14.75  ? 458  LYS C CB  1 
ATOM   8867  C  CG  . LYS C  1 371 ? 59.611  -11.022 58.546  1.00 18.71  ? 458  LYS C CG  1 
ATOM   8868  C  CD  . LYS C  1 371 ? 59.701  -12.479 58.058  1.00 22.91  ? 458  LYS C CD  1 
ATOM   8869  C  CE  . LYS C  1 371 ? 61.010  -12.734 57.317  1.00 26.63  ? 458  LYS C CE  1 
ATOM   8870  N  NZ  . LYS C  1 371 ? 60.868  -12.970 55.839  1.00 30.04  ? 458  LYS C NZ  1 
ATOM   8871  N  N   . LYS C  1 372 ? 58.141  -7.171  56.294  1.00 15.75  ? 459  LYS C N   1 
ATOM   8872  C  CA  . LYS C  1 372 ? 57.994  -6.268  55.167  1.00 16.46  ? 459  LYS C CA  1 
ATOM   8873  C  C   . LYS C  1 372 ? 58.619  -4.921  55.516  1.00 16.64  ? 459  LYS C C   1 
ATOM   8874  O  O   . LYS C  1 372 ? 58.922  -4.659  56.691  1.00 16.23  ? 459  LYS C O   1 
ATOM   8875  C  CB  . LYS C  1 372 ? 56.506  -6.075  54.823  1.00 17.22  ? 459  LYS C CB  1 
ATOM   8876  C  CG  . LYS C  1 372 ? 55.678  -7.379  54.719  1.00 19.31  ? 459  LYS C CG  1 
ATOM   8877  C  CD  . LYS C  1 372 ? 55.952  -8.143  53.436  1.00 20.62  ? 459  LYS C CD  1 
ATOM   8878  C  CE  . LYS C  1 372 ? 55.195  -9.490  53.364  1.00 19.86  ? 459  LYS C CE  1 
ATOM   8879  N  NZ  . LYS C  1 372 ? 53.726  -9.319  53.141  1.00 22.14  ? 459  LYS C NZ  1 
ATOM   8880  N  N   . ARG C  1 373 ? 58.816  -4.088  54.495  1.00 16.57  ? 460  ARG C N   1 
ATOM   8881  C  CA  . ARG C  1 373 ? 59.205  -2.691  54.665  1.00 18.10  ? 460  ARG C CA  1 
ATOM   8882  C  C   . ARG C  1 373 ? 57.977  -1.810  54.547  1.00 17.67  ? 460  ARG C C   1 
ATOM   8883  O  O   . ARG C  1 373 ? 57.565  -1.431  53.449  1.00 18.22  ? 460  ARG C O   1 
ATOM   8884  C  CB  . ARG C  1 373 ? 60.257  -2.283  53.624  1.00 18.66  ? 460  ARG C CB  1 
ATOM   8885  C  CG  . ARG C  1 373 ? 61.394  -3.284  53.474  1.00 23.51  ? 460  ARG C CG  1 
ATOM   8886  C  CD  . ARG C  1 373 ? 62.235  -3.345  54.737  1.00 29.74  ? 460  ARG C CD  1 
ATOM   8887  N  NE  . ARG C  1 373 ? 63.442  -4.147  54.554  1.00 34.73  ? 460  ARG C NE  1 
ATOM   8888  C  CZ  . ARG C  1 373 ? 64.612  -3.868  55.126  1.00 37.96  ? 460  ARG C CZ  1 
ATOM   8889  N  NH1 . ARG C  1 373 ? 64.743  -2.798  55.914  1.00 39.84  ? 460  ARG C NH1 1 
ATOM   8890  N  NH2 . ARG C  1 373 ? 65.656  -4.659  54.909  1.00 38.94  ? 460  ARG C NH2 1 
ATOM   8891  N  N   . LEU C  1 374 ? 57.388  -1.491  55.694  1.00 16.51  ? 461  LEU C N   1 
ATOM   8892  C  CA  . LEU C  1 374 ? 56.148  -0.736  55.747  1.00 15.92  ? 461  LEU C CA  1 
ATOM   8893  C  C   . LEU C  1 374 ? 56.404  0.749   55.927  1.00 15.74  ? 461  LEU C C   1 
ATOM   8894  O  O   . LEU C  1 374 ? 57.358  1.164   56.615  1.00 16.54  ? 461  LEU C O   1 
ATOM   8895  C  CB  . LEU C  1 374 ? 55.266  -1.252  56.901  1.00 14.47  ? 461  LEU C CB  1 
ATOM   8896  C  CG  . LEU C  1 374 ? 54.914  -2.736  56.948  1.00 14.23  ? 461  LEU C CG  1 
ATOM   8897  C  CD1 . LEU C  1 374 ? 54.093  -2.995  58.191  1.00 13.20  ? 461  LEU C CD1 1 
ATOM   8898  C  CD2 . LEU C  1 374 ? 54.149  -3.195  55.665  1.00 12.99  ? 461  LEU C CD2 1 
ATOM   8899  N  N   . GLY C  1 375 ? 55.550  1.559   55.315  1.00 15.16  ? 462  GLY C N   1 
ATOM   8900  C  CA  . GLY C  1 375 ? 55.551  2.979   55.567  1.00 14.29  ? 462  GLY C CA  1 
ATOM   8901  C  C   . GLY C  1 375 ? 55.101  3.293   56.978  1.00 14.82  ? 462  GLY C C   1 
ATOM   8902  O  O   . GLY C  1 375 ? 54.481  2.473   57.637  1.00 14.40  ? 462  GLY C O   1 
ATOM   8903  N  N   . SER C  1 376 ? 55.412  4.492   57.450  1.00 14.99  ? 463  SER C N   1 
ATOM   8904  C  CA  . SER C  1 376 ? 55.015  4.860   58.815  1.00 14.79  ? 463  SER C CA  1 
ATOM   8905  C  C   . SER C  1 376 ? 54.472  6.266   58.902  1.00 14.24  ? 463  SER C C   1 
ATOM   8906  O  O   . SER C  1 376 ? 54.702  7.071   58.004  1.00 14.24  ? 463  SER C O   1 
ATOM   8907  C  CB  . SER C  1 376 ? 56.213  4.689   59.745  1.00 14.54  ? 463  SER C CB  1 
ATOM   8908  O  OG  . SER C  1 376 ? 57.256  5.546   59.334  1.00 16.22  ? 463  SER C OG  1 
ATOM   8909  N  N   . TRP C  1 377 ? 53.731  6.556   59.977  1.00 13.50  ? 464  TRP C N   1 
ATOM   8910  C  CA  . TRP C  1 377 ? 53.459  7.946   60.407  1.00 13.12  ? 464  TRP C CA  1 
ATOM   8911  C  C   . TRP C  1 377 ? 53.437  8.022   61.931  1.00 12.37  ? 464  TRP C C   1 
ATOM   8912  O  O   . TRP C  1 377 ? 53.624  6.994   62.607  1.00 11.89  ? 464  TRP C O   1 
ATOM   8913  C  CB  . TRP C  1 377 ? 52.196  8.573   59.754  1.00 13.76  ? 464  TRP C CB  1 
ATOM   8914  C  CG  . TRP C  1 377 ? 50.882  7.962   60.098  1.00 12.71  ? 464  TRP C CG  1 
ATOM   8915  C  CD1 . TRP C  1 377 ? 50.667  6.811   60.807  1.00 14.32  ? 464  TRP C CD1 1 
ATOM   8916  C  CD2 . TRP C  1 377 ? 49.585  8.435   59.691  1.00 12.55  ? 464  TRP C CD2 1 
ATOM   8917  N  NE1 . TRP C  1 377 ? 49.303  6.559   60.896  1.00 13.61  ? 464  TRP C NE1 1 
ATOM   8918  C  CE2 . TRP C  1 377 ? 48.622  7.541   60.230  1.00 12.77  ? 464  TRP C CE2 1 
ATOM   8919  C  CE3 . TRP C  1 377 ? 49.141  9.546   58.952  1.00 11.84  ? 464  TRP C CE3 1 
ATOM   8920  C  CZ2 . TRP C  1 377 ? 47.224  7.704   60.034  1.00 11.92  ? 464  TRP C CZ2 1 
ATOM   8921  C  CZ3 . TRP C  1 377 ? 47.745  9.716   58.764  1.00 13.71  ? 464  TRP C CZ3 1 
ATOM   8922  C  CH2 . TRP C  1 377 ? 46.808  8.788   59.301  1.00 12.63  ? 464  TRP C CH2 1 
ATOM   8923  N  N   . SER C  1 378 ? 53.267  9.236   62.448  1.00 11.31  ? 465  SER C N   1 
ATOM   8924  C  CA  . SER C  1 378 ? 53.344  9.505   63.874  1.00 10.34  ? 465  SER C CA  1 
ATOM   8925  C  C   . SER C  1 378 ? 52.024  9.102   64.543  1.00 10.15  ? 465  SER C C   1 
ATOM   8926  O  O   . SER C  1 378 ? 50.940  9.495   64.093  1.00 10.29  ? 465  SER C O   1 
ATOM   8927  C  CB  . SER C  1 378 ? 53.674  10.990  64.123  1.00 10.97  ? 465  SER C CB  1 
ATOM   8928  O  OG  . SER C  1 378 ? 53.620  11.286  65.504  1.00 11.33  ? 465  SER C OG  1 
ATOM   8929  N  N   . TRP C  1 379 ? 52.137  8.298   65.598  1.00 8.94   ? 466  TRP C N   1 
ATOM   8930  C  CA  . TRP C  1 379 ? 50.976  7.836   66.363  1.00 9.71   ? 466  TRP C CA  1 
ATOM   8931  C  C   . TRP C  1 379 ? 50.850  8.592   67.693  1.00 9.33   ? 466  TRP C C   1 
ATOM   8932  O  O   . TRP C  1 379 ? 50.759  7.977   68.763  1.00 9.17   ? 466  TRP C O   1 
ATOM   8933  C  CB  . TRP C  1 379 ? 51.080  6.317   66.582  1.00 9.07   ? 466  TRP C CB  1 
ATOM   8934  C  CG  . TRP C  1 379 ? 51.023  5.511   65.299  1.00 10.40  ? 466  TRP C CG  1 
ATOM   8935  C  CD1 . TRP C  1 379 ? 52.079  5.005   64.593  1.00 10.21  ? 466  TRP C CD1 1 
ATOM   8936  C  CD2 . TRP C  1 379 ? 49.848  5.162   64.565  1.00 8.58   ? 466  TRP C CD2 1 
ATOM   8937  N  NE1 . TRP C  1 379 ? 51.626  4.344   63.469  1.00 10.46  ? 466  TRP C NE1 1 
ATOM   8938  C  CE2 . TRP C  1 379 ? 50.261  4.418   63.436  1.00 9.73   ? 466  TRP C CE2 1 
ATOM   8939  C  CE3 . TRP C  1 379 ? 48.479  5.393   64.763  1.00 7.59   ? 466  TRP C CE3 1 
ATOM   8940  C  CZ2 . TRP C  1 379 ? 49.358  3.907   62.497  1.00 10.26  ? 466  TRP C CZ2 1 
ATOM   8941  C  CZ3 . TRP C  1 379 ? 47.574  4.885   63.819  1.00 8.62   ? 466  TRP C CZ3 1 
ATOM   8942  C  CH2 . TRP C  1 379 ? 48.021  4.143   62.712  1.00 9.43   ? 466  TRP C CH2 1 
ATOM   8943  N  N   . HIS C  1 380 ? 50.855  9.929   67.617  1.00 9.69   ? 467  HIS C N   1 
ATOM   8944  C  CA  . HIS C  1 380 ? 50.777  10.785  68.790  1.00 9.45   ? 467  HIS C CA  1 
ATOM   8945  C  C   . HIS C  1 380 ? 49.369  10.698  69.410  1.00 9.73   ? 467  HIS C C   1 
ATOM   8946  O  O   . HIS C  1 380 ? 48.442  10.176  68.782  1.00 8.84   ? 467  HIS C O   1 
ATOM   8947  C  CB  . HIS C  1 380 ? 51.169  12.232  68.451  1.00 9.91   ? 467  HIS C CB  1 
ATOM   8948  C  CG  . HIS C  1 380 ? 50.669  12.693  67.116  1.00 9.56   ? 467  HIS C CG  1 
ATOM   8949  N  ND1 . HIS C  1 380 ? 49.483  13.372  66.955  1.00 13.19  ? 467  HIS C ND1 1 
ATOM   8950  C  CD2 . HIS C  1 380 ? 51.193  12.555  65.880  1.00 9.45   ? 467  HIS C CD2 1 
ATOM   8951  C  CE1 . HIS C  1 380 ? 49.296  13.628  65.674  1.00 10.58  ? 467  HIS C CE1 1 
ATOM   8952  N  NE2 . HIS C  1 380 ? 50.321  13.140  65.001  1.00 13.28  ? 467  HIS C NE2 1 
ATOM   8953  N  N   . ASP C  1 381 ? 49.230  11.198  70.640  1.00 9.55   ? 468  ASP C N   1 
ATOM   8954  C  CA  . ASP C  1 381 ? 47.995  11.035  71.418  1.00 9.60   ? 468  ASP C CA  1 
ATOM   8955  C  C   . ASP C  1 381 ? 46.762  11.586  70.670  1.00 9.94   ? 468  ASP C C   1 
ATOM   8956  O  O   . ASP C  1 381 ? 45.727  10.923  70.574  1.00 10.39  ? 468  ASP C O   1 
ATOM   8957  C  CB  . ASP C  1 381 ? 48.148  11.729  72.786  1.00 8.96   ? 468  ASP C CB  1 
ATOM   8958  C  CG  . ASP C  1 381 ? 46.847  11.838  73.525  1.00 7.31   ? 468  ASP C CG  1 
ATOM   8959  O  OD1 . ASP C  1 381 ? 46.390  10.791  74.075  1.00 9.02   ? 468  ASP C OD1 1 
ATOM   8960  O  OD2 . ASP C  1 381 ? 46.256  12.955  73.557  1.00 7.76   ? 468  ASP C OD2 1 
ATOM   8961  N  N   . GLY C  1 382 ? 46.877  12.816  70.166  1.00 9.78   ? 469  GLY C N   1 
ATOM   8962  C  CA  . GLY C  1 382 ? 45.836  13.380  69.314  1.00 9.81   ? 469  GLY C CA  1 
ATOM   8963  C  C   . GLY C  1 382 ? 44.812  14.278  69.997  1.00 10.19  ? 469  GLY C C   1 
ATOM   8964  O  O   . GLY C  1 382 ? 43.955  14.853  69.311  1.00 10.45  ? 469  GLY C O   1 
ATOM   8965  N  N   . ALA C  1 383 ? 44.888  14.421  71.324  1.00 9.05   ? 470  ALA C N   1 
ATOM   8966  C  CA  . ALA C  1 383 ? 43.989  15.371  72.013  1.00 10.18  ? 470  ALA C CA  1 
ATOM   8967  C  C   . ALA C  1 383 ? 44.476  16.830  71.955  1.00 10.82  ? 470  ALA C C   1 
ATOM   8968  O  O   . ALA C  1 383 ? 45.675  17.086  71.927  1.00 10.64  ? 470  ALA C O   1 
ATOM   8969  C  CB  . ALA C  1 383 ? 43.754  14.962  73.445  1.00 9.07   ? 470  ALA C CB  1 
ATOM   8970  N  N   . GLU C  1 384 ? 43.532  17.766  71.943  1.00 11.83  ? 471  GLU C N   1 
ATOM   8971  C  CA  . GLU C  1 384 ? 43.849  19.191  71.948  1.00 12.64  ? 471  GLU C CA  1 
ATOM   8972  C  C   . GLU C  1 384 ? 43.731  19.667  73.374  1.00 12.00  ? 471  GLU C C   1 
ATOM   8973  O  O   . GLU C  1 384 ? 42.642  19.674  73.952  1.00 11.20  ? 471  GLU C O   1 
ATOM   8974  C  CB  . GLU C  1 384 ? 42.903  19.960  71.038  1.00 13.10  ? 471  GLU C CB  1 
ATOM   8975  C  CG  . GLU C  1 384 ? 42.886  19.427  69.615  1.00 19.11  ? 471  GLU C CG  1 
ATOM   8976  C  CD  . GLU C  1 384 ? 43.706  20.275  68.668  1.00 26.64  ? 471  GLU C CD  1 
ATOM   8977  O  OE1 . GLU C  1 384 ? 43.167  20.618  67.582  1.00 29.69  ? 471  GLU C OE1 1 
ATOM   8978  O  OE2 . GLU C  1 384 ? 44.860  20.640  69.021  1.00 28.84  ? 471  GLU C OE2 1 
ATOM   8979  N  N   . ILE C  1 385 ? 44.864  20.057  73.946  1.00 11.89  ? 472  ILE C N   1 
ATOM   8980  C  CA  . ILE C  1 385 ? 44.898  20.456  75.352  1.00 12.47  ? 472  ILE C CA  1 
ATOM   8981  C  C   . ILE C  1 385 ? 43.966  21.649  75.605  1.00 12.07  ? 472  ILE C C   1 
ATOM   8982  O  O   . ILE C  1 385 ? 43.437  21.796  76.695  1.00 11.21  ? 472  ILE C O   1 
ATOM   8983  C  CB  . ILE C  1 385 ? 46.367  20.672  75.883  1.00 12.46  ? 472  ILE C CB  1 
ATOM   8984  C  CG1 . ILE C  1 385 ? 46.450  20.481  77.419  1.00 13.91  ? 472  ILE C CG1 1 
ATOM   8985  C  CG2 . ILE C  1 385 ? 46.930  22.038  75.475  1.00 14.63  ? 472  ILE C CG2 1 
ATOM   8986  C  CD1 . ILE C  1 385 ? 46.298  19.019  77.860  1.00 12.57  ? 472  ILE C CD1 1 
ATOM   8987  N  N   . ILE C  1 386 ? 43.754  22.489  74.587  1.00 12.59  ? 473  ILE C N   1 
ATOM   8988  C  CA  . ILE C  1 386 ? 42.960  23.710  74.759  1.00 13.60  ? 473  ILE C CA  1 
ATOM   8989  C  C   . ILE C  1 386 ? 41.521  23.352  75.133  1.00 12.39  ? 473  ILE C C   1 
ATOM   8990  O  O   . ILE C  1 386 ? 40.863  24.079  75.875  1.00 11.86  ? 473  ILE C O   1 
ATOM   8991  C  CB  . ILE C  1 386 ? 42.992  24.640  73.483  1.00 14.65  ? 473  ILE C CB  1 
ATOM   8992  C  CG1 . ILE C  1 386 ? 44.417  25.110  73.173  1.00 18.10  ? 473  ILE C CG1 1 
ATOM   8993  C  CG2 . ILE C  1 386 ? 42.104  25.886  73.667  1.00 15.88  ? 473  ILE C CG2 1 
ATOM   8994  C  CD1 . ILE C  1 386 ? 45.031  26.096  74.164  1.00 23.64  ? 473  ILE C CD1 1 
ATOM   8995  N  N   . TYR C  1 387 ? 41.053  22.197  74.656  1.00 11.05  ? 474  TYR C N   1 
ATOM   8996  C  CA  . TYR C  1 387 ? 39.693  21.736  74.953  1.00 10.60  ? 474  TYR C CA  1 
ATOM   8997  C  C   . TYR C  1 387 ? 39.466  21.446  76.454  1.00 10.30  ? 474  TYR C C   1 
ATOM   8998  O  O   . TYR C  1 387 ? 38.323  21.447  76.936  1.00 10.75  ? 474  TYR C O   1 
ATOM   8999  C  CB  . TYR C  1 387 ? 39.352  20.486  74.110  1.00 9.22   ? 474  TYR C CB  1 
ATOM   9000  C  CG  . TYR C  1 387 ? 39.146  20.689  72.612  1.00 10.41  ? 474  TYR C CG  1 
ATOM   9001  C  CD1 . TYR C  1 387 ? 39.265  19.606  71.729  1.00 9.74   ? 474  TYR C CD1 1 
ATOM   9002  C  CD2 . TYR C  1 387 ? 38.789  21.937  72.073  1.00 10.59  ? 474  TYR C CD2 1 
ATOM   9003  C  CE1 . TYR C  1 387 ? 39.080  19.760  70.363  1.00 8.08   ? 474  TYR C CE1 1 
ATOM   9004  C  CE2 . TYR C  1 387 ? 38.591  22.095  70.694  1.00 11.30  ? 474  TYR C CE2 1 
ATOM   9005  C  CZ  . TYR C  1 387 ? 38.728  21.001  69.850  1.00 10.88  ? 474  TYR C CZ  1 
ATOM   9006  O  OH  . TYR C  1 387 ? 38.522  21.128  68.496  1.00 11.41  ? 474  TYR C OH  1 
ATOM   9007  N  N   . PHE C  1 388 ? 40.558  21.192  77.176  1.00 10.75  ? 475  PHE C N   1 
ATOM   9008  C  CA  . PHE C  1 388 ? 40.514  20.831  78.600  1.00 11.33  ? 475  PHE C CA  1 
ATOM   9009  C  C   . PHE C  1 388 ? 40.715  22.072  79.471  1.00 12.89  ? 475  PHE C C   1 
ATOM   9010  O  O   . PHE C  1 388 ? 40.718  21.985  80.712  1.00 12.50  ? 475  PHE C O   1 
ATOM   9011  C  CB  . PHE C  1 388 ? 41.613  19.793  78.914  1.00 10.99  ? 475  PHE C CB  1 
ATOM   9012  C  CG  . PHE C  1 388 ? 41.310  18.414  78.398  1.00 10.86  ? 475  PHE C CG  1 
ATOM   9013  C  CD1 . PHE C  1 388 ? 41.754  18.011  77.130  1.00 10.03  ? 475  PHE C CD1 1 
ATOM   9014  C  CD2 . PHE C  1 388 ? 40.606  17.504  79.192  1.00 9.30   ? 475  PHE C CD2 1 
ATOM   9015  C  CE1 . PHE C  1 388 ? 41.486  16.698  76.661  1.00 10.97  ? 475  PHE C CE1 1 
ATOM   9016  C  CE2 . PHE C  1 388 ? 40.341  16.198  78.727  1.00 7.47   ? 475  PHE C CE2 1 
ATOM   9017  C  CZ  . PHE C  1 388 ? 40.777  15.801  77.473  1.00 9.55   ? 475  PHE C CZ  1 
ATOM   9018  N  N   . GLU C  1 389 ? 40.878  23.229  78.818  1.00 14.33  ? 476  GLU C N   1 
ATOM   9019  C  CA  . GLU C  1 389 ? 41.184  24.470  79.532  1.00 16.04  ? 476  GLU C CA  1 
ATOM   9020  C  C   . GLU C  1 389 ? 39.897  25.240  79.804  1.00 16.84  ? 476  GLU C C   1 
ATOM   9021  O  O   . GLU C  1 389 ? 38.784  24.799  79.417  1.00 17.01  ? 476  GLU C O   1 
ATOM   9022  C  CB  . GLU C  1 389 ? 42.203  25.328  78.743  1.00 16.44  ? 476  GLU C CB  1 
ATOM   9023  C  CG  . GLU C  1 389 ? 43.599  24.683  78.606  1.00 16.66  ? 476  GLU C CG  1 
ATOM   9024  C  CD  . GLU C  1 389 ? 44.548  25.487  77.720  1.00 17.14  ? 476  GLU C CD  1 
ATOM   9025  O  OE1 . GLU C  1 389 ? 44.172  26.609  77.314  1.00 17.47  ? 476  GLU C OE1 1 
ATOM   9026  O  OE2 . GLU C  1 389 ? 45.669  25.005  77.433  1.00 19.38  ? 476  GLU C OE2 1 
ATOM   9027  O  OXT . GLU C  1 389 ? 39.932  26.316  80.427  1.00 18.07  ? 476  GLU C OXT 1 
ATOM   9028  N  N   . ARG D  1 1   ? 31.053  -29.216 90.513  1.00 26.64  ? 88   ARG D N   1 
ATOM   9029  C  CA  . ARG D  1 1   ? 30.786  -28.424 91.756  1.00 27.04  ? 88   ARG D CA  1 
ATOM   9030  C  C   . ARG D  1 1   ? 30.146  -29.294 92.822  1.00 25.86  ? 88   ARG D C   1 
ATOM   9031  O  O   . ARG D  1 1   ? 29.386  -30.208 92.506  1.00 26.07  ? 88   ARG D O   1 
ATOM   9032  C  CB  . ARG D  1 1   ? 29.857  -27.248 91.476  1.00 27.70  ? 88   ARG D CB  1 
ATOM   9033  C  CG  . ARG D  1 1   ? 30.407  -26.188 90.521  1.00 30.71  ? 88   ARG D CG  1 
ATOM   9034  C  CD  . ARG D  1 1   ? 29.795  -24.815 90.790  1.00 34.95  ? 88   ARG D CD  1 
ATOM   9035  N  NE  . ARG D  1 1   ? 28.403  -24.597 90.348  1.00 39.32  ? 88   ARG D NE  1 
ATOM   9036  C  CZ  . ARG D  1 1   ? 27.457  -25.519 90.103  1.00 41.46  ? 88   ARG D CZ  1 
ATOM   9037  N  NH1 . ARG D  1 1   ? 27.687  -26.822 90.226  1.00 41.79  ? 88   ARG D NH1 1 
ATOM   9038  N  NH2 . ARG D  1 1   ? 26.241  -25.123 89.726  1.00 42.30  ? 88   ARG D NH2 1 
ATOM   9039  N  N   . THR D  1 2   ? 30.438  -28.986 94.085  1.00 24.25  ? 89   THR D N   1 
ATOM   9040  C  CA  . THR D  1 2   ? 29.931  -29.749 95.227  1.00 22.58  ? 89   THR D CA  1 
ATOM   9041  C  C   . THR D  1 2   ? 29.600  -28.753 96.326  1.00 20.72  ? 89   THR D C   1 
ATOM   9042  O  O   . THR D  1 2   ? 30.050  -27.602 96.281  1.00 20.05  ? 89   THR D O   1 
ATOM   9043  C  CB  . THR D  1 2   ? 30.997  -30.731 95.781  1.00 23.09  ? 89   THR D CB  1 
ATOM   9044  O  OG1 . THR D  1 2   ? 32.200  -30.009 96.081  1.00 25.31  ? 89   THR D OG1 1 
ATOM   9045  C  CG2 . THR D  1 2   ? 31.333  -31.825 94.771  1.00 25.09  ? 89   THR D CG2 1 
ATOM   9046  N  N   . PHE D  1 3   ? 28.836  -29.188 97.324  1.00 18.17  ? 90   PHE D N   1 
ATOM   9047  C  CA  . PHE D  1 3   ? 28.564  -28.307 98.461  1.00 16.56  ? 90   PHE D CA  1 
ATOM   9048  C  C   . PHE D  1 3   ? 29.839  -27.989 99.232  1.00 15.60  ? 90   PHE D C   1 
ATOM   9049  O  O   . PHE D  1 3   ? 30.656  -28.888 99.492  1.00 15.03  ? 90   PHE D O   1 
ATOM   9050  C  CB  . PHE D  1 3   ? 27.556  -28.936 99.403  1.00 17.14  ? 90   PHE D CB  1 
ATOM   9051  C  CG  . PHE D  1 3   ? 26.131  -28.851 98.926  1.00 16.82  ? 90   PHE D CG  1 
ATOM   9052  C  CD1 . PHE D  1 3   ? 25.315  -29.976 98.962  1.00 18.52  ? 90   PHE D CD1 1 
ATOM   9053  C  CD2 . PHE D  1 3   ? 25.584  -27.637 98.486  1.00 15.94  ? 90   PHE D CD2 1 
ATOM   9054  C  CE1 . PHE D  1 3   ? 23.975  -29.898 98.554  1.00 17.84  ? 90   PHE D CE1 1 
ATOM   9055  C  CE2 . PHE D  1 3   ? 24.255  -27.561 98.077  1.00 15.09  ? 90   PHE D CE2 1 
ATOM   9056  C  CZ  . PHE D  1 3   ? 23.451  -28.694 98.115  1.00 18.63  ? 90   PHE D CZ  1 
ATOM   9057  N  N   . LEU D  1 4   ? 29.998  -26.720 99.621  1.00 14.22  ? 91   LEU D N   1 
ATOM   9058  C  CA  . LEU D  1 4   ? 31.073  -26.320 100.538 1.00 13.76  ? 91   LEU D CA  1 
ATOM   9059  C  C   . LEU D  1 4   ? 30.913  -26.963 101.920 1.00 13.97  ? 91   LEU D C   1 
ATOM   9060  O  O   . LEU D  1 4   ? 29.840  -26.890 102.531 1.00 13.60  ? 91   LEU D O   1 
ATOM   9061  C  CB  . LEU D  1 4   ? 31.123  -24.782 100.693 1.00 13.67  ? 91   LEU D CB  1 
ATOM   9062  C  CG  . LEU D  1 4   ? 32.002  -24.225 101.829 1.00 13.22  ? 91   LEU D CG  1 
ATOM   9063  C  CD1 . LEU D  1 4   ? 33.519  -24.453 101.583 1.00 12.02  ? 91   LEU D CD1 1 
ATOM   9064  C  CD2 . LEU D  1 4   ? 31.705  -22.743 102.045 1.00 12.93  ? 91   LEU D CD2 1 
ATOM   9065  N  N   . ASN D  1 5   ? 31.990  -27.582 102.407 1.00 13.93  ? 92   ASN D N   1 
ATOM   9066  C  CA  . ASN D  1 5   ? 32.042  -28.033 103.785 1.00 15.25  ? 92   ASN D CA  1 
ATOM   9067  C  C   . ASN D  1 5   ? 33.160  -27.341 104.528 1.00 15.14  ? 92   ASN D C   1 
ATOM   9068  O  O   . ASN D  1 5   ? 34.293  -27.251 104.029 1.00 15.07  ? 92   ASN D O   1 
ATOM   9069  C  CB  . ASN D  1 5   ? 32.180  -29.556 103.871 1.00 15.24  ? 92   ASN D CB  1 
ATOM   9070  C  CG  . ASN D  1 5   ? 31.234  -30.271 102.917 1.00 17.82  ? 92   ASN D CG  1 
ATOM   9071  O  OD1 . ASN D  1 5   ? 30.079  -29.882 102.755 1.00 18.32  ? 92   ASN D OD1 1 
ATOM   9072  N  ND2 . ASN D  1 5   ? 31.737  -31.293 102.249 1.00 21.29  ? 92   ASN D ND2 1 
ATOM   9073  N  N   . LEU D  1 6   ? 32.835  -26.869 105.726 1.00 15.01  ? 93   LEU D N   1 
ATOM   9074  C  CA  . LEU D  1 6   ? 33.723  -26.025 106.498 1.00 15.53  ? 93   LEU D CA  1 
ATOM   9075  C  C   . LEU D  1 6   ? 34.828  -26.825 107.203 1.00 16.12  ? 93   LEU D C   1 
ATOM   9076  O  O   . LEU D  1 6   ? 35.052  -26.671 108.395 1.00 16.95  ? 93   LEU D O   1 
ATOM   9077  C  CB  . LEU D  1 6   ? 32.904  -25.177 107.480 1.00 15.55  ? 93   LEU D CB  1 
ATOM   9078  C  CG  . LEU D  1 6   ? 31.792  -24.289 106.887 1.00 14.21  ? 93   LEU D CG  1 
ATOM   9079  C  CD1 . LEU D  1 6   ? 30.958  -23.658 108.007 1.00 14.92  ? 93   LEU D CD1 1 
ATOM   9080  C  CD2 . LEU D  1 6   ? 32.359  -23.207 105.935 1.00 14.23  ? 93   LEU D CD2 1 
ATOM   9081  N  N   . THR D  1 7   ? 35.551  -27.623 106.422 1.00 17.34  ? 94   THR D N   1 
ATOM   9082  C  CA  . THR D  1 7   ? 36.497  -28.629 106.934 1.00 18.56  ? 94   THR D CA  1 
ATOM   9083  C  C   . THR D  1 7   ? 37.839  -28.081 107.424 1.00 18.35  ? 94   THR D C   1 
ATOM   9084  O  O   . THR D  1 7   ? 38.558  -28.766 108.158 1.00 19.83  ? 94   THR D O   1 
ATOM   9085  C  CB  . THR D  1 7   ? 36.766  -29.716 105.860 1.00 18.96  ? 94   THR D CB  1 
ATOM   9086  O  OG1 . THR D  1 7   ? 37.340  -29.106 104.692 1.00 23.17  ? 94   THR D OG1 1 
ATOM   9087  C  CG2 . THR D  1 7   ? 35.487  -30.370 105.450 1.00 18.94  ? 94   THR D CG2 1 
ATOM   9088  N  N   . LYS D  1 8   ? 38.177  -26.854 107.034 1.00 16.50  ? 95   LYS D N   1 
ATOM   9089  C  CA  . LYS D  1 8   ? 39.538  -26.334 107.211 1.00 15.32  ? 95   LYS D CA  1 
ATOM   9090  C  C   . LYS D  1 8   ? 39.627  -25.442 108.453 1.00 14.52  ? 95   LYS D C   1 
ATOM   9091  O  O   . LYS D  1 8   ? 38.632  -24.831 108.843 1.00 14.31  ? 95   LYS D O   1 
ATOM   9092  C  CB  . LYS D  1 8   ? 39.977  -25.565 105.939 1.00 14.68  ? 95   LYS D CB  1 
ATOM   9093  C  CG  . LYS D  1 8   ? 40.043  -26.455 104.684 1.00 15.44  ? 95   LYS D CG  1 
ATOM   9094  C  CD  . LYS D  1 8   ? 40.494  -25.697 103.436 1.00 15.10  ? 95   LYS D CD  1 
ATOM   9095  C  CE  . LYS D  1 8   ? 40.397  -26.563 102.186 1.00 16.50  ? 95   LYS D CE  1 
ATOM   9096  N  NZ  . LYS D  1 8   ? 40.835  -25.843 100.935 1.00 15.58  ? 95   LYS D NZ  1 
ATOM   9097  N  N   . PRO D  1 9   ? 40.825  -25.338 109.066 1.00 13.79  ? 96   PRO D N   1 
ATOM   9098  C  CA  . PRO D  1 9   ? 40.963  -24.399 110.170 1.00 13.21  ? 96   PRO D CA  1 
ATOM   9099  C  C   . PRO D  1 9   ? 41.182  -22.971 109.628 1.00 12.41  ? 96   PRO D C   1 
ATOM   9100  O  O   . PRO D  1 9   ? 41.425  -22.817 108.431 1.00 12.14  ? 96   PRO D O   1 
ATOM   9101  C  CB  . PRO D  1 9   ? 42.231  -24.899 110.870 1.00 13.24  ? 96   PRO D CB  1 
ATOM   9102  C  CG  . PRO D  1 9   ? 43.078  -25.361 109.746 1.00 12.58  ? 96   PRO D CG  1 
ATOM   9103  C  CD  . PRO D  1 9   ? 42.101  -26.026 108.781 1.00 13.60  ? 96   PRO D CD  1 
ATOM   9104  N  N   . LEU D  1 10  ? 41.079  -21.950 110.482 1.00 13.10  ? 97   LEU D N   1 
ATOM   9105  C  CA  . LEU D  1 10  ? 41.455  -20.582 110.076 1.00 13.13  ? 97   LEU D CA  1 
ATOM   9106  C  C   . LEU D  1 10  ? 42.952  -20.506 109.862 1.00 13.47  ? 97   LEU D C   1 
ATOM   9107  O  O   . LEU D  1 10  ? 43.714  -21.141 110.597 1.00 13.13  ? 97   LEU D O   1 
ATOM   9108  C  CB  . LEU D  1 10  ? 41.076  -19.520 111.121 1.00 13.76  ? 97   LEU D CB  1 
ATOM   9109  C  CG  . LEU D  1 10  ? 39.690  -18.867 111.194 1.00 15.84  ? 97   LEU D CG  1 
ATOM   9110  C  CD1 . LEU D  1 10  ? 39.733  -17.638 112.123 1.00 13.11  ? 97   LEU D CD1 1 
ATOM   9111  C  CD2 . LEU D  1 10  ? 39.105  -18.518 109.811 1.00 12.68  ? 97   LEU D CD2 1 
ATOM   9112  N  N   . CYS D  1 11  ? 43.376  -19.713 108.873 1.00 12.78  ? 98   CYS D N   1 
ATOM   9113  C  CA  . CYS D  1 11  ? 44.802  -19.433 108.674 1.00 12.72  ? 98   CYS D CA  1 
ATOM   9114  C  C   . CYS D  1 11  ? 45.347  -18.578 109.820 1.00 12.02  ? 98   CYS D C   1 
ATOM   9115  O  O   . CYS D  1 11  ? 44.615  -17.798 110.412 1.00 11.55  ? 98   CYS D O   1 
ATOM   9116  C  CB  . CYS D  1 11  ? 45.036  -18.680 107.357 1.00 13.00  ? 98   CYS D CB  1 
ATOM   9117  S  SG  . CYS D  1 11  ? 44.506  -19.532 105.874 1.00 12.92  ? 98   CYS D SG  1 
ATOM   9118  N  N   . GLU D  1 12  ? 46.636  -18.731 110.122 1.00 11.76  ? 99   GLU D N   1 
ATOM   9119  C  CA  . GLU D  1 12  ? 47.320  -17.846 111.046 1.00 12.44  ? 99   GLU D CA  1 
ATOM   9120  C  C   . GLU D  1 12  ? 47.347  -16.439 110.432 1.00 11.87  ? 99   GLU D C   1 
ATOM   9121  O  O   . GLU D  1 12  ? 47.590  -16.299 109.223 1.00 12.03  ? 99   GLU D O   1 
ATOM   9122  C  CB  . GLU D  1 12  ? 48.750  -18.348 111.286 1.00 12.19  ? 99   GLU D CB  1 
ATOM   9123  C  CG  . GLU D  1 12  ? 49.670  -17.361 112.051 1.00 13.43  ? 99   GLU D CG  1 
ATOM   9124  C  CD  . GLU D  1 12  ? 51.070  -17.919 112.272 1.00 15.81  ? 99   GLU D CD  1 
ATOM   9125  O  OE1 . GLU D  1 12  ? 51.987  -17.138 112.595 1.00 16.61  ? 99   GLU D OE1 1 
ATOM   9126  O  OE2 . GLU D  1 12  ? 51.252  -19.156 112.125 1.00 20.24  ? 99   GLU D OE2 1 
ATOM   9127  N  N   . VAL D  1 13  ? 47.090  -15.418 111.253 1.00 11.22  ? 100  VAL D N   1 
ATOM   9128  C  CA  . VAL D  1 13  ? 47.071  -14.033 110.775 1.00 10.94  ? 100  VAL D CA  1 
ATOM   9129  C  C   . VAL D  1 13  ? 47.933  -13.127 111.667 1.00 10.98  ? 100  VAL D C   1 
ATOM   9130  O  O   . VAL D  1 13  ? 47.697  -13.006 112.888 1.00 10.50  ? 100  VAL D O   1 
ATOM   9131  C  CB  . VAL D  1 13  ? 45.614  -13.466 110.635 1.00 10.55  ? 100  VAL D CB  1 
ATOM   9132  C  CG1 . VAL D  1 13  ? 45.643  -12.021 110.164 1.00 9.70   ? 100  VAL D CG1 1 
ATOM   9133  C  CG2 . VAL D  1 13  ? 44.768  -14.313 109.666 1.00 10.10  ? 100  VAL D CG2 1 
ATOM   9134  N  N   . ASN D  1 14  ? 48.934  -12.496 111.051 1.00 10.75  ? 101  ASN D N   1 
ATOM   9135  C  CA  . ASN D  1 14  ? 49.821  -11.588 111.767 1.00 10.15  ? 101  ASN D CA  1 
ATOM   9136  C  C   . ASN D  1 14  ? 49.714  -10.127 111.337 1.00 9.88   ? 101  ASN D C   1 
ATOM   9137  O  O   . ASN D  1 14  ? 50.138  -9.224  112.060 1.00 10.76  ? 101  ASN D O   1 
ATOM   9138  C  CB  . ASN D  1 14  ? 51.256  -12.120 111.687 1.00 10.36  ? 101  ASN D CB  1 
ATOM   9139  C  CG  . ASN D  1 14  ? 51.413  -13.421 112.466 1.00 11.21  ? 101  ASN D CG  1 
ATOM   9140  O  OD1 . ASN D  1 14  ? 51.024  -13.485 113.629 1.00 12.16  ? 101  ASN D OD1 1 
ATOM   9141  N  ND2 . ASN D  1 14  ? 51.916  -14.474 111.808 1.00 11.13  ? 101  ASN D ND2 1 
ATOM   9142  N  N   . SER D  1 15  ? 49.138  -9.903  110.165 1.00 9.21   ? 102  SER D N   1 
ATOM   9143  C  CA  . SER D  1 15  ? 48.849  -8.560  109.643 1.00 9.25   ? 102  SER D CA  1 
ATOM   9144  C  C   . SER D  1 15  ? 47.803  -8.708  108.532 1.00 9.34   ? 102  SER D C   1 
ATOM   9145  O  O   . SER D  1 15  ? 47.294  -9.816  108.276 1.00 8.29   ? 102  SER D O   1 
ATOM   9146  C  CB  . SER D  1 15  ? 50.109  -7.843  109.139 1.00 8.77   ? 102  SER D CB  1 
ATOM   9147  O  OG  . SER D  1 15  ? 50.633  -8.470  108.004 1.00 11.53  ? 102  SER D OG  1 
ATOM   9148  N  N   . TRP D  1 16  ? 47.478  -7.604  107.870 1.00 8.46   ? 103  TRP D N   1 
ATOM   9149  C  CA  . TRP D  1 16  ? 46.385  -7.629  106.892 1.00 8.75   ? 103  TRP D CA  1 
ATOM   9150  C  C   . TRP D  1 16  ? 46.875  -7.001  105.582 1.00 8.49   ? 103  TRP D C   1 
ATOM   9151  O  O   . TRP D  1 16  ? 47.471  -5.932  105.617 1.00 9.04   ? 103  TRP D O   1 
ATOM   9152  C  CB  . TRP D  1 16  ? 45.186  -6.861  107.465 1.00 8.72   ? 103  TRP D CB  1 
ATOM   9153  C  CG  . TRP D  1 16  ? 44.670  -7.492  108.739 1.00 9.94   ? 103  TRP D CG  1 
ATOM   9154  C  CD1 . TRP D  1 16  ? 45.071  -7.222  110.024 1.00 8.89   ? 103  TRP D CD1 1 
ATOM   9155  C  CD2 . TRP D  1 16  ? 43.692  -8.534  108.828 1.00 9.53   ? 103  TRP D CD2 1 
ATOM   9156  N  NE1 . TRP D  1 16  ? 44.379  -8.026  110.912 1.00 8.96   ? 103  TRP D NE1 1 
ATOM   9157  C  CE2 . TRP D  1 16  ? 43.524  -8.836  110.206 1.00 10.49  ? 103  TRP D CE2 1 
ATOM   9158  C  CE3 . TRP D  1 16  ? 42.916  -9.221  107.880 1.00 9.19   ? 103  TRP D CE3 1 
ATOM   9159  C  CZ2 . TRP D  1 16  ? 42.630  -9.823  110.653 1.00 8.73   ? 103  TRP D CZ2 1 
ATOM   9160  C  CZ3 . TRP D  1 16  ? 42.017  -10.180 108.321 1.00 9.34   ? 103  TRP D CZ3 1 
ATOM   9161  C  CH2 . TRP D  1 16  ? 41.873  -10.471 109.703 1.00 9.50   ? 103  TRP D CH2 1 
ATOM   9162  N  N   . HIS D  1 17  ? 46.664  -7.687  104.457 1.00 7.87   ? 104  HIS D N   1 
ATOM   9163  C  CA  . HIS D  1 17  ? 47.057  -7.170  103.134 1.00 8.41   ? 104  HIS D CA  1 
ATOM   9164  C  C   . HIS D  1 17  ? 45.844  -6.598  102.400 1.00 7.92   ? 104  HIS D C   1 
ATOM   9165  O  O   . HIS D  1 17  ? 44.731  -7.049  102.603 1.00 8.03   ? 104  HIS D O   1 
ATOM   9166  C  CB  . HIS D  1 17  ? 47.743  -8.263  102.267 1.00 7.84   ? 104  HIS D CB  1 
ATOM   9167  C  CG  . HIS D  1 17  ? 46.798  -9.276  101.674 1.00 9.91   ? 104  HIS D CG  1 
ATOM   9168  N  ND1 . HIS D  1 17  ? 46.084  -9.041  100.517 1.00 6.46   ? 104  HIS D ND1 1 
ATOM   9169  C  CD2 . HIS D  1 17  ? 46.474  -10.536 102.064 1.00 9.79   ? 104  HIS D CD2 1 
ATOM   9170  C  CE1 . HIS D  1 17  ? 45.355  -10.108 100.225 1.00 11.77  ? 104  HIS D CE1 1 
ATOM   9171  N  NE2 . HIS D  1 17  ? 45.566  -11.026 101.153 1.00 9.04   ? 104  HIS D NE2 1 
ATOM   9172  N  N   . ILE D  1 18  ? 46.080  -5.648  101.508 1.00 8.37   ? 105  ILE D N   1 
ATOM   9173  C  CA  . ILE D  1 18  ? 44.995  -5.054  100.714 1.00 7.74   ? 105  ILE D CA  1 
ATOM   9174  C  C   . ILE D  1 18  ? 44.417  -6.057  99.699  1.00 8.34   ? 105  ILE D C   1 
ATOM   9175  O  O   . ILE D  1 18  ? 45.180  -6.677  98.926  1.00 8.72   ? 105  ILE D O   1 
ATOM   9176  C  CB  . ILE D  1 18  ? 45.443  -3.705  100.025 1.00 7.26   ? 105  ILE D CB  1 
ATOM   9177  C  CG1 . ILE D  1 18  ? 44.231  -2.975  99.410  1.00 6.51   ? 105  ILE D CG1 1 
ATOM   9178  C  CG2 . ILE D  1 18  ? 46.564  -3.931  98.971  1.00 6.29   ? 105  ILE D CG2 1 
ATOM   9179  C  CD1 . ILE D  1 18  ? 43.165  -2.550  100.419 1.00 4.84   ? 105  ILE D CD1 1 
ATOM   9180  N  N   . LEU D  1 19  ? 43.084  -6.225  99.715  1.00 7.19   ? 106  LEU D N   1 
ATOM   9181  C  CA  . LEU D  1 19  ? 42.398  -7.100  98.744  1.00 7.44   ? 106  LEU D CA  1 
ATOM   9182  C  C   . LEU D  1 19  ? 41.746  -6.314  97.614  1.00 7.58   ? 106  LEU D C   1 
ATOM   9183  O  O   . LEU D  1 19  ? 41.980  -6.599  96.443  1.00 6.68   ? 106  LEU D O   1 
ATOM   9184  C  CB  . LEU D  1 19  ? 41.331  -7.984  99.421  1.00 7.57   ? 106  LEU D CB  1 
ATOM   9185  C  CG  . LEU D  1 19  ? 40.623  -9.023  98.531  1.00 8.11   ? 106  LEU D CG  1 
ATOM   9186  C  CD1 . LEU D  1 19  ? 41.516  -10.262 98.298  1.00 9.03   ? 106  LEU D CD1 1 
ATOM   9187  C  CD2 . LEU D  1 19  ? 39.276  -9.420  99.137  1.00 6.16   ? 106  LEU D CD2 1 
ATOM   9188  N  N   . SER D  1 20  ? 40.915  -5.336  97.987  1.00 8.20   ? 107  SER D N   1 
ATOM   9189  C  CA  . SER D  1 20  ? 40.191  -4.514  97.020  1.00 8.44   ? 107  SER D CA  1 
ATOM   9190  C  C   . SER D  1 20  ? 39.827  -3.158  97.598  1.00 8.48   ? 107  SER D C   1 
ATOM   9191  O  O   . SER D  1 20  ? 39.744  -2.981  98.815  1.00 9.12   ? 107  SER D O   1 
ATOM   9192  C  CB  . SER D  1 20  ? 38.913  -5.222  96.554  1.00 7.99   ? 107  SER D CB  1 
ATOM   9193  O  OG  . SER D  1 20  ? 38.444  -4.640  95.350  1.00 7.44   ? 107  SER D OG  1 
ATOM   9194  N  N   . LYS D  1 21  ? 39.616  -2.205  96.703  1.00 8.81   ? 108  LYS D N   1 
ATOM   9195  C  CA  . LYS D  1 21  ? 39.133  -0.875  97.049  1.00 8.43   ? 108  LYS D CA  1 
ATOM   9196  C  C   . LYS D  1 21  ? 38.439  -0.334  95.806  1.00 8.88   ? 108  LYS D C   1 
ATOM   9197  O  O   . LYS D  1 21  ? 39.021  -0.387  94.704  1.00 9.16   ? 108  LYS D O   1 
ATOM   9198  C  CB  . LYS D  1 21  ? 40.301  0.031   97.449  1.00 8.43   ? 108  LYS D CB  1 
ATOM   9199  C  CG  . LYS D  1 21  ? 39.844  1.340   98.088  1.00 8.95   ? 108  LYS D CG  1 
ATOM   9200  C  CD  . LYS D  1 21  ? 41.036  2.242   98.411  1.00 7.25   ? 108  LYS D CD  1 
ATOM   9201  C  CE  . LYS D  1 21  ? 40.601  3.336   99.372  1.00 7.85   ? 108  LYS D CE  1 
ATOM   9202  N  NZ  . LYS D  1 21  ? 39.652  4.260   98.694  1.00 8.29   ? 108  LYS D NZ  1 
ATOM   9203  N  N   . ASP D  1 22  ? 37.203  0.159   95.941  1.00 7.56   ? 109  ASP D N   1 
ATOM   9204  C  CA  . ASP D  1 22  ? 36.492  0.600   94.730  1.00 7.74   ? 109  ASP D CA  1 
ATOM   9205  C  C   . ASP D  1 22  ? 36.507  2.111   94.467  1.00 7.61   ? 109  ASP D C   1 
ATOM   9206  O  O   . ASP D  1 22  ? 36.130  2.536   93.369  1.00 8.27   ? 109  ASP D O   1 
ATOM   9207  C  CB  . ASP D  1 22  ? 35.055  0.063   94.672  1.00 7.52   ? 109  ASP D CB  1 
ATOM   9208  C  CG  . ASP D  1 22  ? 34.136  0.680   95.732  1.00 8.49   ? 109  ASP D CG  1 
ATOM   9209  O  OD1 . ASP D  1 22  ? 34.601  1.471   96.609  1.00 6.44   ? 109  ASP D OD1 1 
ATOM   9210  O  OD2 . ASP D  1 22  ? 32.916  0.367   95.664  1.00 9.95   ? 109  ASP D OD2 1 
ATOM   9211  N  N   . ASN D  1 23  ? 36.915  2.915   95.452  1.00 6.76   ? 110  ASN D N   1 
ATOM   9212  C  CA  . ASN D  1 23  ? 37.024  4.380   95.232  1.00 7.31   ? 110  ASN D CA  1 
ATOM   9213  C  C   . ASN D  1 23  ? 35.747  4.968   94.620  1.00 7.47   ? 110  ASN D C   1 
ATOM   9214  O  O   . ASN D  1 23  ? 35.798  5.865   93.756  1.00 7.11   ? 110  ASN D O   1 
ATOM   9215  C  CB  . ASN D  1 23  ? 38.239  4.664   94.342  1.00 7.02   ? 110  ASN D CB  1 
ATOM   9216  C  CG  . ASN D  1 23  ? 39.554  4.283   95.024  1.00 9.50   ? 110  ASN D CG  1 
ATOM   9217  O  OD1 . ASN D  1 23  ? 39.926  4.879   96.043  1.00 10.38  ? 110  ASN D OD1 1 
ATOM   9218  N  ND2 . ASN D  1 23  ? 40.252  3.280   94.476  1.00 9.12   ? 110  ASN D ND2 1 
ATOM   9219  N  N   . ALA D  1 24  ? 34.604  4.456   95.084  1.00 6.98   ? 111  ALA D N   1 
ATOM   9220  C  CA  . ALA D  1 24  ? 33.323  4.742   94.434  1.00 7.61   ? 111  ALA D CA  1 
ATOM   9221  C  C   . ALA D  1 24  ? 32.945  6.235   94.454  1.00 7.53   ? 111  ALA D C   1 
ATOM   9222  O  O   . ALA D  1 24  ? 32.367  6.735   93.490  1.00 8.00   ? 111  ALA D O   1 
ATOM   9223  C  CB  . ALA D  1 24  ? 32.192  3.908   95.031  1.00 7.04   ? 111  ALA D CB  1 
ATOM   9224  N  N   . ILE D  1 25  ? 33.235  6.918   95.563  1.00 7.85   ? 112  ILE D N   1 
ATOM   9225  C  CA  . ILE D  1 25  ? 32.852  8.337   95.698  1.00 8.06   ? 112  ILE D CA  1 
ATOM   9226  C  C   . ILE D  1 25  ? 33.732  9.258   94.836  1.00 7.86   ? 112  ILE D C   1 
ATOM   9227  O  O   . ILE D  1 25  ? 33.230  10.185  94.164  1.00 8.74   ? 112  ILE D O   1 
ATOM   9228  C  CB  . ILE D  1 25  ? 32.851  8.773   97.196  1.00 7.79   ? 112  ILE D CB  1 
ATOM   9229  C  CG1 . ILE D  1 25  ? 31.991  7.812   98.040  1.00 7.03   ? 112  ILE D CG1 1 
ATOM   9230  C  CG2 . ILE D  1 25  ? 32.388  10.220  97.347  1.00 7.05   ? 112  ILE D CG2 1 
ATOM   9231  C  CD1 . ILE D  1 25  ? 30.457  7.810   97.710  1.00 8.34   ? 112  ILE D CD1 1 
ATOM   9232  N  N   . ARG D  1 26  ? 35.043  8.995   94.836  1.00 7.44   ? 113  ARG D N   1 
ATOM   9233  C  CA  . ARG D  1 26  ? 35.957  9.709   93.952  1.00 7.40   ? 113  ARG D CA  1 
ATOM   9234  C  C   . ARG D  1 26  ? 35.468  9.601   92.509  1.00 7.71   ? 113  ARG D C   1 
ATOM   9235  O  O   . ARG D  1 26  ? 35.266  10.609  91.823  1.00 8.48   ? 113  ARG D O   1 
ATOM   9236  C  CB  . ARG D  1 26  ? 37.358  9.121   94.077  1.00 7.22   ? 113  ARG D CB  1 
ATOM   9237  C  CG  . ARG D  1 26  ? 38.095  9.485   95.390  1.00 6.20   ? 113  ARG D CG  1 
ATOM   9238  C  CD  . ARG D  1 26  ? 39.462  8.809   95.474  1.00 7.35   ? 113  ARG D CD  1 
ATOM   9239  N  NE  . ARG D  1 26  ? 40.276  9.030   94.286  1.00 9.11   ? 113  ARG D NE  1 
ATOM   9240  C  CZ  . ARG D  1 26  ? 41.113  10.051  94.108  1.00 8.89   ? 113  ARG D CZ  1 
ATOM   9241  N  NH1 . ARG D  1 26  ? 41.272  10.978  95.050  1.00 10.06  ? 113  ARG D NH1 1 
ATOM   9242  N  NH2 . ARG D  1 26  ? 41.803  10.131  92.984  1.00 8.81   ? 113  ARG D NH2 1 
ATOM   9243  N  N   . ILE D  1 27  ? 35.241  8.369   92.060  1.00 7.20   ? 114  ILE D N   1 
ATOM   9244  C  CA  . ILE D  1 27  ? 34.851  8.126   90.677  1.00 8.12   ? 114  ILE D CA  1 
ATOM   9245  C  C   . ILE D  1 27  ? 33.442  8.664   90.401  1.00 8.34   ? 114  ILE D C   1 
ATOM   9246  O  O   . ILE D  1 27  ? 33.207  9.293   89.350  1.00 8.78   ? 114  ILE D O   1 
ATOM   9247  C  CB  . ILE D  1 27  ? 34.955  6.612   90.348  1.00 7.29   ? 114  ILE D CB  1 
ATOM   9248  C  CG1 . ILE D  1 27  ? 36.421  6.163   90.407  1.00 7.30   ? 114  ILE D CG1 1 
ATOM   9249  C  CG2 . ILE D  1 27  ? 34.290  6.283   88.992  1.00 9.03   ? 114  ILE D CG2 1 
ATOM   9250  C  CD1 . ILE D  1 27  ? 36.601  4.616   90.394  1.00 8.51   ? 114  ILE D CD1 1 
ATOM   9251  N  N   . GLY D  1 28  ? 32.529  8.430   91.351  1.00 7.79   ? 115  GLY D N   1 
ATOM   9252  C  CA  . GLY D  1 28  ? 31.124  8.868   91.249  1.00 8.19   ? 115  GLY D CA  1 
ATOM   9253  C  C   . GLY D  1 28  ? 30.888  10.366  91.272  1.00 8.29   ? 115  GLY D C   1 
ATOM   9254  O  O   . GLY D  1 28  ? 29.758  10.820  91.042  1.00 9.04   ? 115  GLY D O   1 
ATOM   9255  N  N   . GLU D  1 29  ? 31.940  11.134  91.543  1.00 8.48   ? 116  GLU D N   1 
ATOM   9256  C  CA  . GLU D  1 29  ? 31.881  12.602  91.436  1.00 9.93   ? 116  GLU D CA  1 
ATOM   9257  C  C   . GLU D  1 29  ? 31.587  13.007  89.981  1.00 10.57  ? 116  GLU D C   1 
ATOM   9258  O  O   . GLU D  1 29  ? 30.998  14.057  89.729  1.00 10.18  ? 116  GLU D O   1 
ATOM   9259  C  CB  . GLU D  1 29  ? 33.183  13.245  91.977  1.00 9.50   ? 116  GLU D CB  1 
ATOM   9260  C  CG  . GLU D  1 29  ? 33.170  14.789  92.074  1.00 10.09  ? 116  GLU D CG  1 
ATOM   9261  C  CD  . GLU D  1 29  ? 33.440  15.512  90.724  1.00 10.30  ? 116  GLU D CD  1 
ATOM   9262  O  OE1 . GLU D  1 29  ? 32.860  16.590  90.500  1.00 10.56  ? 116  GLU D OE1 1 
ATOM   9263  O  OE2 . GLU D  1 29  ? 34.214  15.000  89.894  1.00 9.76   ? 116  GLU D OE2 1 
ATOM   9264  N  N   . ASP D  1 30  ? 31.989  12.168  89.023  1.00 11.39  ? 117  ASP D N   1 
ATOM   9265  C  CA  . ASP D  1 30  ? 31.755  12.483  87.610  1.00 13.76  ? 117  ASP D CA  1 
ATOM   9266  C  C   . ASP D  1 30  ? 31.057  11.344  86.817  1.00 13.94  ? 117  ASP D C   1 
ATOM   9267  O  O   . ASP D  1 30  ? 30.130  11.593  86.025  1.00 16.68  ? 117  ASP D O   1 
ATOM   9268  C  CB  . ASP D  1 30  ? 33.062  12.973  86.964  1.00 14.30  ? 117  ASP D CB  1 
ATOM   9269  C  CG  . ASP D  1 30  ? 32.908  13.319  85.484  1.00 19.30  ? 117  ASP D CG  1 
ATOM   9270  O  OD1 . ASP D  1 30  ? 33.693  12.781  84.630  1.00 24.79  ? 117  ASP D OD1 1 
ATOM   9271  O  OD2 . ASP D  1 30  ? 31.996  14.117  85.189  1.00 18.85  ? 117  ASP D OD2 1 
ATOM   9272  N  N   . ALA D  1 31  ? 31.418  10.099  87.082  1.00 12.93  ? 118  ALA D N   1 
ATOM   9273  C  CA  . ALA D  1 31  ? 30.826  8.958   86.385  1.00 10.58  ? 118  ALA D CA  1 
ATOM   9274  C  C   . ALA D  1 31  ? 29.466  8.574   86.992  1.00 10.41  ? 118  ALA D C   1 
ATOM   9275  O  O   . ALA D  1 31  ? 29.089  9.064   88.078  1.00 9.66   ? 118  ALA D O   1 
ATOM   9276  C  CB  . ALA D  1 31  ? 31.796  7.774   86.411  1.00 10.81  ? 118  ALA D CB  1 
ATOM   9277  N  N   . HIS D  1 32  ? 28.730  7.709   86.294  1.00 8.58   ? 119  HIS D N   1 
ATOM   9278  C  CA  . HIS D  1 32  ? 27.393  7.317   86.750  1.00 8.02   ? 119  HIS D CA  1 
ATOM   9279  C  C   . HIS D  1 32  ? 27.497  6.183   87.774  1.00 8.02   ? 119  HIS D C   1 
ATOM   9280  O  O   . HIS D  1 32  ? 27.476  5.027   87.398  1.00 7.86   ? 119  HIS D O   1 
ATOM   9281  C  CB  . HIS D  1 32  ? 26.503  6.901   85.569  1.00 8.52   ? 119  HIS D CB  1 
ATOM   9282  C  CG  . HIS D  1 32  ? 26.277  7.994   84.550  1.00 8.16   ? 119  HIS D CG  1 
ATOM   9283  N  ND1 . HIS D  1 32  ? 26.065  7.731   83.215  1.00 8.71   ? 119  HIS D ND1 1 
ATOM   9284  C  CD2 . HIS D  1 32  ? 26.260  9.345   84.672  1.00 9.28   ? 119  HIS D CD2 1 
ATOM   9285  C  CE1 . HIS D  1 32  ? 25.900  8.868   82.560  1.00 10.05  ? 119  HIS D CE1 1 
ATOM   9286  N  NE2 . HIS D  1 32  ? 26.031  9.863   83.417  1.00 7.71   ? 119  HIS D NE2 1 
ATOM   9287  N  N   . ILE D  1 33  ? 27.588  6.539   89.050  1.00 7.32   ? 120  ILE D N   1 
ATOM   9288  C  CA  . ILE D  1 33  ? 27.784  5.585   90.156  1.00 8.28   ? 120  ILE D CA  1 
ATOM   9289  C  C   . ILE D  1 33  ? 26.574  5.644   91.092  1.00 8.55   ? 120  ILE D C   1 
ATOM   9290  O  O   . ILE D  1 33  ? 26.182  6.732   91.518  1.00 8.72   ? 120  ILE D O   1 
ATOM   9291  C  CB  . ILE D  1 33  ? 29.071  5.938   90.929  1.00 7.60   ? 120  ILE D CB  1 
ATOM   9292  C  CG1 . ILE D  1 33  ? 30.281  5.854   89.981  1.00 8.48   ? 120  ILE D CG1 1 
ATOM   9293  C  CG2 . ILE D  1 33  ? 29.235  5.051   92.194  1.00 8.39   ? 120  ILE D CG2 1 
ATOM   9294  C  CD1 . ILE D  1 33  ? 30.487  4.478   89.323  1.00 7.12   ? 120  ILE D CD1 1 
ATOM   9295  N  N   . LEU D  1 34  ? 26.008  4.484   91.410  1.00 8.66   ? 121  LEU D N   1 
ATOM   9296  C  CA  . LEU D  1 34  ? 24.800  4.395   92.225  1.00 8.19   ? 121  LEU D CA  1 
ATOM   9297  C  C   . LEU D  1 34  ? 25.105  4.800   93.662  1.00 8.02   ? 121  LEU D C   1 
ATOM   9298  O  O   . LEU D  1 34  ? 26.210  4.540   94.151  1.00 8.99   ? 121  LEU D O   1 
ATOM   9299  C  CB  . LEU D  1 34  ? 24.249  2.952   92.186  1.00 7.98   ? 121  LEU D CB  1 
ATOM   9300  C  CG  . LEU D  1 34  ? 23.658  2.457   90.842  1.00 8.55   ? 121  LEU D CG  1 
ATOM   9301  C  CD1 . LEU D  1 34  ? 23.528  0.932   90.812  1.00 7.60   ? 121  LEU D CD1 1 
ATOM   9302  C  CD2 . LEU D  1 34  ? 22.292  3.110   90.517  1.00 5.25   ? 121  LEU D CD2 1 
ATOM   9303  N  N   . VAL D  1 35  ? 24.149  5.458   94.319  1.00 7.47   ? 122  VAL D N   1 
ATOM   9304  C  CA  . VAL D  1 35  ? 24.195  5.642   95.786  1.00 7.31   ? 122  VAL D CA  1 
ATOM   9305  C  C   . VAL D  1 35  ? 23.929  4.291   96.458  1.00 7.50   ? 122  VAL D C   1 
ATOM   9306  O  O   . VAL D  1 35  ? 22.969  3.572   96.110  1.00 8.21   ? 122  VAL D O   1 
ATOM   9307  C  CB  . VAL D  1 35  ? 23.173  6.700   96.274  1.00 7.80   ? 122  VAL D CB  1 
ATOM   9308  C  CG1 . VAL D  1 35  ? 23.172  6.810   97.803  1.00 7.47   ? 122  VAL D CG1 1 
ATOM   9309  C  CG2 . VAL D  1 35  ? 23.490  8.052   95.660  1.00 6.25   ? 122  VAL D CG2 1 
ATOM   9310  N  N   . THR D  1 36  ? 24.785  3.946   97.417  1.00 7.02   ? 123  THR D N   1 
ATOM   9311  C  CA  . THR D  1 36  ? 24.643  2.699   98.170  1.00 6.69   ? 123  THR D CA  1 
ATOM   9312  C  C   . THR D  1 36  ? 24.802  2.996   99.676  1.00 7.24   ? 123  THR D C   1 
ATOM   9313  O  O   . THR D  1 36  ? 25.082  4.144   100.087 1.00 7.79   ? 123  THR D O   1 
ATOM   9314  C  CB  . THR D  1 36  ? 25.693  1.671   97.701  1.00 6.53   ? 123  THR D CB  1 
ATOM   9315  O  OG1 . THR D  1 36  ? 27.005  2.211   97.918  1.00 7.68   ? 123  THR D OG1 1 
ATOM   9316  C  CG2 . THR D  1 36  ? 25.541  1.386   96.197  1.00 5.97   ? 123  THR D CG2 1 
ATOM   9317  N  N   . ARG D  1 37  ? 24.583  1.967   100.478 1.00 7.18   ? 124  ARG D N   1 
ATOM   9318  C  CA  . ARG D  1 37  ? 25.129  1.854   101.835 1.00 8.26   ? 124  ARG D CA  1 
ATOM   9319  C  C   . ARG D  1 37  ? 25.019  0.371   102.213 1.00 7.70   ? 124  ARG D C   1 
ATOM   9320  O  O   . ARG D  1 37  ? 24.488  -0.414  101.433 1.00 8.37   ? 124  ARG D O   1 
ATOM   9321  C  CB  . ARG D  1 37  ? 24.416  2.773   102.841 1.00 7.39   ? 124  ARG D CB  1 
ATOM   9322  C  CG  . ARG D  1 37  ? 25.256  3.990   103.254 1.00 8.82   ? 124  ARG D CG  1 
ATOM   9323  C  CD  . ARG D  1 37  ? 25.011  4.390   104.728 1.00 10.12  ? 124  ARG D CD  1 
ATOM   9324  N  NE  . ARG D  1 37  ? 25.591  3.371   105.603 1.00 8.79   ? 124  ARG D NE  1 
ATOM   9325  C  CZ  . ARG D  1 37  ? 25.166  3.064   106.831 1.00 10.61  ? 124  ARG D CZ  1 
ATOM   9326  N  NH1 . ARG D  1 37  ? 25.766  2.073   107.491 1.00 9.25   ? 124  ARG D NH1 1 
ATOM   9327  N  NH2 . ARG D  1 37  ? 24.155  3.738   107.399 1.00 10.36  ? 124  ARG D NH2 1 
ATOM   9328  N  N   . GLU D  1 38  ? 25.534  -0.003  103.373 1.00 7.92   ? 125  GLU D N   1 
ATOM   9329  C  CA  . GLU D  1 38  ? 25.474  -1.396  103.860 1.00 7.79   ? 125  GLU D CA  1 
ATOM   9330  C  C   . GLU D  1 38  ? 26.114  -2.398  102.889 1.00 7.80   ? 125  GLU D C   1 
ATOM   9331  O  O   . GLU D  1 38  ? 25.481  -3.387  102.507 1.00 9.47   ? 125  GLU D O   1 
ATOM   9332  C  CB  . GLU D  1 38  ? 24.023  -1.813  104.190 1.00 8.35   ? 125  GLU D CB  1 
ATOM   9333  C  CG  . GLU D  1 38  ? 23.377  -0.977  105.327 1.00 9.26   ? 125  GLU D CG  1 
ATOM   9334  C  CD  . GLU D  1 38  ? 22.712  0.310   104.841 1.00 11.08  ? 125  GLU D CD  1 
ATOM   9335  O  OE1 . GLU D  1 38  ? 22.537  1.254   105.670 1.00 10.15  ? 125  GLU D OE1 1 
ATOM   9336  O  OE2 . GLU D  1 38  ? 22.342  0.389   103.657 1.00 8.11   ? 125  GLU D OE2 1 
ATOM   9337  N  N   . PRO D  1 39  ? 27.380  -2.154  102.498 1.00 7.68   ? 126  PRO D N   1 
ATOM   9338  C  CA  . PRO D  1 39  ? 28.080  -3.011  101.556 1.00 8.05   ? 126  PRO D CA  1 
ATOM   9339  C  C   . PRO D  1 39  ? 28.640  -4.258  102.229 1.00 7.45   ? 126  PRO D C   1 
ATOM   9340  O  O   . PRO D  1 39  ? 28.678  -4.330  103.462 1.00 8.90   ? 126  PRO D O   1 
ATOM   9341  C  CB  . PRO D  1 39  ? 29.260  -2.126  101.110 1.00 6.84   ? 126  PRO D CB  1 
ATOM   9342  C  CG  . PRO D  1 39  ? 29.643  -1.428  102.370 1.00 8.38   ? 126  PRO D CG  1 
ATOM   9343  C  CD  . PRO D  1 39  ? 28.234  -1.032  102.938 1.00 7.35   ? 126  PRO D CD  1 
ATOM   9344  N  N   . TYR D  1 40  ? 29.062  -5.218  101.422 1.00 8.24   ? 127  TYR D N   1 
ATOM   9345  C  CA  . TYR D  1 40  ? 29.859  -6.331  101.883 1.00 7.42   ? 127  TYR D CA  1 
ATOM   9346  C  C   . TYR D  1 40  ? 30.519  -7.012  100.692 1.00 8.15   ? 127  TYR D C   1 
ATOM   9347  O  O   . TYR D  1 40  ? 30.399  -6.546  99.560  1.00 8.44   ? 127  TYR D O   1 
ATOM   9348  C  CB  . TYR D  1 40  ? 29.036  -7.332  102.733 1.00 8.10   ? 127  TYR D CB  1 
ATOM   9349  C  CG  . TYR D  1 40  ? 27.714  -7.819  102.171 1.00 7.97   ? 127  TYR D CG  1 
ATOM   9350  C  CD1 . TYR D  1 40  ? 26.558  -7.044  102.285 1.00 6.85   ? 127  TYR D CD1 1 
ATOM   9351  C  CD2 . TYR D  1 40  ? 27.595  -9.117  101.622 1.00 7.76   ? 127  TYR D CD2 1 
ATOM   9352  C  CE1 . TYR D  1 40  ? 25.313  -7.531  101.824 1.00 8.06   ? 127  TYR D CE1 1 
ATOM   9353  C  CE2 . TYR D  1 40  ? 26.380  -9.601  101.157 1.00 8.36   ? 127  TYR D CE2 1 
ATOM   9354  C  CZ  . TYR D  1 40  ? 25.238  -8.805  101.266 1.00 9.52   ? 127  TYR D CZ  1 
ATOM   9355  O  OH  . TYR D  1 40  ? 24.024  -9.284  100.823 1.00 9.43   ? 127  TYR D OH  1 
ATOM   9356  N  N   . LEU D  1 41  ? 31.234  -8.104  100.953 1.00 7.66   ? 128  LEU D N   1 
ATOM   9357  C  CA  . LEU D  1 41  ? 31.719  -8.951  99.865  1.00 7.43   ? 128  LEU D CA  1 
ATOM   9358  C  C   . LEU D  1 41  ? 31.311  -10.383 100.157 1.00 7.26   ? 128  LEU D C   1 
ATOM   9359  O  O   . LEU D  1 41  ? 31.131  -10.778 101.313 1.00 7.27   ? 128  LEU D O   1 
ATOM   9360  C  CB  . LEU D  1 41  ? 33.252  -8.925  99.746  1.00 7.25   ? 128  LEU D CB  1 
ATOM   9361  C  CG  . LEU D  1 41  ? 34.226  -7.745  99.543  1.00 10.78  ? 128  LEU D CG  1 
ATOM   9362  C  CD1 . LEU D  1 41  ? 34.937  -7.740  98.177  1.00 12.53  ? 128  LEU D CD1 1 
ATOM   9363  C  CD2 . LEU D  1 41  ? 33.851  -6.371  100.080 1.00 7.26   ? 128  LEU D CD2 1 
ATOM   9364  N  N   . SER D  1 42  ? 31.186  -11.160 99.094  1.00 7.85   ? 129  SER D N   1 
ATOM   9365  C  CA  . SER D  1 42  ? 30.933  -12.587 99.216  1.00 8.74   ? 129  SER D CA  1 
ATOM   9366  C  C   . SER D  1 42  ? 31.576  -13.274 98.020  1.00 9.73   ? 129  SER D C   1 
ATOM   9367  O  O   . SER D  1 42  ? 31.554  -12.736 96.896  1.00 10.05  ? 129  SER D O   1 
ATOM   9368  C  CB  . SER D  1 42  ? 29.424  -12.834 99.260  1.00 8.16   ? 129  SER D CB  1 
ATOM   9369  O  OG  . SER D  1 42  ? 29.142  -14.181 99.556  1.00 8.65   ? 129  SER D OG  1 
ATOM   9370  N  N   . CYS D  1 43  ? 32.155  -14.451 98.262  1.00 10.83  ? 130  CYS D N   1 
ATOM   9371  C  CA  . CYS D  1 43  ? 32.843  -15.211 97.211  1.00 11.66  ? 130  CYS D CA  1 
ATOM   9372  C  C   . CYS D  1 43  ? 32.063  -16.448 96.779  1.00 12.40  ? 130  CYS D C   1 
ATOM   9373  O  O   . CYS D  1 43  ? 31.044  -16.803 97.381  1.00 11.34  ? 130  CYS D O   1 
ATOM   9374  C  CB  . CYS D  1 43  ? 34.238  -15.623 97.683  1.00 12.70  ? 130  CYS D CB  1 
ATOM   9375  S  SG  . CYS D  1 43  ? 35.134  -14.202 98.368  1.00 14.08  ? 130  CYS D SG  1 
ATOM   9376  N  N   . ASP D  1 44  ? 32.570  -17.082 95.719  1.00 12.38  ? 131  ASP D N   1 
ATOM   9377  C  CA  . ASP D  1 44  ? 32.037  -18.316 95.174  1.00 13.28  ? 131  ASP D CA  1 
ATOM   9378  C  C   . ASP D  1 44  ? 33.210  -19.065 94.513  1.00 13.09  ? 131  ASP D C   1 
ATOM   9379  O  O   . ASP D  1 44  ? 34.346  -18.587 94.565  1.00 13.21  ? 131  ASP D O   1 
ATOM   9380  C  CB  . ASP D  1 44  ? 30.848  -18.051 94.223  1.00 12.27  ? 131  ASP D CB  1 
ATOM   9381  C  CG  . ASP D  1 44  ? 31.226  -17.247 92.980  1.00 16.31  ? 131  ASP D CG  1 
ATOM   9382  O  OD1 . ASP D  1 44  ? 30.385  -16.453 92.524  1.00 20.62  ? 131  ASP D OD1 1 
ATOM   9383  O  OD2 . ASP D  1 44  ? 32.330  -17.400 92.441  1.00 19.07  ? 131  ASP D OD2 1 
ATOM   9384  N  N   . PRO D  1 45  ? 32.962  -20.265 93.948  1.00 13.46  ? 132  PRO D N   1 
ATOM   9385  C  CA  . PRO D  1 45  ? 34.075  -20.975 93.322  1.00 14.03  ? 132  PRO D CA  1 
ATOM   9386  C  C   . PRO D  1 45  ? 34.834  -20.180 92.240  1.00 14.33  ? 132  PRO D C   1 
ATOM   9387  O  O   . PRO D  1 45  ? 36.009  -20.435 92.010  1.00 14.18  ? 132  PRO D O   1 
ATOM   9388  C  CB  . PRO D  1 45  ? 33.396  -22.231 92.731  1.00 13.73  ? 132  PRO D CB  1 
ATOM   9389  C  CG  . PRO D  1 45  ? 32.220  -22.472 93.652  1.00 14.61  ? 132  PRO D CG  1 
ATOM   9390  C  CD  . PRO D  1 45  ? 31.716  -21.055 93.911  1.00 13.45  ? 132  PRO D CD  1 
ATOM   9391  N  N   . GLN D  1 46  ? 34.180  -19.228 91.588  1.00 15.25  ? 133  GLN D N   1 
ATOM   9392  C  CA  . GLN D  1 46  ? 34.830  -18.462 90.504  1.00 16.87  ? 133  GLN D CA  1 
ATOM   9393  C  C   . GLN D  1 46  ? 35.632  -17.240 91.010  1.00 16.88  ? 133  GLN D C   1 
ATOM   9394  O  O   . GLN D  1 46  ? 36.527  -16.742 90.318  1.00 17.27  ? 133  GLN D O   1 
ATOM   9395  C  CB  . GLN D  1 46  ? 33.788  -18.023 89.472  1.00 17.34  ? 133  GLN D CB  1 
ATOM   9396  C  CG  . GLN D  1 46  ? 33.373  -19.088 88.458  1.00 21.06  ? 133  GLN D CG  1 
ATOM   9397  C  CD  . GLN D  1 46  ? 32.908  -20.404 89.073  1.00 27.08  ? 133  GLN D CD  1 
ATOM   9398  O  OE1 . GLN D  1 46  ? 31.827  -20.486 89.668  1.00 30.68  ? 133  GLN D OE1 1 
ATOM   9399  N  NE2 . GLN D  1 46  ? 33.726  -21.451 88.918  1.00 29.09  ? 133  GLN D NE2 1 
ATOM   9400  N  N   . GLY D  1 47  ? 35.319  -16.762 92.213  1.00 16.74  ? 134  GLY D N   1 
ATOM   9401  C  CA  . GLY D  1 47  ? 35.998  -15.571 92.762  1.00 16.55  ? 134  GLY D CA  1 
ATOM   9402  C  C   . GLY D  1 47  ? 35.129  -14.828 93.761  1.00 16.12  ? 134  GLY D C   1 
ATOM   9403  O  O   . GLY D  1 47  ? 34.309  -15.451 94.423  1.00 16.07  ? 134  GLY D O   1 
ATOM   9404  N  N   . CYS D  1 48  ? 35.316  -13.509 93.870  1.00 14.30  ? 135  CYS D N   1 
ATOM   9405  C  CA  . CYS D  1 48  ? 34.601  -12.699 94.863  1.00 12.95  ? 135  CYS D CA  1 
ATOM   9406  C  C   . CYS D  1 48  ? 33.938  -11.492 94.216  1.00 12.15  ? 135  CYS D C   1 
ATOM   9407  O  O   . CYS D  1 48  ? 34.430  -10.968 93.214  1.00 11.49  ? 135  CYS D O   1 
ATOM   9408  C  CB  . CYS D  1 48  ? 35.543  -12.243 95.988  1.00 13.17  ? 135  CYS D CB  1 
ATOM   9409  S  SG  . CYS D  1 48  ? 36.401  -13.617 96.881  1.00 15.87  ? 135  CYS D SG  1 
ATOM   9410  N  N   . ARG D  1 49  ? 32.829  -11.052 94.812  1.00 10.41  ? 136  ARG D N   1 
ATOM   9411  C  CA  . ARG D  1 49  ? 32.045  -9.943  94.296  1.00 9.35   ? 136  ARG D CA  1 
ATOM   9412  C  C   . ARG D  1 49  ? 31.734  -8.978  95.428  1.00 8.67   ? 136  ARG D C   1 
ATOM   9413  O  O   . ARG D  1 49  ? 31.712  -9.389  96.595  1.00 7.50   ? 136  ARG D O   1 
ATOM   9414  C  CB  . ARG D  1 49  ? 30.740  -10.479 93.717  1.00 10.26  ? 136  ARG D CB  1 
ATOM   9415  C  CG  . ARG D  1 49  ? 30.929  -11.082 92.332  1.00 10.32  ? 136  ARG D CG  1 
ATOM   9416  C  CD  . ARG D  1 49  ? 29.667  -11.822 91.914  1.00 12.00  ? 136  ARG D CD  1 
ATOM   9417  N  NE  . ARG D  1 49  ? 28.559  -10.939 91.531  1.00 10.34  ? 136  ARG D NE  1 
ATOM   9418  C  CZ  . ARG D  1 49  ? 28.521  -10.249 90.391  1.00 11.93  ? 136  ARG D CZ  1 
ATOM   9419  N  NH1 . ARG D  1 49  ? 27.465  -9.498  90.087  1.00 9.86   ? 136  ARG D NH1 1 
ATOM   9420  N  NH2 . ARG D  1 49  ? 29.538  -10.315 89.541  1.00 9.56   ? 136  ARG D NH2 1 
ATOM   9421  N  N   . MET D  1 50  ? 31.542  -7.699  95.096  1.00 7.82   ? 137  MET D N   1 
ATOM   9422  C  CA  . MET D  1 50  ? 31.081  -6.708  96.070  1.00 7.78   ? 137  MET D CA  1 
ATOM   9423  C  C   . MET D  1 50  ? 29.547  -6.674  96.031  1.00 7.75   ? 137  MET D C   1 
ATOM   9424  O  O   . MET D  1 50  ? 28.967  -6.937  94.968  1.00 8.32   ? 137  MET D O   1 
ATOM   9425  C  CB  . MET D  1 50  ? 31.639  -5.331  95.732  1.00 7.09   ? 137  MET D CB  1 
ATOM   9426  C  CG  . MET D  1 50  ? 33.089  -5.188  96.121  1.00 8.42   ? 137  MET D CG  1 
ATOM   9427  S  SD  . MET D  1 50  ? 33.893  -3.738  95.435  1.00 9.42   ? 137  MET D SD  1 
ATOM   9428  C  CE  . MET D  1 50  ? 35.394  -3.741  96.411  1.00 7.98   ? 137  MET D CE  1 
ATOM   9429  N  N   . PHE D  1 51  ? 28.926  -6.371  97.183  1.00 7.38   ? 138  PHE D N   1 
ATOM   9430  C  CA  . PHE D  1 51  ? 27.464  -6.295  97.366  1.00 7.27   ? 138  PHE D CA  1 
ATOM   9431  C  C   . PHE D  1 51  ? 27.143  -4.998  98.121  1.00 7.66   ? 138  PHE D C   1 
ATOM   9432  O  O   . PHE D  1 51  ? 27.963  -4.531  98.915  1.00 7.98   ? 138  PHE D O   1 
ATOM   9433  C  CB  . PHE D  1 51  ? 26.969  -7.496  98.223  1.00 7.13   ? 138  PHE D CB  1 
ATOM   9434  C  CG  . PHE D  1 51  ? 27.016  -8.832  97.510  1.00 6.98   ? 138  PHE D CG  1 
ATOM   9435  C  CD1 . PHE D  1 51  ? 28.235  -9.479  97.286  1.00 9.76   ? 138  PHE D CD1 1 
ATOM   9436  C  CD2 . PHE D  1 51  ? 25.842  -9.458  97.089  1.00 8.35   ? 138  PHE D CD2 1 
ATOM   9437  C  CE1 . PHE D  1 51  ? 28.293  -10.723 96.629  1.00 9.55   ? 138  PHE D CE1 1 
ATOM   9438  C  CE2 . PHE D  1 51  ? 25.883  -10.723 96.438  1.00 9.58   ? 138  PHE D CE2 1 
ATOM   9439  C  CZ  . PHE D  1 51  ? 27.112  -11.347 96.202  1.00 8.67   ? 138  PHE D CZ  1 
ATOM   9440  N  N   . ALA D  1 52  ? 25.951  -4.428  97.903  1.00 7.32   ? 139  ALA D N   1 
ATOM   9441  C  CA  . ALA D  1 52  ? 25.490  -3.300  98.723  1.00 7.44   ? 139  ALA D CA  1 
ATOM   9442  C  C   . ALA D  1 52  ? 24.026  -3.044  98.435  1.00 7.85   ? 139  ALA D C   1 
ATOM   9443  O  O   . ALA D  1 52  ? 23.465  -3.569  97.455  1.00 6.98   ? 139  ALA D O   1 
ATOM   9444  C  CB  . ALA D  1 52  ? 26.304  -2.030  98.413  1.00 7.28   ? 139  ALA D CB  1 
ATOM   9445  N  N   . LEU D  1 53  ? 23.413  -2.244  99.287  1.00 6.94   ? 140  LEU D N   1 
ATOM   9446  C  CA  . LEU D  1 53  ? 22.035  -1.837  99.055  1.00 7.48   ? 140  LEU D CA  1 
ATOM   9447  C  C   . LEU D  1 53  ? 22.018  -0.527  98.280  1.00 7.60   ? 140  LEU D C   1 
ATOM   9448  O  O   . LEU D  1 53  ? 22.360  0.532   98.816  1.00 8.42   ? 140  LEU D O   1 
ATOM   9449  C  CB  . LEU D  1 53  ? 21.285  -1.675  100.380 1.00 7.78   ? 140  LEU D CB  1 
ATOM   9450  C  CG  . LEU D  1 53  ? 21.095  -2.952  101.204 1.00 7.07   ? 140  LEU D CG  1 
ATOM   9451  C  CD1 . LEU D  1 53  ? 20.474  -2.608  102.564 1.00 6.25   ? 140  LEU D CD1 1 
ATOM   9452  C  CD2 . LEU D  1 53  ? 20.240  -3.951  100.435 1.00 6.57   ? 140  LEU D CD2 1 
ATOM   9453  N  N   . SER D  1 54  ? 21.642  -0.612  97.008  1.00 7.28   ? 141  SER D N   1 
ATOM   9454  C  CA  . SER D  1 54  ? 21.440  0.588   96.184  1.00 7.55   ? 141  SER D CA  1 
ATOM   9455  C  C   . SER D  1 54  ? 20.313  1.448   96.751  1.00 7.59   ? 141  SER D C   1 
ATOM   9456  O  O   . SER D  1 54  ? 19.432  0.919   97.443  1.00 7.22   ? 141  SER D O   1 
ATOM   9457  C  CB  . SER D  1 54  ? 21.098  0.207   94.750  1.00 6.95   ? 141  SER D CB  1 
ATOM   9458  O  OG  . SER D  1 54  ? 20.933  1.387   93.988  1.00 8.73   ? 141  SER D OG  1 
ATOM   9459  N  N   . GLN D  1 55  ? 20.355  2.756   96.449  1.00 7.29   ? 142  GLN D N   1 
ATOM   9460  C  CA  . GLN D  1 55  ? 19.263  3.676   96.785  1.00 8.16   ? 142  GLN D CA  1 
ATOM   9461  C  C   . GLN D  1 55  ? 18.434  4.010   95.548  1.00 7.77   ? 142  GLN D C   1 
ATOM   9462  O  O   . GLN D  1 55  ? 17.512  4.810   95.613  1.00 7.77   ? 142  GLN D O   1 
ATOM   9463  C  CB  . GLN D  1 55  ? 19.783  4.960   97.462  1.00 8.13   ? 142  GLN D CB  1 
ATOM   9464  C  CG  . GLN D  1 55  ? 20.300  4.722   98.879  1.00 8.36   ? 142  GLN D CG  1 
ATOM   9465  C  CD  . GLN D  1 55  ? 19.200  4.770   99.965  1.00 8.28   ? 142  GLN D CD  1 
ATOM   9466  O  OE1 . GLN D  1 55  ? 17.982  4.682   99.684  1.00 9.51   ? 142  GLN D OE1 1 
ATOM   9467  N  NE2 . GLN D  1 55  ? 19.639  4.887   101.216 1.00 8.26   ? 142  GLN D NE2 1 
ATOM   9468  N  N   . GLY D  1 56  ? 18.765  3.367   94.427  1.00 7.79   ? 143  GLY D N   1 
ATOM   9469  C  CA  . GLY D  1 56  ? 18.006  3.556   93.197  1.00 8.01   ? 143  GLY D CA  1 
ATOM   9470  C  C   . GLY D  1 56  ? 18.173  4.943   92.616  1.00 7.81   ? 143  GLY D C   1 
ATOM   9471  O  O   . GLY D  1 56  ? 17.211  5.546   92.153  1.00 7.62   ? 143  GLY D O   1 
ATOM   9472  N  N   . THR D  1 57  ? 19.411  5.434   92.641  1.00 8.37   ? 144  THR D N   1 
ATOM   9473  C  CA  . THR D  1 57  ? 19.769  6.731   92.088  1.00 9.21   ? 144  THR D CA  1 
ATOM   9474  C  C   . THR D  1 57  ? 21.281  6.802   91.956  1.00 8.92   ? 144  THR D C   1 
ATOM   9475  O  O   . THR D  1 57  ? 21.992  6.094   92.665  1.00 9.10   ? 144  THR D O   1 
ATOM   9476  C  CB  . THR D  1 57  ? 19.272  7.909   93.001  1.00 9.49   ? 144  THR D CB  1 
ATOM   9477  O  OG1 . THR D  1 57  ? 19.689  9.150   92.438  1.00 10.94  ? 144  THR D OG1 1 
ATOM   9478  C  CG2 . THR D  1 57  ? 19.814  7.769   94.468  1.00 8.74   ? 144  THR D CG2 1 
ATOM   9479  N  N   . THR D  1 58  ? 21.772  7.658   91.066  1.00 8.75   ? 145  THR D N   1 
ATOM   9480  C  CA  . THR D  1 58  ? 23.213  7.941   91.029  1.00 8.10   ? 145  THR D CA  1 
ATOM   9481  C  C   . THR D  1 58  ? 23.588  9.012   92.066  1.00 7.85   ? 145  THR D C   1 
ATOM   9482  O  O   . THR D  1 58  ? 22.731  9.752   92.569  1.00 7.32   ? 145  THR D O   1 
ATOM   9483  C  CB  . THR D  1 58  ? 23.681  8.426   89.654  1.00 8.60   ? 145  THR D CB  1 
ATOM   9484  O  OG1 . THR D  1 58  ? 22.976  9.631   89.323  1.00 9.77   ? 145  THR D OG1 1 
ATOM   9485  C  CG2 . THR D  1 58  ? 23.399  7.347   88.594  1.00 8.81   ? 145  THR D CG2 1 
ATOM   9486  N  N   . LEU D  1 59  ? 24.879  9.084   92.361  1.00 7.47   ? 146  LEU D N   1 
ATOM   9487  C  CA  . LEU D  1 59  ? 25.403  9.958   93.395  1.00 8.33   ? 146  LEU D CA  1 
ATOM   9488  C  C   . LEU D  1 59  ? 25.273  11.449  93.017  1.00 8.57   ? 146  LEU D C   1 
ATOM   9489  O  O   . LEU D  1 59  ? 24.920  12.264  93.867  1.00 8.80   ? 146  LEU D O   1 
ATOM   9490  C  CB  . LEU D  1 59  ? 26.869  9.579   93.688  1.00 7.62   ? 146  LEU D CB  1 
ATOM   9491  C  CG  . LEU D  1 59  ? 27.587  10.378  94.766  1.00 8.35   ? 146  LEU D CG  1 
ATOM   9492  C  CD1 . LEU D  1 59  ? 26.966  10.100  96.145  1.00 7.70   ? 146  LEU D CD1 1 
ATOM   9493  C  CD2 . LEU D  1 59  ? 29.106  10.051  94.771  1.00 7.50   ? 146  LEU D CD2 1 
ATOM   9494  N  N   . ARG D  1 60  ? 25.560  11.794  91.755  1.00 9.31   ? 147  ARG D N   1 
ATOM   9495  C  CA  . ARG D  1 60  ? 25.374  13.179  91.265  1.00 8.65   ? 147  ARG D CA  1 
ATOM   9496  C  C   . ARG D  1 60  ? 23.935  13.519  90.887  1.00 9.02   ? 147  ARG D C   1 
ATOM   9497  O  O   . ARG D  1 60  ? 23.600  14.688  90.600  1.00 9.38   ? 147  ARG D O   1 
ATOM   9498  C  CB  . ARG D  1 60  ? 26.275  13.446  90.046  1.00 9.53   ? 147  ARG D CB  1 
ATOM   9499  C  CG  . ARG D  1 60  ? 27.733  13.768  90.395  1.00 7.53   ? 147  ARG D CG  1 
ATOM   9500  C  CD  . ARG D  1 60  ? 27.836  14.882  91.452  1.00 9.18   ? 147  ARG D CD  1 
ATOM   9501  N  NE  . ARG D  1 60  ? 29.132  15.571  91.402  1.00 10.00  ? 147  ARG D NE  1 
ATOM   9502  C  CZ  . ARG D  1 60  ? 29.366  16.749  91.986  1.00 10.57  ? 147  ARG D CZ  1 
ATOM   9503  N  NH1 . ARG D  1 60  ? 28.392  17.342  92.682  1.00 11.57  ? 147  ARG D NH1 1 
ATOM   9504  N  NH2 . ARG D  1 60  ? 30.564  17.329  91.889  1.00 8.54   ? 147  ARG D NH2 1 
ATOM   9505  N  N   . GLY D  1 61  ? 23.072  12.514  90.883  1.00 9.29   ? 148  GLY D N   1 
ATOM   9506  C  CA  . GLY D  1 61  ? 21.684  12.730  90.453  1.00 9.96   ? 148  GLY D CA  1 
ATOM   9507  C  C   . GLY D  1 61  ? 20.905  13.524  91.487  1.00 9.59   ? 148  GLY D C   1 
ATOM   9508  O  O   . GLY D  1 61  ? 21.246  13.530  92.690  1.00 9.54   ? 148  GLY D O   1 
ATOM   9509  N  N   . ARG D  1 62  ? 19.854  14.201  91.042  1.00 9.88   ? 149  ARG D N   1 
ATOM   9510  C  CA  . ARG D  1 62  ? 19.037  14.975  91.986  1.00 10.01  ? 149  ARG D CA  1 
ATOM   9511  C  C   . ARG D  1 62  ? 18.367  14.097  93.045  1.00 10.36  ? 149  ARG D C   1 
ATOM   9512  O  O   . ARG D  1 62  ? 18.088  14.571  94.160  1.00 9.66   ? 149  ARG D O   1 
ATOM   9513  C  CB  . ARG D  1 62  ? 18.040  15.877  91.242  1.00 10.10  ? 149  ARG D CB  1 
ATOM   9514  C  CG  . ARG D  1 62  ? 18.716  17.105  90.708  1.00 12.83  ? 149  ARG D CG  1 
ATOM   9515  C  CD  . ARG D  1 62  ? 17.822  17.954  89.809  1.00 18.10  ? 149  ARG D CD  1 
ATOM   9516  N  NE  . ARG D  1 62  ? 18.592  19.094  89.317  1.00 19.77  ? 149  ARG D NE  1 
ATOM   9517  C  CZ  . ARG D  1 62  ? 18.255  19.874  88.295  1.00 22.95  ? 149  ARG D CZ  1 
ATOM   9518  N  NH1 . ARG D  1 62  ? 17.122  19.679  87.620  1.00 21.18  ? 149  ARG D NH1 1 
ATOM   9519  N  NH2 . ARG D  1 62  ? 19.063  20.875  87.958  1.00 21.70  ? 149  ARG D NH2 1 
ATOM   9520  N  N   . HIS D  1 63  ? 18.159  12.807  92.720  1.00 9.85   ? 150  HIS D N   1 
ATOM   9521  C  CA  . HIS D  1 63  ? 17.514  11.859  93.650  1.00 9.74   ? 150  HIS D CA  1 
ATOM   9522  C  C   . HIS D  1 63  ? 18.442  11.362  94.789  1.00 9.34   ? 150  HIS D C   1 
ATOM   9523  O  O   . HIS D  1 63  ? 17.995  10.649  95.685  1.00 8.35   ? 150  HIS D O   1 
ATOM   9524  C  CB  . HIS D  1 63  ? 16.833  10.692  92.908  1.00 9.33   ? 150  HIS D CB  1 
ATOM   9525  C  CG  . HIS D  1 63  ? 15.772  11.124  91.927  1.00 9.09   ? 150  HIS D CG  1 
ATOM   9526  N  ND1 . HIS D  1 63  ? 14.471  11.404  92.296  1.00 12.52  ? 150  HIS D ND1 1 
ATOM   9527  C  CD2 . HIS D  1 63  ? 15.826  11.321  90.590  1.00 5.93   ? 150  HIS D CD2 1 
ATOM   9528  C  CE1 . HIS D  1 63  ? 13.770  11.739  91.223  1.00 7.82   ? 150  HIS D CE1 1 
ATOM   9529  N  NE2 . HIS D  1 63  ? 14.571  11.710  90.178  1.00 9.63   ? 150  HIS D NE2 1 
ATOM   9530  N  N   . ALA D  1 64  ? 19.718  11.757  94.751  1.00 9.64   ? 151  ALA D N   1 
ATOM   9531  C  CA  . ALA D  1 64  ? 20.631  11.463  95.856  1.00 9.78   ? 151  ALA D CA  1 
ATOM   9532  C  C   . ALA D  1 64  ? 20.210  12.272  97.091  1.00 10.05  ? 151  ALA D C   1 
ATOM   9533  O  O   . ALA D  1 64  ? 20.556  11.945  98.219  1.00 9.61   ? 151  ALA D O   1 
ATOM   9534  C  CB  . ALA D  1 64  ? 22.065  11.769  95.464  1.00 9.80   ? 151  ALA D CB  1 
ATOM   9535  N  N   . ASN D  1 65  ? 19.429  13.326  96.858  1.00 10.07  ? 152  ASN D N   1 
ATOM   9536  C  CA  . ASN D  1 65  ? 18.917  14.159  97.937  1.00 10.81  ? 152  ASN D CA  1 
ATOM   9537  C  C   . ASN D  1 65  ? 17.928  13.347  98.800  1.00 10.44  ? 152  ASN D C   1 
ATOM   9538  O  O   . ASN D  1 65  ? 16.929  12.789  98.298  1.00 10.84  ? 152  ASN D O   1 
ATOM   9539  C  CB  . ASN D  1 65  ? 18.300  15.413  97.332  1.00 10.35  ? 152  ASN D CB  1 
ATOM   9540  C  CG  . ASN D  1 65  ? 17.613  16.277  98.343  1.00 11.42  ? 152  ASN D CG  1 
ATOM   9541  O  OD1 . ASN D  1 65  ? 17.839  16.188  99.558  1.00 10.25  ? 152  ASN D OD1 1 
ATOM   9542  N  ND2 . ASN D  1 65  ? 16.710  17.101  97.842  1.00 13.84  ? 152  ASN D ND2 1 
ATOM   9543  N  N   . GLY D  1 66  ? 18.258  13.196  100.083 1.00 10.26  ? 153  GLY D N   1 
ATOM   9544  C  CA  . GLY D  1 66  ? 17.398  12.434  101.002 1.00 10.17  ? 153  GLY D CA  1 
ATOM   9545  C  C   . GLY D  1 66  ? 17.868  11.005  101.291 1.00 10.21  ? 153  GLY D C   1 
ATOM   9546  O  O   . GLY D  1 66  ? 17.225  10.277  102.052 1.00 11.13  ? 153  GLY D O   1 
ATOM   9547  N  N   . THR D  1 67  ? 18.986  10.589  100.696 1.00 10.13  ? 154  THR D N   1 
ATOM   9548  C  CA  . THR D  1 67  ? 19.442  9.197   100.842 1.00 10.44  ? 154  THR D CA  1 
ATOM   9549  C  C   . THR D  1 67  ? 20.056  8.834   102.219 1.00 10.67  ? 154  THR D C   1 
ATOM   9550  O  O   . THR D  1 67  ? 20.517  7.708   102.409 1.00 10.80  ? 154  THR D O   1 
ATOM   9551  C  CB  . THR D  1 67  ? 20.390  8.770   99.686  1.00 10.30  ? 154  THR D CB  1 
ATOM   9552  O  OG1 . THR D  1 67  ? 21.429  9.742   99.531  1.00 11.01  ? 154  THR D OG1 1 
ATOM   9553  C  CG2 . THR D  1 67  ? 19.598  8.661   98.375  1.00 7.70   ? 154  THR D CG2 1 
ATOM   9554  N  N   . ILE D  1 68  ? 20.050  9.764   103.175 1.00 11.19  ? 155  ILE D N   1 
ATOM   9555  C  CA  . ILE D  1 68  ? 20.253  9.355   104.577 1.00 12.28  ? 155  ILE D CA  1 
ATOM   9556  C  C   . ILE D  1 68  ? 19.178  8.331   105.009 1.00 12.45  ? 155  ILE D C   1 
ATOM   9557  O  O   . ILE D  1 68  ? 19.449  7.436   105.834 1.00 12.78  ? 155  ILE D O   1 
ATOM   9558  C  CB  . ILE D  1 68  ? 20.317  10.542  105.592 1.00 12.07  ? 155  ILE D CB  1 
ATOM   9559  C  CG1 . ILE D  1 68  ? 20.973  10.030  106.907 1.00 13.81  ? 155  ILE D CG1 1 
ATOM   9560  C  CG2 . ILE D  1 68  ? 18.893  11.178  105.774 1.00 12.08  ? 155  ILE D CG2 1 
ATOM   9561  C  CD1 . ILE D  1 68  ? 21.335  11.073  107.970 1.00 14.18  ? 155  ILE D CD1 1 
ATOM   9562  N  N   . HIS D  1 69  ? 17.986  8.458   104.421 1.00 12.34  ? 156  HIS D N   1 
ATOM   9563  C  CA  . HIS D  1 69  ? 16.829  7.611   104.735 1.00 12.62  ? 156  HIS D CA  1 
ATOM   9564  C  C   . HIS D  1 69  ? 17.164  6.126   104.454 1.00 12.31  ? 156  HIS D C   1 
ATOM   9565  O  O   . HIS D  1 69  ? 17.661  5.786   103.365 1.00 11.95  ? 156  HIS D O   1 
ATOM   9566  C  CB  . HIS D  1 69  ? 15.614  8.099   103.926 1.00 12.85  ? 156  HIS D CB  1 
ATOM   9567  C  CG  . HIS D  1 69  ? 14.303  7.505   104.347 1.00 15.83  ? 156  HIS D CG  1 
ATOM   9568  N  ND1 . HIS D  1 69  ? 13.659  7.865   105.511 1.00 19.86  ? 156  HIS D ND1 1 
ATOM   9569  C  CD2 . HIS D  1 69  ? 13.490  6.614   103.731 1.00 16.60  ? 156  HIS D CD2 1 
ATOM   9570  C  CE1 . HIS D  1 69  ? 12.527  7.187   105.615 1.00 19.89  ? 156  HIS D CE1 1 
ATOM   9571  N  NE2 . HIS D  1 69  ? 12.399  6.425   104.544 1.00 18.86  ? 156  HIS D NE2 1 
ATOM   9572  N  N   . ASP D  1 70  ? 16.899  5.266   105.437 1.00 11.77  ? 157  ASP D N   1 
ATOM   9573  C  CA  . ASP D  1 70  ? 17.291  3.836   105.370 1.00 11.93  ? 157  ASP D CA  1 
ATOM   9574  C  C   . ASP D  1 70  ? 16.387  2.933   104.534 1.00 11.61  ? 157  ASP D C   1 
ATOM   9575  O  O   . ASP D  1 70  ? 16.861  1.949   103.961 1.00 11.43  ? 157  ASP D O   1 
ATOM   9576  C  CB  . ASP D  1 70  ? 17.371  3.230   106.775 1.00 12.20  ? 157  ASP D CB  1 
ATOM   9577  C  CG  . ASP D  1 70  ? 18.467  3.832   107.623 1.00 13.34  ? 157  ASP D CG  1 
ATOM   9578  O  OD1 . ASP D  1 70  ? 19.621  3.906   107.180 1.00 12.46  ? 157  ASP D OD1 1 
ATOM   9579  O  OD2 . ASP D  1 70  ? 18.170  4.194   108.780 1.00 20.64  ? 157  ASP D OD2 1 
ATOM   9580  N  N   . ARG D  1 71  ? 15.088  3.220   104.498 1.00 11.13  ? 158  ARG D N   1 
ATOM   9581  C  CA  . ARG D  1 71  ? 14.146  2.265   103.940 1.00 11.43  ? 158  ARG D CA  1 
ATOM   9582  C  C   . ARG D  1 71  ? 13.222  2.931   102.936 1.00 11.46  ? 158  ARG D C   1 
ATOM   9583  O  O   . ARG D  1 71  ? 12.538  3.912   103.260 1.00 11.51  ? 158  ARG D O   1 
ATOM   9584  C  CB  . ARG D  1 71  ? 13.347  1.545   105.047 1.00 11.31  ? 158  ARG D CB  1 
ATOM   9585  C  CG  . ARG D  1 71  ? 14.192  0.632   105.940 1.00 11.44  ? 158  ARG D CG  1 
ATOM   9586  C  CD  . ARG D  1 71  ? 13.416  0.049   107.124 1.00 12.54  ? 158  ARG D CD  1 
ATOM   9587  N  NE  . ARG D  1 71  ? 12.884  1.088   108.005 1.00 12.14  ? 158  ARG D NE  1 
ATOM   9588  C  CZ  . ARG D  1 71  ? 13.586  1.765   108.916 1.00 13.54  ? 158  ARG D CZ  1 
ATOM   9589  N  NH1 . ARG D  1 71  ? 14.873  1.517   109.130 1.00 12.60  ? 158  ARG D NH1 1 
ATOM   9590  N  NH2 . ARG D  1 71  ? 12.986  2.701   109.640 1.00 14.00  ? 158  ARG D NH2 1 
ATOM   9591  N  N   . SER D  1 72  ? 13.205  2.384   101.718 1.00 10.69  ? 159  SER D N   1 
ATOM   9592  C  CA  . SER D  1 72  ? 12.327  2.885   100.657 1.00 9.76   ? 159  SER D CA  1 
ATOM   9593  C  C   . SER D  1 72  ? 12.024  1.763   99.672  1.00 9.66   ? 159  SER D C   1 
ATOM   9594  O  O   . SER D  1 72  ? 12.705  0.732   99.694  1.00 9.08   ? 159  SER D O   1 
ATOM   9595  C  CB  . SER D  1 72  ? 12.987  4.070   99.940  1.00 9.42   ? 159  SER D CB  1 
ATOM   9596  O  OG  . SER D  1 72  ? 13.829  3.632   98.879  1.00 11.43  ? 159  SER D OG  1 
ATOM   9597  N  N   . PRO D  1 73  ? 11.001  1.951   98.814  1.00 9.12   ? 160  PRO D N   1 
ATOM   9598  C  CA  . PRO D  1 73  ? 10.706  0.963   97.778  1.00 8.92   ? 160  PRO D CA  1 
ATOM   9599  C  C   . PRO D  1 73  ? 11.689  1.018   96.605  1.00 8.79   ? 160  PRO D C   1 
ATOM   9600  O  O   . PRO D  1 73  ? 11.491  0.285   95.638  1.00 9.30   ? 160  PRO D O   1 
ATOM   9601  C  CB  . PRO D  1 73  ? 9.306   1.389   97.268  1.00 8.92   ? 160  PRO D CB  1 
ATOM   9602  C  CG  . PRO D  1 73  ? 8.798   2.395   98.261  1.00 8.58   ? 160  PRO D CG  1 
ATOM   9603  C  CD  . PRO D  1 73  ? 10.030  3.067   98.781  1.00 8.88   ? 160  PRO D CD  1 
ATOM   9604  N  N   . PHE D  1 74  ? 12.707  1.887   96.680  1.00 8.38   ? 161  PHE D N   1 
ATOM   9605  C  CA  . PHE D  1 74  ? 13.666  2.120   95.579  1.00 7.97   ? 161  PHE D CA  1 
ATOM   9606  C  C   . PHE D  1 74  ? 15.057  1.512   95.825  1.00 8.04   ? 161  PHE D C   1 
ATOM   9607  O  O   . PHE D  1 74  ? 15.979  1.714   95.012  1.00 7.47   ? 161  PHE D O   1 
ATOM   9608  C  CB  . PHE D  1 74  ? 13.800  3.629   95.299  1.00 7.70   ? 161  PHE D CB  1 
ATOM   9609  C  CG  . PHE D  1 74  ? 12.520  4.365   95.495  1.00 9.99   ? 161  PHE D CG  1 
ATOM   9610  C  CD1 . PHE D  1 74  ? 12.432  5.418   96.398  1.00 11.10  ? 161  PHE D CD1 1 
ATOM   9611  C  CD2 . PHE D  1 74  ? 11.359  3.930   94.833  1.00 9.51   ? 161  PHE D CD2 1 
ATOM   9612  C  CE1 . PHE D  1 74  ? 11.199  6.067   96.616  1.00 10.74  ? 161  PHE D CE1 1 
ATOM   9613  C  CE2 . PHE D  1 74  ? 10.116  4.558   95.069  1.00 10.54  ? 161  PHE D CE2 1 
ATOM   9614  C  CZ  . PHE D  1 74  ? 10.054  5.628   95.952  1.00 11.01  ? 161  PHE D CZ  1 
ATOM   9615  N  N   . ARG D  1 75  ? 15.178  0.781   96.934  1.00 7.33   ? 162  ARG D N   1 
ATOM   9616  C  CA  . ARG D  1 75  ? 16.416  0.112   97.323  1.00 8.09   ? 162  ARG D CA  1 
ATOM   9617  C  C   . ARG D  1 75  ? 16.419  -1.347  96.847  1.00 7.64   ? 162  ARG D C   1 
ATOM   9618  O  O   . ARG D  1 75  ? 15.356  -1.972  96.681  1.00 6.68   ? 162  ARG D O   1 
ATOM   9619  C  CB  . ARG D  1 75  ? 16.600  0.165   98.847  1.00 8.13   ? 162  ARG D CB  1 
ATOM   9620  C  CG  . ARG D  1 75  ? 16.790  1.561   99.415  1.00 9.59   ? 162  ARG D CG  1 
ATOM   9621  C  CD  . ARG D  1 75  ? 17.549  1.501   100.729 1.00 8.29   ? 162  ARG D CD  1 
ATOM   9622  N  NE  . ARG D  1 75  ? 19.009  1.522   100.530 1.00 8.73   ? 162  ARG D NE  1 
ATOM   9623  C  CZ  . ARG D  1 75  ? 19.902  1.624   101.519 1.00 9.21   ? 162  ARG D CZ  1 
ATOM   9624  N  NH1 . ARG D  1 75  ? 19.498  1.712   102.788 1.00 8.79   ? 162  ARG D NH1 1 
ATOM   9625  N  NH2 . ARG D  1 75  ? 21.209  1.647   101.244 1.00 7.17   ? 162  ARG D NH2 1 
ATOM   9626  N  N   . ALA D  1 76  ? 17.616  -1.883  96.602  1.00 7.36   ? 163  ALA D N   1 
ATOM   9627  C  CA  . ALA D  1 76  ? 17.755  -3.249  96.140  1.00 8.23   ? 163  ALA D CA  1 
ATOM   9628  C  C   . ALA D  1 76  ? 19.164  -3.749  96.478  1.00 8.27   ? 163  ALA D C   1 
ATOM   9629  O  O   . ALA D  1 76  ? 20.128  -2.967  96.496  1.00 9.12   ? 163  ALA D O   1 
ATOM   9630  C  CB  . ALA D  1 76  ? 17.544  -3.299  94.645  1.00 7.82   ? 163  ALA D CB  1 
ATOM   9631  N  N   . LEU D  1 77  ? 19.294  -5.040  96.721  1.00 7.31   ? 164  LEU D N   1 
ATOM   9632  C  CA  . LEU D  1 77  ? 20.636  -5.619  96.844  1.00 7.23   ? 164  LEU D CA  1 
ATOM   9633  C  C   . LEU D  1 77  ? 21.222  -5.782  95.446  1.00 6.86   ? 164  LEU D C   1 
ATOM   9634  O  O   . LEU D  1 77  ? 20.603  -6.399  94.589  1.00 7.32   ? 164  LEU D O   1 
ATOM   9635  C  CB  . LEU D  1 77  ? 20.626  -6.953  97.596  1.00 7.47   ? 164  LEU D CB  1 
ATOM   9636  C  CG  . LEU D  1 77  ? 21.964  -7.694  97.629  1.00 6.89   ? 164  LEU D CG  1 
ATOM   9637  C  CD1 . LEU D  1 77  ? 23.006  -6.864  98.398  1.00 5.50   ? 164  LEU D CD1 1 
ATOM   9638  C  CD2 . LEU D  1 77  ? 21.835  -9.137  98.233  1.00 7.25   ? 164  LEU D CD2 1 
ATOM   9639  N  N   . ILE D  1 78  ? 22.388  -5.170  95.235  1.00 6.80   ? 165  ILE D N   1 
ATOM   9640  C  CA  . ILE D  1 78  ? 23.124  -5.262  93.982  1.00 7.05   ? 165  ILE D CA  1 
ATOM   9641  C  C   . ILE D  1 78  ? 24.480  -5.912  94.231  1.00 7.10   ? 165  ILE D C   1 
ATOM   9642  O  O   . ILE D  1 78  ? 25.056  -5.746  95.303  1.00 7.13   ? 165  ILE D O   1 
ATOM   9643  C  CB  . ILE D  1 78  ? 23.332  -3.863  93.304  1.00 7.23   ? 165  ILE D CB  1 
ATOM   9644  C  CG1 . ILE D  1 78  ? 23.942  -2.838  94.289  1.00 6.54   ? 165  ILE D CG1 1 
ATOM   9645  C  CG2 . ILE D  1 78  ? 22.017  -3.367  92.638  1.00 7.35   ? 165  ILE D CG2 1 
ATOM   9646  C  CD1 . ILE D  1 78  ? 24.506  -1.553  93.616  1.00 7.55   ? 165  ILE D CD1 1 
ATOM   9647  N  N   . SER D  1 79  ? 24.969  -6.667  93.251  1.00 6.67   ? 166  SER D N   1 
ATOM   9648  C  CA  . SER D  1 79  ? 26.332  -7.165  93.294  1.00 7.31   ? 166  SER D CA  1 
ATOM   9649  C  C   . SER D  1 79  ? 27.073  -6.791  92.028  1.00 7.18   ? 166  SER D C   1 
ATOM   9650  O  O   . SER D  1 79  ? 26.461  -6.500  90.994  1.00 7.42   ? 166  SER D O   1 
ATOM   9651  C  CB  . SER D  1 79  ? 26.380  -8.693  93.523  1.00 7.79   ? 166  SER D CB  1 
ATOM   9652  O  OG  . SER D  1 79  ? 25.793  -9.425  92.451  1.00 8.87   ? 166  SER D OG  1 
ATOM   9653  N  N   . TRP D  1 80  ? 28.404  -6.813  92.112  1.00 7.22   ? 167  TRP D N   1 
ATOM   9654  C  CA  . TRP D  1 80  ? 29.240  -6.484  90.982  1.00 7.57   ? 167  TRP D CA  1 
ATOM   9655  C  C   . TRP D  1 80  ? 30.671  -7.025  91.163  1.00 7.87   ? 167  TRP D C   1 
ATOM   9656  O  O   . TRP D  1 80  ? 31.094  -7.393  92.272  1.00 6.79   ? 167  TRP D O   1 
ATOM   9657  C  CB  . TRP D  1 80  ? 29.260  -4.964  90.767  1.00 7.58   ? 167  TRP D CB  1 
ATOM   9658  C  CG  . TRP D  1 80  ? 29.898  -4.119  91.875  1.00 8.16   ? 167  TRP D CG  1 
ATOM   9659  C  CD1 . TRP D  1 80  ? 31.188  -3.652  91.898  1.00 7.70   ? 167  TRP D CD1 1 
ATOM   9660  C  CD2 . TRP D  1 80  ? 29.266  -3.624  93.077  1.00 6.15   ? 167  TRP D CD2 1 
ATOM   9661  N  NE1 . TRP D  1 80  ? 31.392  -2.902  93.041  1.00 7.59   ? 167  TRP D NE1 1 
ATOM   9662  C  CE2 . TRP D  1 80  ? 30.232  -2.862  93.773  1.00 9.00   ? 167  TRP D CE2 1 
ATOM   9663  C  CE3 . TRP D  1 80  ? 27.971  -3.748  93.631  1.00 6.78   ? 167  TRP D CE3 1 
ATOM   9664  C  CZ2 . TRP D  1 80  ? 29.953  -2.206  95.002  1.00 8.64   ? 167  TRP D CZ2 1 
ATOM   9665  C  CZ3 . TRP D  1 80  ? 27.694  -3.113  94.865  1.00 7.88   ? 167  TRP D CZ3 1 
ATOM   9666  C  CH2 . TRP D  1 80  ? 28.690  -2.353  95.534  1.00 8.34   ? 167  TRP D CH2 1 
ATOM   9667  N  N   . GLU D  1 81  ? 31.416  -7.050  90.063  1.00 8.43   ? 168  GLU D N   1 
ATOM   9668  C  CA  . GLU D  1 81  ? 32.778  -7.606  90.072  1.00 9.35   ? 168  GLU D CA  1 
ATOM   9669  C  C   . GLU D  1 81  ? 33.652  -6.808  91.045  1.00 8.83   ? 168  GLU D C   1 
ATOM   9670  O  O   . GLU D  1 81  ? 33.650  -5.568  91.021  1.00 8.70   ? 168  GLU D O   1 
ATOM   9671  C  CB  . GLU D  1 81  ? 33.364  -7.555  88.667  1.00 9.67   ? 168  GLU D CB  1 
ATOM   9672  C  CG  . GLU D  1 81  ? 34.712  -8.231  88.540  1.00 14.27  ? 168  GLU D CG  1 
ATOM   9673  C  CD  . GLU D  1 81  ? 35.247  -8.148  87.118  1.00 19.67  ? 168  GLU D CD  1 
ATOM   9674  O  OE1 . GLU D  1 81  ? 34.562  -8.672  86.204  1.00 19.25  ? 168  GLU D OE1 1 
ATOM   9675  O  OE2 . GLU D  1 81  ? 36.332  -7.538  86.921  1.00 21.17  ? 168  GLU D OE2 1 
ATOM   9676  N  N   . MET D  1 82  ? 34.366  -7.528  91.905  1.00 8.49   ? 169  MET D N   1 
ATOM   9677  C  CA  . MET D  1 82  ? 35.164  -6.919  92.988  1.00 9.43   ? 169  MET D CA  1 
ATOM   9678  C  C   . MET D  1 82  ? 36.147  -5.892  92.457  1.00 9.01   ? 169  MET D C   1 
ATOM   9679  O  O   . MET D  1 82  ? 36.903  -6.169  91.511  1.00 8.43   ? 169  MET D O   1 
ATOM   9680  C  CB  . MET D  1 82  ? 35.896  -8.017  93.788  1.00 9.11   ? 169  MET D CB  1 
ATOM   9681  C  CG  . MET D  1 82  ? 36.789  -7.514  94.905  1.00 10.21  ? 169  MET D CG  1 
ATOM   9682  S  SD  . MET D  1 82  ? 37.516  -8.848  95.901  1.00 10.46  ? 169  MET D SD  1 
ATOM   9683  C  CE  . MET D  1 82  ? 38.786  -9.476  94.819  1.00 10.53  ? 169  MET D CE  1 
ATOM   9684  N  N   . GLY D  1 83  ? 36.132  -4.699  93.051  1.00 7.79   ? 170  GLY D N   1 
ATOM   9685  C  CA  . GLY D  1 83  ? 37.090  -3.681  92.642  1.00 9.16   ? 170  GLY D CA  1 
ATOM   9686  C  C   . GLY D  1 83  ? 36.498  -2.579  91.796  1.00 9.79   ? 170  GLY D C   1 
ATOM   9687  O  O   . GLY D  1 83  ? 36.906  -1.425  91.920  1.00 9.30   ? 170  GLY D O   1 
ATOM   9688  N  N   . GLN D  1 84  ? 35.555  -2.941  90.921  1.00 9.92   ? 171  GLN D N   1 
ATOM   9689  C  CA  . GLN D  1 84  ? 34.799  -1.956  90.155  1.00 10.36  ? 171  GLN D CA  1 
ATOM   9690  C  C   . GLN D  1 84  ? 33.921  -1.135  91.107  1.00 9.30   ? 171  GLN D C   1 
ATOM   9691  O  O   . GLN D  1 84  ? 33.574  -1.604  92.195  1.00 9.93   ? 171  GLN D O   1 
ATOM   9692  C  CB  . GLN D  1 84  ? 33.910  -2.648  89.116  1.00 9.69   ? 171  GLN D CB  1 
ATOM   9693  C  CG  . GLN D  1 84  ? 34.700  -3.263  87.963  1.00 11.70  ? 171  GLN D CG  1 
ATOM   9694  C  CD  . GLN D  1 84  ? 33.806  -3.966  86.943  1.00 13.19  ? 171  GLN D CD  1 
ATOM   9695  O  OE1 . GLN D  1 84  ? 32.588  -3.964  87.058  1.00 13.79  ? 171  GLN D OE1 1 
ATOM   9696  N  NE2 . GLN D  1 84  ? 34.428  -4.588  85.946  1.00 19.42  ? 171  GLN D NE2 1 
ATOM   9697  N  N   . ALA D  1 85  ? 33.579  0.085   90.704  1.00 9.04   ? 172  ALA D N   1 
ATOM   9698  C  CA  . ALA D  1 85  ? 32.575  0.872   91.436  1.00 8.26   ? 172  ALA D CA  1 
ATOM   9699  C  C   . ALA D  1 85  ? 31.179  0.531   90.913  1.00 7.50   ? 172  ALA D C   1 
ATOM   9700  O  O   . ALA D  1 85  ? 31.026  0.097   89.761  1.00 7.74   ? 172  ALA D O   1 
ATOM   9701  C  CB  . ALA D  1 85  ? 32.867  2.392   91.344  1.00 8.60   ? 172  ALA D CB  1 
ATOM   9702  N  N   . PRO D  1 86  ? 30.155  0.679   91.764  1.00 6.89   ? 173  PRO D N   1 
ATOM   9703  C  CA  . PRO D  1 86  ? 28.814  0.260   91.319  1.00 7.02   ? 173  PRO D CA  1 
ATOM   9704  C  C   . PRO D  1 86  ? 28.118  1.270   90.417  1.00 7.25   ? 173  PRO D C   1 
ATOM   9705  O  O   . PRO D  1 86  ? 27.708  2.331   90.890  1.00 7.38   ? 173  PRO D O   1 
ATOM   9706  C  CB  . PRO D  1 86  ? 28.053  0.061   92.639  1.00 6.85   ? 173  PRO D CB  1 
ATOM   9707  C  CG  . PRO D  1 86  ? 28.701  1.051   93.596  1.00 7.58   ? 173  PRO D CG  1 
ATOM   9708  C  CD  . PRO D  1 86  ? 30.166  1.159   93.165  1.00 6.88   ? 173  PRO D CD  1 
ATOM   9709  N  N   . SER D  1 87  ? 27.984  0.940   89.135  1.00 7.49   ? 174  SER D N   1 
ATOM   9710  C  CA  . SER D  1 87  ? 27.205  1.777   88.214  1.00 8.03   ? 174  SER D CA  1 
ATOM   9711  C  C   . SER D  1 87  ? 25.872  1.095   87.837  1.00 8.46   ? 174  SER D C   1 
ATOM   9712  O  O   . SER D  1 87  ? 25.682  -0.094  88.124  1.00 8.04   ? 174  SER D O   1 
ATOM   9713  C  CB  . SER D  1 87  ? 28.024  2.091   86.961  1.00 8.17   ? 174  SER D CB  1 
ATOM   9714  O  OG  . SER D  1 87  ? 28.109  0.940   86.126  1.00 9.13   ? 174  SER D OG  1 
ATOM   9715  N  N   . PRO D  1 88  ? 24.944  1.846   87.193  1.00 8.95   ? 175  PRO D N   1 
ATOM   9716  C  CA  . PRO D  1 88  ? 23.766  1.217   86.603  1.00 9.51   ? 175  PRO D CA  1 
ATOM   9717  C  C   . PRO D  1 88  ? 24.111  0.216   85.474  1.00 9.55   ? 175  PRO D C   1 
ATOM   9718  O  O   . PRO D  1 88  ? 23.228  -0.520  84.993  1.00 9.64   ? 175  PRO D O   1 
ATOM   9719  C  CB  . PRO D  1 88  ? 22.972  2.405   86.024  1.00 9.41   ? 175  PRO D CB  1 
ATOM   9720  C  CG  . PRO D  1 88  ? 23.526  3.618   86.644  1.00 9.26   ? 175  PRO D CG  1 
ATOM   9721  C  CD  . PRO D  1 88  ? 24.944  3.311   87.003  1.00 9.01   ? 175  PRO D CD  1 
ATOM   9722  N  N   . TYR D  1 89  ? 25.379  0.157   85.079  1.00 8.43   ? 176  TYR D N   1 
ATOM   9723  C  CA  . TYR D  1 89  ? 25.743  -0.601  83.884  1.00 9.30   ? 176  TYR D CA  1 
ATOM   9724  C  C   . TYR D  1 89  ? 26.408  -1.956  84.183  1.00 9.63   ? 176  TYR D C   1 
ATOM   9725  O  O   . TYR D  1 89  ? 26.393  -2.857  83.332  1.00 10.48  ? 176  TYR D O   1 
ATOM   9726  C  CB  . TYR D  1 89  ? 26.622  0.260   82.927  1.00 9.10   ? 176  TYR D CB  1 
ATOM   9727  C  CG  . TYR D  1 89  ? 26.101  1.686   82.722  1.00 9.36   ? 176  TYR D CG  1 
ATOM   9728  C  CD1 . TYR D  1 89  ? 26.938  2.786   82.921  1.00 9.81   ? 176  TYR D CD1 1 
ATOM   9729  C  CD2 . TYR D  1 89  ? 24.760  1.930   82.365  1.00 8.31   ? 176  TYR D CD2 1 
ATOM   9730  C  CE1 . TYR D  1 89  ? 26.473  4.106   82.745  1.00 8.29   ? 176  TYR D CE1 1 
ATOM   9731  C  CE2 . TYR D  1 89  ? 24.282  3.240   82.183  1.00 8.79   ? 176  TYR D CE2 1 
ATOM   9732  C  CZ  . TYR D  1 89  ? 25.144  4.328   82.391  1.00 10.11  ? 176  TYR D CZ  1 
ATOM   9733  O  OH  . TYR D  1 89  ? 24.690  5.639   82.235  1.00 8.62   ? 176  TYR D OH  1 
ATOM   9734  N  N   . ASN D  1 90  ? 27.008  -2.095  85.367  1.00 9.58   ? 177  ASN D N   1 
ATOM   9735  C  CA  . ASN D  1 90  ? 27.829  -3.276  85.689  1.00 9.56   ? 177  ASN D CA  1 
ATOM   9736  C  C   . ASN D  1 90  ? 27.302  -4.021  86.926  1.00 10.28  ? 177  ASN D C   1 
ATOM   9737  O  O   . ASN D  1 90  ? 27.990  -4.898  87.468  1.00 9.43   ? 177  ASN D O   1 
ATOM   9738  C  CB  . ASN D  1 90  ? 29.300  -2.855  85.923  1.00 10.04  ? 177  ASN D CB  1 
ATOM   9739  C  CG  . ASN D  1 90  ? 29.487  -2.086  87.241  1.00 10.61  ? 177  ASN D CG  1 
ATOM   9740  O  OD1 . ASN D  1 90  ? 28.583  -1.381  87.687  1.00 9.84   ? 177  ASN D OD1 1 
ATOM   9741  N  ND2 . ASN D  1 90  ? 30.644  -2.251  87.876  1.00 9.21   ? 177  ASN D ND2 1 
ATOM   9742  N  N   . THR D  1 91  ? 26.091  -3.665  87.383  1.00 10.00  ? 178  THR D N   1 
ATOM   9743  C  CA  . THR D  1 91  ? 25.566  -4.191  88.650  1.00 10.62  ? 178  THR D CA  1 
ATOM   9744  C  C   . THR D  1 91  ? 24.422  -5.182  88.401  1.00 10.91  ? 178  THR D C   1 
ATOM   9745  O  O   . THR D  1 91  ? 23.560  -4.973  87.523  1.00 12.15  ? 178  THR D O   1 
ATOM   9746  C  CB  . THR D  1 91  ? 25.049  -3.064  89.590  1.00 10.07  ? 178  THR D CB  1 
ATOM   9747  O  OG1 . THR D  1 91  ? 24.233  -2.158  88.832  1.00 10.69  ? 178  THR D OG1 1 
ATOM   9748  C  CG2 . THR D  1 91  ? 26.210  -2.277  90.242  1.00 10.02  ? 178  THR D CG2 1 
ATOM   9749  N  N   . ARG D  1 92  ? 24.423  -6.255  89.180  1.00 10.85  ? 179  ARG D N   1 
ATOM   9750  C  CA  . ARG D  1 92  ? 23.377  -7.260  89.125  1.00 10.27  ? 179  ARG D CA  1 
ATOM   9751  C  C   . ARG D  1 92  ? 22.406  -7.053  90.278  1.00 9.41   ? 179  ARG D C   1 
ATOM   9752  O  O   . ARG D  1 92  ? 22.815  -6.996  91.442  1.00 8.91   ? 179  ARG D O   1 
ATOM   9753  C  CB  . ARG D  1 92  ? 23.997  -8.659  89.232  1.00 10.91  ? 179  ARG D CB  1 
ATOM   9754  C  CG  . ARG D  1 92  ? 22.968  -9.776  89.420  1.00 13.20  ? 179  ARG D CG  1 
ATOM   9755  C  CD  . ARG D  1 92  ? 23.668  -11.122 89.564  1.00 19.65  ? 179  ARG D CD  1 
ATOM   9756  N  NE  . ARG D  1 92  ? 24.317  -11.515 88.313  1.00 27.00  ? 179  ARG D NE  1 
ATOM   9757  C  CZ  . ARG D  1 92  ? 25.470  -12.185 88.222  1.00 28.76  ? 179  ARG D CZ  1 
ATOM   9758  N  NH1 . ARG D  1 92  ? 26.149  -12.537 89.312  1.00 29.14  ? 179  ARG D NH1 1 
ATOM   9759  N  NH2 . ARG D  1 92  ? 25.955  -12.495 87.020  1.00 31.45  ? 179  ARG D NH2 1 
ATOM   9760  N  N   . VAL D  1 93  ? 21.117  -7.004  89.976  1.00 9.19   ? 180  VAL D N   1 
ATOM   9761  C  CA  . VAL D  1 93  ? 20.131  -6.957  91.065  1.00 10.10  ? 180  VAL D CA  1 
ATOM   9762  C  C   . VAL D  1 93  ? 19.880  -8.366  91.637  1.00 10.54  ? 180  VAL D C   1 
ATOM   9763  O  O   . VAL D  1 93  ? 19.408  -9.268  90.935  1.00 10.67  ? 180  VAL D O   1 
ATOM   9764  C  CB  . VAL D  1 93  ? 18.798  -6.273  90.639  1.00 10.54  ? 180  VAL D CB  1 
ATOM   9765  C  CG1 . VAL D  1 93  ? 17.827  -6.238  91.837  1.00 8.69   ? 180  VAL D CG1 1 
ATOM   9766  C  CG2 . VAL D  1 93  ? 19.078  -4.843  90.097  1.00 11.08  ? 180  VAL D CG2 1 
ATOM   9767  N  N   . GLU D  1 94  ? 20.201  -8.537  92.917  1.00 10.07  ? 181  GLU D N   1 
ATOM   9768  C  CA  . GLU D  1 94  ? 20.080  -9.823  93.611  1.00 10.49  ? 181  GLU D CA  1 
ATOM   9769  C  C   . GLU D  1 94  ? 18.657  -10.054 94.171  1.00 10.09  ? 181  GLU D C   1 
ATOM   9770  O  O   . GLU D  1 94  ? 18.155  -11.186 94.195  1.00 11.23  ? 181  GLU D O   1 
ATOM   9771  C  CB  . GLU D  1 94  ? 21.108  -9.878  94.752  1.00 10.49  ? 181  GLU D CB  1 
ATOM   9772  C  CG  . GLU D  1 94  ? 22.594  -9.882  94.299  1.00 10.74  ? 181  GLU D CG  1 
ATOM   9773  C  CD  . GLU D  1 94  ? 23.055  -11.251 93.784  1.00 11.87  ? 181  GLU D CD  1 
ATOM   9774  O  OE1 . GLU D  1 94  ? 22.467  -12.279 94.181  1.00 10.59  ? 181  GLU D OE1 1 
ATOM   9775  O  OE2 . GLU D  1 94  ? 24.019  -11.318 92.987  1.00 10.06  ? 181  GLU D OE2 1 
ATOM   9776  N  N   . CYS D  1 95  ? 18.032  -8.978  94.631  1.00 9.89   ? 182  CYS D N   1 
ATOM   9777  C  CA  . CYS D  1 95  ? 16.683  -8.983  95.201  1.00 9.71   ? 182  CYS D CA  1 
ATOM   9778  C  C   . CYS D  1 95  ? 16.328  -7.530  95.532  1.00 9.42   ? 182  CYS D C   1 
ATOM   9779  O  O   . CYS D  1 95  ? 17.185  -6.647  95.453  1.00 8.72   ? 182  CYS D O   1 
ATOM   9780  C  CB  . CYS D  1 95  ? 16.579  -9.899  96.441  1.00 10.33  ? 182  CYS D CB  1 
ATOM   9781  S  SG  . CYS D  1 95  ? 17.909  -9.830  97.712  1.00 13.69  ? 182  CYS D SG  1 
ATOM   9782  N  N   . ILE D  1 96  ? 15.064  -7.284  95.862  1.00 9.00   ? 183  ILE D N   1 
ATOM   9783  C  CA  . ILE D  1 96  ? 14.576  -5.928  96.101  1.00 8.57   ? 183  ILE D CA  1 
ATOM   9784  C  C   . ILE D  1 96  ? 14.313  -5.724  97.588  1.00 9.07   ? 183  ILE D C   1 
ATOM   9785  O  O   . ILE D  1 96  ? 13.652  -6.554  98.209  1.00 9.50   ? 183  ILE D O   1 
ATOM   9786  C  CB  . ILE D  1 96  ? 13.253  -5.668  95.307  1.00 8.33   ? 183  ILE D CB  1 
ATOM   9787  C  CG1 . ILE D  1 96  ? 13.421  -5.971  93.804  1.00 7.82   ? 183  ILE D CG1 1 
ATOM   9788  C  CG2 . ILE D  1 96  ? 12.765  -4.252  95.540  1.00 9.69   ? 183  ILE D CG2 1 
ATOM   9789  C  CD1 . ILE D  1 96  ? 14.541  -5.153  93.083  1.00 7.62   ? 183  ILE D CD1 1 
ATOM   9790  N  N   . GLY D  1 97  ? 14.807  -4.611  98.147  1.00 8.99   ? 184  GLY D N   1 
ATOM   9791  C  CA  . GLY D  1 97  ? 14.594  -4.302  99.564  1.00 8.13   ? 184  GLY D CA  1 
ATOM   9792  C  C   . GLY D  1 97  ? 15.740  -3.562  100.225 1.00 8.66   ? 184  GLY D C   1 
ATOM   9793  O  O   . GLY D  1 97  ? 16.669  -3.110  99.541  1.00 8.43   ? 184  GLY D O   1 
ATOM   9794  N  N   . TRP D  1 98  ? 15.670  -3.478  101.555 1.00 8.26   ? 185  TRP D N   1 
ATOM   9795  C  CA  . TRP D  1 98  ? 16.446  -2.521  102.349 1.00 8.65   ? 185  TRP D CA  1 
ATOM   9796  C  C   . TRP D  1 98  ? 17.208  -3.168  103.534 1.00 8.23   ? 185  TRP D C   1 
ATOM   9797  O  O   . TRP D  1 98  ? 17.735  -2.481  104.443 1.00 7.50   ? 185  TRP D O   1 
ATOM   9798  C  CB  . TRP D  1 98  ? 15.553  -1.350  102.807 1.00 9.15   ? 185  TRP D CB  1 
ATOM   9799  C  CG  . TRP D  1 98  ? 14.160  -1.723  103.301 1.00 8.77   ? 185  TRP D CG  1 
ATOM   9800  C  CD1 . TRP D  1 98  ? 12.965  -1.352  102.734 1.00 7.39   ? 185  TRP D CD1 1 
ATOM   9801  C  CD2 . TRP D  1 98  ? 13.823  -2.520  104.450 1.00 9.88   ? 185  TRP D CD2 1 
ATOM   9802  N  NE1 . TRP D  1 98  ? 11.913  -1.867  103.454 1.00 8.67   ? 185  TRP D NE1 1 
ATOM   9803  C  CE2 . TRP D  1 98  ? 12.404  -2.588  104.511 1.00 9.30   ? 185  TRP D CE2 1 
ATOM   9804  C  CE3 . TRP D  1 98  ? 14.575  -3.180  105.439 1.00 9.49   ? 185  TRP D CE3 1 
ATOM   9805  C  CZ2 . TRP D  1 98  ? 11.723  -3.293  105.522 1.00 10.41  ? 185  TRP D CZ2 1 
ATOM   9806  C  CZ3 . TRP D  1 98  ? 13.879  -3.878  106.461 1.00 9.46   ? 185  TRP D CZ3 1 
ATOM   9807  C  CH2 . TRP D  1 98  ? 12.480  -3.930  106.478 1.00 8.05   ? 185  TRP D CH2 1 
ATOM   9808  N  N   . SER D  1 99  ? 17.261  -4.502  103.506 1.00 8.45   ? 186  SER D N   1 
ATOM   9809  C  CA  . SER D  1 99  ? 18.127  -5.289  104.415 1.00 9.01   ? 186  SER D CA  1 
ATOM   9810  C  C   . SER D  1 99  ? 18.408  -6.612  103.726 1.00 9.02   ? 186  SER D C   1 
ATOM   9811  O  O   . SER D  1 99  ? 17.519  -7.141  103.040 1.00 8.96   ? 186  SER D O   1 
ATOM   9812  C  CB  . SER D  1 99  ? 17.463  -5.506  105.782 1.00 8.84   ? 186  SER D CB  1 
ATOM   9813  O  OG  . SER D  1 99  ? 18.328  -6.223  106.662 1.00 9.63   ? 186  SER D OG  1 
ATOM   9814  N  N   . SER D  1 100 ? 19.647  -7.114  103.835 1.00 8.21   ? 187  SER D N   1 
ATOM   9815  C  CA  . SER D  1 100 ? 20.047  -8.273  103.032 1.00 8.22   ? 187  SER D CA  1 
ATOM   9816  C  C   . SER D  1 100 ? 21.125  -9.161  103.657 1.00 7.95   ? 187  SER D C   1 
ATOM   9817  O  O   . SER D  1 100 ? 21.798  -8.773  104.616 1.00 8.13   ? 187  SER D O   1 
ATOM   9818  C  CB  . SER D  1 100 ? 20.505  -7.833  101.601 1.00 7.63   ? 187  SER D CB  1 
ATOM   9819  O  OG  . SER D  1 100 ? 21.878  -7.453  101.581 1.00 8.40   ? 187  SER D OG  1 
ATOM   9820  N  N   . THR D  1 101 ? 21.272  -10.348 103.066 1.00 7.73   ? 188  THR D N   1 
ATOM   9821  C  CA  . THR D  1 101 ? 22.431  -11.206 103.236 1.00 7.92   ? 188  THR D CA  1 
ATOM   9822  C  C   . THR D  1 101 ? 22.539  -12.013 101.964 1.00 7.38   ? 188  THR D C   1 
ATOM   9823  O  O   . THR D  1 101 ? 21.587  -12.038 101.155 1.00 7.74   ? 188  THR D O   1 
ATOM   9824  C  CB  . THR D  1 101 ? 22.330  -12.141 104.501 1.00 7.80   ? 188  THR D CB  1 
ATOM   9825  O  OG1 . THR D  1 101 ? 23.561  -12.874 104.675 1.00 9.66   ? 188  THR D OG1 1 
ATOM   9826  C  CG2 . THR D  1 101 ? 21.145  -13.127 104.397 1.00 8.51   ? 188  THR D CG2 1 
ATOM   9827  N  N   . SER D  1 102 ? 23.695  -12.646 101.769 1.00 7.41   ? 189  SER D N   1 
ATOM   9828  C  CA  . SER D  1 102 ? 23.925  -13.510 100.608 1.00 7.74   ? 189  SER D CA  1 
ATOM   9829  C  C   . SER D  1 102 ? 25.095  -14.447 100.904 1.00 7.87   ? 189  SER D C   1 
ATOM   9830  O  O   . SER D  1 102 ? 26.010  -14.089 101.631 1.00 7.57   ? 189  SER D O   1 
ATOM   9831  C  CB  . SER D  1 102 ? 24.227  -12.655 99.359  1.00 8.17   ? 189  SER D CB  1 
ATOM   9832  O  OG  . SER D  1 102 ? 24.269  -13.425 98.168  1.00 6.90   ? 189  SER D OG  1 
ATOM   9833  N  N   . CYS D  1 103 ? 25.062  -15.649 100.342 1.00 7.23   ? 190  CYS D N   1 
ATOM   9834  C  CA  . CYS D  1 103 ? 26.174  -16.590 100.473 1.00 8.25   ? 190  CYS D CA  1 
ATOM   9835  C  C   . CYS D  1 103 ? 25.998  -17.667 99.408  1.00 8.45   ? 190  CYS D C   1 
ATOM   9836  O  O   . CYS D  1 103 ? 24.871  -17.939 98.970  1.00 8.91   ? 190  CYS D O   1 
ATOM   9837  C  CB  . CYS D  1 103 ? 26.249  -17.225 101.871 1.00 7.66   ? 190  CYS D CB  1 
ATOM   9838  S  SG  . CYS D  1 103 ? 24.684  -17.843 102.575 1.00 10.26  ? 190  CYS D SG  1 
ATOM   9839  N  N   . HIS D  1 104 ? 27.122  -18.260 99.006  1.00 8.79   ? 191  HIS D N   1 
ATOM   9840  C  CA  . HIS D  1 104 ? 27.163  -19.346 98.032  1.00 9.37   ? 191  HIS D CA  1 
ATOM   9841  C  C   . HIS D  1 104 ? 27.414  -20.660 98.780  1.00 10.17  ? 191  HIS D C   1 
ATOM   9842  O  O   . HIS D  1 104 ? 28.266  -20.718 99.673  1.00 11.02  ? 191  HIS D O   1 
ATOM   9843  C  CB  . HIS D  1 104 ? 28.284  -19.075 97.021  1.00 8.97   ? 191  HIS D CB  1 
ATOM   9844  C  CG  . HIS D  1 104 ? 28.124  -19.789 95.708  1.00 8.57   ? 191  HIS D CG  1 
ATOM   9845  N  ND1 . HIS D  1 104 ? 28.386  -21.131 95.556  1.00 8.48   ? 191  HIS D ND1 1 
ATOM   9846  C  CD2 . HIS D  1 104 ? 27.787  -19.330 94.476  1.00 9.69   ? 191  HIS D CD2 1 
ATOM   9847  C  CE1 . HIS D  1 104 ? 28.175  -21.481 94.297  1.00 9.57   ? 191  HIS D CE1 1 
ATOM   9848  N  NE2 . HIS D  1 104 ? 27.812  -20.406 93.618  1.00 9.66   ? 191  HIS D NE2 1 
ATOM   9849  N  N   . ASP D  1 105 ? 26.660  -21.705 98.429  1.00 10.73  ? 192  ASP D N   1 
ATOM   9850  C  CA  . ASP D  1 105 ? 26.781  -22.990 99.131  1.00 11.30  ? 192  ASP D CA  1 
ATOM   9851  C  C   . ASP D  1 105 ? 27.770  -23.965 98.454  1.00 11.19  ? 192  ASP D C   1 
ATOM   9852  O  O   . ASP D  1 105 ? 27.939  -25.115 98.918  1.00 11.87  ? 192  ASP D O   1 
ATOM   9853  C  CB  . ASP D  1 105 ? 25.398  -23.622 99.370  1.00 11.06  ? 192  ASP D CB  1 
ATOM   9854  C  CG  . ASP D  1 105 ? 24.703  -24.034 98.079  1.00 11.99  ? 192  ASP D CG  1 
ATOM   9855  O  OD1 . ASP D  1 105 ? 25.356  -24.036 97.019  1.00 12.81  ? 192  ASP D OD1 1 
ATOM   9856  O  OD2 . ASP D  1 105 ? 23.500  -24.388 98.132  1.00 12.65  ? 192  ASP D OD2 1 
ATOM   9857  N  N   . GLY D  1 106 ? 28.407  -23.497 97.373  1.00 10.55  ? 193  GLY D N   1 
ATOM   9858  C  CA  . GLY D  1 106 ? 29.328  -24.292 96.556  1.00 11.44  ? 193  GLY D CA  1 
ATOM   9859  C  C   . GLY D  1 106 ? 28.683  -24.679 95.229  1.00 12.15  ? 193  GLY D C   1 
ATOM   9860  O  O   . GLY D  1 106 ? 29.385  -24.948 94.237  1.00 13.02  ? 193  GLY D O   1 
ATOM   9861  N  N   . MET D  1 107 ? 27.344  -24.683 95.218  1.00 12.39  ? 194  MET D N   1 
ATOM   9862  C  CA  . MET D  1 107 ? 26.549  -24.967 94.016  1.00 13.51  ? 194  MET D CA  1 
ATOM   9863  C  C   . MET D  1 107 ? 25.954  -23.692 93.402  1.00 13.08  ? 194  MET D C   1 
ATOM   9864  O  O   . MET D  1 107 ? 26.160  -23.408 92.210  1.00 12.21  ? 194  MET D O   1 
ATOM   9865  C  CB  . MET D  1 107 ? 25.421  -25.971 94.316  1.00 14.13  ? 194  MET D CB  1 
ATOM   9866  C  CG  . MET D  1 107 ? 25.892  -27.297 94.888  1.00 17.44  ? 194  MET D CG  1 
ATOM   9867  S  SD  . MET D  1 107 ? 26.846  -28.269 93.696  1.00 23.69  ? 194  MET D SD  1 
ATOM   9868  C  CE  . MET D  1 107 ? 25.587  -28.601 92.466  1.00 21.19  ? 194  MET D CE  1 
ATOM   9869  N  N   . SER D  1 108 ? 25.218  -22.937 94.222  1.00 12.44  ? 195  SER D N   1 
ATOM   9870  C  CA  . SER D  1 108 ? 24.537  -21.719 93.783  1.00 12.15  ? 195  SER D CA  1 
ATOM   9871  C  C   . SER D  1 108 ? 24.519  -20.669 94.906  1.00 11.51  ? 195  SER D C   1 
ATOM   9872  O  O   . SER D  1 108 ? 24.823  -20.975 96.077  1.00 11.94  ? 195  SER D O   1 
ATOM   9873  C  CB  . SER D  1 108 ? 23.104  -22.033 93.322  1.00 12.37  ? 195  SER D CB  1 
ATOM   9874  O  OG  . SER D  1 108 ? 23.103  -22.893 92.180  1.00 13.45  ? 195  SER D OG  1 
ATOM   9875  N  N   . ARG D  1 109 ? 24.165  -19.434 94.546  1.00 10.79  ? 196  ARG D N   1 
ATOM   9876  C  CA  . ARG D  1 109 ? 24.094  -18.337 95.512  1.00 9.98   ? 196  ARG D CA  1 
ATOM   9877  C  C   . ARG D  1 109 ? 22.670  -18.196 96.061  1.00 10.76  ? 196  ARG D C   1 
ATOM   9878  O  O   . ARG D  1 109 ? 21.707  -18.145 95.292  1.00 10.80  ? 196  ARG D O   1 
ATOM   9879  C  CB  . ARG D  1 109 ? 24.558  -17.024 94.858  1.00 9.25   ? 196  ARG D CB  1 
ATOM   9880  C  CG  . ARG D  1 109 ? 24.430  -15.769 95.780  1.00 7.82   ? 196  ARG D CG  1 
ATOM   9881  C  CD  . ARG D  1 109 ? 25.331  -14.609 95.333  1.00 9.65   ? 196  ARG D CD  1 
ATOM   9882  N  NE  . ARG D  1 109 ? 26.762  -14.927 95.456  1.00 8.48   ? 196  ARG D NE  1 
ATOM   9883  C  CZ  . ARG D  1 109 ? 27.431  -14.959 96.612  1.00 9.54   ? 196  ARG D CZ  1 
ATOM   9884  N  NH1 . ARG D  1 109 ? 28.729  -15.254 96.612  1.00 8.69   ? 196  ARG D NH1 1 
ATOM   9885  N  NH2 . ARG D  1 109 ? 26.818  -14.683 97.766  1.00 7.90   ? 196  ARG D NH2 1 
ATOM   9886  N  N   . MET D  1 110 ? 22.554  -18.156 97.393  1.00 10.74  ? 197  MET D N   1 
ATOM   9887  C  CA  . MET D  1 110 ? 21.347  -17.712 98.068  1.00 9.96   ? 197  MET D CA  1 
ATOM   9888  C  C   . MET D  1 110 ? 21.439  -16.206 98.393  1.00 9.87   ? 197  MET D C   1 
ATOM   9889  O  O   . MET D  1 110 ? 22.438  -15.756 98.967  1.00 9.54   ? 197  MET D O   1 
ATOM   9890  C  CB  . MET D  1 110 ? 21.134  -18.496 99.375  1.00 9.76   ? 197  MET D CB  1 
ATOM   9891  C  CG  . MET D  1 110 ? 19.872  -18.058 100.144 1.00 10.29  ? 197  MET D CG  1 
ATOM   9892  S  SD  . MET D  1 110 ? 19.564  -18.998 101.653 1.00 10.88  ? 197  MET D SD  1 
ATOM   9893  C  CE  . MET D  1 110 ? 20.900  -18.416 102.705 1.00 10.25  ? 197  MET D CE  1 
ATOM   9894  N  N   . SER D  1 111 ? 20.392  -15.444 98.049  1.00 9.04   ? 198  SER D N   1 
ATOM   9895  C  CA  . SER D  1 111 ? 20.327  -14.019 98.422  1.00 9.87   ? 198  SER D CA  1 
ATOM   9896  C  C   . SER D  1 111 ? 18.983  -13.725 99.074  1.00 9.94   ? 198  SER D C   1 
ATOM   9897  O  O   . SER D  1 111 ? 17.947  -14.255 98.640  1.00 10.68  ? 198  SER D O   1 
ATOM   9898  C  CB  . SER D  1 111 ? 20.540  -13.117 97.206  1.00 9.07   ? 198  SER D CB  1 
ATOM   9899  O  OG  . SER D  1 111 ? 21.863  -13.245 96.691  1.00 10.23  ? 198  SER D OG  1 
ATOM   9900  N  N   . ILE D  1 112 ? 18.996  -12.910 100.119 1.00 9.88   ? 199  ILE D N   1 
ATOM   9901  C  CA  . ILE D  1 112 ? 17.775  -12.609 100.886 1.00 10.50  ? 199  ILE D CA  1 
ATOM   9902  C  C   . ILE D  1 112 ? 17.632  -11.116 101.062 1.00 10.48  ? 199  ILE D C   1 
ATOM   9903  O  O   . ILE D  1 112 ? 18.579  -10.460 101.464 1.00 11.07  ? 199  ILE D O   1 
ATOM   9904  C  CB  . ILE D  1 112 ? 17.794  -13.296 102.297 1.00 9.78   ? 199  ILE D CB  1 
ATOM   9905  C  CG1 . ILE D  1 112 ? 18.029  -14.798 102.170 1.00 10.00  ? 199  ILE D CG1 1 
ATOM   9906  C  CG2 . ILE D  1 112 ? 16.497  -12.969 103.137 1.00 9.37   ? 199  ILE D CG2 1 
ATOM   9907  C  CD1 . ILE D  1 112 ? 18.106  -15.516 103.533 1.00 11.73  ? 199  ILE D CD1 1 
ATOM   9908  N  N   . CYS D  1 113 ? 16.444  -10.584 100.755 1.00 10.46  ? 200  CYS D N   1 
ATOM   9909  C  CA  . CYS D  1 113 ? 16.134  -9.168  100.967 1.00 10.31  ? 200  CYS D CA  1 
ATOM   9910  C  C   . CYS D  1 113 ? 14.815  -9.036  101.704 1.00 9.08   ? 200  CYS D C   1 
ATOM   9911  O  O   . CYS D  1 113 ? 13.861  -9.755  101.390 1.00 9.66   ? 200  CYS D O   1 
ATOM   9912  C  CB  . CYS D  1 113 ? 15.968  -8.453  99.617  1.00 10.49  ? 200  CYS D CB  1 
ATOM   9913  S  SG  . CYS D  1 113 ? 17.474  -8.124  98.728  1.00 14.12  ? 200  CYS D SG  1 
ATOM   9914  N  N   . MET D  1 114 ? 14.763  -8.127  102.676 1.00 9.07   ? 201  MET D N   1 
ATOM   9915  C  CA  . MET D  1 114 ? 13.504  -7.695  103.291 1.00 9.46   ? 201  MET D CA  1 
ATOM   9916  C  C   . MET D  1 114 ? 13.058  -6.388  102.658 1.00 9.83   ? 201  MET D C   1 
ATOM   9917  O  O   . MET D  1 114 ? 13.890  -5.509  102.386 1.00 9.73   ? 201  MET D O   1 
ATOM   9918  C  CB  . MET D  1 114 ? 13.655  -7.467  104.803 1.00 8.76   ? 201  MET D CB  1 
ATOM   9919  C  CG  . MET D  1 114 ? 13.824  -8.725  105.643 1.00 11.31  ? 201  MET D CG  1 
ATOM   9920  S  SD  . MET D  1 114 ? 15.312  -9.677  105.300 1.00 11.80  ? 201  MET D SD  1 
ATOM   9921  C  CE  . MET D  1 114 ? 15.283  -10.733 106.772 1.00 11.08  ? 201  MET D CE  1 
ATOM   9922  N  N   . SER D  1 115 ? 11.747  -6.249  102.451 1.00 9.49   ? 202  SER D N   1 
ATOM   9923  C  CA  . SER D  1 115 ? 11.165  -5.002  101.990 1.00 10.35  ? 202  SER D CA  1 
ATOM   9924  C  C   . SER D  1 115 ? 9.801   -4.820  102.645 1.00 10.51  ? 202  SER D C   1 
ATOM   9925  O  O   . SER D  1 115 ? 9.333   -5.700  103.366 1.00 10.67  ? 202  SER D O   1 
ATOM   9926  C  CB  . SER D  1 115 ? 10.992  -4.991  100.460 1.00 10.49  ? 202  SER D CB  1 
ATOM   9927  O  OG  . SER D  1 115 ? 9.845   -5.754  100.078 1.00 13.14  ? 202  SER D OG  1 
ATOM   9928  N  N   . GLY D  1 116 ? 9.179   -3.677  102.394 1.00 11.21  ? 203  GLY D N   1 
ATOM   9929  C  CA  . GLY D  1 116 ? 7.840   -3.407  102.910 1.00 11.58  ? 203  GLY D CA  1 
ATOM   9930  C  C   . GLY D  1 116 ? 7.870   -2.325  103.970 1.00 11.63  ? 203  GLY D C   1 
ATOM   9931  O  O   . GLY D  1 116 ? 8.934   -1.828  104.328 1.00 11.28  ? 203  GLY D O   1 
ATOM   9932  N  N   . PRO D  1 117 ? 6.691   -1.987  104.514 1.00 11.63  ? 204  PRO D N   1 
ATOM   9933  C  CA  . PRO D  1 117 ? 6.579   -0.983  105.547 1.00 11.89  ? 204  PRO D CA  1 
ATOM   9934  C  C   . PRO D  1 117 ? 7.065   -1.563  106.881 1.00 11.80  ? 204  PRO D C   1 
ATOM   9935  O  O   . PRO D  1 117 ? 7.163   -2.792  107.015 1.00 12.44  ? 204  PRO D O   1 
ATOM   9936  C  CB  . PRO D  1 117 ? 5.067   -0.691  105.574 1.00 11.60  ? 204  PRO D CB  1 
ATOM   9937  C  CG  . PRO D  1 117 ? 4.451   -1.999  105.252 1.00 12.16  ? 204  PRO D CG  1 
ATOM   9938  C  CD  . PRO D  1 117 ? 5.383   -2.607  104.205 1.00 12.09  ? 204  PRO D CD  1 
ATOM   9939  N  N   . ASN D  1 118 ? 7.365   -0.692  107.840 1.00 12.51  ? 205  ASN D N   1 
ATOM   9940  C  CA  . ASN D  1 118 ? 7.934   -1.107  109.132 1.00 13.75  ? 205  ASN D CA  1 
ATOM   9941  C  C   . ASN D  1 118 ? 7.088   -2.147  109.864 1.00 13.43  ? 205  ASN D C   1 
ATOM   9942  O  O   . ASN D  1 118 ? 7.640   -3.101  110.430 1.00 13.94  ? 205  ASN D O   1 
ATOM   9943  C  CB  . ASN D  1 118 ? 8.194   0.090   110.059 1.00 13.23  ? 205  ASN D CB  1 
ATOM   9944  C  CG  . ASN D  1 118 ? 9.241   1.050   109.527 1.00 15.80  ? 205  ASN D CG  1 
ATOM   9945  O  OD1 . ASN D  1 118 ? 9.965   0.760   108.565 1.00 14.76  ? 205  ASN D OD1 1 
ATOM   9946  N  ND2 . ASN D  1 118 ? 9.339   2.213   110.173 1.00 18.18  ? 205  ASN D ND2 1 
ATOM   9947  N  N   . ASN D  1 119 ? 5.758   -1.991  109.827 1.00 13.51  ? 206  ASN D N   1 
ATOM   9948  C  CA  . ASN D  1 119 ? 4.873   -2.925  110.537 1.00 14.07  ? 206  ASN D CA  1 
ATOM   9949  C  C   . ASN D  1 119 ? 4.481   -4.166  109.752 1.00 14.23  ? 206  ASN D C   1 
ATOM   9950  O  O   . ASN D  1 119 ? 3.663   -4.955  110.230 1.00 14.43  ? 206  ASN D O   1 
ATOM   9951  C  CB  . ASN D  1 119 ? 3.587   -2.240  111.052 1.00 14.01  ? 206  ASN D CB  1 
ATOM   9952  C  CG  . ASN D  1 119 ? 2.685   -1.711  109.927 1.00 15.65  ? 206  ASN D CG  1 
ATOM   9953  O  OD1 . ASN D  1 119 ? 2.892   -1.990  108.742 1.00 16.97  ? 206  ASN D OD1 1 
ATOM   9954  N  ND2 . ASN D  1 119 ? 1.682   -0.927  110.307 1.00 18.04  ? 206  ASN D ND2 1 
ATOM   9955  N  N   . ASN D  1 120 ? 5.054   -4.350  108.564 1.00 13.37  ? 207  ASN D N   1 
ATOM   9956  C  CA  . ASN D  1 120 ? 4.551   -5.384  107.656 1.00 13.34  ? 207  ASN D CA  1 
ATOM   9957  C  C   . ASN D  1 120 ? 5.574   -5.849  106.614 1.00 12.00  ? 207  ASN D C   1 
ATOM   9958  O  O   . ASN D  1 120 ? 5.209   -6.120  105.462 1.00 11.02  ? 207  ASN D O   1 
ATOM   9959  C  CB  . ASN D  1 120 ? 3.361   -4.792  106.920 1.00 13.85  ? 207  ASN D CB  1 
ATOM   9960  C  CG  . ASN D  1 120 ? 2.181   -5.704  106.869 1.00 17.44  ? 207  ASN D CG  1 
ATOM   9961  O  OD1 . ASN D  1 120 ? 2.140   -6.789  107.455 1.00 16.70  ? 207  ASN D OD1 1 
ATOM   9962  N  ND2 . ASN D  1 120 ? 1.183   -5.260  106.116 1.00 20.47  ? 207  ASN D ND2 1 
ATOM   9963  N  N   . ALA D  1 121 ? 6.836   -5.971  107.028 1.00 11.13  ? 208  ALA D N   1 
ATOM   9964  C  CA  . ALA D  1 121 ? 7.921   -6.290  106.106 1.00 10.31  ? 208  ALA D CA  1 
ATOM   9965  C  C   . ALA D  1 121 ? 7.911   -7.784  105.803 1.00 10.45  ? 208  ALA D C   1 
ATOM   9966  O  O   . ALA D  1 121 ? 7.242   -8.573  106.487 1.00 10.34  ? 208  ALA D O   1 
ATOM   9967  C  CB  . ALA D  1 121 ? 9.273   -5.873  106.703 1.00 9.46   ? 208  ALA D CB  1 
ATOM   9968  N  N   . SER D  1 122 ? 8.653   -8.176  104.772 1.00 10.90  ? 209  SER D N   1 
ATOM   9969  C  CA  . SER D  1 122 ? 8.736   -9.576  104.414 1.00 11.19  ? 209  SER D CA  1 
ATOM   9970  C  C   . SER D  1 122 ? 10.076  -9.837  103.771 1.00 11.28  ? 209  SER D C   1 
ATOM   9971  O  O   . SER D  1 122 ? 10.612  -8.967  103.093 1.00 11.01  ? 209  SER D O   1 
ATOM   9972  C  CB  . SER D  1 122 ? 7.580   -9.989  103.495 1.00 11.54  ? 209  SER D CB  1 
ATOM   9973  O  OG  . SER D  1 122 ? 7.583   -9.245  102.292 1.00 13.29  ? 209  SER D OG  1 
ATOM   9974  N  N   . ALA D  1 123 ? 10.614  -11.026 104.025 1.00 10.86  ? 210  ALA D N   1 
ATOM   9975  C  CA  . ALA D  1 123 ? 11.823  -11.475 103.357 1.00 10.80  ? 210  ALA D CA  1 
ATOM   9976  C  C   . ALA D  1 123 ? 11.453  -12.303 102.126 1.00 10.49  ? 210  ALA D C   1 
ATOM   9977  O  O   . ALA D  1 123 ? 10.503  -13.108 102.171 1.00 10.13  ? 210  ALA D O   1 
ATOM   9978  C  CB  . ALA D  1 123 ? 12.693  -12.298 104.309 1.00 10.87  ? 210  ALA D CB  1 
ATOM   9979  N  N   . VAL D  1 124 ? 12.194  -12.095 101.031 1.00 9.83   ? 211  VAL D N   1 
ATOM   9980  C  CA  . VAL D  1 124 ? 12.197  -13.039 99.890  1.00 10.02  ? 211  VAL D CA  1 
ATOM   9981  C  C   . VAL D  1 124 ? 13.584  -13.670 99.767  1.00 9.98   ? 211  VAL D C   1 
ATOM   9982  O  O   . VAL D  1 124 ? 14.594  -12.964 99.726  1.00 9.67   ? 211  VAL D O   1 
ATOM   9983  C  CB  . VAL D  1 124 ? 11.781  -12.356 98.535  1.00 9.73   ? 211  VAL D CB  1 
ATOM   9984  C  CG1 . VAL D  1 124 ? 11.649  -13.401 97.421  1.00 11.05  ? 211  VAL D CG1 1 
ATOM   9985  C  CG2 . VAL D  1 124 ? 10.460  -11.582 98.710  1.00 10.97  ? 211  VAL D CG2 1 
ATOM   9986  N  N   . VAL D  1 125 ? 13.598  -15.000 99.709  1.00 9.73   ? 212  VAL D N   1 
ATOM   9987  C  CA  . VAL D  1 125 ? 14.802  -15.822 99.687  1.00 9.43   ? 212  VAL D CA  1 
ATOM   9988  C  C   . VAL D  1 125 ? 14.962  -16.348 98.270  1.00 9.41   ? 212  VAL D C   1 
ATOM   9989  O  O   . VAL D  1 125 ? 14.072  -17.049 97.735  1.00 9.88   ? 212  VAL D O   1 
ATOM   9990  C  CB  . VAL D  1 125 ? 14.683  -17.030 100.685 1.00 8.12   ? 212  VAL D CB  1 
ATOM   9991  C  CG1 . VAL D  1 125 ? 15.977  -17.830 100.703 1.00 7.58   ? 212  VAL D CG1 1 
ATOM   9992  C  CG2 . VAL D  1 125 ? 14.316  -16.522 102.107 1.00 9.01   ? 212  VAL D CG2 1 
ATOM   9993  N  N   . TRP D  1 126 ? 16.090  -16.003 97.669  1.00 9.28   ? 213  TRP D N   1 
ATOM   9994  C  CA  . TRP D  1 126 ? 16.395  -16.320 96.280  1.00 9.84   ? 213  TRP D CA  1 
ATOM   9995  C  C   . TRP D  1 126 ? 17.501  -17.365 96.292  1.00 10.32  ? 213  TRP D C   1 
ATOM   9996  O  O   . TRP D  1 126 ? 18.362  -17.331 97.173  1.00 10.35  ? 213  TRP D O   1 
ATOM   9997  C  CB  . TRP D  1 126 ? 16.920  -15.077 95.548  1.00 9.20   ? 213  TRP D CB  1 
ATOM   9998  C  CG  . TRP D  1 126 ? 15.898  -13.966 95.343  1.00 9.33   ? 213  TRP D CG  1 
ATOM   9999  C  CD1 . TRP D  1 126 ? 15.269  -13.206 96.322  1.00 9.99   ? 213  TRP D CD1 1 
ATOM   10000 C  CD2 . TRP D  1 126 ? 15.379  -13.500 94.089  1.00 9.84   ? 213  TRP D CD2 1 
ATOM   10001 N  NE1 . TRP D  1 126 ? 14.402  -12.300 95.734  1.00 8.06   ? 213  TRP D NE1 1 
ATOM   10002 C  CE2 . TRP D  1 126 ? 14.456  -12.452 94.375  1.00 9.05   ? 213  TRP D CE2 1 
ATOM   10003 C  CE3 . TRP D  1 126 ? 15.613  -13.857 92.747  1.00 9.42   ? 213  TRP D CE3 1 
ATOM   10004 C  CZ2 . TRP D  1 126 ? 13.762  -11.763 93.366  1.00 8.79   ? 213  TRP D CZ2 1 
ATOM   10005 C  CZ3 . TRP D  1 126 ? 14.927  -13.176 91.745  1.00 9.00   ? 213  TRP D CZ3 1 
ATOM   10006 C  CH2 . TRP D  1 126 ? 14.014  -12.133 92.063  1.00 8.99   ? 213  TRP D CH2 1 
ATOM   10007 N  N   . TYR D  1 127 ? 17.485  -18.270 95.312  1.00 10.41  ? 214  TYR D N   1 
ATOM   10008 C  CA  . TYR D  1 127 ? 18.535  -19.284 95.169  1.00 11.14  ? 214  TYR D CA  1 
ATOM   10009 C  C   . TYR D  1 127 ? 18.778  -19.537 93.685  1.00 11.66  ? 214  TYR D C   1 
ATOM   10010 O  O   . TYR D  1 127 ? 17.828  -19.813 92.932  1.00 11.92  ? 214  TYR D O   1 
ATOM   10011 C  CB  . TYR D  1 127 ? 18.148  -20.594 95.879  1.00 10.96  ? 214  TYR D CB  1 
ATOM   10012 C  CG  . TYR D  1 127 ? 19.240  -21.655 95.870  1.00 10.95  ? 214  TYR D CG  1 
ATOM   10013 C  CD1 . TYR D  1 127 ? 19.158  -22.775 95.028  1.00 12.89  ? 214  TYR D CD1 1 
ATOM   10014 C  CD2 . TYR D  1 127 ? 20.344  -21.546 96.704  1.00 11.63  ? 214  TYR D CD2 1 
ATOM   10015 C  CE1 . TYR D  1 127 ? 20.174  -23.769 95.027  1.00 13.15  ? 214  TYR D CE1 1 
ATOM   10016 C  CE2 . TYR D  1 127 ? 21.354  -22.533 96.723  1.00 12.11  ? 214  TYR D CE2 1 
ATOM   10017 C  CZ  . TYR D  1 127 ? 21.269  -23.623 95.876  1.00 12.51  ? 214  TYR D CZ  1 
ATOM   10018 O  OH  . TYR D  1 127 ? 22.269  -24.579 95.907  1.00 12.50  ? 214  TYR D OH  1 
ATOM   10019 N  N   . GLY D  1 128 ? 20.037  -19.436 93.263  1.00 12.05  ? 215  GLY D N   1 
ATOM   10020 C  CA  . GLY D  1 128 ? 20.368  -19.531 91.834  1.00 12.90  ? 215  GLY D CA  1 
ATOM   10021 C  C   . GLY D  1 128 ? 19.614  -18.528 90.970  1.00 13.10  ? 215  GLY D C   1 
ATOM   10022 O  O   . GLY D  1 128 ? 19.224  -18.843 89.837  1.00 13.24  ? 215  GLY D O   1 
ATOM   10023 N  N   . GLY D  1 129 ? 19.386  -17.325 91.514  1.00 13.12  ? 216  GLY D N   1 
ATOM   10024 C  CA  . GLY D  1 129 ? 18.758  -16.239 90.773  1.00 12.29  ? 216  GLY D CA  1 
ATOM   10025 C  C   . GLY D  1 129 ? 17.239  -16.334 90.638  1.00 12.18  ? 216  GLY D C   1 
ATOM   10026 O  O   . GLY D  1 129 ? 16.646  -15.579 89.860  1.00 11.29  ? 216  GLY D O   1 
ATOM   10027 N  N   . ARG D  1 130 ? 16.598  -17.244 91.386  1.00 12.08  ? 217  ARG D N   1 
ATOM   10028 C  CA  . ARG D  1 130 ? 15.129  -17.397 91.346  1.00 12.01  ? 217  ARG D CA  1 
ATOM   10029 C  C   . ARG D  1 130 ? 14.546  -17.280 92.771  1.00 11.87  ? 217  ARG D C   1 
ATOM   10030 O  O   . ARG D  1 130 ? 15.196  -17.693 93.723  1.00 11.78  ? 217  ARG D O   1 
ATOM   10031 C  CB  . ARG D  1 130 ? 14.739  -18.753 90.712  1.00 12.03  ? 217  ARG D CB  1 
ATOM   10032 C  CG  . ARG D  1 130 ? 15.097  -18.876 89.201  1.00 12.49  ? 217  ARG D CG  1 
ATOM   10033 C  CD  . ARG D  1 130 ? 14.818  -20.253 88.539  1.00 13.43  ? 217  ARG D CD  1 
ATOM   10034 N  NE  . ARG D  1 130 ? 14.357  -20.046 87.161  1.00 15.12  ? 217  ARG D NE  1 
ATOM   10035 C  CZ  . ARG D  1 130 ? 15.050  -20.182 86.019  1.00 19.62  ? 217  ARG D CZ  1 
ATOM   10036 N  NH1 . ARG D  1 130 ? 16.313  -20.607 86.001  1.00 17.80  ? 217  ARG D NH1 1 
ATOM   10037 N  NH2 . ARG D  1 130 ? 14.445  -19.888 84.850  1.00 16.87  ? 217  ARG D NH2 1 
ATOM   10038 N  N   . PRO D  1 131 ? 13.327  -16.723 92.930  1.00 11.67  ? 218  PRO D N   1 
ATOM   10039 C  CA  . PRO D  1 131 ? 12.757  -16.672 94.292  1.00 11.79  ? 218  PRO D CA  1 
ATOM   10040 C  C   . PRO D  1 131 ? 12.234  -18.055 94.718  1.00 12.08  ? 218  PRO D C   1 
ATOM   10041 O  O   . PRO D  1 131 ? 11.563  -18.723 93.934  1.00 11.89  ? 218  PRO D O   1 
ATOM   10042 C  CB  . PRO D  1 131 ? 11.604  -15.682 94.162  1.00 12.13  ? 218  PRO D CB  1 
ATOM   10043 C  CG  . PRO D  1 131 ? 11.197  -15.758 92.740  1.00 11.06  ? 218  PRO D CG  1 
ATOM   10044 C  CD  . PRO D  1 131 ? 12.412  -16.151 91.928  1.00 11.68  ? 218  PRO D CD  1 
ATOM   10045 N  N   . ILE D  1 132 ? 12.541  -18.454 95.951  1.00 11.58  ? 219  ILE D N   1 
ATOM   10046 C  CA  . ILE D  1 132 ? 12.172  -19.770 96.475  1.00 11.59  ? 219  ILE D CA  1 
ATOM   10047 C  C   . ILE D  1 132 ? 11.160  -19.689 97.614  1.00 12.44  ? 219  ILE D C   1 
ATOM   10048 O  O   . ILE D  1 132 ? 10.145  -20.397 97.580  1.00 12.78  ? 219  ILE D O   1 
ATOM   10049 C  CB  . ILE D  1 132 ? 13.418  -20.579 96.958  1.00 10.85  ? 219  ILE D CB  1 
ATOM   10050 C  CG1 . ILE D  1 132 ? 14.553  -20.507 95.914  1.00 11.43  ? 219  ILE D CG1 1 
ATOM   10051 C  CG2 . ILE D  1 132 ? 13.035  -22.053 97.320  1.00 11.11  ? 219  ILE D CG2 1 
ATOM   10052 C  CD1 . ILE D  1 132 ? 14.272  -21.178 94.564  1.00 11.59  ? 219  ILE D CD1 1 
ATOM   10053 N  N   . THR D  1 133 ? 11.451  -18.855 98.615  1.00 12.11  ? 220  THR D N   1 
ATOM   10054 C  CA  . THR D  1 133 ? 10.696  -18.787 99.875  1.00 13.01  ? 220  THR D CA  1 
ATOM   10055 C  C   . THR D  1 133 ? 10.391  -17.324 100.248 1.00 12.92  ? 220  THR D C   1 
ATOM   10056 O  O   . THR D  1 133 ? 11.184  -16.412 99.972  1.00 12.73  ? 220  THR D O   1 
ATOM   10057 C  CB  . THR D  1 133 ? 11.511  -19.464 101.026 1.00 12.67  ? 220  THR D CB  1 
ATOM   10058 O  OG1 . THR D  1 133 ? 11.807  -20.821 100.667 1.00 13.62  ? 220  THR D OG1 1 
ATOM   10059 C  CG2 . THR D  1 133 ? 10.783  -19.415 102.377 1.00 13.79  ? 220  THR D CG2 1 
ATOM   10060 N  N   . GLU D  1 134 ? 9.228   -17.102 100.857 1.00 12.84  ? 221  GLU D N   1 
ATOM   10061 C  CA  . GLU D  1 134 ? 8.925   -15.802 101.443 1.00 12.53  ? 221  GLU D CA  1 
ATOM   10062 C  C   . GLU D  1 134 ? 8.608   -15.987 102.924 1.00 12.48  ? 221  GLU D C   1 
ATOM   10063 O  O   . GLU D  1 134 ? 8.043   -17.023 103.314 1.00 12.01  ? 221  GLU D O   1 
ATOM   10064 C  CB  . GLU D  1 134 ? 7.758   -15.117 100.720 1.00 12.95  ? 221  GLU D CB  1 
ATOM   10065 C  CG  . GLU D  1 134 ? 7.862   -15.142 99.186  1.00 13.72  ? 221  GLU D CG  1 
ATOM   10066 C  CD  . GLU D  1 134 ? 7.471   -16.496 98.623  1.00 16.28  ? 221  GLU D CD  1 
ATOM   10067 O  OE1 . GLU D  1 134 ? 8.207   -17.025 97.770  1.00 19.74  ? 221  GLU D OE1 1 
ATOM   10068 O  OE2 . GLU D  1 134 ? 6.445   -17.053 99.067  1.00 17.45  ? 221  GLU D OE2 1 
ATOM   10069 N  N   . ILE D  1 135 ? 8.988   -14.994 103.728 1.00 11.92  ? 222  ILE D N   1 
ATOM   10070 C  CA  . ILE D  1 135 ? 8.851   -15.033 105.196 1.00 12.16  ? 222  ILE D CA  1 
ATOM   10071 C  C   . ILE D  1 135 ? 8.269   -13.712 105.686 1.00 11.86  ? 222  ILE D C   1 
ATOM   10072 O  O   . ILE D  1 135 ? 8.917   -12.672 105.600 1.00 10.65  ? 222  ILE D O   1 
ATOM   10073 C  CB  . ILE D  1 135 ? 10.230  -15.273 105.902 1.00 12.70  ? 222  ILE D CB  1 
ATOM   10074 C  CG1 . ILE D  1 135 ? 10.918  -16.545 105.367 1.00 11.52  ? 222  ILE D CG1 1 
ATOM   10075 C  CG2 . ILE D  1 135 ? 10.095  -15.290 107.458 1.00 11.90  ? 222  ILE D CG2 1 
ATOM   10076 C  CD1 . ILE D  1 135 ? 12.419  -16.633 105.736 1.00 12.84  ? 222  ILE D CD1 1 
ATOM   10077 N  N   . PRO D  1 136 ? 7.029   -13.751 106.205 1.00 12.25  ? 223  PRO D N   1 
ATOM   10078 C  CA  . PRO D  1 136 ? 6.417   -12.544 106.748 1.00 11.73  ? 223  PRO D CA  1 
ATOM   10079 C  C   . PRO D  1 136 ? 7.013   -12.144 108.104 1.00 11.62  ? 223  PRO D C   1 
ATOM   10080 O  O   . PRO D  1 136 ? 7.460   -13.001 108.868 1.00 11.20  ? 223  PRO D O   1 
ATOM   10081 C  CB  . PRO D  1 136 ? 4.936   -12.926 106.872 1.00 12.39  ? 223  PRO D CB  1 
ATOM   10082 C  CG  . PRO D  1 136 ? 4.925   -14.414 106.982 1.00 12.93  ? 223  PRO D CG  1 
ATOM   10083 C  CD  . PRO D  1 136 ? 6.143   -14.930 106.283 1.00 12.04  ? 223  PRO D CD  1 
ATOM   10084 N  N   . SER D  1 137 ? 7.030   -10.842 108.386 1.00 11.83  ? 224  SER D N   1 
ATOM   10085 C  CA  . SER D  1 137 ? 7.395   -10.328 109.712 1.00 12.19  ? 224  SER D CA  1 
ATOM   10086 C  C   . SER D  1 137 ? 6.653   -11.097 110.832 1.00 12.68  ? 224  SER D C   1 
ATOM   10087 O  O   . SER D  1 137 ? 5.454   -11.356 110.725 1.00 10.47  ? 224  SER D O   1 
ATOM   10088 C  CB  . SER D  1 137 ? 7.081   -8.827  109.760 1.00 13.11  ? 224  SER D CB  1 
ATOM   10089 O  OG  . SER D  1 137 ? 7.228   -8.234  111.030 1.00 13.01  ? 224  SER D OG  1 
ATOM   10090 N  N   . TRP D  1 138 ? 7.385   -11.490 111.874 1.00 12.63  ? 225  TRP D N   1 
ATOM   10091 C  CA  . TRP D  1 138 ? 6.770   -12.149 113.044 1.00 13.85  ? 225  TRP D CA  1 
ATOM   10092 C  C   . TRP D  1 138 ? 6.529   -11.205 114.228 1.00 14.55  ? 225  TRP D C   1 
ATOM   10093 O  O   . TRP D  1 138 ? 5.804   -11.557 115.173 1.00 15.33  ? 225  TRP D O   1 
ATOM   10094 C  CB  . TRP D  1 138 ? 7.574   -13.393 113.487 1.00 13.60  ? 225  TRP D CB  1 
ATOM   10095 C  CG  . TRP D  1 138 ? 9.055   -13.136 113.735 1.00 14.40  ? 225  TRP D CG  1 
ATOM   10096 C  CD1 . TRP D  1 138 ? 9.637   -12.579 114.854 1.00 14.67  ? 225  TRP D CD1 1 
ATOM   10097 C  CD2 . TRP D  1 138 ? 10.127  -13.430 112.836 1.00 14.08  ? 225  TRP D CD2 1 
ATOM   10098 N  NE1 . TRP D  1 138 ? 11.004  -12.516 114.698 1.00 11.90  ? 225  TRP D NE1 1 
ATOM   10099 C  CE2 . TRP D  1 138 ? 11.328  -13.032 113.466 1.00 14.34  ? 225  TRP D CE2 1 
ATOM   10100 C  CE3 . TRP D  1 138 ? 10.189  -13.983 111.550 1.00 15.48  ? 225  TRP D CE3 1 
ATOM   10101 C  CZ2 . TRP D  1 138 ? 12.572  -13.181 112.856 1.00 12.52  ? 225  TRP D CZ2 1 
ATOM   10102 C  CZ3 . TRP D  1 138 ? 11.430  -14.140 110.944 1.00 13.38  ? 225  TRP D CZ3 1 
ATOM   10103 C  CH2 . TRP D  1 138 ? 12.604  -13.745 111.606 1.00 14.11  ? 225  TRP D CH2 1 
ATOM   10104 N  N   . ALA D  1 139 ? 7.111   -10.004 114.180 1.00 14.29  ? 226  ALA D N   1 
ATOM   10105 C  CA  . ALA D  1 139 ? 6.978   -9.027  115.283 1.00 14.69  ? 226  ALA D CA  1 
ATOM   10106 C  C   . ALA D  1 139 ? 6.458   -7.643  114.883 1.00 14.85  ? 226  ALA D C   1 
ATOM   10107 O  O   . ALA D  1 139 ? 6.316   -6.746  115.734 1.00 15.34  ? 226  ALA D O   1 
ATOM   10108 C  CB  . ALA D  1 139 ? 8.314   -8.920  116.082 1.00 14.00  ? 226  ALA D CB  1 
ATOM   10109 N  N   . GLY D  1 140 ? 6.167   -7.460  113.593 1.00 14.66  ? 227  GLY D N   1 
ATOM   10110 C  CA  . GLY D  1 140 ? 5.621   -6.192  113.083 1.00 14.86  ? 227  GLY D CA  1 
ATOM   10111 C  C   . GLY D  1 140 ? 6.503   -4.975  113.301 1.00 14.73  ? 227  GLY D C   1 
ATOM   10112 O  O   . GLY D  1 140 ? 5.996   -3.855  113.465 1.00 14.50  ? 227  GLY D O   1 
ATOM   10113 N  N   . ASN D  1 141 ? 7.827   -5.176  113.301 1.00 14.03  ? 228  ASN D N   1 
ATOM   10114 C  CA  . ASN D  1 141 ? 8.760   -4.065  113.533 1.00 13.57  ? 228  ASN D CA  1 
ATOM   10115 C  C   . ASN D  1 141 ? 10.108  -4.260  112.823 1.00 12.81  ? 228  ASN D C   1 
ATOM   10116 O  O   . ASN D  1 141 ? 11.105  -4.672  113.440 1.00 11.74  ? 228  ASN D O   1 
ATOM   10117 C  CB  . ASN D  1 141 ? 8.969   -3.810  115.035 1.00 13.96  ? 228  ASN D CB  1 
ATOM   10118 C  CG  . ASN D  1 141 ? 9.590   -2.446  115.331 1.00 16.01  ? 228  ASN D CG  1 
ATOM   10119 O  OD1 . ASN D  1 141 ? 10.120  -1.749  114.442 1.00 15.67  ? 228  ASN D OD1 1 
ATOM   10120 N  ND2 . ASN D  1 141 ? 9.518   -2.049  116.601 1.00 18.35  ? 228  ASN D ND2 1 
ATOM   10121 N  N   . ILE D  1 142 ? 10.093  -3.962  111.522 1.00 11.81  ? 229  ILE D N   1 
ATOM   10122 C  CA  . ILE D  1 142 ? 11.294  -3.946  110.672 1.00 11.70  ? 229  ILE D CA  1 
ATOM   10123 C  C   . ILE D  1 142 ? 12.056  -5.274  110.711 1.00 11.29  ? 229  ILE D C   1 
ATOM   10124 O  O   . ILE D  1 142 ? 13.197  -5.342  111.202 1.00 11.70  ? 229  ILE D O   1 
ATOM   10125 C  CB  . ILE D  1 142 ? 12.220  -2.720  110.986 1.00 11.26  ? 229  ILE D CB  1 
ATOM   10126 C  CG1 . ILE D  1 142 ? 11.383  -1.427  111.047 1.00 11.41  ? 229  ILE D CG1 1 
ATOM   10127 C  CG2 . ILE D  1 142 ? 13.347  -2.610  109.930 1.00 11.63  ? 229  ILE D CG2 1 
ATOM   10128 C  CD1 . ILE D  1 142 ? 12.146  -0.198  111.525 1.00 11.59  ? 229  ILE D CD1 1 
ATOM   10129 N  N   . LEU D  1 143 ? 11.416  -6.335  110.210 1.00 10.64  ? 230  LEU D N   1 
ATOM   10130 C  CA  . LEU D  1 143 ? 12.108  -7.600  109.986 1.00 10.80  ? 230  LEU D CA  1 
ATOM   10131 C  C   . LEU D  1 143 ? 13.378  -7.312  109.192 1.00 10.45  ? 230  LEU D C   1 
ATOM   10132 O  O   . LEU D  1 143 ? 13.330  -6.654  108.158 1.00 10.52  ? 230  LEU D O   1 
ATOM   10133 C  CB  . LEU D  1 143 ? 11.219  -8.605  109.213 1.00 10.95  ? 230  LEU D CB  1 
ATOM   10134 C  CG  . LEU D  1 143 ? 11.889  -9.924  108.782 1.00 10.22  ? 230  LEU D CG  1 
ATOM   10135 C  CD1 . LEU D  1 143 ? 12.323  -10.797 109.972 1.00 11.42  ? 230  LEU D CD1 1 
ATOM   10136 C  CD2 . LEU D  1 143 ? 11.006  -10.709 107.797 1.00 10.99  ? 230  LEU D CD2 1 
ATOM   10137 N  N   . ARG D  1 144 ? 14.515  -7.814  109.666 1.00 10.38  ? 231  ARG D N   1 
ATOM   10138 C  CA  . ARG D  1 144 ? 15.808  -7.375  109.107 1.00 10.39  ? 231  ARG D CA  1 
ATOM   10139 C  C   . ARG D  1 144 ? 16.890  -8.424  109.347 1.00 10.26  ? 231  ARG D C   1 
ATOM   10140 O  O   . ARG D  1 144 ? 16.693  -9.331  110.157 1.00 9.99   ? 231  ARG D O   1 
ATOM   10141 C  CB  . ARG D  1 144 ? 16.224  -6.055  109.739 1.00 10.33  ? 231  ARG D CB  1 
ATOM   10142 C  CG  . ARG D  1 144 ? 16.382  -6.113  111.258 1.00 10.75  ? 231  ARG D CG  1 
ATOM   10143 C  CD  . ARG D  1 144 ? 16.396  -4.721  111.839 1.00 12.95  ? 231  ARG D CD  1 
ATOM   10144 N  NE  . ARG D  1 144 ? 16.453  -4.701  113.305 1.00 11.11  ? 231  ARG D NE  1 
ATOM   10145 C  CZ  . ARG D  1 144 ? 15.389  -4.700  114.123 1.00 14.09  ? 231  ARG D CZ  1 
ATOM   10146 N  NH1 . ARG D  1 144 ? 14.140  -4.741  113.649 1.00 11.77  ? 231  ARG D NH1 1 
ATOM   10147 N  NH2 . ARG D  1 144 ? 15.582  -4.649  115.444 1.00 10.82  ? 231  ARG D NH2 1 
ATOM   10148 N  N   . THR D  1 145 ? 18.037  -8.281  108.669 1.00 10.16  ? 232  THR D N   1 
ATOM   10149 C  CA  . THR D  1 145 ? 19.091  -9.308  108.733 1.00 9.22   ? 232  THR D CA  1 
ATOM   10150 C  C   . THR D  1 145 ? 20.548  -8.761  108.720 1.00 8.94   ? 232  THR D C   1 
ATOM   10151 O  O   . THR D  1 145 ? 20.804  -7.608  109.089 1.00 8.61   ? 232  THR D O   1 
ATOM   10152 C  CB  . THR D  1 145 ? 18.815  -10.476 107.708 1.00 9.74   ? 232  THR D CB  1 
ATOM   10153 O  OG1 . THR D  1 145 ? 19.648  -11.621 107.988 1.00 9.38   ? 232  THR D OG1 1 
ATOM   10154 C  CG2 . THR D  1 145 ? 18.954  -10.043 106.237 1.00 11.19  ? 232  THR D CG2 1 
ATOM   10155 N  N   . GLN D  1 146 ? 21.485  -9.600  108.298 1.00 8.60   ? 233  GLN D N   1 
ATOM   10156 C  CA  . GLN D  1 146 ? 22.907  -9.422  108.612 1.00 8.47   ? 233  GLN D CA  1 
ATOM   10157 C  C   . GLN D  1 146 ? 23.614  -8.195  108.015 1.00 7.74   ? 233  GLN D C   1 
ATOM   10158 O  O   . GLN D  1 146 ? 24.453  -7.583  108.690 1.00 6.84   ? 233  GLN D O   1 
ATOM   10159 C  CB  . GLN D  1 146 ? 23.668  -10.703 108.247 1.00 7.97   ? 233  GLN D CB  1 
ATOM   10160 C  CG  . GLN D  1 146 ? 23.164  -11.942 108.990 1.00 9.24   ? 233  GLN D CG  1 
ATOM   10161 C  CD  . GLN D  1 146 ? 23.960  -13.189 108.688 1.00 10.40  ? 233  GLN D CD  1 
ATOM   10162 O  OE1 . GLN D  1 146 ? 25.037  -13.148 108.041 1.00 11.33  ? 233  GLN D OE1 1 
ATOM   10163 N  NE2 . GLN D  1 146 ? 23.465  -14.303 109.166 1.00 8.95   ? 233  GLN D NE2 1 
ATOM   10164 N  N   . GLU D  1 147 ? 23.305  -7.867  106.755 1.00 7.81   ? 234  GLU D N   1 
ATOM   10165 C  CA  . GLU D  1 147 ? 24.040  -6.832  105.970 1.00 8.42   ? 234  GLU D CA  1 
ATOM   10166 C  C   . GLU D  1 147 ? 25.507  -7.223  105.710 1.00 9.12   ? 234  GLU D C   1 
ATOM   10167 O  O   . GLU D  1 147 ? 26.353  -6.361  105.421 1.00 9.31   ? 234  GLU D O   1 
ATOM   10168 C  CB  . GLU D  1 147 ? 23.987  -5.424  106.602 1.00 8.31   ? 234  GLU D CB  1 
ATOM   10169 C  CG  . GLU D  1 147 ? 22.695  -5.025  107.341 1.00 9.10   ? 234  GLU D CG  1 
ATOM   10170 C  CD  . GLU D  1 147 ? 21.450  -5.032  106.488 1.00 10.18  ? 234  GLU D CD  1 
ATOM   10171 O  OE1 . GLU D  1 147 ? 20.389  -4.709  107.067 1.00 10.00  ? 234  GLU D OE1 1 
ATOM   10172 O  OE2 . GLU D  1 147 ? 21.501  -5.355  105.268 1.00 9.59   ? 234  GLU D OE2 1 
ATOM   10173 N  N   . SER D  1 148 ? 25.799  -8.515  105.838 1.00 8.55   ? 235  SER D N   1 
ATOM   10174 C  CA  . SER D  1 148 ? 27.031  -9.115  105.292 1.00 8.96   ? 235  SER D CA  1 
ATOM   10175 C  C   . SER D  1 148 ? 26.730  -10.577 105.006 1.00 8.70   ? 235  SER D C   1 
ATOM   10176 O  O   . SER D  1 148 ? 25.584  -11.023 105.180 1.00 9.29   ? 235  SER D O   1 
ATOM   10177 C  CB  . SER D  1 148 ? 28.239  -8.945  106.214 1.00 8.99   ? 235  SER D CB  1 
ATOM   10178 O  OG  . SER D  1 148 ? 28.041  -9.603  107.462 1.00 8.53   ? 235  SER D OG  1 
ATOM   10179 N  N   . GLU D  1 149 ? 27.729  -11.316 104.541 1.00 7.83   ? 236  GLU D N   1 
ATOM   10180 C  CA  . GLU D  1 149 ? 27.469  -12.667 104.017 1.00 8.25   ? 236  GLU D CA  1 
ATOM   10181 C  C   . GLU D  1 149 ? 27.077  -13.718 105.058 1.00 8.34   ? 236  GLU D C   1 
ATOM   10182 O  O   . GLU D  1 149 ? 27.516  -13.686 106.226 1.00 7.78   ? 236  GLU D O   1 
ATOM   10183 C  CB  . GLU D  1 149 ? 28.620  -13.154 103.133 1.00 7.34   ? 236  GLU D CB  1 
ATOM   10184 C  CG  . GLU D  1 149 ? 29.803  -13.752 103.906 1.00 9.91   ? 236  GLU D CG  1 
ATOM   10185 C  CD  . GLU D  1 149 ? 30.791  -14.523 103.018 1.00 7.71   ? 236  GLU D CD  1 
ATOM   10186 O  OE1 . GLU D  1 149 ? 30.641  -14.500 101.775 1.00 7.14   ? 236  GLU D OE1 1 
ATOM   10187 O  OE2 . GLU D  1 149 ? 31.756  -15.112 103.565 1.00 7.62   ? 236  GLU D OE2 1 
ATOM   10188 N  N   . CYS D  1 150 ? 26.212  -14.634 104.630 1.00 9.08   ? 237  CYS D N   1 
ATOM   10189 C  CA  . CYS D  1 150 ? 25.960  -15.843 105.402 1.00 9.65   ? 237  CYS D CA  1 
ATOM   10190 C  C   . CYS D  1 150 ? 27.065  -16.878 105.089 1.00 10.13  ? 237  CYS D C   1 
ATOM   10191 O  O   . CYS D  1 150 ? 28.013  -16.593 104.322 1.00 10.42  ? 237  CYS D O   1 
ATOM   10192 C  CB  . CYS D  1 150 ? 24.521  -16.367 105.205 1.00 8.31   ? 237  CYS D CB  1 
ATOM   10193 S  SG  . CYS D  1 150 ? 23.828  -16.250 103.520 1.00 9.69   ? 237  CYS D SG  1 
ATOM   10194 N  N   . VAL D  1 151 ? 26.971  -18.052 105.703 1.00 10.85  ? 238  VAL D N   1 
ATOM   10195 C  CA  . VAL D  1 151 ? 27.981  -19.121 105.543 1.00 11.39  ? 238  VAL D CA  1 
ATOM   10196 C  C   . VAL D  1 151 ? 27.231  -20.448 105.418 1.00 10.77  ? 238  VAL D C   1 
ATOM   10197 O  O   . VAL D  1 151 ? 26.222  -20.641 106.096 1.00 11.06  ? 238  VAL D O   1 
ATOM   10198 C  CB  . VAL D  1 151 ? 28.929  -19.197 106.771 1.00 11.83  ? 238  VAL D CB  1 
ATOM   10199 C  CG1 . VAL D  1 151 ? 30.047  -20.225 106.543 1.00 12.75  ? 238  VAL D CG1 1 
ATOM   10200 C  CG2 . VAL D  1 151 ? 29.537  -17.812 107.090 1.00 13.53  ? 238  VAL D CG2 1 
ATOM   10201 N  N   . CYS D  1 152 ? 27.723  -21.356 104.582 1.00 10.60  ? 239  CYS D N   1 
ATOM   10202 C  CA  . CYS D  1 152 ? 27.042  -22.653 104.330 1.00 10.73  ? 239  CYS D CA  1 
ATOM   10203 C  C   . CYS D  1 152 ? 27.954  -23.831 104.658 1.00 11.07  ? 239  CYS D C   1 
ATOM   10204 O  O   . CYS D  1 152 ? 29.186  -23.711 104.560 1.00 11.40  ? 239  CYS D O   1 
ATOM   10205 C  CB  . CYS D  1 152 ? 26.608  -22.756 102.866 1.00 11.03  ? 239  CYS D CB  1 
ATOM   10206 S  SG  . CYS D  1 152 ? 25.650  -21.315 102.293 1.00 10.27  ? 239  CYS D SG  1 
ATOM   10207 N  N   . HIS D  1 153 ? 27.346  -24.971 105.029 1.00 11.32  ? 240  HIS D N   1 
ATOM   10208 C  CA  . HIS D  1 153 ? 28.089  -26.194 105.345 1.00 11.09  ? 240  HIS D CA  1 
ATOM   10209 C  C   . HIS D  1 153 ? 27.234  -27.399 104.930 1.00 11.12  ? 240  HIS D C   1 
ATOM   10210 O  O   . HIS D  1 153 ? 26.117  -27.568 105.443 1.00 10.78  ? 240  HIS D O   1 
ATOM   10211 C  CB  . HIS D  1 153 ? 28.407  -26.277 106.842 1.00 10.76  ? 240  HIS D CB  1 
ATOM   10212 C  CG  . HIS D  1 153 ? 29.151  -27.518 107.230 1.00 11.44  ? 240  HIS D CG  1 
ATOM   10213 N  ND1 . HIS D  1 153 ? 28.546  -28.584 107.870 1.00 13.87  ? 240  HIS D ND1 1 
ATOM   10214 C  CD2 . HIS D  1 153 ? 30.449  -27.863 107.072 1.00 8.95   ? 240  HIS D CD2 1 
ATOM   10215 C  CE1 . HIS D  1 153 ? 29.443  -29.530 108.090 1.00 9.37   ? 240  HIS D CE1 1 
ATOM   10216 N  NE2 . HIS D  1 153 ? 30.602  -29.124 107.606 1.00 15.77  ? 240  HIS D NE2 1 
ATOM   10217 N  N   . LYS D  1 154 ? 27.734  -28.186 103.968 1.00 11.05  ? 241  LYS D N   1 
ATOM   10218 C  CA  . LYS D  1 154 ? 26.976  -29.324 103.412 1.00 12.07  ? 241  LYS D CA  1 
ATOM   10219 C  C   . LYS D  1 154 ? 25.584  -28.886 102.889 1.00 12.49  ? 241  LYS D C   1 
ATOM   10220 O  O   . LYS D  1 154 ? 24.597  -29.610 103.040 1.00 12.70  ? 241  LYS D O   1 
ATOM   10221 C  CB  . LYS D  1 154 ? 26.849  -30.435 104.467 1.00 12.46  ? 241  LYS D CB  1 
ATOM   10222 C  CG  . LYS D  1 154 ? 28.192  -31.048 104.918 1.00 13.76  ? 241  LYS D CG  1 
ATOM   10223 C  CD  . LYS D  1 154 ? 27.984  -32.110 106.001 1.00 12.77  ? 241  LYS D CD  1 
ATOM   10224 C  CE  . LYS D  1 154 ? 29.300  -32.839 106.292 1.00 17.23  ? 241  LYS D CE  1 
ATOM   10225 N  NZ  . LYS D  1 154 ? 29.109  -33.780 107.459 1.00 19.45  ? 241  LYS D NZ  1 
ATOM   10226 N  N   . GLY D  1 155 ? 25.514  -27.694 102.288 1.00 12.14  ? 242  GLY D N   1 
ATOM   10227 C  CA  . GLY D  1 155 ? 24.248  -27.154 101.747 1.00 11.91  ? 242  GLY D CA  1 
ATOM   10228 C  C   . GLY D  1 155 ? 23.341  -26.421 102.732 1.00 12.04  ? 242  GLY D C   1 
ATOM   10229 O  O   . GLY D  1 155 ? 22.347  -25.809 102.334 1.00 11.88  ? 242  GLY D O   1 
ATOM   10230 N  N   . VAL D  1 156 ? 23.674  -26.476 104.019 1.00 11.54  ? 243  VAL D N   1 
ATOM   10231 C  CA  . VAL D  1 156 ? 22.921  -25.737 105.035 1.00 12.05  ? 243  VAL D CA  1 
ATOM   10232 C  C   . VAL D  1 156 ? 23.537  -24.377 105.346 1.00 11.96  ? 243  VAL D C   1 
ATOM   10233 O  O   . VAL D  1 156 ? 24.681  -24.307 105.793 1.00 11.98  ? 243  VAL D O   1 
ATOM   10234 C  CB  . VAL D  1 156 ? 22.782  -26.536 106.339 1.00 11.97  ? 243  VAL D CB  1 
ATOM   10235 C  CG1 . VAL D  1 156 ? 21.989  -25.750 107.336 1.00 11.89  ? 243  VAL D CG1 1 
ATOM   10236 C  CG2 . VAL D  1 156 ? 22.116  -27.924 106.050 1.00 12.05  ? 243  VAL D CG2 1 
ATOM   10237 N  N   . CYS D  1 157 ? 22.755  -23.310 105.111 1.00 11.63  ? 244  CYS D N   1 
ATOM   10238 C  CA  . CYS D  1 157 ? 23.199  -21.906 105.315 1.00 11.61  ? 244  CYS D CA  1 
ATOM   10239 C  C   . CYS D  1 157 ? 22.362  -21.239 106.411 1.00 11.76  ? 244  CYS D C   1 
ATOM   10240 O  O   . CYS D  1 157 ? 21.203  -20.832 106.165 1.00 11.58  ? 244  CYS D O   1 
ATOM   10241 C  CB  . CYS D  1 157 ? 23.124  -21.086 104.009 1.00 10.97  ? 244  CYS D CB  1 
ATOM   10242 S  SG  . CYS D  1 157 ? 23.733  -21.956 102.509 1.00 11.51  ? 244  CYS D SG  1 
ATOM   10243 N  N   . PRO D  1 158 ? 22.919  -21.158 107.642 1.00 11.76  ? 245  PRO D N   1 
ATOM   10244 C  CA  . PRO D  1 158 ? 22.181  -20.454 108.679 1.00 11.34  ? 245  PRO D CA  1 
ATOM   10245 C  C   . PRO D  1 158 ? 22.187  -18.954 108.430 1.00 11.02  ? 245  PRO D C   1 
ATOM   10246 O  O   . PRO D  1 158 ? 23.193  -18.412 107.960 1.00 9.75   ? 245  PRO D O   1 
ATOM   10247 C  CB  . PRO D  1 158 ? 22.957  -20.780 109.966 1.00 11.84  ? 245  PRO D CB  1 
ATOM   10248 C  CG  . PRO D  1 158 ? 23.901  -21.944 109.600 1.00 11.20  ? 245  PRO D CG  1 
ATOM   10249 C  CD  . PRO D  1 158 ? 24.200  -21.697 108.149 1.00 11.88  ? 245  PRO D CD  1 
ATOM   10250 N  N   . VAL D  1 159 ? 21.069  -18.302 108.751 1.00 10.54  ? 246  VAL D N   1 
ATOM   10251 C  CA  . VAL D  1 159 ? 20.942  -16.845 108.653 1.00 10.16  ? 246  VAL D CA  1 
ATOM   10252 C  C   . VAL D  1 159 ? 20.293  -16.306 109.937 1.00 10.49  ? 246  VAL D C   1 
ATOM   10253 O  O   . VAL D  1 159 ? 19.245  -16.801 110.365 1.00 11.52  ? 246  VAL D O   1 
ATOM   10254 C  CB  . VAL D  1 159 ? 20.091  -16.436 107.411 1.00 9.72   ? 246  VAL D CB  1 
ATOM   10255 C  CG1 . VAL D  1 159 ? 19.859  -14.929 107.365 1.00 8.43   ? 246  VAL D CG1 1 
ATOM   10256 C  CG2 . VAL D  1 159 ? 20.767  -16.895 106.097 1.00 9.88   ? 246  VAL D CG2 1 
ATOM   10257 N  N   . VAL D  1 160 ? 20.928  -15.299 110.538 1.00 10.98  ? 247  VAL D N   1 
ATOM   10258 C  CA  . VAL D  1 160 ? 20.397  -14.612 111.720 1.00 10.34  ? 247  VAL D CA  1 
ATOM   10259 C  C   . VAL D  1 160 ? 19.498  -13.430 111.305 1.00 10.71  ? 247  VAL D C   1 
ATOM   10260 O  O   . VAL D  1 160 ? 19.909  -12.571 110.534 1.00 11.01  ? 247  VAL D O   1 
ATOM   10261 C  CB  . VAL D  1 160 ? 21.530  -14.105 112.655 1.00 10.94  ? 247  VAL D CB  1 
ATOM   10262 C  CG1 . VAL D  1 160 ? 20.943  -13.552 113.951 1.00 9.81   ? 247  VAL D CG1 1 
ATOM   10263 C  CG2 . VAL D  1 160 ? 22.513  -15.231 112.979 1.00 10.27  ? 247  VAL D CG2 1 
ATOM   10264 N  N   . MET D  1 161 ? 18.268  -13.396 111.823 1.00 10.41  ? 248  MET D N   1 
ATOM   10265 C  CA  . MET D  1 161 ? 17.319  -12.304 111.549 1.00 10.07  ? 248  MET D CA  1 
ATOM   10266 C  C   . MET D  1 161 ? 16.714  -11.757 112.845 1.00 10.63  ? 248  MET D C   1 
ATOM   10267 O  O   . MET D  1 161 ? 16.564  -12.508 113.832 1.00 10.84  ? 248  MET D O   1 
ATOM   10268 C  CB  . MET D  1 161 ? 16.149  -12.805 110.688 1.00 9.15   ? 248  MET D CB  1 
ATOM   10269 C  CG  . MET D  1 161 ? 16.528  -13.348 109.336 1.00 8.95   ? 248  MET D CG  1 
ATOM   10270 S  SD  . MET D  1 161 ? 15.116  -14.030 108.413 1.00 10.87  ? 248  MET D SD  1 
ATOM   10271 C  CE  . MET D  1 161 ? 16.043  -14.754 107.053 1.00 10.94  ? 248  MET D CE  1 
ATOM   10272 N  N   . THR D  1 162 ? 16.316  -10.484 112.815 1.00 10.46  ? 249  THR D N   1 
ATOM   10273 C  CA  . THR D  1 162 ? 15.695  -9.852  113.976 1.00 11.26  ? 249  THR D CA  1 
ATOM   10274 C  C   . THR D  1 162 ? 14.423  -9.124  113.559 1.00 11.63  ? 249  THR D C   1 
ATOM   10275 O  O   . THR D  1 162 ? 14.336  -8.558  112.469 1.00 11.76  ? 249  THR D O   1 
ATOM   10276 C  CB  . THR D  1 162 ? 16.697  -8.899  114.691 1.00 10.98  ? 249  THR D CB  1 
ATOM   10277 O  OG1 . THR D  1 162 ? 17.827  -9.659  115.137 1.00 12.20  ? 249  THR D OG1 1 
ATOM   10278 C  CG2 . THR D  1 162 ? 16.063  -8.194  115.889 1.00 10.97  ? 249  THR D CG2 1 
ATOM   10279 N  N   . ASP D  1 163 ? 13.412  -9.164  114.416 1.00 11.55  ? 250  ASP D N   1 
ATOM   10280 C  CA  . ASP D  1 163 ? 12.204  -8.379  114.181 1.00 11.92  ? 250  ASP D CA  1 
ATOM   10281 C  C   . ASP D  1 163 ? 11.804  -7.881  115.567 1.00 12.82  ? 250  ASP D C   1 
ATOM   10282 O  O   . ASP D  1 163 ? 11.819  -8.649  116.527 1.00 12.59  ? 250  ASP D O   1 
ATOM   10283 C  CB  . ASP D  1 163 ? 11.143  -9.278  113.535 1.00 11.67  ? 250  ASP D CB  1 
ATOM   10284 C  CG  . ASP D  1 163 ? 9.936   -8.512  112.984 1.00 12.12  ? 250  ASP D CG  1 
ATOM   10285 O  OD1 . ASP D  1 163 ? 9.150   -9.163  112.271 1.00 13.63  ? 250  ASP D OD1 1 
ATOM   10286 O  OD2 . ASP D  1 163 ? 9.744   -7.308  113.266 1.00 12.11  ? 250  ASP D OD2 1 
ATOM   10287 N  N   . GLY D  1 164 ? 11.508  -6.592  115.675 1.00 12.93  ? 251  GLY D N   1 
ATOM   10288 C  CA  . GLY D  1 164 ? 11.263  -5.961  116.978 1.00 13.94  ? 251  GLY D CA  1 
ATOM   10289 C  C   . GLY D  1 164 ? 12.023  -4.670  117.198 1.00 13.99  ? 251  GLY D C   1 
ATOM   10290 O  O   . GLY D  1 164 ? 12.708  -4.180  116.290 1.00 14.68  ? 251  GLY D O   1 
ATOM   10291 N  N   . PRO D  1 165 ? 11.893  -4.074  118.399 1.00 14.22  ? 252  PRO D N   1 
ATOM   10292 C  CA  . PRO D  1 165 ? 12.555  -2.803  118.700 1.00 14.75  ? 252  PRO D CA  1 
ATOM   10293 C  C   . PRO D  1 165 ? 14.079  -2.827  118.511 1.00 15.15  ? 252  PRO D C   1 
ATOM   10294 O  O   . PRO D  1 165 ? 14.720  -3.841  118.778 1.00 15.15  ? 252  PRO D O   1 
ATOM   10295 C  CB  . PRO D  1 165 ? 12.216  -2.570  120.190 1.00 14.83  ? 252  PRO D CB  1 
ATOM   10296 C  CG  . PRO D  1 165 ? 10.981  -3.386  120.446 1.00 14.82  ? 252  PRO D CG  1 
ATOM   10297 C  CD  . PRO D  1 165 ? 11.085  -4.574  119.534 1.00 14.76  ? 252  PRO D CD  1 
ATOM   10298 N  N   . ALA D  1 166 ? 14.630  -1.718  118.030 1.00 15.28  ? 253  ALA D N   1 
ATOM   10299 C  CA  . ALA D  1 166 ? 16.081  -1.510  117.998 1.00 16.26  ? 253  ALA D CA  1 
ATOM   10300 C  C   . ALA D  1 166 ? 16.641  -1.120  119.368 1.00 16.61  ? 253  ALA D C   1 
ATOM   10301 O  O   . ALA D  1 166 ? 17.837  -1.252  119.613 1.00 17.05  ? 253  ALA D O   1 
ATOM   10302 C  CB  . ALA D  1 166 ? 16.438  -0.443  116.953 1.00 16.20  ? 253  ALA D CB  1 
ATOM   10303 N  N   . ASN D  1 167 ? 15.779  -0.647  120.264 1.00 17.52  ? 254  ASN D N   1 
ATOM   10304 C  CA  . ASN D  1 167 ? 16.224  -0.074  121.542 1.00 17.96  ? 254  ASN D CA  1 
ATOM   10305 C  C   . ASN D  1 167 ? 15.661  -0.807  122.773 1.00 18.51  ? 254  ASN D C   1 
ATOM   10306 O  O   . ASN D  1 167 ? 15.503  -0.214  123.849 1.00 18.41  ? 254  ASN D O   1 
ATOM   10307 C  CB  . ASN D  1 167 ? 15.889  1.432   121.587 1.00 18.43  ? 254  ASN D CB  1 
ATOM   10308 C  CG  . ASN D  1 167 ? 14.379  1.707   121.585 1.00 19.01  ? 254  ASN D CG  1 
ATOM   10309 O  OD1 . ASN D  1 167 ? 13.568  0.794   121.446 1.00 18.67  ? 254  ASN D OD1 1 
ATOM   10310 N  ND2 . ASN D  1 167 ? 14.004  2.981   121.757 1.00 21.18  ? 254  ASN D ND2 1 
ATOM   10311 N  N   . ASN D  1 168 ? 15.353  -2.090  122.594 1.00 18.04  ? 255  ASN D N   1 
ATOM   10312 C  CA  . ASN D  1 168 ? 14.754  -2.927  123.636 1.00 19.13  ? 255  ASN D CA  1 
ATOM   10313 C  C   . ASN D  1 168 ? 14.836  -4.382  123.214 1.00 19.00  ? 255  ASN D C   1 
ATOM   10314 O  O   . ASN D  1 168 ? 15.309  -4.683  122.109 1.00 18.46  ? 255  ASN D O   1 
ATOM   10315 C  CB  . ASN D  1 168 ? 13.284  -2.543  123.849 1.00 19.39  ? 255  ASN D CB  1 
ATOM   10316 C  CG  . ASN D  1 168 ? 12.851  -2.687  125.293 1.00 21.11  ? 255  ASN D CG  1 
ATOM   10317 O  OD1 . ASN D  1 168 ? 13.077  -3.717  125.923 1.00 21.53  ? 255  ASN D OD1 1 
ATOM   10318 N  ND2 . ASN D  1 168 ? 12.221  -1.650  125.822 1.00 24.99  ? 255  ASN D ND2 1 
ATOM   10319 N  N   . ARG D  1 169 ? 14.366  -5.284  124.074 1.00 18.98  ? 256  ARG D N   1 
ATOM   10320 C  CA  . ARG D  1 169 ? 14.302  -6.695  123.734 1.00 19.46  ? 256  ARG D CA  1 
ATOM   10321 C  C   . ARG D  1 169 ? 13.524  -6.906  122.419 1.00 18.49  ? 256  ARG D C   1 
ATOM   10322 O  O   . ARG D  1 169 ? 12.459  -6.309  122.211 1.00 18.32  ? 256  ARG D O   1 
ATOM   10323 C  CB  . ARG D  1 169 ? 13.680  -7.509  124.877 1.00 19.29  ? 256  ARG D CB  1 
ATOM   10324 C  CG  . ARG D  1 169 ? 14.010  -8.998  124.766 1.00 21.83  ? 256  ARG D CG  1 
ATOM   10325 C  CD  . ARG D  1 169 ? 13.717  -9.790  126.044 1.00 22.29  ? 256  ARG D CD  1 
ATOM   10326 N  NE  . ARG D  1 169 ? 14.473  -9.385  127.236 1.00 28.36  ? 256  ARG D NE  1 
ATOM   10327 C  CZ  . ARG D  1 169 ? 15.770  -9.620  127.460 1.00 30.64  ? 256  ARG D CZ  1 
ATOM   10328 N  NH1 . ARG D  1 169 ? 16.546  -10.218 126.550 1.00 30.61  ? 256  ARG D NH1 1 
ATOM   10329 N  NH2 . ARG D  1 169 ? 16.305  -9.223  128.608 1.00 32.22  ? 256  ARG D NH2 1 
ATOM   10330 N  N   . ALA D  1 170 ? 14.071  -7.739  121.535 1.00 16.98  ? 257  ALA D N   1 
ATOM   10331 C  CA  . ALA D  1 170 ? 13.458  -8.027  120.224 1.00 15.47  ? 257  ALA D CA  1 
ATOM   10332 C  C   . ALA D  1 170 ? 13.379  -9.539  119.999 1.00 14.94  ? 257  ALA D C   1 
ATOM   10333 O  O   . ALA D  1 170 ? 13.837  -10.325 120.841 1.00 15.07  ? 257  ALA D O   1 
ATOM   10334 C  CB  . ALA D  1 170 ? 14.255  -7.351  119.093 1.00 14.83  ? 257  ALA D CB  1 
ATOM   10335 N  N   . ALA D  1 171 ? 12.803  -9.953  118.873 1.00 12.94  ? 258  ALA D N   1 
ATOM   10336 C  CA  . ALA D  1 171 ? 12.680  -11.379 118.559 1.00 11.52  ? 258  ALA D CA  1 
ATOM   10337 C  C   . ALA D  1 171 ? 13.643  -11.821 117.451 1.00 11.08  ? 258  ALA D C   1 
ATOM   10338 O  O   . ALA D  1 171 ? 13.384  -11.615 116.261 1.00 11.35  ? 258  ALA D O   1 
ATOM   10339 C  CB  . ALA D  1 171 ? 11.208  -11.718 118.187 1.00 10.46  ? 258  ALA D CB  1 
ATOM   10340 N  N   . THR D  1 172 ? 14.748  -12.449 117.847 1.00 10.22  ? 259  THR D N   1 
ATOM   10341 C  CA  . THR D  1 172 ? 15.777  -12.873 116.916 1.00 9.93   ? 259  THR D CA  1 
ATOM   10342 C  C   . THR D  1 172 ? 15.574  -14.364 116.659 1.00 10.59  ? 259  THR D C   1 
ATOM   10343 O  O   . THR D  1 172 ? 15.212  -15.111 117.577 1.00 9.82   ? 259  THR D O   1 
ATOM   10344 C  CB  . THR D  1 172 ? 17.214  -12.535 117.475 1.00 9.86   ? 259  THR D CB  1 
ATOM   10345 O  OG1 . THR D  1 172 ? 17.392  -11.106 117.501 1.00 10.35  ? 259  THR D OG1 1 
ATOM   10346 C  CG2 . THR D  1 172 ? 18.324  -13.164 116.629 1.00 8.52   ? 259  THR D CG2 1 
ATOM   10347 N  N   . LYS D  1 173 ? 15.758  -14.780 115.405 1.00 10.78  ? 260  LYS D N   1 
ATOM   10348 C  CA  . LYS D  1 173 ? 15.660  -16.178 115.029 1.00 12.20  ? 260  LYS D CA  1 
ATOM   10349 C  C   . LYS D  1 173 ? 16.825  -16.575 114.154 1.00 12.95  ? 260  LYS D C   1 
ATOM   10350 O  O   . LYS D  1 173 ? 17.328  -15.766 113.397 1.00 12.84  ? 260  LYS D O   1 
ATOM   10351 C  CB  . LYS D  1 173 ? 14.363  -16.452 114.268 1.00 12.30  ? 260  LYS D CB  1 
ATOM   10352 C  CG  . LYS D  1 173 ? 13.093  -16.161 115.087 1.00 11.74  ? 260  LYS D CG  1 
ATOM   10353 C  CD  . LYS D  1 173 ? 11.820  -16.475 114.295 1.00 12.64  ? 260  LYS D CD  1 
ATOM   10354 C  CE  . LYS D  1 173 ? 10.585  -16.151 115.146 1.00 16.79  ? 260  LYS D CE  1 
ATOM   10355 N  NZ  . LYS D  1 173 ? 9.349   -16.772 114.558 1.00 20.71  ? 260  LYS D NZ  1 
ATOM   10356 N  N   . ILE D  1 174 ? 17.249  -17.831 114.260 1.00 13.32  ? 261  ILE D N   1 
ATOM   10357 C  CA  . ILE D  1 174 ? 18.205  -18.375 113.307 1.00 13.84  ? 261  ILE D CA  1 
ATOM   10358 C  C   . ILE D  1 174 ? 17.423  -19.275 112.358 1.00 13.67  ? 261  ILE D C   1 
ATOM   10359 O  O   . ILE D  1 174 ? 16.745  -20.236 112.789 1.00 14.33  ? 261  ILE D O   1 
ATOM   10360 C  CB  . ILE D  1 174 ? 19.363  -19.135 114.013 1.00 13.68  ? 261  ILE D CB  1 
ATOM   10361 C  CG1 . ILE D  1 174 ? 19.972  -18.268 115.128 1.00 14.85  ? 261  ILE D CG1 1 
ATOM   10362 C  CG2 . ILE D  1 174 ? 20.413  -19.662 112.989 1.00 14.51  ? 261  ILE D CG2 1 
ATOM   10363 C  CD1 . ILE D  1 174 ? 21.260  -18.810 115.700 1.00 16.09  ? 261  ILE D CD1 1 
ATOM   10364 N  N   . ILE D  1 175 ? 17.494  -18.953 111.066 1.00 12.78  ? 262  ILE D N   1 
ATOM   10365 C  CA  . ILE D  1 175 ? 16.811  -19.751 110.062 1.00 12.61  ? 262  ILE D CA  1 
ATOM   10366 C  C   . ILE D  1 175 ? 17.825  -20.526 109.218 1.00 12.46  ? 262  ILE D C   1 
ATOM   10367 O  O   . ILE D  1 175 ? 18.771  -19.947 108.670 1.00 12.01  ? 262  ILE D O   1 
ATOM   10368 C  CB  . ILE D  1 175 ? 15.806  -18.924 109.219 1.00 12.21  ? 262  ILE D CB  1 
ATOM   10369 C  CG1 . ILE D  1 175 ? 14.804  -18.214 110.159 1.00 12.79  ? 262  ILE D CG1 1 
ATOM   10370 C  CG2 . ILE D  1 175 ? 15.097  -19.827 108.175 1.00 11.23  ? 262  ILE D CG2 1 
ATOM   10371 C  CD1 . ILE D  1 175 ? 13.613  -17.534 109.471 1.00 13.08  ? 262  ILE D CD1 1 
ATOM   10372 N  N   . TYR D  1 176 ? 17.620  -21.837 109.151 1.00 12.28  ? 263  TYR D N   1 
ATOM   10373 C  CA  . TYR D  1 176 ? 18.551  -22.740 108.478 1.00 12.70  ? 263  TYR D CA  1 
ATOM   10374 C  C   . TYR D  1 176 ? 18.005  -23.077 107.101 1.00 12.68  ? 263  TYR D C   1 
ATOM   10375 O  O   . TYR D  1 176 ? 16.938  -23.676 106.994 1.00 13.40  ? 263  TYR D O   1 
ATOM   10376 C  CB  . TYR D  1 176 ? 18.758  -24.015 109.317 1.00 12.86  ? 263  TYR D CB  1 
ATOM   10377 C  CG  . TYR D  1 176 ? 19.336  -23.737 110.686 1.00 12.83  ? 263  TYR D CG  1 
ATOM   10378 C  CD1 . TYR D  1 176 ? 18.501  -23.420 111.774 1.00 14.06  ? 263  TYR D CD1 1 
ATOM   10379 C  CD2 . TYR D  1 176 ? 20.717  -23.787 110.902 1.00 12.98  ? 263  TYR D CD2 1 
ATOM   10380 C  CE1 . TYR D  1 176 ? 19.037  -23.164 113.045 1.00 13.54  ? 263  TYR D CE1 1 
ATOM   10381 C  CE2 . TYR D  1 176 ? 21.263  -23.517 112.163 1.00 10.98  ? 263  TYR D CE2 1 
ATOM   10382 C  CZ  . TYR D  1 176 ? 20.422  -23.215 113.224 1.00 12.75  ? 263  TYR D CZ  1 
ATOM   10383 O  OH  . TYR D  1 176 ? 20.956  -22.948 114.465 1.00 12.69  ? 263  TYR D OH  1 
ATOM   10384 N  N   . PHE D  1 177 ? 18.723  -22.666 106.055 1.00 12.57  ? 264  PHE D N   1 
ATOM   10385 C  CA  . PHE D  1 177 ? 18.274  -22.834 104.667 1.00 12.20  ? 264  PHE D CA  1 
ATOM   10386 C  C   . PHE D  1 177 ? 19.027  -23.925 103.911 1.00 12.62  ? 264  PHE D C   1 
ATOM   10387 O  O   . PHE D  1 177 ? 20.209  -24.155 104.154 1.00 12.76  ? 264  PHE D O   1 
ATOM   10388 C  CB  . PHE D  1 177 ? 18.463  -21.505 103.909 1.00 11.73  ? 264  PHE D CB  1 
ATOM   10389 C  CG  . PHE D  1 177 ? 17.533  -20.413 104.341 1.00 10.88  ? 264  PHE D CG  1 
ATOM   10390 C  CD1 . PHE D  1 177 ? 17.983  -19.381 105.181 1.00 10.60  ? 264  PHE D CD1 1 
ATOM   10391 C  CD2 . PHE D  1 177 ? 16.204  -20.401 103.898 1.00 9.94   ? 264  PHE D CD2 1 
ATOM   10392 C  CE1 . PHE D  1 177 ? 17.114  -18.346 105.586 1.00 11.17  ? 264  PHE D CE1 1 
ATOM   10393 C  CE2 . PHE D  1 177 ? 15.324  -19.371 104.295 1.00 10.16  ? 264  PHE D CE2 1 
ATOM   10394 C  CZ  . PHE D  1 177 ? 15.789  -18.335 105.130 1.00 10.03  ? 264  PHE D CZ  1 
ATOM   10395 N  N   . LYS D  1 178 ? 18.354  -24.571 102.972 1.00 13.15  ? 265  LYS D N   1 
ATOM   10396 C  CA  . LYS D  1 178 ? 19.035  -25.425 101.991 1.00 14.18  ? 265  LYS D CA  1 
ATOM   10397 C  C   . LYS D  1 178 ? 18.358  -25.279 100.644 1.00 14.03  ? 265  LYS D C   1 
ATOM   10398 O  O   . LYS D  1 178 ? 17.158  -25.543 100.519 1.00 13.23  ? 265  LYS D O   1 
ATOM   10399 C  CB  . LYS D  1 178 ? 19.048  -26.900 102.418 1.00 13.56  ? 265  LYS D CB  1 
ATOM   10400 C  CG  . LYS D  1 178 ? 19.812  -27.819 101.451 1.00 14.19  ? 265  LYS D CG  1 
ATOM   10401 C  CD  . LYS D  1 178 ? 20.023  -29.201 102.069 1.00 16.65  ? 265  LYS D CD  1 
ATOM   10402 C  CE  . LYS D  1 178 ? 20.752  -30.136 101.121 1.00 21.25  ? 265  LYS D CE  1 
ATOM   10403 N  NZ  . LYS D  1 178 ? 20.677  -31.544 101.616 1.00 24.59  ? 265  LYS D NZ  1 
ATOM   10404 N  N   . GLU D  1 179 ? 19.138  -24.857 99.644  1.00 14.33  ? 266  GLU D N   1 
ATOM   10405 C  CA  . GLU D  1 179 ? 18.611  -24.539 98.307  1.00 14.69  ? 266  GLU D CA  1 
ATOM   10406 C  C   . GLU D  1 179 ? 17.427  -23.543 98.408  1.00 13.98  ? 266  GLU D C   1 
ATOM   10407 O  O   . GLU D  1 179 ? 16.429  -23.634 97.674  1.00 13.64  ? 266  GLU D O   1 
ATOM   10408 C  CB  . GLU D  1 179 ? 18.277  -25.823 97.518  1.00 14.36  ? 266  GLU D CB  1 
ATOM   10409 C  CG  . GLU D  1 179 ? 19.510  -26.694 97.295  1.00 15.50  ? 266  GLU D CG  1 
ATOM   10410 C  CD  . GLU D  1 179 ? 19.215  -28.063 96.701  1.00 18.03  ? 266  GLU D CD  1 
ATOM   10411 O  OE1 . GLU D  1 179 ? 18.098  -28.590 96.883  1.00 20.68  ? 266  GLU D OE1 1 
ATOM   10412 O  OE2 . GLU D  1 179 ? 20.129  -28.621 96.056  1.00 23.77  ? 266  GLU D OE2 1 
ATOM   10413 N  N   . GLY D  1 180 ? 17.558  -22.601 99.338  1.00 12.91  ? 267  GLY D N   1 
ATOM   10414 C  CA  . GLY D  1 180 ? 16.550  -21.543 99.534  1.00 13.10  ? 267  GLY D CA  1 
ATOM   10415 C  C   . GLY D  1 180 ? 15.317  -21.971 100.333 1.00 13.34  ? 267  GLY D C   1 
ATOM   10416 O  O   . GLY D  1 180 ? 14.420  -21.166 100.569 1.00 13.65  ? 267  GLY D O   1 
ATOM   10417 N  N   . LYS D  1 181 ? 15.277  -23.236 100.757 1.00 13.64  ? 268  LYS D N   1 
ATOM   10418 C  CA  . LYS D  1 181 ? 14.134  -23.745 101.545 1.00 14.47  ? 268  LYS D CA  1 
ATOM   10419 C  C   . LYS D  1 181 ? 14.434  -23.843 103.037 1.00 13.86  ? 268  LYS D C   1 
ATOM   10420 O  O   . LYS D  1 181 ? 15.536  -24.231 103.436 1.00 13.51  ? 268  LYS D O   1 
ATOM   10421 C  CB  . LYS D  1 181 ? 13.692  -25.125 101.028 1.00 14.34  ? 268  LYS D CB  1 
ATOM   10422 C  CG  . LYS D  1 181 ? 13.275  -25.128 99.562  1.00 17.91  ? 268  LYS D CG  1 
ATOM   10423 C  CD  . LYS D  1 181 ? 13.154  -26.569 99.072  1.00 23.66  ? 268  LYS D CD  1 
ATOM   10424 C  CE  . LYS D  1 181 ? 13.516  -26.653 97.599  1.00 27.71  ? 268  LYS D CE  1 
ATOM   10425 N  NZ  . LYS D  1 181 ? 14.488  -27.773 97.263  1.00 30.67  ? 268  LYS D NZ  1 
ATOM   10426 N  N   . ILE D  1 182 ? 13.422  -23.551 103.854 1.00 14.25  ? 269  ILE D N   1 
ATOM   10427 C  CA  . ILE D  1 182 ? 13.578  -23.524 105.309 1.00 14.11  ? 269  ILE D CA  1 
ATOM   10428 C  C   . ILE D  1 182 ? 13.653  -24.960 105.848 1.00 14.73  ? 269  ILE D C   1 
ATOM   10429 O  O   . ILE D  1 182 ? 12.700  -25.716 105.701 1.00 15.44  ? 269  ILE D O   1 
ATOM   10430 C  CB  . ILE D  1 182 ? 12.424  -22.749 105.994 1.00 14.57  ? 269  ILE D CB  1 
ATOM   10431 C  CG1 . ILE D  1 182 ? 12.442  -21.261 105.577 1.00 12.74  ? 269  ILE D CG1 1 
ATOM   10432 C  CG2 . ILE D  1 182 ? 12.494  -22.917 107.540 1.00 13.84  ? 269  ILE D CG2 1 
ATOM   10433 C  CD1 . ILE D  1 182 ? 11.224  -20.469 106.021 1.00 14.55  ? 269  ILE D CD1 1 
ATOM   10434 N  N   . GLN D  1 183 ? 14.794  -25.314 106.442 1.00 14.86  ? 270  GLN D N   1 
ATOM   10435 C  CA  . GLN D  1 183 ? 15.012  -26.606 107.109 1.00 15.03  ? 270  GLN D CA  1 
ATOM   10436 C  C   . GLN D  1 183 ? 14.588  -26.614 108.573 1.00 15.35  ? 270  GLN D C   1 
ATOM   10437 O  O   . GLN D  1 183 ? 14.185  -27.653 109.104 1.00 15.21  ? 270  GLN D O   1 
ATOM   10438 C  CB  . GLN D  1 183 ? 16.494  -27.021 107.036 1.00 15.21  ? 270  GLN D CB  1 
ATOM   10439 C  CG  . GLN D  1 183 ? 17.071  -27.075 105.636 1.00 14.73  ? 270  GLN D CG  1 
ATOM   10440 C  CD  . GLN D  1 183 ? 16.270  -27.942 104.700 1.00 15.91  ? 270  GLN D CD  1 
ATOM   10441 O  OE1 . GLN D  1 183 ? 16.363  -29.164 104.740 1.00 16.68  ? 270  GLN D OE1 1 
ATOM   10442 N  NE2 . GLN D  1 183 ? 15.487  -27.316 103.839 1.00 14.29  ? 270  GLN D NE2 1 
ATOM   10443 N  N   . LYS D  1 184 ? 14.672  -25.457 109.225 1.00 15.42  ? 271  LYS D N   1 
ATOM   10444 C  CA  . LYS D  1 184 ? 14.483  -25.365 110.678 1.00 15.90  ? 271  LYS D CA  1 
ATOM   10445 C  C   . LYS D  1 184 ? 14.538  -23.899 111.030 1.00 15.46  ? 271  LYS D C   1 
ATOM   10446 O  O   . LYS D  1 184 ? 15.294  -23.153 110.409 1.00 15.58  ? 271  LYS D O   1 
ATOM   10447 C  CB  . LYS D  1 184 ? 15.617  -26.089 111.432 1.00 15.66  ? 271  LYS D CB  1 
ATOM   10448 C  CG  . LYS D  1 184 ? 15.429  -26.200 112.970 1.00 16.70  ? 271  LYS D CG  1 
ATOM   10449 C  CD  . LYS D  1 184 ? 16.644  -26.907 113.634 1.00 16.57  ? 271  LYS D CD  1 
ATOM   10450 C  CE  . LYS D  1 184 ? 16.387  -27.278 115.105 1.00 17.28  ? 271  LYS D CE  1 
ATOM   10451 N  NZ  . LYS D  1 184 ? 17.583  -27.988 115.716 1.00 16.39  ? 271  LYS D NZ  1 
ATOM   10452 N  N   . ILE D  1 185 ? 13.759  -23.512 112.036 1.00 15.04  ? 272  ILE D N   1 
ATOM   10453 C  CA  . ILE D  1 185 ? 13.756  -22.161 112.603 1.00 15.50  ? 272  ILE D CA  1 
ATOM   10454 C  C   . ILE D  1 185 ? 13.943  -22.276 114.114 1.00 15.97  ? 272  ILE D C   1 
ATOM   10455 O  O   . ILE D  1 185 ? 13.232  -23.050 114.766 1.00 16.63  ? 272  ILE D O   1 
ATOM   10456 C  CB  . ILE D  1 185 ? 12.421  -21.412 112.304 1.00 15.27  ? 272  ILE D CB  1 
ATOM   10457 C  CG1 . ILE D  1 185 ? 12.184  -21.288 110.794 1.00 16.39  ? 272  ILE D CG1 1 
ATOM   10458 C  CG2 . ILE D  1 185 ? 12.387  -20.060 113.016 1.00 16.03  ? 272  ILE D CG2 1 
ATOM   10459 C  CD1 . ILE D  1 185 ? 10.807  -20.631 110.408 1.00 15.71  ? 272  ILE D CD1 1 
ATOM   10460 N  N   . GLU D  1 186 ? 14.892  -21.513 114.668 1.00 15.57  ? 273  GLU D N   1 
ATOM   10461 C  CA  . GLU D  1 186 ? 15.148  -21.499 116.108 1.00 15.14  ? 273  GLU D CA  1 
ATOM   10462 C  C   . GLU D  1 186 ? 14.997  -20.079 116.633 1.00 14.87  ? 273  GLU D C   1 
ATOM   10463 O  O   . GLU D  1 186 ? 15.477  -19.134 116.003 1.00 14.09  ? 273  GLU D O   1 
ATOM   10464 C  CB  . GLU D  1 186 ? 16.580  -21.942 116.419 1.00 14.82  ? 273  GLU D CB  1 
ATOM   10465 C  CG  . GLU D  1 186 ? 16.915  -23.410 116.211 1.00 16.08  ? 273  GLU D CG  1 
ATOM   10466 C  CD  . GLU D  1 186 ? 18.229  -23.770 116.901 1.00 16.00  ? 273  GLU D CD  1 
ATOM   10467 O  OE1 . GLU D  1 186 ? 19.277  -23.196 116.552 1.00 14.90  ? 273  GLU D OE1 1 
ATOM   10468 O  OE2 . GLU D  1 186 ? 18.212  -24.600 117.823 1.00 16.46  ? 273  GLU D OE2 1 
ATOM   10469 N  N   . GLU D  1 187 ? 14.367  -19.934 117.796 1.00 14.49  ? 274  GLU D N   1 
ATOM   10470 C  CA  . GLU D  1 187 ? 14.433  -18.689 118.532 1.00 15.08  ? 274  GLU D CA  1 
ATOM   10471 C  C   . GLU D  1 187 ? 15.806  -18.573 119.177 1.00 14.49  ? 274  GLU D C   1 
ATOM   10472 O  O   . GLU D  1 187 ? 16.372  -19.578 119.611 1.00 14.30  ? 274  GLU D O   1 
ATOM   10473 C  CB  . GLU D  1 187 ? 13.357  -18.630 119.612 1.00 15.78  ? 274  GLU D CB  1 
ATOM   10474 C  CG  . GLU D  1 187 ? 11.977  -18.345 119.068 1.00 20.72  ? 274  GLU D CG  1 
ATOM   10475 C  CD  . GLU D  1 187 ? 10.895  -18.736 120.054 1.00 27.91  ? 274  GLU D CD  1 
ATOM   10476 O  OE1 . GLU D  1 187 ? 11.168  -18.736 121.276 1.00 29.90  ? 274  GLU D OE1 1 
ATOM   10477 O  OE2 . GLU D  1 187 ? 9.774   -19.062 119.600 1.00 33.15  ? 274  GLU D OE2 1 
ATOM   10478 N  N   . LEU D  1 188 ? 16.329  -17.352 119.224 1.00 13.94  ? 275  LEU D N   1 
ATOM   10479 C  CA  . LEU D  1 188 ? 17.607  -17.063 119.891 1.00 14.05  ? 275  LEU D CA  1 
ATOM   10480 C  C   . LEU D  1 188 ? 17.577  -17.576 121.335 1.00 14.01  ? 275  LEU D C   1 
ATOM   10481 O  O   . LEU D  1 188 ? 16.621  -17.321 122.070 1.00 13.53  ? 275  LEU D O   1 
ATOM   10482 C  CB  . LEU D  1 188 ? 17.900  -15.547 119.886 1.00 13.96  ? 275  LEU D CB  1 
ATOM   10483 C  CG  . LEU D  1 188 ? 19.188  -15.067 120.574 1.00 13.48  ? 275  LEU D CG  1 
ATOM   10484 C  CD1 . LEU D  1 188 ? 20.424  -15.473 119.746 1.00 15.73  ? 275  LEU D CD1 1 
ATOM   10485 C  CD2 . LEU D  1 188 ? 19.160  -13.564 120.877 1.00 14.02  ? 275  LEU D CD2 1 
ATOM   10486 N  N   . ALA D  1 189 ? 18.620  -18.304 121.720 1.00 14.83  ? 276  ALA D N   1 
ATOM   10487 C  CA  . ALA D  1 189 ? 18.797  -18.757 123.107 1.00 15.25  ? 276  ALA D CA  1 
ATOM   10488 C  C   . ALA D  1 189 ? 20.144  -18.243 123.647 1.00 15.57  ? 276  ALA D C   1 
ATOM   10489 O  O   . ALA D  1 189 ? 20.957  -17.721 122.881 1.00 15.53  ? 276  ALA D O   1 
ATOM   10490 C  CB  . ALA D  1 189 ? 18.716  -20.290 123.172 1.00 15.55  ? 276  ALA D CB  1 
ATOM   10491 N  N   . GLY D  1 190 ? 20.363  -18.370 124.957 1.00 15.45  ? 277  GLY D N   1 
ATOM   10492 C  CA  . GLY D  1 190 ? 21.619  -17.971 125.565 1.00 15.34  ? 277  GLY D CA  1 
ATOM   10493 C  C   . GLY D  1 190 ? 21.641  -16.573 126.142 1.00 15.21  ? 277  GLY D C   1 
ATOM   10494 O  O   . GLY D  1 190 ? 20.597  -15.986 126.436 1.00 14.56  ? 277  GLY D O   1 
ATOM   10495 N  N   . ASN D  1 191 ? 22.855  -16.054 126.314 1.00 15.68  ? 278  ASN D N   1 
ATOM   10496 C  CA  . ASN D  1 191 ? 23.090  -14.853 127.115 1.00 15.62  ? 278  ASN D CA  1 
ATOM   10497 C  C   . ASN D  1 191 ? 23.142  -13.521 126.345 1.00 15.25  ? 278  ASN D C   1 
ATOM   10498 O  O   . ASN D  1 191 ? 23.129  -12.465 126.958 1.00 15.05  ? 278  ASN D O   1 
ATOM   10499 C  CB  . ASN D  1 191 ? 24.347  -15.049 127.991 1.00 16.47  ? 278  ASN D CB  1 
ATOM   10500 C  CG  . ASN D  1 191 ? 24.096  -15.995 129.182 1.00 18.68  ? 278  ASN D CG  1 
ATOM   10501 O  OD1 . ASN D  1 191 ? 22.955  -16.212 129.599 1.00 21.14  ? 278  ASN D OD1 1 
ATOM   10502 N  ND2 . ASN D  1 191 ? 25.163  -16.559 129.716 1.00 20.46  ? 278  ASN D ND2 1 
ATOM   10503 N  N   . ALA D  1 192 ? 23.193  -13.562 125.011 1.00 14.96  ? 279  ALA D N   1 
ATOM   10504 C  CA  . ALA D  1 192 ? 23.095  -12.329 124.218 1.00 13.99  ? 279  ALA D CA  1 
ATOM   10505 C  C   . ALA D  1 192 ? 21.712  -11.722 124.434 1.00 13.86  ? 279  ALA D C   1 
ATOM   10506 O  O   . ALA D  1 192 ? 20.707  -12.419 124.284 1.00 13.59  ? 279  ALA D O   1 
ATOM   10507 C  CB  . ALA D  1 192 ? 23.348  -12.614 122.715 1.00 14.11  ? 279  ALA D CB  1 
ATOM   10508 N  N   . GLN D  1 193 ? 21.662  -10.439 124.799 1.00 13.05  ? 280  GLN D N   1 
ATOM   10509 C  CA  . GLN D  1 193 ? 20.390  -9.771  125.167 1.00 14.25  ? 280  GLN D CA  1 
ATOM   10510 C  C   . GLN D  1 193 ? 19.666  -9.059  124.008 1.00 13.44  ? 280  GLN D C   1 
ATOM   10511 O  O   . GLN D  1 193 ? 18.455  -8.757  124.093 1.00 13.32  ? 280  GLN D O   1 
ATOM   10512 C  CB  . GLN D  1 193 ? 20.625  -8.787  126.328 1.00 13.54  ? 280  GLN D CB  1 
ATOM   10513 C  CG  . GLN D  1 193 ? 21.035  -9.474  127.660 1.00 14.93  ? 280  GLN D CG  1 
ATOM   10514 C  CD  . GLN D  1 193 ? 20.834  -8.578  128.896 1.00 16.30  ? 280  GLN D CD  1 
ATOM   10515 O  OE1 . GLN D  1 193 ? 19.964  -7.693  128.916 1.00 21.80  ? 280  GLN D OE1 1 
ATOM   10516 N  NE2 . GLN D  1 193 ? 21.630  -8.820  129.938 1.00 18.37  ? 280  GLN D NE2 1 
ATOM   10517 N  N   . HIS D  1 194 ? 20.414  -8.776  122.941 1.00 13.70  ? 281  HIS D N   1 
ATOM   10518 C  CA  . HIS D  1 194 ? 19.889  -8.110  121.739 1.00 12.93  ? 281  HIS D CA  1 
ATOM   10519 C  C   . HIS D  1 194 ? 20.868  -8.370  120.598 1.00 12.77  ? 281  HIS D C   1 
ATOM   10520 O  O   . HIS D  1 194 ? 22.098  -8.326  120.793 1.00 12.60  ? 281  HIS D O   1 
ATOM   10521 C  CB  . HIS D  1 194 ? 19.713  -6.594  121.978 1.00 13.39  ? 281  HIS D CB  1 
ATOM   10522 C  CG  . HIS D  1 194 ? 19.057  -5.873  120.840 1.00 13.38  ? 281  HIS D CG  1 
ATOM   10523 N  ND1 . HIS D  1 194 ? 17.686  -5.764  120.713 1.00 13.20  ? 281  HIS D ND1 1 
ATOM   10524 C  CD2 . HIS D  1 194 ? 19.585  -5.225  119.777 1.00 12.87  ? 281  HIS D CD2 1 
ATOM   10525 C  CE1 . HIS D  1 194 ? 17.401  -5.079  119.617 1.00 13.47  ? 281  HIS D CE1 1 
ATOM   10526 N  NE2 . HIS D  1 194 ? 18.537  -4.749  119.027 1.00 16.09  ? 281  HIS D NE2 1 
ATOM   10527 N  N   . ILE D  1 195 ? 20.317  -8.646  119.417 1.00 12.50  ? 282  ILE D N   1 
ATOM   10528 C  CA  . ILE D  1 195 ? 21.112  -9.058  118.256 1.00 12.01  ? 282  ILE D CA  1 
ATOM   10529 C  C   . ILE D  1 195 ? 20.754  -8.256  117.009 1.00 12.24  ? 282  ILE D C   1 
ATOM   10530 O  O   . ILE D  1 195 ? 19.572  -8.198  116.615 1.00 12.15  ? 282  ILE D O   1 
ATOM   10531 C  CB  . ILE D  1 195 ? 20.932  -10.585 117.943 1.00 12.32  ? 282  ILE D CB  1 
ATOM   10532 C  CG1 . ILE D  1 195 ? 21.509  -11.462 119.056 1.00 11.31  ? 282  ILE D CG1 1 
ATOM   10533 C  CG2 . ILE D  1 195 ? 21.571  -10.947 116.589 1.00 12.68  ? 282  ILE D CG2 1 
ATOM   10534 C  CD1 . ILE D  1 195 ? 23.030  -11.370 119.208 1.00 12.83  ? 282  ILE D CD1 1 
ATOM   10535 N  N   . GLU D  1 196 ? 21.779  -7.665  116.382 1.00 11.48  ? 283  GLU D N   1 
ATOM   10536 C  CA  . GLU D  1 196 ? 21.623  -6.979  115.104 1.00 11.26  ? 283  GLU D CA  1 
ATOM   10537 C  C   . GLU D  1 196 ? 22.797  -7.309  114.189 1.00 10.02  ? 283  GLU D C   1 
ATOM   10538 O  O   . GLU D  1 196 ? 23.923  -7.525  114.675 1.00 9.19   ? 283  GLU D O   1 
ATOM   10539 C  CB  . GLU D  1 196 ? 21.606  -5.455  115.280 1.00 11.31  ? 283  GLU D CB  1 
ATOM   10540 C  CG  . GLU D  1 196 ? 20.500  -4.888  116.213 1.00 13.54  ? 283  GLU D CG  1 
ATOM   10541 C  CD  . GLU D  1 196 ? 19.156  -4.712  115.529 1.00 17.42  ? 283  GLU D CD  1 
ATOM   10542 O  OE1 . GLU D  1 196 ? 18.255  -4.109  116.143 1.00 20.21  ? 283  GLU D OE1 1 
ATOM   10543 O  OE2 . GLU D  1 196 ? 18.977  -5.172  114.388 1.00 18.26  ? 283  GLU D OE2 1 
ATOM   10544 N  N   . GLU D  1 197 ? 22.524  -7.341  112.883 1.00 9.31   ? 284  GLU D N   1 
ATOM   10545 C  CA  . GLU D  1 197 ? 23.590  -7.199  111.860 1.00 9.66   ? 284  GLU D CA  1 
ATOM   10546 C  C   . GLU D  1 197 ? 24.785  -8.134  112.073 1.00 9.71   ? 284  GLU D C   1 
ATOM   10547 O  O   . GLU D  1 197 ? 25.944  -7.708  112.084 1.00 9.46   ? 284  GLU D O   1 
ATOM   10548 C  CB  . GLU D  1 197 ? 24.044  -5.723  111.781 1.00 9.94   ? 284  GLU D CB  1 
ATOM   10549 C  CG  . GLU D  1 197 ? 22.920  -4.802  111.285 1.00 9.29   ? 284  GLU D CG  1 
ATOM   10550 C  CD  . GLU D  1 197 ? 23.187  -3.312  111.461 1.00 9.54   ? 284  GLU D CD  1 
ATOM   10551 O  OE1 . GLU D  1 197 ? 24.097  -2.932  112.233 1.00 9.02   ? 284  GLU D OE1 1 
ATOM   10552 O  OE2 . GLU D  1 197 ? 22.474  -2.512  110.809 1.00 11.35  ? 284  GLU D OE2 1 
ATOM   10553 N  N   . CYS D  1 198 ? 24.518  -9.433  112.167 1.00 9.66   ? 285  CYS D N   1 
ATOM   10554 C  CA  . CYS D  1 198 ? 25.598  -10.358 112.521 1.00 9.76   ? 285  CYS D CA  1 
ATOM   10555 C  C   . CYS D  1 198 ? 26.627  -10.458 111.397 1.00 9.93   ? 285  CYS D C   1 
ATOM   10556 O  O   . CYS D  1 198 ? 26.265  -10.443 110.213 1.00 9.89   ? 285  CYS D O   1 
ATOM   10557 C  CB  . CYS D  1 198 ? 25.036  -11.736 112.831 1.00 10.25  ? 285  CYS D CB  1 
ATOM   10558 S  SG  . CYS D  1 198 ? 24.137  -11.858 114.404 1.00 12.97  ? 285  CYS D SG  1 
ATOM   10559 N  N   . SER D  1 199 ? 27.903  -10.545 111.778 1.00 9.03   ? 286  SER D N   1 
ATOM   10560 C  CA  . SER D  1 199 ? 28.995  -10.830 110.824 1.00 9.42   ? 286  SER D CA  1 
ATOM   10561 C  C   . SER D  1 199 ? 29.522  -12.234 111.113 1.00 9.34   ? 286  SER D C   1 
ATOM   10562 O  O   . SER D  1 199 ? 30.027  -12.488 112.220 1.00 9.86   ? 286  SER D O   1 
ATOM   10563 C  CB  . SER D  1 199 ? 30.126  -9.810  110.981 1.00 8.55   ? 286  SER D CB  1 
ATOM   10564 O  OG  . SER D  1 199 ? 29.672  -8.498  110.734 1.00 9.96   ? 286  SER D OG  1 
ATOM   10565 N  N   . CYS D  1 200 ? 29.422  -13.128 110.127 1.00 9.63   ? 287  CYS D N   1 
ATOM   10566 C  CA  . CYS D  1 200 ? 29.619  -14.571 110.351 1.00 10.41  ? 287  CYS D CA  1 
ATOM   10567 C  C   . CYS D  1 200 ? 30.686  -15.194 109.451 1.00 10.59  ? 287  CYS D C   1 
ATOM   10568 O  O   . CYS D  1 200 ? 30.846  -14.786 108.301 1.00 10.94  ? 287  CYS D O   1 
ATOM   10569 C  CB  . CYS D  1 200 ? 28.302  -15.331 110.155 1.00 10.13  ? 287  CYS D CB  1 
ATOM   10570 S  SG  . CYS D  1 200 ? 26.852  -14.624 110.997 1.00 11.99  ? 287  CYS D SG  1 
ATOM   10571 N  N   . TYR D  1 201 ? 31.389  -16.191 109.985 1.00 10.11  ? 288  TYR D N   1 
ATOM   10572 C  CA  . TYR D  1 201 ? 32.383  -16.934 109.213 1.00 10.78  ? 288  TYR D CA  1 
ATOM   10573 C  C   . TYR D  1 201 ? 32.440  -18.379 109.722 1.00 10.84  ? 288  TYR D C   1 
ATOM   10574 O  O   . TYR D  1 201 ? 32.024  -18.667 110.856 1.00 10.81  ? 288  TYR D O   1 
ATOM   10575 C  CB  . TYR D  1 201 ? 33.753  -16.242 109.290 1.00 10.40  ? 288  TYR D CB  1 
ATOM   10576 C  CG  . TYR D  1 201 ? 34.395  -16.422 110.645 1.00 11.03  ? 288  TYR D CG  1 
ATOM   10577 C  CD1 . TYR D  1 201 ? 34.161  -15.520 111.671 1.00 10.45  ? 288  TYR D CD1 1 
ATOM   10578 C  CD2 . TYR D  1 201 ? 35.191  -17.547 110.904 1.00 10.76  ? 288  TYR D CD2 1 
ATOM   10579 C  CE1 . TYR D  1 201 ? 34.714  -15.703 112.929 1.00 9.94   ? 288  TYR D CE1 1 
ATOM   10580 C  CE2 . TYR D  1 201 ? 35.742  -17.759 112.159 1.00 10.18  ? 288  TYR D CE2 1 
ATOM   10581 C  CZ  . TYR D  1 201 ? 35.497  -16.816 113.174 1.00 10.35  ? 288  TYR D CZ  1 
ATOM   10582 O  OH  . TYR D  1 201 ? 36.054  -16.991 114.423 1.00 9.65   ? 288  TYR D OH  1 
ATOM   10583 N  N   . GLY D  1 202 ? 32.962  -19.284 108.899 1.00 11.11  ? 289  GLY D N   1 
ATOM   10584 C  CA  . GLY D  1 202 ? 33.038  -20.693 109.283 1.00 11.27  ? 289  GLY D CA  1 
ATOM   10585 C  C   . GLY D  1 202 ? 34.467  -21.200 109.297 1.00 11.67  ? 289  GLY D C   1 
ATOM   10586 O  O   . GLY D  1 202 ? 35.298  -20.763 108.500 1.00 11.09  ? 289  GLY D O   1 
ATOM   10587 N  N   . ALA D  1 203 ? 34.748  -22.105 110.227 1.00 12.37  ? 290  ALA D N   1 
ATOM   10588 C  CA  . ALA D  1 203 ? 36.037  -22.790 110.320 1.00 12.78  ? 290  ALA D CA  1 
ATOM   10589 C  C   . ALA D  1 203 ? 35.874  -24.018 111.216 1.00 13.59  ? 290  ALA D C   1 
ATOM   10590 O  O   . ALA D  1 203 ? 35.168  -23.968 112.232 1.00 12.72  ? 290  ALA D O   1 
ATOM   10591 C  CB  . ALA D  1 203 ? 37.110  -21.870 110.883 1.00 12.32  ? 290  ALA D CB  1 
ATOM   10592 N  N   . GLY D  1 204 ? 36.538  -25.109 110.836 1.00 14.08  ? 291  GLY D N   1 
ATOM   10593 C  CA  . GLY D  1 204 ? 36.514  -26.347 111.632 1.00 15.42  ? 291  GLY D CA  1 
ATOM   10594 C  C   . GLY D  1 204 ? 35.115  -26.797 112.010 1.00 15.20  ? 291  GLY D C   1 
ATOM   10595 O  O   . GLY D  1 204 ? 34.868  -27.135 113.182 1.00 16.45  ? 291  GLY D O   1 
ATOM   10596 N  N   . GLY D  1 205 ? 34.196  -26.743 111.043 1.00 15.17  ? 292  GLY D N   1 
ATOM   10597 C  CA  . GLY D  1 205 ? 32.794  -27.164 111.222 1.00 14.27  ? 292  GLY D CA  1 
ATOM   10598 C  C   . GLY D  1 205 ? 31.887  -26.329 112.125 1.00 14.60  ? 292  GLY D C   1 
ATOM   10599 O  O   . GLY D  1 205 ? 30.775  -26.776 112.481 1.00 13.72  ? 292  GLY D O   1 
ATOM   10600 N  N   . VAL D  1 206 ? 32.340  -25.121 112.481 1.00 13.80  ? 293  VAL D N   1 
ATOM   10601 C  CA  . VAL D  1 206 ? 31.617  -24.228 113.401 1.00 14.09  ? 293  VAL D CA  1 
ATOM   10602 C  C   . VAL D  1 206 ? 31.448  -22.886 112.719 1.00 13.88  ? 293  VAL D C   1 
ATOM   10603 O  O   . VAL D  1 206 ? 32.394  -22.382 112.090 1.00 12.85  ? 293  VAL D O   1 
ATOM   10604 C  CB  . VAL D  1 206 ? 32.384  -23.989 114.725 1.00 14.78  ? 293  VAL D CB  1 
ATOM   10605 C  CG1 . VAL D  1 206 ? 31.644  -22.981 115.623 1.00 15.80  ? 293  VAL D CG1 1 
ATOM   10606 C  CG2 . VAL D  1 206 ? 32.625  -25.312 115.476 1.00 15.49  ? 293  VAL D CG2 1 
ATOM   10607 N  N   . ILE D  1 207 ? 30.248  -22.319 112.832 1.00 13.17  ? 294  ILE D N   1 
ATOM   10608 C  CA  . ILE D  1 207 ? 29.992  -20.974 112.331 1.00 12.35  ? 294  ILE D CA  1 
ATOM   10609 C  C   . ILE D  1 207 ? 29.902  -20.042 113.532 1.00 13.33  ? 294  ILE D C   1 
ATOM   10610 O  O   . ILE D  1 207 ? 29.209  -20.336 114.513 1.00 12.92  ? 294  ILE D O   1 
ATOM   10611 C  CB  . ILE D  1 207 ? 28.710  -20.921 111.449 1.00 12.33  ? 294  ILE D CB  1 
ATOM   10612 C  CG1 . ILE D  1 207 ? 28.870  -21.801 110.206 1.00 11.61  ? 294  ILE D CG1 1 
ATOM   10613 C  CG2 . ILE D  1 207 ? 28.326  -19.451 111.094 1.00 12.37  ? 294  ILE D CG2 1 
ATOM   10614 C  CD1 . ILE D  1 207 ? 27.553  -22.136 109.480 1.00 12.63  ? 294  ILE D CD1 1 
ATOM   10615 N  N   . LYS D  1 208 ? 30.635  -18.938 113.462 1.00 11.60  ? 295  LYS D N   1 
ATOM   10616 C  CA  . LYS D  1 208 ? 30.613  -17.925 114.490 1.00 12.98  ? 295  LYS D CA  1 
ATOM   10617 C  C   . LYS D  1 208 ? 30.106  -16.605 113.926 1.00 12.34  ? 295  LYS D C   1 
ATOM   10618 O  O   . LYS D  1 208 ? 30.597  -16.129 112.924 1.00 11.98  ? 295  LYS D O   1 
ATOM   10619 C  CB  . LYS D  1 208 ? 31.994  -17.748 115.096 1.00 13.28  ? 295  LYS D CB  1 
ATOM   10620 C  CG  . LYS D  1 208 ? 32.421  -18.892 116.012 1.00 12.76  ? 295  LYS D CG  1 
ATOM   10621 C  CD  . LYS D  1 208 ? 33.683  -18.553 116.783 1.00 12.23  ? 295  LYS D CD  1 
ATOM   10622 C  CE  . LYS D  1 208 ? 34.472  -19.811 117.123 1.00 13.08  ? 295  LYS D CE  1 
ATOM   10623 N  NZ  . LYS D  1 208 ? 35.697  -19.600 117.953 1.00 13.29  ? 295  LYS D NZ  1 
ATOM   10624 N  N   . CYS D  1 209 ? 29.125  -16.035 114.606 1.00 11.78  ? 296  CYS D N   1 
ATOM   10625 C  CA  . CYS D  1 209 ? 28.535  -14.757 114.221 1.00 11.76  ? 296  CYS D CA  1 
ATOM   10626 C  C   . CYS D  1 209 ? 28.784  -13.749 115.317 1.00 11.66  ? 296  CYS D C   1 
ATOM   10627 O  O   . CYS D  1 209 ? 28.417  -13.979 116.483 1.00 12.48  ? 296  CYS D O   1 
ATOM   10628 C  CB  . CYS D  1 209 ? 27.028  -14.879 114.009 1.00 11.22  ? 296  CYS D CB  1 
ATOM   10629 S  SG  . CYS D  1 209 ? 26.551  -15.875 112.587 1.00 12.88  ? 296  CYS D SG  1 
ATOM   10630 N  N   . ILE D  1 210 ? 29.404  -12.630 114.935 1.00 11.31  ? 297  ILE D N   1 
ATOM   10631 C  CA  . ILE D  1 210 ? 29.762  -11.561 115.848 1.00 10.28  ? 297  ILE D CA  1 
ATOM   10632 C  C   . ILE D  1 210 ? 28.852  -10.401 115.491 1.00 11.04  ? 297  ILE D C   1 
ATOM   10633 O  O   . ILE D  1 210 ? 28.845  -9.938  114.341 1.00 10.11  ? 297  ILE D O   1 
ATOM   10634 C  CB  . ILE D  1 210 ? 31.269  -11.154 115.703 1.00 10.42  ? 297  ILE D CB  1 
ATOM   10635 C  CG1 . ILE D  1 210 ? 32.226  -12.226 116.268 1.00 9.76   ? 297  ILE D CG1 1 
ATOM   10636 C  CG2 . ILE D  1 210 ? 31.544  -9.807  116.419 1.00 8.34   ? 297  ILE D CG2 1 
ATOM   10637 C  CD1 . ILE D  1 210 ? 32.107  -13.690 115.694 1.00 10.53  ? 297  ILE D CD1 1 
ATOM   10638 N  N   . CYS D  1 211 ? 28.053  -9.958  116.463 1.00 10.98  ? 298  CYS D N   1 
ATOM   10639 C  CA  . CYS D  1 211 ? 26.897  -9.128  116.137 1.00 11.09  ? 298  CYS D CA  1 
ATOM   10640 C  C   . CYS D  1 211 ? 26.928  -7.768  116.834 1.00 11.06  ? 298  CYS D C   1 
ATOM   10641 O  O   . CYS D  1 211 ? 27.953  -7.381  117.414 1.00 10.82  ? 298  CYS D O   1 
ATOM   10642 C  CB  . CYS D  1 211 ? 25.585  -9.905  116.410 1.00 11.26  ? 298  CYS D CB  1 
ATOM   10643 S  SG  . CYS D  1 211 ? 25.610  -11.667 115.870 1.00 12.05  ? 298  CYS D SG  1 
ATOM   10644 N  N   . ARG D  1 212 ? 25.796  -7.066  116.788 1.00 10.60  ? 299  ARG D N   1 
ATOM   10645 C  CA  . ARG D  1 212 ? 25.642  -5.731  117.395 1.00 10.59  ? 299  ARG D CA  1 
ATOM   10646 C  C   . ARG D  1 212 ? 24.488  -5.771  118.407 1.00 10.86  ? 299  ARG D C   1 
ATOM   10647 O  O   . ARG D  1 212 ? 23.348  -6.073  118.051 1.00 9.81   ? 299  ARG D O   1 
ATOM   10648 C  CB  . ARG D  1 212 ? 25.372  -4.703  116.283 1.00 10.34  ? 299  ARG D CB  1 
ATOM   10649 C  CG  . ARG D  1 212 ? 24.845  -3.310  116.705 1.00 11.05  ? 299  ARG D CG  1 
ATOM   10650 C  CD  . ARG D  1 212 ? 24.378  -2.554  115.465 1.00 10.76  ? 299  ARG D CD  1 
ATOM   10651 N  NE  . ARG D  1 212 ? 23.663  -1.312  115.755 1.00 11.70  ? 299  ARG D NE  1 
ATOM   10652 C  CZ  . ARG D  1 212 ? 23.434  -0.349  114.864 1.00 11.70  ? 299  ARG D CZ  1 
ATOM   10653 N  NH1 . ARG D  1 212 ? 23.872  -0.453  113.597 1.00 8.90   ? 299  ARG D NH1 1 
ATOM   10654 N  NH2 . ARG D  1 212 ? 22.763  0.736   115.239 1.00 10.43  ? 299  ARG D NH2 1 
ATOM   10655 N  N   . ASP D  1 213 ? 24.793  -5.491  119.667 1.00 11.08  ? 300  ASP D N   1 
ATOM   10656 C  CA  . ASP D  1 213 ? 23.744  -5.328  120.693 1.00 11.07  ? 300  ASP D CA  1 
ATOM   10657 C  C   . ASP D  1 213 ? 23.395  -3.851  120.700 1.00 11.74  ? 300  ASP D C   1 
ATOM   10658 O  O   . ASP D  1 213 ? 24.176  -3.019  121.179 1.00 11.62  ? 300  ASP D O   1 
ATOM   10659 C  CB  . ASP D  1 213 ? 24.250  -5.861  122.067 1.00 11.45  ? 300  ASP D CB  1 
ATOM   10660 C  CG  . ASP D  1 213 ? 23.323  -5.525  123.245 1.00 11.67  ? 300  ASP D CG  1 
ATOM   10661 O  OD1 . ASP D  1 213 ? 23.637  -5.936  124.380 1.00 10.73  ? 300  ASP D OD1 1 
ATOM   10662 O  OD2 . ASP D  1 213 ? 22.333  -4.804  123.080 1.00 11.59  ? 300  ASP D OD2 1 
ATOM   10663 N  N   . ASN D  1 214 ? 22.240  -3.515  120.120 1.00 11.94  ? 301  ASN D N   1 
ATOM   10664 C  CA  . ASN D  1 214 ? 21.851  -2.105  119.996 1.00 12.64  ? 301  ASN D CA  1 
ATOM   10665 C  C   . ASN D  1 214 ? 21.146  -1.588  121.246 1.00 13.35  ? 301  ASN D C   1 
ATOM   10666 O  O   . ASN D  1 214 ? 20.817  -0.408  121.343 1.00 13.41  ? 301  ASN D O   1 
ATOM   10667 C  CB  . ASN D  1 214 ? 20.951  -1.889  118.776 1.00 12.19  ? 301  ASN D CB  1 
ATOM   10668 C  CG  . ASN D  1 214 ? 21.094  -0.477  118.183 1.00 13.68  ? 301  ASN D CG  1 
ATOM   10669 O  OD1 . ASN D  1 214 ? 22.196  -0.041  117.848 1.00 13.26  ? 301  ASN D OD1 1 
ATOM   10670 N  ND2 . ASN D  1 214 ? 19.983  0.238   118.078 1.00 13.11  ? 301  ASN D ND2 1 
ATOM   10671 N  N   . TRP D  1 215 ? 20.909  -2.489  122.190 1.00 14.05  ? 302  TRP D N   1 
ATOM   10672 C  CA  . TRP D  1 215 ? 20.094  -2.161  123.360 1.00 14.21  ? 302  TRP D CA  1 
ATOM   10673 C  C   . TRP D  1 215 ? 20.963  -1.728  124.537 1.00 14.81  ? 302  TRP D C   1 
ATOM   10674 O  O   . TRP D  1 215 ? 20.709  -0.688  125.141 1.00 14.96  ? 302  TRP D O   1 
ATOM   10675 C  CB  . TRP D  1 215 ? 19.269  -3.374  123.737 1.00 14.42  ? 302  TRP D CB  1 
ATOM   10676 C  CG  . TRP D  1 215 ? 18.304  -3.210  124.892 1.00 15.24  ? 302  TRP D CG  1 
ATOM   10677 C  CD1 . TRP D  1 215 ? 17.739  -2.049  125.369 1.00 15.26  ? 302  TRP D CD1 1 
ATOM   10678 C  CD2 . TRP D  1 215 ? 17.756  -4.278  125.680 1.00 15.42  ? 302  TRP D CD2 1 
ATOM   10679 N  NE1 . TRP D  1 215 ? 16.883  -2.338  126.421 1.00 15.53  ? 302  TRP D NE1 1 
ATOM   10680 C  CE2 . TRP D  1 215 ? 16.872  -3.699  126.622 1.00 16.19  ? 302  TRP D CE2 1 
ATOM   10681 C  CE3 . TRP D  1 215 ? 17.922  -5.668  125.669 1.00 15.54  ? 302  TRP D CE3 1 
ATOM   10682 C  CZ2 . TRP D  1 215 ? 16.172  -4.467  127.560 1.00 16.21  ? 302  TRP D CZ2 1 
ATOM   10683 C  CZ3 . TRP D  1 215 ? 17.226  -6.429  126.601 1.00 15.81  ? 302  TRP D CZ3 1 
ATOM   10684 C  CH2 . TRP D  1 215 ? 16.360  -5.826  127.529 1.00 16.77  ? 302  TRP D CH2 1 
ATOM   10685 N  N   . LYS D  1 216 ? 21.978  -2.533  124.861 1.00 14.32  ? 303  LYS D N   1 
ATOM   10686 C  CA  . LYS D  1 216 ? 22.807  -2.293  126.041 1.00 14.37  ? 303  LYS D CA  1 
ATOM   10687 C  C   . LYS D  1 216 ? 24.323  -2.312  125.795 1.00 14.00  ? 303  LYS D C   1 
ATOM   10688 O  O   . LYS D  1 216 ? 25.028  -1.350  126.112 1.00 13.69  ? 303  LYS D O   1 
ATOM   10689 C  CB  . LYS D  1 216 ? 22.480  -3.343  127.112 1.00 14.52  ? 303  LYS D CB  1 
ATOM   10690 C  CG  . LYS D  1 216 ? 21.197  -3.111  127.866 1.00 15.61  ? 303  LYS D CG  1 
ATOM   10691 C  CD  . LYS D  1 216 ? 20.895  -4.319  128.768 1.00 15.81  ? 303  LYS D CD  1 
ATOM   10692 C  CE  . LYS D  1 216 ? 19.532  -4.175  129.450 1.00 17.34  ? 303  LYS D CE  1 
ATOM   10693 N  NZ  . LYS D  1 216 ? 19.183  -5.383  130.251 1.00 19.16  ? 303  LYS D NZ  1 
ATOM   10694 N  N   . GLY D  1 217 ? 24.814  -3.419  125.248 1.00 13.45  ? 304  GLY D N   1 
ATOM   10695 C  CA  . GLY D  1 217 ? 26.242  -3.733  125.264 1.00 13.37  ? 304  GLY D CA  1 
ATOM   10696 C  C   . GLY D  1 217 ? 27.104  -2.996  124.253 1.00 13.74  ? 304  GLY D C   1 
ATOM   10697 O  O   . GLY D  1 217 ? 26.716  -2.857  123.086 1.00 13.83  ? 304  GLY D O   1 
ATOM   10698 N  N   . ALA D  1 218 ? 28.254  -2.517  124.725 1.00 12.93  ? 305  ALA D N   1 
ATOM   10699 C  CA  . ALA D  1 218 ? 29.364  -2.026  123.894 1.00 13.54  ? 305  ALA D CA  1 
ATOM   10700 C  C   . ALA D  1 218 ? 30.321  -3.176  123.597 1.00 13.44  ? 305  ALA D C   1 
ATOM   10701 O  O   . ALA D  1 218 ? 31.214  -3.048  122.752 1.00 13.38  ? 305  ALA D O   1 
ATOM   10702 C  CB  . ALA D  1 218 ? 30.112  -0.922  124.603 1.00 13.72  ? 305  ALA D CB  1 
ATOM   10703 N  N   . ASN D  1 219 ? 30.162  -4.285  124.328 1.00 12.92  ? 306  ASN D N   1 
ATOM   10704 C  CA  . ASN D  1 219 ? 30.774  -5.559  123.930 1.00 12.66  ? 306  ASN D CA  1 
ATOM   10705 C  C   . ASN D  1 219 ? 29.824  -6.256  122.965 1.00 11.99  ? 306  ASN D C   1 
ATOM   10706 O  O   . ASN D  1 219 ? 28.596  -6.097  123.056 1.00 12.25  ? 306  ASN D O   1 
ATOM   10707 C  CB  . ASN D  1 219 ? 31.145  -6.451  125.145 1.00 13.07  ? 306  ASN D CB  1 
ATOM   10708 C  CG  . ASN D  1 219 ? 29.955  -6.704  126.120 1.00 13.51  ? 306  ASN D CG  1 
ATOM   10709 O  OD1 . ASN D  1 219 ? 28.949  -6.008  126.088 1.00 12.15  ? 306  ASN D OD1 1 
ATOM   10710 N  ND2 . ASN D  1 219 ? 30.104  -7.716  126.992 1.00 12.39  ? 306  ASN D ND2 1 
ATOM   10711 N  N   . ARG D  1 220 ? 30.385  -6.995  122.015 1.00 11.33  ? 307  ARG D N   1 
ATOM   10712 C  CA  . ARG D  1 220 ? 29.585  -7.582  120.944 1.00 10.44  ? 307  ARG D CA  1 
ATOM   10713 C  C   . ARG D  1 220 ? 29.120  -8.983  121.303 1.00 11.28  ? 307  ARG D C   1 
ATOM   10714 O  O   . ARG D  1 220 ? 29.919  -9.804  121.759 1.00 11.71  ? 307  ARG D O   1 
ATOM   10715 C  CB  . ARG D  1 220 ? 30.393  -7.639  119.643 1.00 11.22  ? 307  ARG D CB  1 
ATOM   10716 C  CG  . ARG D  1 220 ? 30.696  -6.273  119.032 1.00 8.30   ? 307  ARG D CG  1 
ATOM   10717 C  CD  . ARG D  1 220 ? 31.238  -6.389  117.573 1.00 8.64   ? 307  ARG D CD  1 
ATOM   10718 N  NE  . ARG D  1 220 ? 31.420  -5.055  116.974 1.00 8.66   ? 307  ARG D NE  1 
ATOM   10719 C  CZ  . ARG D  1 220 ? 30.425  -4.279  116.545 1.00 7.27   ? 307  ARG D CZ  1 
ATOM   10720 N  NH1 . ARG D  1 220 ? 29.150  -4.690  116.632 1.00 7.40   ? 307  ARG D NH1 1 
ATOM   10721 N  NH2 . ARG D  1 220 ? 30.698  -3.070  116.068 1.00 8.49   ? 307  ARG D NH2 1 
ATOM   10722 N  N   . PRO D  1 221 ? 27.826  -9.268  121.071 1.00 11.38  ? 308  PRO D N   1 
ATOM   10723 C  CA  . PRO D  1 221 ? 27.304  -10.618 121.227 1.00 11.09  ? 308  PRO D CA  1 
ATOM   10724 C  C   . PRO D  1 221 ? 27.980  -11.576 120.239 1.00 11.01  ? 308  PRO D C   1 
ATOM   10725 O  O   . PRO D  1 221 ? 28.388  -11.160 119.157 1.00 11.27  ? 308  PRO D O   1 
ATOM   10726 C  CB  . PRO D  1 221 ? 25.815  -10.475 120.877 1.00 11.58  ? 308  PRO D CB  1 
ATOM   10727 C  CG  . PRO D  1 221 ? 25.522  -9.033  120.857 1.00 11.22  ? 308  PRO D CG  1 
ATOM   10728 C  CD  . PRO D  1 221 ? 26.795  -8.308  120.622 1.00 10.91  ? 308  PRO D CD  1 
ATOM   10729 N  N   . VAL D  1 222 ? 28.130  -12.839 120.632 1.00 10.86  ? 309  VAL D N   1 
ATOM   10730 C  CA  . VAL D  1 222 ? 28.692  -13.860 119.766 1.00 11.05  ? 309  VAL D CA  1 
ATOM   10731 C  C   . VAL D  1 222 ? 27.747  -15.058 119.777 1.00 12.24  ? 309  VAL D C   1 
ATOM   10732 O  O   . VAL D  1 222 ? 27.471  -15.622 120.855 1.00 12.38  ? 309  VAL D O   1 
ATOM   10733 C  CB  . VAL D  1 222 ? 30.110  -14.314 120.232 1.00 10.62  ? 309  VAL D CB  1 
ATOM   10734 C  CG1 . VAL D  1 222 ? 30.690  -15.401 119.284 1.00 10.68  ? 309  VAL D CG1 1 
ATOM   10735 C  CG2 . VAL D  1 222 ? 31.088  -13.125 120.309 1.00 11.75  ? 309  VAL D CG2 1 
ATOM   10736 N  N   . ILE D  1 223 ? 27.236  -15.414 118.591 1.00 11.51  ? 310  ILE D N   1 
ATOM   10737 C  CA  . ILE D  1 223 ? 26.407  -16.600 118.397 1.00 12.51  ? 310  ILE D CA  1 
ATOM   10738 C  C   . ILE D  1 223 ? 27.261  -17.691 117.767 1.00 12.30  ? 310  ILE D C   1 
ATOM   10739 O  O   . ILE D  1 223 ? 27.876  -17.474 116.721 1.00 12.89  ? 310  ILE D O   1 
ATOM   10740 C  CB  . ILE D  1 223 ? 25.167  -16.316 117.491 1.00 11.91  ? 310  ILE D CB  1 
ATOM   10741 C  CG1 . ILE D  1 223 ? 24.315  -15.165 118.069 1.00 13.13  ? 310  ILE D CG1 1 
ATOM   10742 C  CG2 . ILE D  1 223 ? 24.344  -17.596 117.294 1.00 12.74  ? 310  ILE D CG2 1 
ATOM   10743 C  CD1 . ILE D  1 223 ? 23.266  -14.633 117.114 1.00 12.46  ? 310  ILE D CD1 1 
ATOM   10744 N  N   . THR D  1 224 ? 27.289  -18.868 118.393 1.00 12.15  ? 311  THR D N   1 
ATOM   10745 C  CA  . THR D  1 224 ? 28.085  -19.979 117.874 1.00 12.58  ? 311  THR D CA  1 
ATOM   10746 C  C   . THR D  1 224 ? 27.111  -21.029 117.331 1.00 12.28  ? 311  THR D C   1 
ATOM   10747 O  O   . THR D  1 224 ? 26.250  -21.487 118.065 1.00 11.96  ? 311  THR D O   1 
ATOM   10748 C  CB  . THR D  1 224 ? 28.992  -20.608 118.977 1.00 12.34  ? 311  THR D CB  1 
ATOM   10749 O  OG1 . THR D  1 224 ? 29.917  -19.633 119.493 1.00 12.72  ? 311  THR D OG1 1 
ATOM   10750 C  CG2 . THR D  1 224 ? 29.777  -21.770 118.423 1.00 14.40  ? 311  THR D CG2 1 
ATOM   10751 N  N   . ILE D  1 225 ? 27.230  -21.371 116.049 1.00 11.52  ? 312  ILE D N   1 
ATOM   10752 C  CA  . ILE D  1 225 ? 26.222  -22.203 115.383 1.00 11.57  ? 312  ILE D CA  1 
ATOM   10753 C  C   . ILE D  1 225 ? 26.832  -23.522 114.900 1.00 11.58  ? 312  ILE D C   1 
ATOM   10754 O  O   . ILE D  1 225 ? 27.884  -23.539 114.268 1.00 11.99  ? 312  ILE D O   1 
ATOM   10755 C  CB  . ILE D  1 225 ? 25.600  -21.484 114.150 1.00 10.75  ? 312  ILE D CB  1 
ATOM   10756 C  CG1 . ILE D  1 225 ? 24.998  -20.125 114.560 1.00 11.86  ? 312  ILE D CG1 1 
ATOM   10757 C  CG2 . ILE D  1 225 ? 24.592  -22.395 113.436 1.00 10.62  ? 312  ILE D CG2 1 
ATOM   10758 C  CD1 . ILE D  1 225 ? 24.501  -19.297 113.378 1.00 12.07  ? 312  ILE D CD1 1 
ATOM   10759 N  N   . ASP D  1 226 ? 26.147  -24.616 115.226 1.00 12.36  ? 313  ASP D N   1 
ATOM   10760 C  CA  . ASP D  1 226 ? 26.458  -25.936 114.713 1.00 12.56  ? 313  ASP D CA  1 
ATOM   10761 C  C   . ASP D  1 226 ? 25.535  -26.172 113.514 1.00 12.62  ? 313  ASP D C   1 
ATOM   10762 O  O   . ASP D  1 226 ? 24.338  -26.372 113.693 1.00 13.19  ? 313  ASP D O   1 
ATOM   10763 C  CB  . ASP D  1 226 ? 26.264  -26.971 115.839 1.00 13.08  ? 313  ASP D CB  1 
ATOM   10764 C  CG  . ASP D  1 226 ? 26.492  -28.407 115.380 1.00 13.52  ? 313  ASP D CG  1 
ATOM   10765 O  OD1 . ASP D  1 226 ? 26.804  -29.263 116.242 1.00 16.03  ? 313  ASP D OD1 1 
ATOM   10766 O  OD2 . ASP D  1 226 ? 26.367  -28.675 114.174 1.00 13.76  ? 313  ASP D OD2 1 
ATOM   10767 N  N   . PRO D  1 227 ? 26.084  -26.113 112.271 1.00 13.06  ? 314  PRO D N   1 
ATOM   10768 C  CA  . PRO D  1 227 ? 25.261  -26.208 111.067 1.00 13.28  ? 314  PRO D CA  1 
ATOM   10769 C  C   . PRO D  1 227 ? 24.797  -27.627 110.713 1.00 13.98  ? 314  PRO D C   1 
ATOM   10770 O  O   . PRO D  1 227 ? 23.947  -27.800 109.824 1.00 14.25  ? 314  PRO D O   1 
ATOM   10771 C  CB  . PRO D  1 227 ? 26.182  -25.652 109.969 1.00 13.22  ? 314  PRO D CB  1 
ATOM   10772 C  CG  . PRO D  1 227 ? 27.567  -25.970 110.442 1.00 12.87  ? 314  PRO D CG  1 
ATOM   10773 C  CD  . PRO D  1 227 ? 27.524  -25.968 111.950 1.00 13.04  ? 314  PRO D CD  1 
ATOM   10774 N  N   . GLU D  1 228 ? 25.320  -28.630 111.417 1.00 14.63  ? 315  GLU D N   1 
ATOM   10775 C  CA  . GLU D  1 228 ? 24.865  -30.014 111.206 1.00 15.61  ? 315  GLU D CA  1 
ATOM   10776 C  C   . GLU D  1 228 ? 23.684  -30.373 112.114 1.00 15.82  ? 315  GLU D C   1 
ATOM   10777 O  O   . GLU D  1 228 ? 22.638  -30.849 111.635 1.00 16.29  ? 315  GLU D O   1 
ATOM   10778 C  CB  . GLU D  1 228 ? 26.022  -30.989 111.386 1.00 15.38  ? 315  GLU D CB  1 
ATOM   10779 C  CG  . GLU D  1 228 ? 27.048  -30.883 110.270 1.00 17.14  ? 315  GLU D CG  1 
ATOM   10780 C  CD  . GLU D  1 228 ? 28.111  -31.951 110.366 1.00 19.03  ? 315  GLU D CD  1 
ATOM   10781 O  OE1 . GLU D  1 228 ? 28.997  -31.995 109.496 1.00 17.61  ? 315  GLU D OE1 1 
ATOM   10782 O  OE2 . GLU D  1 228 ? 28.054  -32.761 111.308 1.00 19.46  ? 315  GLU D OE2 1 
ATOM   10783 N  N   . MET D  1 229 ? 23.859  -30.140 113.416 1.00 16.18  ? 316  MET D N   1 
ATOM   10784 C  CA  . MET D  1 229 ? 22.783  -30.268 114.393 1.00 16.69  ? 316  MET D CA  1 
ATOM   10785 C  C   . MET D  1 229 ? 21.720  -29.173 114.242 1.00 16.40  ? 316  MET D C   1 
ATOM   10786 O  O   . MET D  1 229 ? 20.588  -29.323 114.721 1.00 15.62  ? 316  MET D O   1 
ATOM   10787 C  CB  . MET D  1 229 ? 23.354  -30.218 115.811 1.00 16.87  ? 316  MET D CB  1 
ATOM   10788 C  CG  . MET D  1 229 ? 24.294  -31.364 116.146 1.00 19.42  ? 316  MET D CG  1 
ATOM   10789 S  SD  . MET D  1 229 ? 23.584  -32.973 115.738 1.00 26.61  ? 316  MET D SD  1 
ATOM   10790 C  CE  . MET D  1 229 ? 22.223  -33.119 116.886 1.00 25.54  ? 316  MET D CE  1 
ATOM   10791 N  N   . MET D  1 230 ? 22.089  -28.077 113.580 1.00 15.84  ? 317  MET D N   1 
ATOM   10792 C  CA  . MET D  1 230 ? 21.220  -26.893 113.460 1.00 15.94  ? 317  MET D CA  1 
ATOM   10793 C  C   . MET D  1 230 ? 20.774  -26.362 114.829 1.00 15.01  ? 317  MET D C   1 
ATOM   10794 O  O   . MET D  1 230 ? 19.566  -26.150 115.098 1.00 14.15  ? 317  MET D O   1 
ATOM   10795 C  CB  . MET D  1 230 ? 20.048  -27.170 112.518 1.00 16.11  ? 317  MET D CB  1 
ATOM   10796 C  CG  . MET D  1 230 ? 20.515  -27.646 111.138 1.00 16.80  ? 317  MET D CG  1 
ATOM   10797 S  SD  . MET D  1 230 ? 19.152  -27.648 109.968 1.00 16.91  ? 317  MET D SD  1 
ATOM   10798 C  CE  . MET D  1 230 ? 18.295  -29.174 110.372 1.00 20.88  ? 317  MET D CE  1 
ATOM   10799 N  N   . THR D  1 231 ? 21.777  -26.146 115.683 1.00 14.41  ? 318  THR D N   1 
ATOM   10800 C  CA  . THR D  1 231 ? 21.605  -25.580 117.020 1.00 13.99  ? 318  THR D CA  1 
ATOM   10801 C  C   . THR D  1 231 ? 22.664  -24.489 117.266 1.00 14.17  ? 318  THR D C   1 
ATOM   10802 O  O   . THR D  1 231 ? 23.656  -24.396 116.536 1.00 13.77  ? 318  THR D O   1 
ATOM   10803 C  CB  . THR D  1 231 ? 21.714  -26.663 118.133 1.00 14.61  ? 318  THR D CB  1 
ATOM   10804 O  OG1 . THR D  1 231 ? 22.940  -27.398 117.984 1.00 12.10  ? 318  THR D OG1 1 
ATOM   10805 C  CG2 . THR D  1 231 ? 20.534  -27.634 118.064 1.00 14.35  ? 318  THR D CG2 1 
ATOM   10806 N  N   . HIS D  1 232 ? 22.471  -23.712 118.326 1.00 13.25  ? 319  HIS D N   1 
ATOM   10807 C  CA  . HIS D  1 232 ? 23.330  -22.576 118.600 1.00 14.37  ? 319  HIS D CA  1 
ATOM   10808 C  C   . HIS D  1 232 ? 23.394  -22.281 120.090 1.00 14.57  ? 319  HIS D C   1 
ATOM   10809 O  O   . HIS D  1 232 ? 22.557  -22.754 120.873 1.00 15.46  ? 319  HIS D O   1 
ATOM   10810 C  CB  . HIS D  1 232 ? 22.802  -21.352 117.846 1.00 13.59  ? 319  HIS D CB  1 
ATOM   10811 C  CG  . HIS D  1 232 ? 21.595  -20.739 118.466 1.00 14.25  ? 319  HIS D CG  1 
ATOM   10812 N  ND1 . HIS D  1 232 ? 20.318  -21.192 118.213 1.00 15.52  ? 319  HIS D ND1 1 
ATOM   10813 C  CD2 . HIS D  1 232 ? 21.461  -19.694 119.321 1.00 16.04  ? 319  HIS D CD2 1 
ATOM   10814 C  CE1 . HIS D  1 232 ? 19.449  -20.456 118.883 1.00 14.06  ? 319  HIS D CE1 1 
ATOM   10815 N  NE2 . HIS D  1 232 ? 20.114  -19.538 119.560 1.00 14.38  ? 319  HIS D NE2 1 
ATOM   10816 N  N   . THR D  1 233 ? 24.404  -21.513 120.473 1.00 14.65  ? 320  THR D N   1 
ATOM   10817 C  CA  . THR D  1 233 ? 24.515  -20.933 121.808 1.00 14.54  ? 320  THR D CA  1 
ATOM   10818 C  C   . THR D  1 233 ? 24.848  -19.464 121.591 1.00 14.11  ? 320  THR D C   1 
ATOM   10819 O  O   . THR D  1 233 ? 25.240  -19.093 120.477 1.00 13.94  ? 320  THR D O   1 
ATOM   10820 C  CB  . THR D  1 233 ? 25.639  -21.611 122.637 1.00 14.94  ? 320  THR D CB  1 
ATOM   10821 O  OG1 . THR D  1 233 ? 26.868  -21.631 121.887 1.00 14.93  ? 320  THR D OG1 1 
ATOM   10822 C  CG2 . THR D  1 233 ? 25.232  -23.056 123.013 1.00 13.59  ? 320  THR D CG2 1 
ATOM   10823 N  N   . SER D  1 234 ? 24.702  -18.638 122.627 1.00 13.94  ? 321  SER D N   1 
ATOM   10824 C  CA  . SER D  1 234 ? 25.085  -17.221 122.532 1.00 13.90  ? 321  SER D CA  1 
ATOM   10825 C  C   . SER D  1 234 ? 25.597  -16.633 123.850 1.00 14.13  ? 321  SER D C   1 
ATOM   10826 O  O   . SER D  1 234 ? 25.183  -17.050 124.942 1.00 14.47  ? 321  SER D O   1 
ATOM   10827 C  CB  . SER D  1 234 ? 23.922  -16.375 122.002 1.00 13.08  ? 321  SER D CB  1 
ATOM   10828 O  OG  . SER D  1 234 ? 23.020  -16.024 123.039 1.00 14.15  ? 321  SER D OG  1 
ATOM   10829 N  N   . LYS D  1 235 ? 26.507  -15.672 123.738 1.00 14.37  ? 322  LYS D N   1 
ATOM   10830 C  CA  . LYS D  1 235 ? 27.018  -14.923 124.891 1.00 14.74  ? 322  LYS D CA  1 
ATOM   10831 C  C   . LYS D  1 235 ? 27.628  -13.639 124.362 1.00 13.78  ? 322  LYS D C   1 
ATOM   10832 O  O   . LYS D  1 235 ? 27.236  -13.163 123.281 1.00 13.00  ? 322  LYS D O   1 
ATOM   10833 C  CB  . LYS D  1 235 ? 28.036  -15.748 125.724 1.00 14.64  ? 322  LYS D CB  1 
ATOM   10834 C  CG  . LYS D  1 235 ? 29.266  -16.226 124.936 1.00 15.14  ? 322  LYS D CG  1 
ATOM   10835 C  CD  . LYS D  1 235 ? 29.970  -17.383 125.629 1.00 17.18  ? 322  LYS D CD  1 
ATOM   10836 C  CE  . LYS D  1 235 ? 30.753  -16.962 126.833 1.00 21.19  ? 322  LYS D CE  1 
ATOM   10837 N  NZ  . LYS D  1 235 ? 31.265  -18.174 127.576 1.00 24.58  ? 322  LYS D NZ  1 
ATOM   10838 N  N   . TYR D  1 236 ? 28.570  -13.068 125.104 1.00 13.10  ? 323  TYR D N   1 
ATOM   10839 C  CA  . TYR D  1 236 ? 29.284  -11.883 124.628 1.00 12.98  ? 323  TYR D CA  1 
ATOM   10840 C  C   . TYR D  1 236 ? 30.764  -12.192 124.443 1.00 13.66  ? 323  TYR D C   1 
ATOM   10841 O  O   . TYR D  1 236 ? 31.292  -13.134 125.044 1.00 13.51  ? 323  TYR D O   1 
ATOM   10842 C  CB  . TYR D  1 236 ? 29.099  -10.702 125.600 1.00 12.49  ? 323  TYR D CB  1 
ATOM   10843 C  CG  . TYR D  1 236 ? 27.729  -10.081 125.547 1.00 12.91  ? 323  TYR D CG  1 
ATOM   10844 C  CD1 . TYR D  1 236 ? 26.650  -10.682 126.195 1.00 12.40  ? 323  TYR D CD1 1 
ATOM   10845 C  CD2 . TYR D  1 236 ? 27.508  -8.889  124.855 1.00 9.86   ? 323  TYR D CD2 1 
ATOM   10846 C  CE1 . TYR D  1 236 ? 25.365  -10.117 126.143 1.00 12.20  ? 323  TYR D CE1 1 
ATOM   10847 C  CE2 . TYR D  1 236 ? 26.245  -8.325  124.787 1.00 11.87  ? 323  TYR D CE2 1 
ATOM   10848 C  CZ  . TYR D  1 236 ? 25.172  -8.943  125.440 1.00 12.83  ? 323  TYR D CZ  1 
ATOM   10849 O  OH  . TYR D  1 236 ? 23.911  -8.375  125.392 1.00 11.61  ? 323  TYR D OH  1 
ATOM   10850 N  N   . LEU D  1 237 ? 31.441  -11.405 123.610 1.00 13.79  ? 324  LEU D N   1 
ATOM   10851 C  CA  . LEU D  1 237 ? 32.906  -11.412 123.608 1.00 14.78  ? 324  LEU D CA  1 
ATOM   10852 C  C   . LEU D  1 237 ? 33.385  -11.119 125.022 1.00 14.70  ? 324  LEU D C   1 
ATOM   10853 O  O   . LEU D  1 237 ? 32.979  -10.108 125.616 1.00 14.14  ? 324  LEU D O   1 
ATOM   10854 C  CB  . LEU D  1 237 ? 33.468  -10.342 122.673 1.00 15.07  ? 324  LEU D CB  1 
ATOM   10855 C  CG  . LEU D  1 237 ? 33.742  -10.725 121.226 1.00 17.70  ? 324  LEU D CG  1 
ATOM   10856 C  CD1 . LEU D  1 237 ? 34.276  -9.525  120.443 1.00 16.92  ? 324  LEU D CD1 1 
ATOM   10857 C  CD2 . LEU D  1 237 ? 34.699  -11.888 121.172 1.00 19.17  ? 324  LEU D CD2 1 
ATOM   10858 N  N   . CYS D  1 238 ? 34.220  -12.008 125.562 1.00 14.41  ? 325  CYS D N   1 
ATOM   10859 C  CA  . CYS D  1 238 ? 34.741  -11.845 126.934 1.00 14.67  ? 325  CYS D CA  1 
ATOM   10860 C  C   . CYS D  1 238 ? 35.694  -10.668 127.115 1.00 13.89  ? 325  CYS D C   1 
ATOM   10861 O  O   . CYS D  1 238 ? 35.737  -10.071 128.189 1.00 14.17  ? 325  CYS D O   1 
ATOM   10862 C  CB  . CYS D  1 238 ? 35.465  -13.112 127.411 1.00 14.72  ? 325  CYS D CB  1 
ATOM   10863 S  SG  . CYS D  1 238 ? 34.430  -14.599 127.484 1.00 18.09  ? 325  CYS D SG  1 
ATOM   10864 N  N   . SER D  1 239 ? 36.484  -10.357 126.092 1.00 13.29  ? 326  SER D N   1 
ATOM   10865 C  CA  . SER D  1 239 ? 37.557  -9.373  126.243 1.00 12.43  ? 326  SER D CA  1 
ATOM   10866 C  C   . SER D  1 239 ? 37.091  -8.008  126.773 1.00 12.70  ? 326  SER D C   1 
ATOM   10867 O  O   . SER D  1 239 ? 35.987  -7.566  126.454 1.00 11.66  ? 326  SER D O   1 
ATOM   10868 C  CB  . SER D  1 239 ? 38.316  -9.186  124.922 1.00 12.77  ? 326  SER D CB  1 
ATOM   10869 O  OG  . SER D  1 239 ? 39.284  -8.165  125.087 1.00 12.96  ? 326  SER D OG  1 
ATOM   10870 N  N   . LYS D  1 240 ? 37.943  -7.374  127.585 1.00 11.80  ? 327  LYS D N   1 
ATOM   10871 C  CA  . LYS D  1 240 ? 37.785  -5.974  128.016 1.00 13.10  ? 327  LYS D CA  1 
ATOM   10872 C  C   . LYS D  1 240 ? 37.937  -4.972  126.852 1.00 12.24  ? 327  LYS D C   1 
ATOM   10873 O  O   . LYS D  1 240 ? 37.646  -3.766  126.997 1.00 12.29  ? 327  LYS D O   1 
ATOM   10874 C  CB  . LYS D  1 240 ? 38.847  -5.661  129.086 1.00 12.83  ? 327  LYS D CB  1 
ATOM   10875 C  CG  . LYS D  1 240 ? 40.277  -5.704  128.524 1.00 14.37  ? 327  LYS D CG  1 
ATOM   10876 C  CD  . LYS D  1 240 ? 41.321  -5.872  129.614 1.00 17.05  ? 327  LYS D CD  1 
ATOM   10877 C  CE  . LYS D  1 240 ? 42.716  -5.632  129.056 1.00 16.80  ? 327  LYS D CE  1 
ATOM   10878 N  NZ  . LYS D  1 240 ? 43.746  -5.873  130.129 1.00 19.78  ? 327  LYS D NZ  1 
ATOM   10879 N  N   . VAL D  1 241 ? 38.446  -5.452  125.715 1.00 12.42  ? 328  VAL D N   1 
ATOM   10880 C  CA  . VAL D  1 241 ? 38.613  -4.573  124.552 1.00 12.16  ? 328  VAL D CA  1 
ATOM   10881 C  C   . VAL D  1 241 ? 37.248  -4.472  123.889 1.00 11.69  ? 328  VAL D C   1 
ATOM   10882 O  O   . VAL D  1 241 ? 36.829  -5.402  123.189 1.00 11.93  ? 328  VAL D O   1 
ATOM   10883 C  CB  . VAL D  1 241 ? 39.669  -5.088  123.542 1.00 11.85  ? 328  VAL D CB  1 
ATOM   10884 C  CG1 . VAL D  1 241 ? 39.827  -4.091  122.396 1.00 12.13  ? 328  VAL D CG1 1 
ATOM   10885 C  CG2 . VAL D  1 241 ? 41.018  -5.293  124.227 1.00 12.62  ? 328  VAL D CG2 1 
ATOM   10886 N  N   . LEU D  1 242 ? 36.566  -3.351  124.134 1.00 11.11  ? 329  LEU D N   1 
ATOM   10887 C  CA  . LEU D  1 242 ? 35.173  -3.142  123.666 1.00 10.99  ? 329  LEU D CA  1 
ATOM   10888 C  C   . LEU D  1 242 ? 35.179  -2.715  122.210 1.00 10.91  ? 329  LEU D C   1 
ATOM   10889 O  O   . LEU D  1 242 ? 36.004  -1.888  121.821 1.00 11.40  ? 329  LEU D O   1 
ATOM   10890 C  CB  . LEU D  1 242 ? 34.473  -2.089  124.531 1.00 10.23  ? 329  LEU D CB  1 
ATOM   10891 C  CG  . LEU D  1 242 ? 34.351  -2.398  126.034 1.00 10.36  ? 329  LEU D CG  1 
ATOM   10892 C  CD1 . LEU D  1 242 ? 33.606  -1.252  126.727 1.00 10.66  ? 329  LEU D CD1 1 
ATOM   10893 C  CD2 . LEU D  1 242 ? 33.671  -3.742  126.293 1.00 11.55  ? 329  LEU D CD2 1 
ATOM   10894 N  N   . THR D  1 243 ? 34.266  -3.250  121.396 1.00 10.63  ? 330  THR D N   1 
ATOM   10895 C  CA  . THR D  1 243 ? 34.404  -3.023  119.952 1.00 10.45  ? 330  THR D CA  1 
ATOM   10896 C  C   . THR D  1 243 ? 33.176  -2.482  119.240 1.00 10.44  ? 330  THR D C   1 
ATOM   10897 O  O   . THR D  1 243 ? 33.194  -2.351  118.022 1.00 10.53  ? 330  THR D O   1 
ATOM   10898 C  CB  . THR D  1 243 ? 34.951  -4.266  119.196 1.00 10.03  ? 330  THR D CB  1 
ATOM   10899 O  OG1 . THR D  1 243 ? 34.018  -5.336  119.316 1.00 8.72   ? 330  THR D OG1 1 
ATOM   10900 C  CG2 . THR D  1 243 ? 36.339  -4.693  119.742 1.00 9.86   ? 330  THR D CG2 1 
ATOM   10901 N  N   . ASP D  1 244 ? 32.120  -2.166  119.991 1.00 10.61  ? 331  ASP D N   1 
ATOM   10902 C  CA  . ASP D  1 244 ? 30.982  -1.480  119.400 1.00 10.13  ? 331  ASP D CA  1 
ATOM   10903 C  C   . ASP D  1 244 ? 31.228  0.037   119.411 1.00 10.00  ? 331  ASP D C   1 
ATOM   10904 O  O   . ASP D  1 244 ? 32.223  0.516   119.964 1.00 9.77   ? 331  ASP D O   1 
ATOM   10905 C  CB  . ASP D  1 244 ? 29.661  -1.874  120.114 1.00 10.15  ? 331  ASP D CB  1 
ATOM   10906 C  CG  . ASP D  1 244 ? 28.436  -1.826  119.175 1.00 10.51  ? 331  ASP D CG  1 
ATOM   10907 O  OD1 . ASP D  1 244 ? 28.548  -1.330  118.034 1.00 9.89   ? 331  ASP D OD1 1 
ATOM   10908 O  OD2 . ASP D  1 244 ? 27.337  -2.251  119.581 1.00 10.78  ? 331  ASP D OD2 1 
ATOM   10909 N  N   . THR D  1 245 ? 30.334  0.799   118.784 1.00 10.12  ? 332  THR D N   1 
ATOM   10910 C  CA  . THR D  1 245 ? 30.422  2.264   118.791 1.00 10.71  ? 332  THR D CA  1 
ATOM   10911 C  C   . THR D  1 245 ? 28.984  2.765   118.883 1.00 11.12  ? 332  THR D C   1 
ATOM   10912 O  O   . THR D  1 245 ? 28.179  2.372   118.050 1.00 9.99   ? 332  THR D O   1 
ATOM   10913 C  CB  . THR D  1 245 ? 31.019  2.798   117.471 1.00 11.00  ? 332  THR D CB  1 
ATOM   10914 O  OG1 . THR D  1 245 ? 32.286  2.163   117.231 1.00 11.29  ? 332  THR D OG1 1 
ATOM   10915 C  CG2 . THR D  1 245 ? 31.190  4.340   117.504 1.00 9.71   ? 332  THR D CG2 1 
ATOM   10916 N  N   . SER D  1 246 ? 28.645  3.646   119.836 1.00 11.22  ? 333  SER D N   1 
ATOM   10917 C  CA  . SER D  1 246 ? 29.550  4.253   120.793 1.00 12.28  ? 333  SER D CA  1 
ATOM   10918 C  C   . SER D  1 246 ? 29.844  3.278   121.926 1.00 12.39  ? 333  SER D C   1 
ATOM   10919 O  O   . SER D  1 246 ? 29.040  2.384   122.207 1.00 13.03  ? 333  SER D O   1 
ATOM   10920 C  CB  . SER D  1 246 ? 28.925  5.536   121.364 1.00 12.05  ? 333  SER D CB  1 
ATOM   10921 O  OG  . SER D  1 246 ? 28.463  6.418   120.341 1.00 12.46  ? 333  SER D OG  1 
ATOM   10922 N  N   . ARG D  1 247 ? 30.975  3.489   122.591 1.00 12.97  ? 334  ARG D N   1 
ATOM   10923 C  CA  . ARG D  1 247 ? 31.398  2.644   123.721 1.00 12.50  ? 334  ARG D CA  1 
ATOM   10924 C  C   . ARG D  1 247 ? 32.108  3.496   124.782 1.00 12.53  ? 334  ARG D C   1 
ATOM   10925 O  O   . ARG D  1 247 ? 32.613  4.589   124.476 1.00 13.15  ? 334  ARG D O   1 
ATOM   10926 C  CB  . ARG D  1 247 ? 32.342  1.540   123.220 1.00 12.69  ? 334  ARG D CB  1 
ATOM   10927 C  CG  . ARG D  1 247 ? 33.639  2.088   122.590 1.00 11.73  ? 334  ARG D CG  1 
ATOM   10928 C  CD  . ARG D  1 247 ? 34.562  0.970   122.113 1.00 11.30  ? 334  ARG D CD  1 
ATOM   10929 N  NE  . ARG D  1 247 ? 35.812  1.526   121.574 1.00 8.57   ? 334  ARG D NE  1 
ATOM   10930 C  CZ  . ARG D  1 247 ? 35.986  1.878   120.301 1.00 10.28  ? 334  ARG D CZ  1 
ATOM   10931 N  NH1 . ARG D  1 247 ? 35.025  1.693   119.405 1.00 7.88   ? 334  ARG D NH1 1 
ATOM   10932 N  NH2 . ARG D  1 247 ? 37.134  2.406   119.916 1.00 8.32   ? 334  ARG D NH2 1 
ATOM   10933 N  N   . PRO D  1 248 ? 32.161  3.001   126.037 1.00 12.98  ? 335  PRO D N   1 
ATOM   10934 C  CA  . PRO D  1 248 ? 32.969  3.704   127.043 1.00 12.65  ? 335  PRO D CA  1 
ATOM   10935 C  C   . PRO D  1 248 ? 34.429  3.279   126.911 1.00 12.67  ? 335  PRO D C   1 
ATOM   10936 O  O   . PRO D  1 248 ? 34.753  2.459   126.043 1.00 13.16  ? 335  PRO D O   1 
ATOM   10937 C  CB  . PRO D  1 248 ? 32.399  3.179   128.365 1.00 12.70  ? 335  PRO D CB  1 
ATOM   10938 C  CG  . PRO D  1 248 ? 31.970  1.783   128.048 1.00 12.17  ? 335  PRO D CG  1 
ATOM   10939 C  CD  . PRO D  1 248 ? 31.527  1.791   126.591 1.00 11.64  ? 335  PRO D CD  1 
ATOM   10940 N  N   . ASN D  1 249 ? 35.293  3.793   127.784 1.00 13.54  ? 336  ASN D N   1 
ATOM   10941 C  CA  . ASN D  1 249 ? 36.661  3.281   127.889 1.00 14.93  ? 336  ASN D CA  1 
ATOM   10942 C  C   . ASN D  1 249 ? 36.645  1.780   128.185 1.00 15.28  ? 336  ASN D C   1 
ATOM   10943 O  O   . ASN D  1 249 ? 35.708  1.276   128.806 1.00 14.73  ? 336  ASN D O   1 
ATOM   10944 C  CB  . ASN D  1 249 ? 37.446  4.014   128.987 1.00 15.43  ? 336  ASN D CB  1 
ATOM   10945 C  CG  . ASN D  1 249 ? 37.620  5.478   128.683 1.00 18.13  ? 336  ASN D CG  1 
ATOM   10946 O  OD1 . ASN D  1 249 ? 37.887  5.851   127.556 1.00 21.20  ? 336  ASN D OD1 1 
ATOM   10947 N  ND2 . ASN D  1 249 ? 37.437  6.318   129.685 1.00 23.19  ? 336  ASN D ND2 1 
ATOM   10948 N  N   . ASP D  1 250 ? 37.668  1.070   127.728 1.00 15.59  ? 337  ASP D N   1 
ATOM   10949 C  CA  . ASP D  1 250 ? 37.784  -0.355  128.055 1.00 16.08  ? 337  ASP D CA  1 
ATOM   10950 C  C   . ASP D  1 250 ? 37.948  -0.483  129.559 1.00 16.43  ? 337  ASP D C   1 
ATOM   10951 O  O   . ASP D  1 250 ? 38.775  0.233   130.147 1.00 17.24  ? 337  ASP D O   1 
ATOM   10952 C  CB  . ASP D  1 250 ? 38.969  -0.986  127.318 1.00 16.66  ? 337  ASP D CB  1 
ATOM   10953 C  CG  . ASP D  1 250 ? 38.774  -0.983  125.805 1.00 16.92  ? 337  ASP D CG  1 
ATOM   10954 O  OD1 . ASP D  1 250 ? 39.785  -1.062  125.072 1.00 18.16  ? 337  ASP D OD1 1 
ATOM   10955 O  OD2 . ASP D  1 250 ? 37.604  -0.899  125.361 1.00 16.40  ? 337  ASP D OD2 1 
ATOM   10956 N  N   . PRO D  1 251 ? 37.126  -1.344  130.191 1.00 16.13  ? 338  PRO D N   1 
ATOM   10957 C  CA  . PRO D  1 251 ? 37.251  -1.583  131.621 1.00 16.31  ? 338  PRO D CA  1 
ATOM   10958 C  C   . PRO D  1 251 ? 38.432  -2.491  131.961 1.00 16.04  ? 338  PRO D C   1 
ATOM   10959 O  O   . PRO D  1 251 ? 39.115  -3.016  131.075 1.00 15.73  ? 338  PRO D O   1 
ATOM   10960 C  CB  . PRO D  1 251 ? 35.927  -2.280  131.966 1.00 15.57  ? 338  PRO D CB  1 
ATOM   10961 C  CG  . PRO D  1 251 ? 35.585  -3.042  130.728 1.00 16.92  ? 338  PRO D CG  1 
ATOM   10962 C  CD  . PRO D  1 251 ? 36.023  -2.127  129.598 1.00 15.73  ? 338  PRO D CD  1 
ATOM   10963 N  N   . THR D  1 252 ? 38.660  -2.669  133.253 1.00 15.54  ? 339  THR D N   1 
ATOM   10964 C  CA  . THR D  1 252 ? 39.674  -3.580  133.744 1.00 15.94  ? 339  THR D CA  1 
ATOM   10965 C  C   . THR D  1 252 ? 39.412  -5.026  133.283 1.00 15.79  ? 339  THR D C   1 
ATOM   10966 O  O   . THR D  1 252 ? 40.349  -5.701  132.872 1.00 16.02  ? 339  THR D O   1 
ATOM   10967 C  CB  . THR D  1 252 ? 39.813  -3.465  135.284 1.00 15.63  ? 339  THR D CB  1 
ATOM   10968 O  OG1 . THR D  1 252 ? 40.098  -2.093  135.609 1.00 17.67  ? 339  THR D OG1 1 
ATOM   10969 C  CG2 . THR D  1 252 ? 40.945  -4.337  135.805 1.00 16.88  ? 339  THR D CG2 1 
ATOM   10970 N  N   . ASN D  1 253 ? 38.155  -5.478  133.322 1.00 15.56  ? 340  ASN D N   1 
ATOM   10971 C  CA  . ASN D  1 253 ? 37.763  -6.789  132.765 1.00 16.14  ? 340  ASN D CA  1 
ATOM   10972 C  C   . ASN D  1 253 ? 36.495  -6.678  131.942 1.00 15.52  ? 340  ASN D C   1 
ATOM   10973 O  O   . ASN D  1 253 ? 35.589  -5.906  132.276 1.00 15.12  ? 340  ASN D O   1 
ATOM   10974 C  CB  . ASN D  1 253 ? 37.408  -7.831  133.841 1.00 17.08  ? 340  ASN D CB  1 
ATOM   10975 C  CG  . ASN D  1 253 ? 38.365  -7.875  134.995 1.00 18.86  ? 340  ASN D CG  1 
ATOM   10976 O  OD1 . ASN D  1 253 ? 37.927  -8.039  136.134 1.00 25.62  ? 340  ASN D OD1 1 
ATOM   10977 N  ND2 . ASN D  1 253 ? 39.661  -7.796  134.728 1.00 21.97  ? 340  ASN D ND2 1 
ATOM   10978 N  N   . GLY D  1 254 ? 36.397  -7.499  130.909 1.00 15.02  ? 341  GLY D N   1 
ATOM   10979 C  CA  . GLY D  1 254 ? 35.151  -7.641  130.182 1.00 14.46  ? 341  GLY D CA  1 
ATOM   10980 C  C   . GLY D  1 254 ? 34.189  -8.579  130.901 1.00 14.84  ? 341  GLY D C   1 
ATOM   10981 O  O   . GLY D  1 254 ? 34.378  -8.906  132.088 1.00 14.63  ? 341  GLY D O   1 
ATOM   10982 N  N   . ASN D  1 255 ? 33.154  -8.999  130.174 1.00 14.33  ? 342  ASN D N   1 
ATOM   10983 C  CA  . ASN D  1 255 ? 32.110  -9.873  130.695 1.00 14.87  ? 342  ASN D CA  1 
ATOM   10984 C  C   . ASN D  1 255 ? 31.631  -10.803 129.585 1.00 14.93  ? 342  ASN D C   1 
ATOM   10985 O  O   . ASN D  1 255 ? 31.075  -10.330 128.586 1.00 14.11  ? 342  ASN D O   1 
ATOM   10986 C  CB  . ASN D  1 255 ? 30.930  -9.034  131.213 1.00 14.95  ? 342  ASN D CB  1 
ATOM   10987 C  CG  . ASN D  1 255 ? 29.982  -9.827  132.130 1.00 15.92  ? 342  ASN D CG  1 
ATOM   10988 O  OD1 . ASN D  1 255 ? 29.418  -9.267  133.086 1.00 18.53  ? 342  ASN D OD1 1 
ATOM   10989 N  ND2 . ASN D  1 255 ? 29.794  -11.113 131.844 1.00 14.09  ? 342  ASN D ND2 1 
ATOM   10990 N  N   . CYS D  1 256 ? 31.858  -12.111 129.759 1.00 15.17  ? 343  CYS D N   1 
ATOM   10991 C  CA  . CYS D  1 256 ? 31.411  -13.139 128.809 1.00 15.65  ? 343  CYS D CA  1 
ATOM   10992 C  C   . CYS D  1 256 ? 29.883  -13.286 128.702 1.00 15.92  ? 343  CYS D C   1 
ATOM   10993 O  O   . CYS D  1 256 ? 29.375  -13.761 127.696 1.00 15.18  ? 343  CYS D O   1 
ATOM   10994 C  CB  . CYS D  1 256 ? 31.964  -14.519 129.213 1.00 15.12  ? 343  CYS D CB  1 
ATOM   10995 S  SG  . CYS D  1 256 ? 33.747  -14.634 129.407 1.00 19.65  ? 343  CYS D SG  1 
ATOM   10996 N  N   . ASP D  1 257 ? 29.158  -12.913 129.753 1.00 16.07  ? 344  ASP D N   1 
ATOM   10997 C  CA  . ASP D  1 257 ? 27.762  -13.345 129.859 1.00 16.81  ? 344  ASP D CA  1 
ATOM   10998 C  C   . ASP D  1 257 ? 26.729  -12.250 130.090 1.00 16.11  ? 344  ASP D C   1 
ATOM   10999 O  O   . ASP D  1 257 ? 25.561  -12.546 130.330 1.00 16.58  ? 344  ASP D O   1 
ATOM   11000 C  CB  . ASP D  1 257 ? 27.653  -14.473 130.883 1.00 17.95  ? 344  ASP D CB  1 
ATOM   11001 C  CG  . ASP D  1 257 ? 28.399  -15.718 130.424 1.00 20.34  ? 344  ASP D CG  1 
ATOM   11002 O  OD1 . ASP D  1 257 ? 29.453  -16.016 130.995 1.00 23.69  ? 344  ASP D OD1 1 
ATOM   11003 O  OD2 . ASP D  1 257 ? 27.954  -16.364 129.443 1.00 24.73  ? 344  ASP D OD2 1 
ATOM   11004 N  N   . ALA D  1 258 ? 27.160  -11.003 129.966 1.00 14.91  ? 345  ALA D N   1 
ATOM   11005 C  CA  . ALA D  1 258 ? 26.289  -9.839  130.110 1.00 14.98  ? 345  ALA D CA  1 
ATOM   11006 C  C   . ALA D  1 258 ? 26.878  -8.620  129.387 1.00 14.46  ? 345  ALA D C   1 
ATOM   11007 O  O   . ALA D  1 258 ? 28.109  -8.519  129.249 1.00 14.09  ? 345  ALA D O   1 
ATOM   11008 C  CB  . ALA D  1 258 ? 26.083  -9.517  131.597 1.00 14.64  ? 345  ALA D CB  1 
ATOM   11009 N  N   . PRO D  1 259 ? 26.010  -7.691  128.928 1.00 14.67  ? 346  PRO D N   1 
ATOM   11010 C  CA  . PRO D  1 259 ? 26.500  -6.453  128.307 1.00 14.76  ? 346  PRO D CA  1 
ATOM   11011 C  C   . PRO D  1 259 ? 27.327  -5.545  129.224 1.00 15.33  ? 346  PRO D C   1 
ATOM   11012 O  O   . PRO D  1 259 ? 27.029  -5.406  130.427 1.00 15.43  ? 346  PRO D O   1 
ATOM   11013 C  CB  . PRO D  1 259 ? 25.218  -5.757  127.826 1.00 14.17  ? 346  PRO D CB  1 
ATOM   11014 C  CG  . PRO D  1 259 ? 24.119  -6.338  128.682 1.00 15.03  ? 346  PRO D CG  1 
ATOM   11015 C  CD  . PRO D  1 259 ? 24.531  -7.760  128.919 1.00 14.98  ? 346  PRO D CD  1 
ATOM   11016 N  N   . ILE D  1 260 ? 28.380  -4.965  128.661 1.00 14.84  ? 347  ILE D N   1 
ATOM   11017 C  CA  . ILE D  1 260 ? 29.066  -3.849  129.295 1.00 15.80  ? 347  ILE D CA  1 
ATOM   11018 C  C   . ILE D  1 260 ? 28.519  -2.573  128.682 1.00 15.63  ? 347  ILE D C   1 
ATOM   11019 O  O   . ILE D  1 260 ? 28.675  -2.307  127.467 1.00 15.11  ? 347  ILE D O   1 
ATOM   11020 C  CB  . ILE D  1 260 ? 30.603  -3.935  129.158 1.00 15.78  ? 347  ILE D CB  1 
ATOM   11021 C  CG1 . ILE D  1 260 ? 31.108  -5.208  129.846 1.00 17.67  ? 347  ILE D CG1 1 
ATOM   11022 C  CG2 . ILE D  1 260 ? 31.274  -2.662  129.719 1.00 15.52  ? 347  ILE D CG2 1 
ATOM   11023 C  CD1 . ILE D  1 260 ? 32.538  -5.500  129.611 1.00 19.69  ? 347  ILE D CD1 1 
ATOM   11024 N  N   . THR D  1 261 ? 27.850  -1.796  129.517 1.00 15.12  ? 348  THR D N   1 
ATOM   11025 C  CA  . THR D  1 261 ? 27.097  -0.642  129.030 1.00 15.75  ? 348  THR D CA  1 
ATOM   11026 C  C   . THR D  1 261 ? 27.896  0.647   129.094 1.00 15.66  ? 348  THR D C   1 
ATOM   11027 O  O   . THR D  1 261 ? 28.996  0.709   129.687 1.00 15.34  ? 348  THR D O   1 
ATOM   11028 C  CB  . THR D  1 261 ? 25.765  -0.478  129.816 1.00 16.27  ? 348  THR D CB  1 
ATOM   11029 O  OG1 . THR D  1 261 ? 26.057  -0.222  131.203 1.00 16.48  ? 348  THR D OG1 1 
ATOM   11030 C  CG2 . THR D  1 261 ? 24.908  -1.753  129.684 1.00 16.69  ? 348  THR D CG2 1 
ATOM   11031 N  N   . GLY D  1 262 ? 27.346  1.686   128.480 1.00 15.21  ? 349  GLY D N   1 
ATOM   11032 C  CA  . GLY D  1 262 ? 28.014  2.977   128.489 1.00 15.25  ? 349  GLY D CA  1 
ATOM   11033 C  C   . GLY D  1 262 ? 28.306  3.460   127.082 1.00 15.57  ? 349  GLY D C   1 
ATOM   11034 O  O   . GLY D  1 262 ? 28.046  2.754   126.100 1.00 15.53  ? 349  GLY D O   1 
ATOM   11035 N  N   . GLY D  1 263 ? 28.861  4.669   126.988 1.00 15.61  ? 350  GLY D N   1 
ATOM   11036 C  CA  . GLY D  1 263 ? 29.208  5.231   125.692 1.00 15.42  ? 350  GLY D CA  1 
ATOM   11037 C  C   . GLY D  1 263 ? 28.146  6.220   125.259 1.00 15.40  ? 350  GLY D C   1 
ATOM   11038 O  O   . GLY D  1 263 ? 27.014  6.180   125.747 1.00 15.51  ? 350  GLY D O   1 
ATOM   11039 N  N   . SER D  1 264 ? 28.506  7.095   124.328 1.00 14.82  ? 351  SER D N   1 
ATOM   11040 C  CA  . SER D  1 264 ? 27.619  8.144   123.881 1.00 15.73  ? 351  SER D CA  1 
ATOM   11041 C  C   . SER D  1 264 ? 28.155  8.700   122.555 1.00 15.22  ? 351  SER D C   1 
ATOM   11042 O  O   . SER D  1 264 ? 29.372  8.797   122.384 1.00 14.92  ? 351  SER D O   1 
ATOM   11043 C  CB  . SER D  1 264 ? 27.571  9.231   124.963 1.00 15.90  ? 351  SER D CB  1 
ATOM   11044 O  OG  . SER D  1 264 ? 26.872  10.370  124.518 1.00 17.42  ? 351  SER D OG  1 
ATOM   11045 N  N   . PRO D  1 265 ? 27.267  9.110   121.632 1.00 15.02  ? 352  PRO D N   1 
ATOM   11046 C  CA  . PRO D  1 265 ? 25.814  9.185   121.731 1.00 15.16  ? 352  PRO D CA  1 
ATOM   11047 C  C   . PRO D  1 265 ? 25.019  8.052   121.051 1.00 14.88  ? 352  PRO D C   1 
ATOM   11048 O  O   . PRO D  1 265 ? 23.796  8.041   121.133 1.00 14.97  ? 352  PRO D O   1 
ATOM   11049 C  CB  . PRO D  1 265 ? 25.524  10.511  121.025 1.00 14.82  ? 352  PRO D CB  1 
ATOM   11050 C  CG  . PRO D  1 265 ? 26.525  10.527  119.902 1.00 15.31  ? 352  PRO D CG  1 
ATOM   11051 C  CD  . PRO D  1 265 ? 27.721  9.692   120.350 1.00 15.71  ? 352  PRO D CD  1 
ATOM   11052 N  N   . ASP D  1 266 ? 25.698  7.115   120.400 1.00 14.46  ? 353  ASP D N   1 
ATOM   11053 C  CA  . ASP D  1 266 ? 25.007  6.117   119.577 1.00 15.10  ? 353  ASP D CA  1 
ATOM   11054 C  C   . ASP D  1 266 ? 25.062  4.694   120.117 1.00 14.46  ? 353  ASP D C   1 
ATOM   11055 O  O   . ASP D  1 266 ? 26.067  4.287   120.730 1.00 14.29  ? 353  ASP D O   1 
ATOM   11056 C  CB  . ASP D  1 266 ? 25.507  6.189   118.126 1.00 15.78  ? 353  ASP D CB  1 
ATOM   11057 C  CG  . ASP D  1 266 ? 25.333  7.591   117.519 1.00 17.77  ? 353  ASP D CG  1 
ATOM   11058 O  OD1 . ASP D  1 266 ? 24.258  8.218   117.708 1.00 20.80  ? 353  ASP D OD1 1 
ATOM   11059 O  OD2 . ASP D  1 266 ? 26.267  8.063   116.845 1.00 16.57  ? 353  ASP D OD2 1 
ATOM   11060 N  N   . PRO D  1 267 ? 23.970  3.925   119.906 1.00 14.11  ? 354  PRO D N   1 
ATOM   11061 C  CA  . PRO D  1 267 ? 23.848  2.609   120.517 1.00 13.21  ? 354  PRO D CA  1 
ATOM   11062 C  C   . PRO D  1 267 ? 24.578  1.438   119.841 1.00 12.19  ? 354  PRO D C   1 
ATOM   11063 O  O   . PRO D  1 267 ? 24.683  0.366   120.449 1.00 11.94  ? 354  PRO D O   1 
ATOM   11064 C  CB  . PRO D  1 267 ? 22.331  2.374   120.500 1.00 13.51  ? 354  PRO D CB  1 
ATOM   11065 C  CG  . PRO D  1 267 ? 21.886  3.019   119.244 1.00 13.32  ? 354  PRO D CG  1 
ATOM   11066 C  CD  . PRO D  1 267 ? 22.752  4.279   119.139 1.00 14.17  ? 354  PRO D CD  1 
ATOM   11067 N  N   . GLY D  1 268 ? 25.081  1.614   118.618 1.00 11.70  ? 355  GLY D N   1 
ATOM   11068 C  CA  . GLY D  1 268 ? 25.733  0.497   117.943 1.00 10.73  ? 355  GLY D CA  1 
ATOM   11069 C  C   . GLY D  1 268 ? 26.142  0.737   116.496 1.00 10.16  ? 355  GLY D C   1 
ATOM   11070 O  O   . GLY D  1 268 ? 25.694  1.685   115.859 1.00 10.32  ? 355  GLY D O   1 
ATOM   11071 N  N   . VAL D  1 269 ? 27.033  -0.122  116.011 1.00 9.75   ? 356  VAL D N   1 
ATOM   11072 C  CA  . VAL D  1 269 ? 27.417  -0.154  114.606 1.00 9.32   ? 356  VAL D CA  1 
ATOM   11073 C  C   . VAL D  1 269 ? 27.668  -1.619  114.252 1.00 8.80   ? 356  VAL D C   1 
ATOM   11074 O  O   . VAL D  1 269 ? 28.127  -2.383  115.100 1.00 8.92   ? 356  VAL D O   1 
ATOM   11075 C  CB  . VAL D  1 269 ? 28.677  0.726   114.312 1.00 8.77   ? 356  VAL D CB  1 
ATOM   11076 C  CG1 . VAL D  1 269 ? 29.935  0.231   115.045 1.00 8.39   ? 356  VAL D CG1 1 
ATOM   11077 C  CG2 . VAL D  1 269 ? 28.935  0.824   112.781 1.00 7.95   ? 356  VAL D CG2 1 
ATOM   11078 N  N   . LYS D  1 270 ? 27.367  -2.016  113.019 1.00 8.57   ? 357  LYS D N   1 
ATOM   11079 C  CA  . LYS D  1 270 ? 27.738  -3.375  112.583 1.00 7.42   ? 357  LYS D CA  1 
ATOM   11080 C  C   . LYS D  1 270 ? 29.271  -3.531  112.632 1.00 7.59   ? 357  LYS D C   1 
ATOM   11081 O  O   . LYS D  1 270 ? 29.998  -2.643  112.188 1.00 7.66   ? 357  LYS D O   1 
ATOM   11082 C  CB  . LYS D  1 270 ? 27.259  -3.652  111.166 1.00 7.54   ? 357  LYS D CB  1 
ATOM   11083 C  CG  . LYS D  1 270 ? 27.573  -5.063  110.688 1.00 6.34   ? 357  LYS D CG  1 
ATOM   11084 C  CD  . LYS D  1 270 ? 27.131  -5.236  109.249 1.00 5.76   ? 357  LYS D CD  1 
ATOM   11085 C  CE  . LYS D  1 270 ? 27.633  -6.538  108.667 1.00 5.42   ? 357  LYS D CE  1 
ATOM   11086 N  NZ  . LYS D  1 270 ? 27.194  -7.769  109.388 1.00 6.67   ? 357  LYS D NZ  1 
ATOM   11087 N  N   . GLY D  1 271 ? 29.722  -4.676  113.157 1.00 7.64   ? 358  GLY D N   1 
ATOM   11088 C  CA  . GLY D  1 271 ? 31.146  -5.002  113.240 1.00 7.66   ? 358  GLY D CA  1 
ATOM   11089 C  C   . GLY D  1 271 ? 31.401  -6.491  113.200 1.00 7.34   ? 358  GLY D C   1 
ATOM   11090 O  O   . GLY D  1 271 ? 30.516  -7.298  112.863 1.00 8.11   ? 358  GLY D O   1 
ATOM   11091 N  N   . PHE D  1 272 ? 32.630  -6.870  113.528 1.00 7.68   ? 359  PHE D N   1 
ATOM   11092 C  CA  . PHE D  1 272 ? 33.046  -8.259  113.342 1.00 7.56   ? 359  PHE D CA  1 
ATOM   11093 C  C   . PHE D  1 272 ? 34.294  -8.556  114.157 1.00 7.90   ? 359  PHE D C   1 
ATOM   11094 O  O   . PHE D  1 272 ? 35.005  -7.626  114.634 1.00 8.49   ? 359  PHE D O   1 
ATOM   11095 C  CB  . PHE D  1 272 ? 33.342  -8.518  111.850 1.00 6.59   ? 359  PHE D CB  1 
ATOM   11096 C  CG  . PHE D  1 272 ? 34.704  -8.051  111.437 1.00 8.22   ? 359  PHE D CG  1 
ATOM   11097 C  CD1 . PHE D  1 272 ? 34.934  -6.692  111.131 1.00 9.17   ? 359  PHE D CD1 1 
ATOM   11098 C  CD2 . PHE D  1 272 ? 35.782  -8.942  111.429 1.00 8.59   ? 359  PHE D CD2 1 
ATOM   11099 C  CE1 . PHE D  1 272 ? 36.211  -6.245  110.766 1.00 8.82   ? 359  PHE D CE1 1 
ATOM   11100 C  CE2 . PHE D  1 272 ? 37.066  -8.508  111.090 1.00 9.01   ? 359  PHE D CE2 1 
ATOM   11101 C  CZ  . PHE D  1 272 ? 37.284  -7.152  110.760 1.00 7.40   ? 359  PHE D CZ  1 
ATOM   11102 N  N   . ALA D  1 273 ? 34.571  -9.860  114.283 1.00 7.80   ? 360  ALA D N   1 
ATOM   11103 C  CA  . ALA D  1 273 ? 35.836  -10.365 114.810 1.00 8.76   ? 360  ALA D CA  1 
ATOM   11104 C  C   . ALA D  1 273 ? 36.087  -11.788 114.282 1.00 8.97   ? 360  ALA D C   1 
ATOM   11105 O  O   . ALA D  1 273 ? 35.162  -12.474 113.843 1.00 9.89   ? 360  ALA D O   1 
ATOM   11106 C  CB  . ALA D  1 273 ? 35.809  -10.392 116.323 1.00 7.24   ? 360  ALA D CB  1 
ATOM   11107 N  N   . PHE D  1 274 ? 37.346  -12.210 114.324 1.00 9.63   ? 361  PHE D N   1 
ATOM   11108 C  CA  . PHE D  1 274 ? 37.719  -13.592 114.074 1.00 9.58   ? 361  PHE D CA  1 
ATOM   11109 C  C   . PHE D  1 274 ? 38.277  -14.109 115.395 1.00 10.20  ? 361  PHE D C   1 
ATOM   11110 O  O   . PHE D  1 274 ? 39.168  -13.486 115.995 1.00 10.15  ? 361  PHE D O   1 
ATOM   11111 C  CB  . PHE D  1 274 ? 38.742  -13.689 112.923 1.00 10.28  ? 361  PHE D CB  1 
ATOM   11112 C  CG  . PHE D  1 274 ? 38.140  -13.411 111.568 1.00 9.19   ? 361  PHE D CG  1 
ATOM   11113 C  CD1 . PHE D  1 274 ? 37.528  -14.440 110.838 1.00 9.37   ? 361  PHE D CD1 1 
ATOM   11114 C  CD2 . PHE D  1 274 ? 38.193  -12.135 111.011 1.00 9.14   ? 361  PHE D CD2 1 
ATOM   11115 C  CE1 . PHE D  1 274 ? 36.959  -14.192 109.554 1.00 8.88   ? 361  PHE D CE1 1 
ATOM   11116 C  CE2 . PHE D  1 274 ? 37.628  -11.880 109.744 1.00 8.65   ? 361  PHE D CE2 1 
ATOM   11117 C  CZ  . PHE D  1 274 ? 37.013  -12.915 109.021 1.00 8.88   ? 361  PHE D CZ  1 
ATOM   11118 N  N   . LEU D  1 275 ? 37.747  -15.254 115.817 1.00 11.41  ? 362  LEU D N   1 
ATOM   11119 C  CA  . LEU D  1 275 ? 37.927  -15.795 117.171 1.00 11.61  ? 362  LEU D CA  1 
ATOM   11120 C  C   . LEU D  1 275 ? 38.455  -17.224 117.089 1.00 12.23  ? 362  LEU D C   1 
ATOM   11121 O  O   . LEU D  1 275 ? 37.728  -18.154 116.729 1.00 12.84  ? 362  LEU D O   1 
ATOM   11122 C  CB  . LEU D  1 275 ? 36.581  -15.727 117.924 1.00 11.15  ? 362  LEU D CB  1 
ATOM   11123 C  CG  . LEU D  1 275 ? 35.937  -14.342 118.080 1.00 11.39  ? 362  LEU D CG  1 
ATOM   11124 C  CD1 . LEU D  1 275 ? 34.544  -14.431 118.769 1.00 11.66  ? 362  LEU D CD1 1 
ATOM   11125 C  CD2 . LEU D  1 275 ? 36.869  -13.339 118.795 1.00 9.77   ? 362  LEU D CD2 1 
ATOM   11126 N  N   . ASP D  1 276 ? 39.737  -17.382 117.411 1.00 13.02  ? 363  ASP D N   1 
ATOM   11127 C  CA  . ASP D  1 276 ? 40.460  -18.637 117.184 1.00 13.77  ? 363  ASP D CA  1 
ATOM   11128 C  C   . ASP D  1 276 ? 41.654  -18.718 118.151 1.00 14.07  ? 363  ASP D C   1 
ATOM   11129 O  O   . ASP D  1 276 ? 42.808  -18.742 117.728 1.00 13.65  ? 363  ASP D O   1 
ATOM   11130 C  CB  . ASP D  1 276 ? 40.925  -18.672 115.721 1.00 13.83  ? 363  ASP D CB  1 
ATOM   11131 C  CG  . ASP D  1 276 ? 41.675  -19.929 115.361 1.00 16.09  ? 363  ASP D CG  1 
ATOM   11132 O  OD1 . ASP D  1 276 ? 42.658  -19.819 114.592 1.00 15.77  ? 363  ASP D OD1 1 
ATOM   11133 O  OD2 . ASP D  1 276 ? 41.294  -21.018 115.849 1.00 18.51  ? 363  ASP D OD2 1 
ATOM   11134 N  N   . GLY D  1 277 ? 41.364  -18.711 119.456 1.00 14.11  ? 364  GLY D N   1 
ATOM   11135 C  CA  . GLY D  1 277 ? 42.411  -18.817 120.482 1.00 14.70  ? 364  GLY D CA  1 
ATOM   11136 C  C   . GLY D  1 277 ? 43.400  -17.676 120.395 1.00 15.23  ? 364  GLY D C   1 
ATOM   11137 O  O   . GLY D  1 277 ? 43.009  -16.520 120.320 1.00 14.36  ? 364  GLY D O   1 
ATOM   11138 N  N   . GLU D  1 278 ? 44.693  -18.005 120.391 1.00 15.10  ? 365  GLU D N   1 
ATOM   11139 C  CA  . GLU D  1 278 ? 45.747  -16.995 120.253 1.00 17.04  ? 365  GLU D CA  1 
ATOM   11140 C  C   . GLU D  1 278 ? 45.596  -16.157 118.964 1.00 14.94  ? 365  GLU D C   1 
ATOM   11141 O  O   . GLU D  1 278 ? 45.926  -14.972 118.957 1.00 14.61  ? 365  GLU D O   1 
ATOM   11142 C  CB  . GLU D  1 278 ? 47.136  -17.647 120.336 1.00 17.06  ? 365  GLU D CB  1 
ATOM   11143 C  CG  . GLU D  1 278 ? 47.540  -18.083 121.775 1.00 21.29  ? 365  GLU D CG  1 
ATOM   11144 C  CD  . GLU D  1 278 ? 48.957  -18.702 121.868 1.00 22.74  ? 365  GLU D CD  1 
ATOM   11145 O  OE1 . GLU D  1 278 ? 49.476  -19.230 120.857 1.00 31.83  ? 365  GLU D OE1 1 
ATOM   11146 O  OE2 . GLU D  1 278 ? 49.558  -18.669 122.972 1.00 30.17  ? 365  GLU D OE2 1 
ATOM   11147 N  N   . ASN D  1 279 ? 45.075  -16.801 117.911 1.00 14.12  ? 366  ASN D N   1 
ATOM   11148 C  CA  . ASN D  1 279 ? 44.889  -16.234 116.558 1.00 12.67  ? 366  ASN D CA  1 
ATOM   11149 C  C   . ASN D  1 279 ? 43.559  -15.448 116.443 1.00 12.84  ? 366  ASN D C   1 
ATOM   11150 O  O   . ASN D  1 279 ? 42.710  -15.758 115.584 1.00 13.36  ? 366  ASN D O   1 
ATOM   11151 C  CB  . ASN D  1 279 ? 44.925  -17.381 115.534 1.00 12.78  ? 366  ASN D CB  1 
ATOM   11152 C  CG  . ASN D  1 279 ? 45.005  -16.898 114.095 1.00 11.93  ? 366  ASN D CG  1 
ATOM   11153 O  OD1 . ASN D  1 279 ? 45.765  -15.968 113.773 1.00 13.78  ? 366  ASN D OD1 1 
ATOM   11154 N  ND2 . ASN D  1 279 ? 44.213  -17.512 113.226 1.00 10.23  ? 366  ASN D ND2 1 
ATOM   11155 N  N   . SER D  1 280 ? 43.377  -14.451 117.319 1.00 11.38  ? 367  SER D N   1 
ATOM   11156 C  CA  . SER D  1 280 ? 42.097  -13.730 117.400 1.00 11.16  ? 367  SER D CA  1 
ATOM   11157 C  C   . SER D  1 280 ? 42.295  -12.263 117.091 1.00 10.92  ? 367  SER D C   1 
ATOM   11158 O  O   . SER D  1 280 ? 43.236  -11.639 117.603 1.00 10.25  ? 367  SER D O   1 
ATOM   11159 C  CB  . SER D  1 280 ? 41.430  -13.886 118.785 1.00 9.76   ? 367  SER D CB  1 
ATOM   11160 O  OG  . SER D  1 280 ? 41.088  -15.247 119.073 1.00 10.91  ? 367  SER D OG  1 
ATOM   11161 N  N   . TRP D  1 281 ? 41.385  -11.710 116.277 1.00 11.14  ? 368  TRP D N   1 
ATOM   11162 C  CA  . TRP D  1 281 ? 41.479  -10.321 115.835 1.00 10.82  ? 368  TRP D CA  1 
ATOM   11163 C  C   . TRP D  1 281 ? 40.129  -9.635  115.928 1.00 11.52  ? 368  TRP D C   1 
ATOM   11164 O  O   . TRP D  1 281 ? 39.116  -10.165 115.439 1.00 11.55  ? 368  TRP D O   1 
ATOM   11165 C  CB  . TRP D  1 281 ? 41.938  -10.243 114.384 1.00 10.64  ? 368  TRP D CB  1 
ATOM   11166 C  CG  . TRP D  1 281 ? 43.409  -10.522 114.133 1.00 9.64   ? 368  TRP D CG  1 
ATOM   11167 C  CD1 . TRP D  1 281 ? 43.994  -11.743 113.900 1.00 9.55   ? 368  TRP D CD1 1 
ATOM   11168 C  CD2 . TRP D  1 281 ? 44.455  -9.546  114.042 1.00 9.77   ? 368  TRP D CD2 1 
ATOM   11169 N  NE1 . TRP D  1 281 ? 45.349  -11.582 113.672 1.00 9.15   ? 368  TRP D NE1 1 
ATOM   11170 C  CE2 . TRP D  1 281 ? 45.658  -10.245 113.753 1.00 11.49  ? 368  TRP D CE2 1 
ATOM   11171 C  CE3 . TRP D  1 281 ? 44.495  -8.145  114.179 1.00 9.93   ? 368  TRP D CE3 1 
ATOM   11172 C  CZ2 . TRP D  1 281 ? 46.893  -9.592  113.593 1.00 10.79  ? 368  TRP D CZ2 1 
ATOM   11173 C  CZ3 . TRP D  1 281 ? 45.736  -7.492  114.012 1.00 10.95  ? 368  TRP D CZ3 1 
ATOM   11174 C  CH2 . TRP D  1 281 ? 46.914  -8.222  113.728 1.00 10.16  ? 368  TRP D CH2 1 
ATOM   11175 N  N   . LEU D  1 282 ? 40.140  -8.447  116.531 1.00 11.41  ? 369  LEU D N   1 
ATOM   11176 C  CA  . LEU D  1 282 ? 38.941  -7.628  116.703 1.00 12.12  ? 369  LEU D CA  1 
ATOM   11177 C  C   . LEU D  1 282 ? 39.074  -6.347  115.887 1.00 11.56  ? 369  LEU D C   1 
ATOM   11178 O  O   . LEU D  1 282 ? 40.079  -5.646  115.998 1.00 12.81  ? 369  LEU D O   1 
ATOM   11179 C  CB  . LEU D  1 282 ? 38.753  -7.235  118.175 1.00 11.92  ? 369  LEU D CB  1 
ATOM   11180 C  CG  . LEU D  1 282 ? 38.926  -8.306  119.250 1.00 13.99  ? 369  LEU D CG  1 
ATOM   11181 C  CD1 . LEU D  1 282 ? 38.510  -7.778  120.624 1.00 12.26  ? 369  LEU D CD1 1 
ATOM   11182 C  CD2 . LEU D  1 282 ? 38.214  -9.622  118.952 1.00 14.24  ? 369  LEU D CD2 1 
ATOM   11183 N  N   . GLY D  1 283 ? 38.076  -6.058  115.062 1.00 10.86  ? 370  GLY D N   1 
ATOM   11184 C  CA  . GLY D  1 283 ? 38.012  -4.754  114.386 1.00 10.50  ? 370  GLY D CA  1 
ATOM   11185 C  C   . GLY D  1 283 ? 37.237  -3.786  115.267 1.00 10.44  ? 370  GLY D C   1 
ATOM   11186 O  O   . GLY D  1 283 ? 36.336  -4.200  116.023 1.00 10.94  ? 370  GLY D O   1 
ATOM   11187 N  N   . ARG D  1 284 ? 37.568  -2.502  115.179 1.00 10.22  ? 371  ARG D N   1 
ATOM   11188 C  CA  . ARG D  1 284 ? 36.710  -1.455  115.761 1.00 10.47  ? 371  ARG D CA  1 
ATOM   11189 C  C   . ARG D  1 284 ? 37.018  -0.084  115.165 1.00 10.26  ? 371  ARG D C   1 
ATOM   11190 O  O   . ARG D  1 284 ? 38.115  0.114   114.616 1.00 10.65  ? 371  ARG D O   1 
ATOM   11191 C  CB  . ARG D  1 284 ? 36.862  -1.422  117.286 1.00 9.43   ? 371  ARG D CB  1 
ATOM   11192 C  CG  . ARG D  1 284 ? 38.225  -1.006  117.828 1.00 10.71  ? 371  ARG D CG  1 
ATOM   11193 C  CD  . ARG D  1 284 ? 38.145  -0.936  119.354 1.00 12.21  ? 371  ARG D CD  1 
ATOM   11194 N  NE  . ARG D  1 284 ? 39.384  -0.462  119.969 1.00 14.68  ? 371  ARG D NE  1 
ATOM   11195 C  CZ  . ARG D  1 284 ? 39.642  -0.438  121.284 1.00 16.26  ? 371  ARG D CZ  1 
ATOM   11196 N  NH1 . ARG D  1 284 ? 38.751  -0.849  122.193 1.00 13.88  ? 371  ARG D NH1 1 
ATOM   11197 N  NH2 . ARG D  1 284 ? 40.823  0.017   121.699 1.00 16.80  ? 371  ARG D NH2 1 
ATOM   11198 N  N   . THR D  1 285 ? 36.066  0.848   115.251 1.00 10.03  ? 372  THR D N   1 
ATOM   11199 C  CA  . THR D  1 285 ? 36.345  2.248   114.908 1.00 10.59  ? 372  THR D CA  1 
ATOM   11200 C  C   . THR D  1 285 ? 37.418  2.756   115.892 1.00 11.00  ? 372  THR D C   1 
ATOM   11201 O  O   . THR D  1 285 ? 37.458  2.324   117.051 1.00 10.63  ? 372  THR D O   1 
ATOM   11202 C  CB  . THR D  1 285 ? 35.078  3.166   114.985 1.00 10.84  ? 372  THR D CB  1 
ATOM   11203 O  OG1 . THR D  1 285 ? 34.595  3.228   116.341 1.00 10.71  ? 372  THR D OG1 1 
ATOM   11204 C  CG2 . THR D  1 285 ? 33.956  2.649   114.085 1.00 9.25   ? 372  THR D CG2 1 
ATOM   11205 N  N   . ILE D  1 286 ? 38.296  3.646   115.438 1.00 11.03  ? 373  ILE D N   1 
ATOM   11206 C  CA  . ILE D  1 286 ? 39.316  4.213   116.355 1.00 12.03  ? 373  ILE D CA  1 
ATOM   11207 C  C   . ILE D  1 286 ? 38.635  5.118   117.395 1.00 12.27  ? 373  ILE D C   1 
ATOM   11208 O  O   . ILE D  1 286 ? 38.934  5.044   118.600 1.00 11.86  ? 373  ILE D O   1 
ATOM   11209 C  CB  . ILE D  1 286 ? 40.454  4.937   115.592 1.00 11.65  ? 373  ILE D CB  1 
ATOM   11210 C  CG1 . ILE D  1 286 ? 41.280  3.904   114.794 1.00 13.38  ? 373  ILE D CG1 1 
ATOM   11211 C  CG2 . ILE D  1 286 ? 41.355  5.711   116.558 1.00 12.07  ? 373  ILE D CG2 1 
ATOM   11212 C  CD1 . ILE D  1 286 ? 42.248  4.508   113.785 1.00 11.48  ? 373  ILE D CD1 1 
ATOM   11213 N  N   . SER D  1 287 ? 37.686  5.933   116.938 1.00 13.03  ? 374  SER D N   1 
ATOM   11214 C  CA  . SER D  1 287 ? 36.858  6.714   117.862 1.00 13.12  ? 374  SER D CA  1 
ATOM   11215 C  C   . SER D  1 287 ? 35.945  5.833   118.716 1.00 13.56  ? 374  SER D C   1 
ATOM   11216 O  O   . SER D  1 287 ? 35.306  4.896   118.214 1.00 13.68  ? 374  SER D O   1 
ATOM   11217 C  CB  . SER D  1 287 ? 36.005  7.728   117.113 1.00 13.08  ? 374  SER D CB  1 
ATOM   11218 O  OG  . SER D  1 287 ? 35.201  8.454   118.024 1.00 12.33  ? 374  SER D OG  1 
ATOM   11219 N  N   . LYS D  1 288 ? 35.873  6.134   120.010 1.00 13.69  ? 375  LYS D N   1 
ATOM   11220 C  CA  . LYS D  1 288 ? 34.914  5.451   120.872 1.00 15.14  ? 375  LYS D CA  1 
ATOM   11221 C  C   . LYS D  1 288 ? 33.485  6.012   120.703 1.00 14.87  ? 375  LYS D C   1 
ATOM   11222 O  O   . LYS D  1 288 ? 32.515  5.350   121.068 1.00 13.91  ? 375  LYS D O   1 
ATOM   11223 C  CB  . LYS D  1 288 ? 35.363  5.465   122.352 1.00 14.88  ? 375  LYS D CB  1 
ATOM   11224 C  CG  . LYS D  1 288 ? 35.311  6.816   123.039 1.00 17.78  ? 375  LYS D CG  1 
ATOM   11225 C  CD  . LYS D  1 288 ? 35.824  6.744   124.488 1.00 19.48  ? 375  LYS D CD  1 
ATOM   11226 C  CE  . LYS D  1 288 ? 35.387  8.001   125.282 1.00 25.62  ? 375  LYS D CE  1 
ATOM   11227 N  NZ  . LYS D  1 288 ? 35.690  7.922   126.752 1.00 28.71  ? 375  LYS D NZ  1 
ATOM   11228 N  N   . ASP D  1 289 ? 33.367  7.227   120.156 1.00 14.96  ? 376  ASP D N   1 
ATOM   11229 C  CA  . ASP D  1 289 ? 32.065  7.918   120.013 1.00 15.64  ? 376  ASP D CA  1 
ATOM   11230 C  C   . ASP D  1 289 ? 31.450  7.869   118.610 1.00 15.04  ? 376  ASP D C   1 
ATOM   11231 O  O   . ASP D  1 289 ? 30.224  7.787   118.464 1.00 15.95  ? 376  ASP D O   1 
ATOM   11232 C  CB  . ASP D  1 289 ? 32.208  9.399   120.367 1.00 16.15  ? 376  ASP D CB  1 
ATOM   11233 C  CG  . ASP D  1 289 ? 32.914  9.638   121.704 1.00 20.43  ? 376  ASP D CG  1 
ATOM   11234 O  OD1 . ASP D  1 289 ? 32.785  8.837   122.661 1.00 20.74  ? 376  ASP D OD1 1 
ATOM   11235 O  OD2 . ASP D  1 289 ? 33.613  10.673  121.776 1.00 26.87  ? 376  ASP D OD2 1 
ATOM   11236 N  N   . SER D  1 290 ? 32.301  7.989   117.592 1.00 14.75  ? 377  SER D N   1 
ATOM   11237 C  CA  . SER D  1 290 ? 31.857  8.191   116.218 1.00 14.18  ? 377  SER D CA  1 
ATOM   11238 C  C   . SER D  1 290 ? 32.393  7.101   115.301 1.00 13.16  ? 377  SER D C   1 
ATOM   11239 O  O   . SER D  1 290 ? 33.368  6.419   115.620 1.00 11.92  ? 377  SER D O   1 
ATOM   11240 C  CB  . SER D  1 290 ? 32.349  9.542   115.674 1.00 14.47  ? 377  SER D CB  1 
ATOM   11241 O  OG  . SER D  1 290 ? 31.941  10.608  116.523 1.00 18.48  ? 377  SER D OG  1 
ATOM   11242 N  N   . ARG D  1 291 ? 31.747  6.985   114.141 1.00 12.48  ? 378  ARG D N   1 
ATOM   11243 C  CA  . ARG D  1 291 ? 32.153  6.054   113.089 1.00 12.13  ? 378  ARG D CA  1 
ATOM   11244 C  C   . ARG D  1 291 ? 33.300  6.663   112.293 1.00 12.35  ? 378  ARG D C   1 
ATOM   11245 O  O   . ARG D  1 291 ? 33.161  6.985   111.104 1.00 13.20  ? 378  ARG D O   1 
ATOM   11246 C  CB  . ARG D  1 291 ? 30.946  5.701   112.206 1.00 11.92  ? 378  ARG D CB  1 
ATOM   11247 C  CG  . ARG D  1 291 ? 29.917  4.852   112.936 1.00 9.89   ? 378  ARG D CG  1 
ATOM   11248 C  CD  . ARG D  1 291 ? 28.574  4.846   112.192 1.00 10.37  ? 378  ARG D CD  1 
ATOM   11249 N  NE  . ARG D  1 291 ? 27.591  4.052   112.929 1.00 12.28  ? 378  ARG D NE  1 
ATOM   11250 C  CZ  . ARG D  1 291 ? 26.411  3.675   112.457 1.00 9.92   ? 378  ARG D CZ  1 
ATOM   11251 N  NH1 . ARG D  1 291 ? 26.047  4.013   111.213 1.00 11.40  ? 378  ARG D NH1 1 
ATOM   11252 N  NH2 . ARG D  1 291 ? 25.609  2.937   113.228 1.00 7.38   ? 378  ARG D NH2 1 
ATOM   11253 N  N   . SER D  1 292 ? 34.423  6.858   112.984 1.00 12.25  ? 379  SER D N   1 
ATOM   11254 C  CA  . SER D  1 292 ? 35.653  7.378   112.388 1.00 12.42  ? 379  SER D CA  1 
ATOM   11255 C  C   . SER D  1 292 ? 36.852  6.512   112.740 1.00 11.99  ? 379  SER D C   1 
ATOM   11256 O  O   . SER D  1 292 ? 36.997  6.024   113.886 1.00 11.00  ? 379  SER D O   1 
ATOM   11257 C  CB  . SER D  1 292 ? 35.921  8.860   112.732 1.00 13.00  ? 379  SER D CB  1 
ATOM   11258 O  OG  . SER D  1 292 ? 36.247  9.020   114.100 1.00 16.65  ? 379  SER D OG  1 
ATOM   11259 N  N   . GLY D  1 293 ? 37.707  6.336   111.734 1.00 11.20  ? 380  GLY D N   1 
ATOM   11260 C  CA  . GLY D  1 293 ? 38.851  5.453   111.815 1.00 10.47  ? 380  GLY D CA  1 
ATOM   11261 C  C   . GLY D  1 293 ? 38.452  3.990   111.850 1.00 10.05  ? 380  GLY D C   1 
ATOM   11262 O  O   . GLY D  1 293 ? 37.279  3.625   112.050 1.00 9.42   ? 380  GLY D O   1 
ATOM   11263 N  N   . TYR D  1 294 ? 39.442  3.141   111.662 1.00 9.59   ? 381  TYR D N   1 
ATOM   11264 C  CA  . TYR D  1 294 ? 39.235  1.705   111.821 1.00 9.16   ? 381  TYR D CA  1 
ATOM   11265 C  C   . TYR D  1 294 ? 40.574  1.073   112.132 1.00 9.80   ? 381  TYR D C   1 
ATOM   11266 O  O   . TYR D  1 294 ? 41.577  1.426   111.511 1.00 9.38   ? 381  TYR D O   1 
ATOM   11267 C  CB  . TYR D  1 294 ? 38.564  1.058   110.593 1.00 8.88   ? 381  TYR D CB  1 
ATOM   11268 C  CG  . TYR D  1 294 ? 37.830  -0.183  111.008 1.00 8.91   ? 381  TYR D CG  1 
ATOM   11269 C  CD1 . TYR D  1 294 ? 38.482  -1.426  111.057 1.00 8.22   ? 381  TYR D CD1 1 
ATOM   11270 C  CD2 . TYR D  1 294 ? 36.490  -0.105  111.448 1.00 9.51   ? 381  TYR D CD2 1 
ATOM   11271 C  CE1 . TYR D  1 294 ? 37.807  -2.592  111.508 1.00 6.35   ? 381  TYR D CE1 1 
ATOM   11272 C  CE2 . TYR D  1 294 ? 35.813  -1.249  111.887 1.00 6.91   ? 381  TYR D CE2 1 
ATOM   11273 C  CZ  . TYR D  1 294 ? 36.473  -2.474  111.927 1.00 7.44   ? 381  TYR D CZ  1 
ATOM   11274 O  OH  . TYR D  1 294 ? 35.761  -3.556  112.372 1.00 7.94   ? 381  TYR D OH  1 
ATOM   11275 N  N   . GLU D  1 295 ? 40.588  0.193   113.136 1.00 10.25  ? 382  GLU D N   1 
ATOM   11276 C  CA  . GLU D  1 295 ? 41.812  -0.485  113.569 1.00 11.50  ? 382  GLU D CA  1 
ATOM   11277 C  C   . GLU D  1 295 ? 41.516  -1.970  113.772 1.00 11.47  ? 382  GLU D C   1 
ATOM   11278 O  O   . GLU D  1 295 ? 40.388  -2.352  114.150 1.00 11.58  ? 382  GLU D O   1 
ATOM   11279 C  CB  . GLU D  1 295 ? 42.358  0.137   114.869 1.00 11.22  ? 382  GLU D CB  1 
ATOM   11280 C  CG  . GLU D  1 295 ? 41.352  0.090   116.048 1.00 12.76  ? 382  GLU D CG  1 
ATOM   11281 C  CD  . GLU D  1 295 ? 41.833  0.814   117.304 1.00 13.42  ? 382  GLU D CD  1 
ATOM   11282 O  OE1 . GLU D  1 295 ? 43.036  1.154   117.398 1.00 14.66  ? 382  GLU D OE1 1 
ATOM   11283 O  OE2 . GLU D  1 295 ? 40.994  1.027   118.211 1.00 15.58  ? 382  GLU D OE2 1 
ATOM   11284 N  N   . MET D  1 296 ? 42.514  -2.797  113.480 1.00 10.78  ? 383  MET D N   1 
ATOM   11285 C  CA  . MET D  1 296 ? 42.479  -4.225  113.787 1.00 11.17  ? 383  MET D CA  1 
ATOM   11286 C  C   . MET D  1 296 ? 43.384  -4.455  114.995 1.00 11.79  ? 383  MET D C   1 
ATOM   11287 O  O   . MET D  1 296 ? 44.506  -3.925  115.054 1.00 12.13  ? 383  MET D O   1 
ATOM   11288 C  CB  . MET D  1 296 ? 42.943  -5.071  112.582 1.00 10.96  ? 383  MET D CB  1 
ATOM   11289 C  CG  . MET D  1 296 ? 41.995  -5.074  111.388 1.00 9.91   ? 383  MET D CG  1 
ATOM   11290 S  SD  . MET D  1 296 ? 40.300  -5.603  111.798 1.00 8.58   ? 383  MET D SD  1 
ATOM   11291 C  CE  . MET D  1 296 ? 40.555  -7.349  112.252 1.00 5.66   ? 383  MET D CE  1 
ATOM   11292 N  N   . LEU D  1 297 ? 42.884  -5.207  115.972 1.00 11.07  ? 384  LEU D N   1 
ATOM   11293 C  CA  . LEU D  1 297 ? 43.633  -5.459  117.207 1.00 11.45  ? 384  LEU D CA  1 
ATOM   11294 C  C   . LEU D  1 297 ? 43.765  -6.972  117.385 1.00 10.85  ? 384  LEU D C   1 
ATOM   11295 O  O   . LEU D  1 297 ? 42.762  -7.671  117.361 1.00 10.62  ? 384  LEU D O   1 
ATOM   11296 C  CB  . LEU D  1 297 ? 42.911  -4.805  118.411 1.00 11.00  ? 384  LEU D CB  1 
ATOM   11297 C  CG  . LEU D  1 297 ? 42.667  -3.278  118.324 1.00 13.52  ? 384  LEU D CG  1 
ATOM   11298 C  CD1 . LEU D  1 297 ? 41.730  -2.807  119.420 1.00 15.16  ? 384  LEU D CD1 1 
ATOM   11299 C  CD2 . LEU D  1 297 ? 43.962  -2.498  118.438 1.00 15.02  ? 384  LEU D CD2 1 
ATOM   11300 N  N   . LYS D  1 298 ? 44.996  -7.483  117.502 1.00 10.97  ? 385  LYS D N   1 
ATOM   11301 C  CA  . LYS D  1 298 ? 45.177  -8.921  117.762 1.00 11.62  ? 385  LYS D CA  1 
ATOM   11302 C  C   . LYS D  1 298 ? 45.064  -9.084  119.272 1.00 11.84  ? 385  LYS D C   1 
ATOM   11303 O  O   . LYS D  1 298 ? 45.872  -8.536  120.019 1.00 11.36  ? 385  LYS D O   1 
ATOM   11304 C  CB  . LYS D  1 298 ? 46.516  -9.461  117.249 1.00 12.21  ? 385  LYS D CB  1 
ATOM   11305 C  CG  . LYS D  1 298 ? 46.570  -11.008 117.185 1.00 11.70  ? 385  LYS D CG  1 
ATOM   11306 C  CD  . LYS D  1 298 ? 47.860  -11.533 116.497 1.00 12.85  ? 385  LYS D CD  1 
ATOM   11307 C  CE  . LYS D  1 298 ? 47.775  -13.028 116.260 1.00 14.55  ? 385  LYS D CE  1 
ATOM   11308 N  NZ  . LYS D  1 298 ? 49.041  -13.571 115.704 1.00 14.88  ? 385  LYS D NZ  1 
ATOM   11309 N  N   . VAL D  1 299 ? 44.012  -9.764  119.707 1.00 12.67  ? 386  VAL D N   1 
ATOM   11310 C  CA  . VAL D  1 299 ? 43.783  -10.000 121.146 1.00 13.47  ? 386  VAL D CA  1 
ATOM   11311 C  C   . VAL D  1 299 ? 43.576  -11.470 121.424 1.00 13.37  ? 386  VAL D C   1 
ATOM   11312 O  O   . VAL D  1 299 ? 42.484  -12.010 121.229 1.00 13.28  ? 386  VAL D O   1 
ATOM   11313 C  CB  . VAL D  1 299 ? 42.793  -8.963  121.838 1.00 15.04  ? 386  VAL D CB  1 
ATOM   11314 C  CG1 . VAL D  1 299 ? 42.167  -7.956  120.860 1.00 15.17  ? 386  VAL D CG1 1 
ATOM   11315 C  CG2 . VAL D  1 299 ? 41.819  -9.559  122.874 1.00 13.18  ? 386  VAL D CG2 1 
ATOM   11316 N  N   . PRO D  1 300 ? 44.676  -12.150 121.801 1.00 13.32  ? 387  PRO D N   1 
ATOM   11317 C  CA  . PRO D  1 300 ? 44.626  -13.590 122.034 1.00 13.40  ? 387  PRO D CA  1 
ATOM   11318 C  C   . PRO D  1 300 ? 43.562  -13.911 123.083 1.00 13.30  ? 387  PRO D C   1 
ATOM   11319 O  O   . PRO D  1 300 ? 43.417  -13.176 124.079 1.00 12.31  ? 387  PRO D O   1 
ATOM   11320 C  CB  . PRO D  1 300 ? 46.044  -13.919 122.520 1.00 14.09  ? 387  PRO D CB  1 
ATOM   11321 C  CG  . PRO D  1 300 ? 46.912  -12.814 121.896 1.00 14.15  ? 387  PRO D CG  1 
ATOM   11322 C  CD  . PRO D  1 300 ? 46.031  -11.601 122.020 1.00 14.07  ? 387  PRO D CD  1 
ATOM   11323 N  N   . ASN D  1 301 ? 42.800  -14.967 122.807 1.00 13.43  ? 388  ASN D N   1 
ATOM   11324 C  CA  . ASN D  1 301 ? 41.741  -15.456 123.681 1.00 13.97  ? 388  ASN D CA  1 
ATOM   11325 C  C   . ASN D  1 301 ? 40.661  -14.428 123.974 1.00 13.89  ? 388  ASN D C   1 
ATOM   11326 O  O   . ASN D  1 301 ? 40.017  -14.479 125.024 1.00 13.62  ? 388  ASN D O   1 
ATOM   11327 C  CB  . ASN D  1 301 ? 42.332  -16.053 124.958 1.00 13.62  ? 388  ASN D CB  1 
ATOM   11328 C  CG  . ASN D  1 301 ? 43.387  -17.095 124.653 1.00 14.74  ? 388  ASN D CG  1 
ATOM   11329 O  OD1 . ASN D  1 301 ? 43.131  -18.043 123.917 1.00 15.18  ? 388  ASN D OD1 1 
ATOM   11330 N  ND2 . ASN D  1 301 ? 44.575  -16.924 125.215 1.00 16.03  ? 388  ASN D ND2 1 
ATOM   11331 N  N   . ALA D  1 302 ? 40.446  -13.506 123.029 1.00 13.73  ? 389  ALA D N   1 
ATOM   11332 C  CA  . ALA D  1 302 ? 39.362  -12.510 123.165 1.00 13.77  ? 389  ALA D CA  1 
ATOM   11333 C  C   . ALA D  1 302 ? 38.002  -13.152 123.467 1.00 13.97  ? 389  ALA D C   1 
ATOM   11334 O  O   . ALA D  1 302 ? 37.190  -12.584 124.201 1.00 14.14  ? 389  ALA D O   1 
ATOM   11335 C  CB  . ALA D  1 302 ? 39.249  -11.646 121.915 1.00 13.63  ? 389  ALA D CB  1 
ATOM   11336 N  N   . GLU D  1 303 ? 37.757  -14.318 122.882 1.00 14.29  ? 390  GLU D N   1 
ATOM   11337 C  CA  . GLU D  1 303 ? 36.481  -15.007 123.041 1.00 15.47  ? 390  GLU D CA  1 
ATOM   11338 C  C   . GLU D  1 303 ? 36.247  -15.578 124.442 1.00 16.18  ? 390  GLU D C   1 
ATOM   11339 O  O   . GLU D  1 303 ? 35.099  -15.800 124.829 1.00 17.32  ? 390  GLU D O   1 
ATOM   11340 C  CB  . GLU D  1 303 ? 36.332  -16.142 122.024 1.00 15.14  ? 390  GLU D CB  1 
ATOM   11341 C  CG  . GLU D  1 303 ? 34.917  -16.658 121.972 1.00 16.46  ? 390  GLU D CG  1 
ATOM   11342 C  CD  . GLU D  1 303 ? 34.685  -17.712 120.913 1.00 18.64  ? 390  GLU D CD  1 
ATOM   11343 O  OE1 . GLU D  1 303 ? 33.501  -18.030 120.682 1.00 19.39  ? 390  GLU D OE1 1 
ATOM   11344 O  OE2 . GLU D  1 303 ? 35.663  -18.215 120.307 1.00 21.86  ? 390  GLU D OE2 1 
ATOM   11345 N  N   . THR D  1 304 ? 37.323  -15.848 125.180 1.00 16.42  ? 391  THR D N   1 
ATOM   11346 C  CA  . THR D  1 304 ? 37.220  -16.591 126.435 1.00 16.93  ? 391  THR D CA  1 
ATOM   11347 C  C   . THR D  1 304 ? 37.788  -15.893 127.679 1.00 17.00  ? 391  THR D C   1 
ATOM   11348 O  O   . THR D  1 304 ? 37.412  -16.245 128.812 1.00 16.92  ? 391  THR D O   1 
ATOM   11349 C  CB  . THR D  1 304 ? 37.913  -17.978 126.294 1.00 16.70  ? 391  THR D CB  1 
ATOM   11350 O  OG1 . THR D  1 304 ? 39.301  -17.786 125.984 1.00 18.07  ? 391  THR D OG1 1 
ATOM   11351 C  CG2 . THR D  1 304 ? 37.259  -18.792 125.208 1.00 17.03  ? 391  THR D CG2 1 
ATOM   11352 N  N   . ASP D  1 305 ? 38.682  -14.925 127.477 1.00 17.10  ? 392  ASP D N   1 
ATOM   11353 C  CA  . ASP D  1 305 ? 39.443  -14.303 128.572 1.00 17.38  ? 392  ASP D CA  1 
ATOM   11354 C  C   . ASP D  1 305 ? 39.024  -12.842 128.807 1.00 16.82  ? 392  ASP D C   1 
ATOM   11355 O  O   . ASP D  1 305 ? 39.253  -11.965 127.973 1.00 16.64  ? 392  ASP D O   1 
ATOM   11356 C  CB  . ASP D  1 305 ? 40.967  -14.429 128.289 1.00 17.79  ? 392  ASP D CB  1 
ATOM   11357 C  CG  . ASP D  1 305 ? 41.853  -13.792 129.383 1.00 20.28  ? 392  ASP D CG  1 
ATOM   11358 O  OD1 . ASP D  1 305 ? 41.349  -13.395 130.464 1.00 20.17  ? 392  ASP D OD1 1 
ATOM   11359 O  OD2 . ASP D  1 305 ? 43.078  -13.654 129.133 1.00 22.74  ? 392  ASP D OD2 1 
ATOM   11360 N  N   . ILE D  1 306 ? 38.416  -12.578 129.965 1.00 16.52  ? 393  ILE D N   1 
ATOM   11361 C  CA  . ILE D  1 306 ? 37.950  -11.227 130.304 1.00 15.58  ? 393  ILE D CA  1 
ATOM   11362 C  C   . ILE D  1 306 ? 39.083  -10.219 130.515 1.00 15.59  ? 393  ILE D C   1 
ATOM   11363 O  O   . ILE D  1 306 ? 38.863  -8.993  130.514 1.00 14.86  ? 393  ILE D O   1 
ATOM   11364 C  CB  . ILE D  1 306 ? 36.975  -11.229 131.548 1.00 15.79  ? 393  ILE D CB  1 
ATOM   11365 C  CG1 . ILE D  1 306 ? 37.701  -11.746 132.804 1.00 16.00  ? 393  ILE D CG1 1 
ATOM   11366 C  CG2 . ILE D  1 306 ? 35.705  -12.054 131.231 1.00 14.09  ? 393  ILE D CG2 1 
ATOM   11367 C  CD1 . ILE D  1 306 ? 36.895  -11.660 134.101 1.00 16.33  ? 393  ILE D CD1 1 
ATOM   11368 N  N   . GLN D  1 307 ? 40.300  -10.727 130.704 1.00 15.76  ? 394  GLN D N   1 
ATOM   11369 C  CA  . GLN D  1 307 ? 41.453  -9.855  130.865 1.00 16.84  ? 394  GLN D CA  1 
ATOM   11370 C  C   . GLN D  1 307 ? 42.258  -9.650  129.578 1.00 16.02  ? 394  GLN D C   1 
ATOM   11371 O  O   . GLN D  1 307 ? 43.207  -8.875  129.572 1.00 16.30  ? 394  GLN D O   1 
ATOM   11372 C  CB  . GLN D  1 307 ? 42.358  -10.369 131.986 1.00 17.97  ? 394  GLN D CB  1 
ATOM   11373 C  CG  . GLN D  1 307 ? 41.635  -10.423 133.337 1.00 22.71  ? 394  GLN D CG  1 
ATOM   11374 C  CD  . GLN D  1 307 ? 42.547  -10.040 134.477 1.00 29.44  ? 394  GLN D CD  1 
ATOM   11375 O  OE1 . GLN D  1 307 ? 43.465  -10.785 134.823 1.00 31.69  ? 394  GLN D OE1 1 
ATOM   11376 N  NE2 . GLN D  1 307 ? 42.311  -8.863  135.064 1.00 31.97  ? 394  GLN D NE2 1 
ATOM   11377 N  N   . SER D  1 308 ? 41.880  -10.341 128.504 1.00 15.53  ? 395  SER D N   1 
ATOM   11378 C  CA  . SER D  1 308 ? 42.620  -10.264 127.240 1.00 15.01  ? 395  SER D CA  1 
ATOM   11379 C  C   . SER D  1 308 ? 42.725  -8.834  126.671 1.00 15.15  ? 395  SER D C   1 
ATOM   11380 O  O   . SER D  1 308 ? 41.727  -8.084  126.584 1.00 15.78  ? 395  SER D O   1 
ATOM   11381 C  CB  . SER D  1 308 ? 42.063  -11.250 126.211 1.00 14.94  ? 395  SER D CB  1 
ATOM   11382 O  OG  . SER D  1 308 ? 40.716  -10.928 125.864 1.00 13.86  ? 395  SER D OG  1 
ATOM   11383 N  N   . GLY D  1 309 ? 43.951  -8.455  126.298 1.00 15.26  ? 396  GLY D N   1 
ATOM   11384 C  CA  . GLY D  1 309 ? 44.229  -7.149  125.700 1.00 14.75  ? 396  GLY D CA  1 
ATOM   11385 C  C   . GLY D  1 309 ? 44.998  -7.310  124.391 1.00 14.40  ? 396  GLY D C   1 
ATOM   11386 O  O   . GLY D  1 309 ? 45.399  -8.421  124.053 1.00 14.23  ? 396  GLY D O   1 
ATOM   11387 N  N   . PRO D  1 310 ? 45.203  -6.206  123.645 1.00 14.41  ? 397  PRO D N   1 
ATOM   11388 C  CA  . PRO D  1 310 ? 45.866  -6.277  122.325 1.00 14.09  ? 397  PRO D CA  1 
ATOM   11389 C  C   . PRO D  1 310 ? 47.360  -6.554  122.445 1.00 14.22  ? 397  PRO D C   1 
ATOM   11390 O  O   . PRO D  1 310 ? 48.005  -6.045  123.378 1.00 14.97  ? 397  PRO D O   1 
ATOM   11391 C  CB  . PRO D  1 310 ? 45.665  -4.870  121.743 1.00 14.38  ? 397  PRO D CB  1 
ATOM   11392 C  CG  . PRO D  1 310 ? 44.682  -4.184  122.653 1.00 15.18  ? 397  PRO D CG  1 
ATOM   11393 C  CD  . PRO D  1 310 ? 44.822  -4.823  123.988 1.00 13.98  ? 397  PRO D CD  1 
ATOM   11394 N  N   . ILE D  1 311 ? 47.893  -7.362  121.527 1.00 13.29  ? 398  ILE D N   1 
ATOM   11395 C  CA  . ILE D  1 311 ? 49.345  -7.563  121.414 1.00 13.70  ? 398  ILE D CA  1 
ATOM   11396 C  C   . ILE D  1 311 ? 49.912  -6.936  120.138 1.00 13.54  ? 398  ILE D C   1 
ATOM   11397 O  O   . ILE D  1 311 ? 51.125  -6.794  119.982 1.00 12.43  ? 398  ILE D O   1 
ATOM   11398 C  CB  . ILE D  1 311 ? 49.752  -9.052  121.542 1.00 13.01  ? 398  ILE D CB  1 
ATOM   11399 C  CG1 . ILE D  1 311 ? 49.204  -9.902  120.371 1.00 13.98  ? 398  ILE D CG1 1 
ATOM   11400 C  CG2 . ILE D  1 311 ? 49.298  -9.564  122.897 1.00 14.84  ? 398  ILE D CG2 1 
ATOM   11401 C  CD1 . ILE D  1 311 ? 49.769  -11.347 120.309 1.00 14.73  ? 398  ILE D CD1 1 
ATOM   11402 N  N   . SER D  1 312 ? 49.018  -6.571  119.230 1.00 13.71  ? 399  SER D N   1 
ATOM   11403 C  CA  . SER D  1 312 ? 49.426  -5.840  118.040 1.00 14.19  ? 399  SER D CA  1 
ATOM   11404 C  C   . SER D  1 312 ? 48.235  -5.101  117.453 1.00 13.79  ? 399  SER D C   1 
ATOM   11405 O  O   . SER D  1 312 ? 47.085  -5.363  117.813 1.00 12.21  ? 399  SER D O   1 
ATOM   11406 C  CB  . SER D  1 312 ? 50.097  -6.770  117.020 1.00 15.26  ? 399  SER D CB  1 
ATOM   11407 O  OG  . SER D  1 312 ? 49.153  -7.669  116.494 1.00 18.40  ? 399  SER D OG  1 
ATOM   11408 N  N   . ASN D  1 313 ? 48.526  -4.144  116.578 1.00 13.36  ? 400  ASN D N   1 
ATOM   11409 C  CA  . ASN D  1 313 ? 47.484  -3.358  115.950 1.00 14.16  ? 400  ASN D CA  1 
ATOM   11410 C  C   . ASN D  1 313 ? 47.865  -2.957  114.536 1.00 13.14  ? 400  ASN D C   1 
ATOM   11411 O  O   . ASN D  1 313 ? 49.057  -2.811  114.217 1.00 12.94  ? 400  ASN D O   1 
ATOM   11412 C  CB  . ASN D  1 313 ? 47.177  -2.104  116.776 1.00 14.54  ? 400  ASN D CB  1 
ATOM   11413 C  CG  . ASN D  1 313 ? 48.241  -1.053  116.645 1.00 18.77  ? 400  ASN D CG  1 
ATOM   11414 O  OD1 . ASN D  1 313 ? 48.054  -0.047  115.950 1.00 24.31  ? 400  ASN D OD1 1 
ATOM   11415 N  ND2 . ASN D  1 313 ? 49.379  -1.279  117.286 1.00 21.95  ? 400  ASN D ND2 1 
ATOM   11416 N  N   . GLN D  1 314 ? 46.842  -2.770  113.701 1.00 11.60  ? 401  GLN D N   1 
ATOM   11417 C  CA  . GLN D  1 314 ? 47.026  -2.217  112.365 1.00 10.85  ? 401  GLN D CA  1 
ATOM   11418 C  C   . GLN D  1 314 ? 45.920  -1.219  112.093 1.00 10.83  ? 401  GLN D C   1 
ATOM   11419 O  O   . GLN D  1 314 ? 44.730  -1.567  112.148 1.00 11.17  ? 401  GLN D O   1 
ATOM   11420 C  CB  . GLN D  1 314 ? 47.012  -3.323  111.306 1.00 10.22  ? 401  GLN D CB  1 
ATOM   11421 C  CG  . GLN D  1 314 ? 47.399  -2.841  109.885 1.00 10.32  ? 401  GLN D CG  1 
ATOM   11422 C  CD  . GLN D  1 314 ? 47.477  -3.989  108.871 1.00 10.49  ? 401  GLN D CD  1 
ATOM   11423 O  OE1 . GLN D  1 314 ? 47.787  -5.157  109.223 1.00 10.77  ? 401  GLN D OE1 1 
ATOM   11424 N  NE2 . GLN D  1 314 ? 47.193  -3.675  107.606 1.00 11.25  ? 401  GLN D NE2 1 
ATOM   11425 N  N   . VAL D  1 315 ? 46.320  0.015   111.806 1.00 10.59  ? 402  VAL D N   1 
ATOM   11426 C  CA  . VAL D  1 315 ? 45.368  1.060   111.443 1.00 10.41  ? 402  VAL D CA  1 
ATOM   11427 C  C   . VAL D  1 315 ? 44.978  0.811   109.985 1.00 10.87  ? 402  VAL D C   1 
ATOM   11428 O  O   . VAL D  1 315 ? 45.844  0.696   109.114 1.00 10.60  ? 402  VAL D O   1 
ATOM   11429 C  CB  . VAL D  1 315 ? 45.944  2.475   111.668 1.00 11.14  ? 402  VAL D CB  1 
ATOM   11430 C  CG1 . VAL D  1 315 ? 45.028  3.540   111.026 1.00 10.18  ? 402  VAL D CG1 1 
ATOM   11431 C  CG2 . VAL D  1 315 ? 46.153  2.715   113.167 1.00 10.39  ? 402  VAL D CG2 1 
ATOM   11432 N  N   . ILE D  1 316 ? 43.671  0.695   109.750 1.00 10.08  ? 403  ILE D N   1 
ATOM   11433 C  CA  . ILE D  1 316 ? 43.129  0.429   108.408 1.00 10.34  ? 403  ILE D CA  1 
ATOM   11434 C  C   . ILE D  1 316 ? 42.640  1.731   107.784 1.00 10.33  ? 403  ILE D C   1 
ATOM   11435 O  O   . ILE D  1 316 ? 42.793  1.951   106.575 1.00 10.13  ? 403  ILE D O   1 
ATOM   11436 C  CB  . ILE D  1 316 ? 41.965  -0.599  108.480 1.00 9.70   ? 403  ILE D CB  1 
ATOM   11437 C  CG1 . ILE D  1 316 ? 42.397  -1.836  109.281 1.00 9.88   ? 403  ILE D CG1 1 
ATOM   11438 C  CG2 . ILE D  1 316 ? 41.433  -0.975  107.066 1.00 8.92   ? 403  ILE D CG2 1 
ATOM   11439 C  CD1 . ILE D  1 316 ? 43.590  -2.638  108.650 1.00 9.81   ? 403  ILE D CD1 1 
ATOM   11440 N  N   . VAL D  1 317 ? 42.043  2.579   108.622 1.00 10.55  ? 404  VAL D N   1 
ATOM   11441 C  CA  . VAL D  1 317 ? 41.572  3.906   108.214 1.00 10.75  ? 404  VAL D CA  1 
ATOM   11442 C  C   . VAL D  1 317 ? 41.973  4.859   109.339 1.00 11.93  ? 404  VAL D C   1 
ATOM   11443 O  O   . VAL D  1 317 ? 41.581  4.643   110.484 1.00 12.34  ? 404  VAL D O   1 
ATOM   11444 C  CB  . VAL D  1 317 ? 40.029  3.948   108.062 1.00 10.23  ? 404  VAL D CB  1 
ATOM   11445 C  CG1 . VAL D  1 317 ? 39.568  5.376   107.694 1.00 10.63  ? 404  VAL D CG1 1 
ATOM   11446 C  CG2 . VAL D  1 317 ? 39.546  2.920   107.026 1.00 9.98   ? 404  VAL D CG2 1 
ATOM   11447 N  N   . ASN D  1 318 ? 42.747  5.907   109.049 1.00 12.71  ? 405  ASN D N   1 
ATOM   11448 C  CA  . ASN D  1 318 ? 43.147  6.788   110.149 1.00 13.96  ? 405  ASN D CA  1 
ATOM   11449 C  C   . ASN D  1 318 ? 41.952  7.539   110.803 1.00 13.61  ? 405  ASN D C   1 
ATOM   11450 O  O   . ASN D  1 318 ? 40.858  7.644   110.218 1.00 12.94  ? 405  ASN D O   1 
ATOM   11451 C  CB  . ASN D  1 318 ? 44.293  7.727   109.726 1.00 14.58  ? 405  ASN D CB  1 
ATOM   11452 C  CG  . ASN D  1 318 ? 43.879  8.707   108.672 1.00 16.07  ? 405  ASN D CG  1 
ATOM   11453 O  OD1 . ASN D  1 318 ? 42.773  9.272   108.723 1.00 20.27  ? 405  ASN D OD1 1 
ATOM   11454 N  ND2 . ASN D  1 318 ? 44.771  8.941   107.699 1.00 16.74  ? 405  ASN D ND2 1 
ATOM   11455 N  N   . ASN D  1 319 ? 42.154  8.060   112.013 1.00 14.27  ? 406  ASN D N   1 
ATOM   11456 C  CA  . ASN D  1 319 ? 41.037  8.656   112.764 1.00 14.94  ? 406  ASN D CA  1 
ATOM   11457 C  C   . ASN D  1 319 ? 40.583  10.041  112.277 1.00 15.43  ? 406  ASN D C   1 
ATOM   11458 O  O   . ASN D  1 319 ? 39.697  10.656  112.883 1.00 15.62  ? 406  ASN D O   1 
ATOM   11459 C  CB  . ASN D  1 319 ? 41.322  8.671   114.273 1.00 15.30  ? 406  ASN D CB  1 
ATOM   11460 C  CG  . ASN D  1 319 ? 40.043  8.859   115.122 1.00 17.05  ? 406  ASN D CG  1 
ATOM   11461 O  OD1 . ASN D  1 319 ? 40.088  9.494   116.197 1.00 22.11  ? 406  ASN D OD1 1 
ATOM   11462 N  ND2 . ASN D  1 319 ? 38.905  8.314   114.652 1.00 13.50  ? 406  ASN D ND2 1 
ATOM   11463 N  N   . GLN D  1 320 ? 41.180  10.524  111.189 1.00 14.71  ? 407  GLN D N   1 
ATOM   11464 C  CA  . GLN D  1 320 ? 40.737  11.779  110.575 1.00 15.08  ? 407  GLN D CA  1 
ATOM   11465 C  C   . GLN D  1 320 ? 39.766  11.492  109.430 1.00 14.67  ? 407  GLN D C   1 
ATOM   11466 O  O   . GLN D  1 320 ? 39.245  12.419  108.799 1.00 15.64  ? 407  GLN D O   1 
ATOM   11467 C  CB  . GLN D  1 320 ? 41.921  12.599  110.074 1.00 15.46  ? 407  GLN D CB  1 
ATOM   11468 C  CG  . GLN D  1 320 ? 42.870  13.059  111.201 1.00 19.37  ? 407  GLN D CG  1 
ATOM   11469 C  CD  . GLN D  1 320 ? 43.740  11.917  111.739 1.00 25.09  ? 407  GLN D CD  1 
ATOM   11470 O  OE1 . GLN D  1 320 ? 44.644  11.430  111.053 1.00 27.70  ? 407  GLN D OE1 1 
ATOM   11471 N  NE2 . GLN D  1 320 ? 43.461  11.483  112.973 1.00 26.69  ? 407  GLN D NE2 1 
ATOM   11472 N  N   . ASN D  1 321 ? 39.510  10.210  109.179 1.00 13.02  ? 408  ASN D N   1 
ATOM   11473 C  CA  . ASN D  1 321 ? 38.591  9.830   108.110 1.00 12.12  ? 408  ASN D CA  1 
ATOM   11474 C  C   . ASN D  1 321 ? 37.393  9.026   108.592 1.00 11.55  ? 408  ASN D C   1 
ATOM   11475 O  O   . ASN D  1 321 ? 37.487  8.315   109.575 1.00 11.22  ? 408  ASN D O   1 
ATOM   11476 C  CB  . ASN D  1 321 ? 39.357  9.054   107.046 1.00 12.15  ? 408  ASN D CB  1 
ATOM   11477 C  CG  . ASN D  1 321 ? 40.225  9.959   106.201 1.00 12.42  ? 408  ASN D CG  1 
ATOM   11478 O  OD1 . ASN D  1 321 ? 39.747  10.586  105.264 1.00 14.59  ? 408  ASN D OD1 1 
ATOM   11479 N  ND2 . ASN D  1 321 ? 41.498  10.032  106.530 1.00 14.67  ? 408  ASN D ND2 1 
ATOM   11480 N  N   . TRP D  1 322 ? 36.288  9.127   107.860 1.00 11.25  ? 409  TRP D N   1 
ATOM   11481 C  CA  . TRP D  1 322 ? 35.068  8.403   108.175 1.00 11.29  ? 409  TRP D CA  1 
ATOM   11482 C  C   . TRP D  1 322 ? 35.140  6.903   107.850 1.00 11.02  ? 409  TRP D C   1 
ATOM   11483 O  O   . TRP D  1 322 ? 35.661  6.496   106.788 1.00 11.44  ? 409  TRP D O   1 
ATOM   11484 C  CB  . TRP D  1 322 ? 33.867  9.076   107.468 1.00 11.93  ? 409  TRP D CB  1 
ATOM   11485 C  CG  . TRP D  1 322 ? 33.717  10.510  107.879 1.00 13.05  ? 409  TRP D CG  1 
ATOM   11486 C  CD1 . TRP D  1 322 ? 33.847  11.619  107.088 1.00 13.39  ? 409  TRP D CD1 1 
ATOM   11487 C  CD2 . TRP D  1 322 ? 33.477  10.987  109.206 1.00 12.96  ? 409  TRP D CD2 1 
ATOM   11488 N  NE1 . TRP D  1 322 ? 33.685  12.750  107.839 1.00 14.49  ? 409  TRP D NE1 1 
ATOM   11489 C  CE2 . TRP D  1 322 ? 33.451  12.392  109.143 1.00 14.54  ? 409  TRP D CE2 1 
ATOM   11490 C  CE3 . TRP D  1 322 ? 33.251  10.355  110.441 1.00 14.06  ? 409  TRP D CE3 1 
ATOM   11491 C  CZ2 . TRP D  1 322 ? 33.227  13.192  110.273 1.00 14.63  ? 409  TRP D CZ2 1 
ATOM   11492 C  CZ3 . TRP D  1 322 ? 33.020  11.166  111.582 1.00 13.46  ? 409  TRP D CZ3 1 
ATOM   11493 C  CH2 . TRP D  1 322 ? 33.010  12.561  111.475 1.00 13.69  ? 409  TRP D CH2 1 
ATOM   11494 N  N   . SER D  1 323 ? 34.626  6.082   108.770 1.00 10.35  ? 410  SER D N   1 
ATOM   11495 C  CA  . SER D  1 323 ? 34.377  4.665   108.482 1.00 9.96   ? 410  SER D CA  1 
ATOM   11496 C  C   . SER D  1 323 ? 32.879  4.363   108.441 1.00 9.32   ? 410  SER D C   1 
ATOM   11497 O  O   . SER D  1 323 ? 32.123  5.085   107.776 1.00 9.26   ? 410  SER D O   1 
ATOM   11498 C  CB  . SER D  1 323 ? 35.130  3.726   109.443 1.00 10.08  ? 410  SER D CB  1 
ATOM   11499 O  OG  . SER D  1 323 ? 34.847  4.014   110.805 1.00 9.20   ? 410  SER D OG  1 
ATOM   11500 N  N   . GLY D  1 324 ? 32.449  3.311   109.131 1.00 9.10   ? 411  GLY D N   1 
ATOM   11501 C  CA  . GLY D  1 324 ? 31.061  2.828   109.013 1.00 9.39   ? 411  GLY D CA  1 
ATOM   11502 C  C   . GLY D  1 324 ? 30.955  1.362   109.403 1.00 8.61   ? 411  GLY D C   1 
ATOM   11503 O  O   . GLY D  1 324 ? 31.706  0.898   110.243 1.00 8.25   ? 411  GLY D O   1 
ATOM   11504 N  N   . TYR D  1 325 ? 29.997  0.648   108.818 1.00 8.38   ? 412  TYR D N   1 
ATOM   11505 C  CA  . TYR D  1 325 ? 29.871  -0.813  109.029 1.00 8.31   ? 412  TYR D CA  1 
ATOM   11506 C  C   . TYR D  1 325 ? 31.148  -1.540  108.638 1.00 8.58   ? 412  TYR D C   1 
ATOM   11507 O  O   . TYR D  1 325 ? 31.905  -1.069  107.764 1.00 9.23   ? 412  TYR D O   1 
ATOM   11508 C  CB  . TYR D  1 325 ? 28.678  -1.357  108.212 1.00 8.19   ? 412  TYR D CB  1 
ATOM   11509 C  CG  . TYR D  1 325 ? 27.328  -1.022  108.828 1.00 8.48   ? 412  TYR D CG  1 
ATOM   11510 C  CD1 . TYR D  1 325 ? 27.216  -0.069  109.854 1.00 7.22   ? 412  TYR D CD1 1 
ATOM   11511 C  CD2 . TYR D  1 325 ? 26.155  -1.649  108.370 1.00 8.56   ? 412  TYR D CD2 1 
ATOM   11512 C  CE1 . TYR D  1 325 ? 25.970  0.213   110.452 1.00 9.95   ? 412  TYR D CE1 1 
ATOM   11513 C  CE2 . TYR D  1 325 ? 24.903  -1.359  108.950 1.00 9.78   ? 412  TYR D CE2 1 
ATOM   11514 C  CZ  . TYR D  1 325 ? 24.830  -0.436  109.985 1.00 9.96   ? 412  TYR D CZ  1 
ATOM   11515 O  OH  . TYR D  1 325 ? 23.613  -0.145  110.546 1.00 10.30  ? 412  TYR D OH  1 
ATOM   11516 N  N   . SER D  1 326 ? 31.372  -2.685  109.276 1.00 8.12   ? 413  SER D N   1 
ATOM   11517 C  CA  . SER D  1 326 ? 32.426  -3.616  108.885 1.00 8.89   ? 413  SER D CA  1 
ATOM   11518 C  C   . SER D  1 326 ? 31.922  -5.025  109.076 1.00 8.63   ? 413  SER D C   1 
ATOM   11519 O  O   . SER D  1 326 ? 31.040  -5.271  109.907 1.00 8.51   ? 413  SER D O   1 
ATOM   11520 C  CB  . SER D  1 326 ? 33.724  -3.382  109.698 1.00 8.43   ? 413  SER D CB  1 
ATOM   11521 O  OG  . SER D  1 326 ? 33.507  -3.373  111.114 1.00 8.98   ? 413  SER D OG  1 
ATOM   11522 N  N   . GLY D  1 327 ? 32.483  -5.961  108.324 1.00 8.74   ? 414  GLY D N   1 
ATOM   11523 C  CA  . GLY D  1 327 ? 31.995  -7.328  108.400 1.00 8.89   ? 414  GLY D CA  1 
ATOM   11524 C  C   . GLY D  1 327 ? 32.990  -8.339  107.863 1.00 8.41   ? 414  GLY D C   1 
ATOM   11525 O  O   . GLY D  1 327 ? 33.970  -7.981  107.196 1.00 8.42   ? 414  GLY D O   1 
ATOM   11526 N  N   . ALA D  1 328 ? 32.703  -9.604  108.151 1.00 8.68   ? 415  ALA D N   1 
ATOM   11527 C  CA  . ALA D  1 328 ? 33.551  -10.743 107.787 1.00 8.49   ? 415  ALA D CA  1 
ATOM   11528 C  C   . ALA D  1 328 ? 33.117  -11.388 106.481 1.00 8.19   ? 415  ALA D C   1 
ATOM   11529 O  O   . ALA D  1 328 ? 31.919  -11.474 106.193 1.00 8.08   ? 415  ALA D O   1 
ATOM   11530 C  CB  . ALA D  1 328 ? 33.525  -11.802 108.905 1.00 8.24   ? 415  ALA D CB  1 
ATOM   11531 N  N   . PHE D  1 329 ? 34.102  -11.840 105.709 1.00 8.58   ? 416  PHE D N   1 
ATOM   11532 C  CA  . PHE D  1 329 ? 33.894  -12.839 104.640 1.00 8.71   ? 416  PHE D CA  1 
ATOM   11533 C  C   . PHE D  1 329 ? 35.144  -13.698 104.471 1.00 9.02   ? 416  PHE D C   1 
ATOM   11534 O  O   . PHE D  1 329 ? 36.220  -13.343 104.957 1.00 9.75   ? 416  PHE D O   1 
ATOM   11535 C  CB  . PHE D  1 329 ? 33.477  -12.191 103.297 1.00 8.66   ? 416  PHE D CB  1 
ATOM   11536 C  CG  . PHE D  1 329 ? 34.554  -11.334 102.660 1.00 9.10   ? 416  PHE D CG  1 
ATOM   11537 C  CD1 . PHE D  1 329 ? 34.817  -10.043 103.139 1.00 8.54   ? 416  PHE D CD1 1 
ATOM   11538 C  CD2 . PHE D  1 329 ? 35.313  -11.821 101.577 1.00 9.00   ? 416  PHE D CD2 1 
ATOM   11539 C  CE1 . PHE D  1 329 ? 35.819  -9.234  102.548 1.00 7.70   ? 416  PHE D CE1 1 
ATOM   11540 C  CE2 . PHE D  1 329 ? 36.327  -11.031 100.990 1.00 8.90   ? 416  PHE D CE2 1 
ATOM   11541 C  CZ  . PHE D  1 329 ? 36.572  -9.727  101.477 1.00 8.54   ? 416  PHE D CZ  1 
ATOM   11542 N  N   . ILE D  1 330 ? 35.007  -14.832 103.779 1.00 8.60   ? 417  ILE D N   1 
ATOM   11543 C  CA  . ILE D  1 330 ? 36.175  -15.674 103.471 1.00 8.59   ? 417  ILE D CA  1 
ATOM   11544 C  C   . ILE D  1 330 ? 36.036  -16.233 102.051 1.00 8.62   ? 417  ILE D C   1 
ATOM   11545 O  O   . ILE D  1 330 ? 34.937  -16.577 101.608 1.00 8.47   ? 417  ILE D O   1 
ATOM   11546 C  CB  . ILE D  1 330 ? 36.348  -16.822 104.527 1.00 8.85   ? 417  ILE D CB  1 
ATOM   11547 C  CG1 . ILE D  1 330 ? 36.647  -16.240 105.925 1.00 8.00   ? 417  ILE D CG1 1 
ATOM   11548 C  CG2 . ILE D  1 330 ? 37.407  -17.862 104.081 1.00 7.14   ? 417  ILE D CG2 1 
ATOM   11549 C  CD1 . ILE D  1 330 ? 36.952  -17.276 107.016 1.00 8.52   ? 417  ILE D CD1 1 
ATOM   11550 N  N   . ASP D  1 331 ? 37.143  -16.290 101.326 1.00 8.94   ? 418  ASP D N   1 
ATOM   11551 C  CA  . ASP D  1 331 ? 37.154  -17.016 100.087 1.00 9.61   ? 418  ASP D CA  1 
ATOM   11552 C  C   . ASP D  1 331 ? 37.333  -18.500 100.447 1.00 9.40   ? 418  ASP D C   1 
ATOM   11553 O  O   . ASP D  1 331 ? 38.461  -19.021 100.485 1.00 9.15   ? 418  ASP D O   1 
ATOM   11554 C  CB  . ASP D  1 331 ? 38.273  -16.547 99.161  1.00 9.86   ? 418  ASP D CB  1 
ATOM   11555 C  CG  . ASP D  1 331 ? 38.283  -17.300 97.829  1.00 11.44  ? 418  ASP D CG  1 
ATOM   11556 O  OD1 . ASP D  1 331 ? 37.348  -18.088 97.570  1.00 11.58  ? 418  ASP D OD1 1 
ATOM   11557 O  OD2 . ASP D  1 331 ? 39.226  -17.080 97.039  1.00 12.42  ? 418  ASP D OD2 1 
ATOM   11558 N  N   . TYR D  1 332 ? 36.208  -19.173 100.684 1.00 9.26   ? 419  TYR D N   1 
ATOM   11559 C  CA  . TYR D  1 332 ? 36.200  -20.590 101.081 1.00 9.83   ? 419  TYR D CA  1 
ATOM   11560 C  C   . TYR D  1 332 ? 36.677  -21.528 99.959  1.00 10.71  ? 419  TYR D C   1 
ATOM   11561 O  O   . TYR D  1 332 ? 36.936  -22.708 100.195 1.00 11.72  ? 419  TYR D O   1 
ATOM   11562 C  CB  . TYR D  1 332 ? 34.806  -20.999 101.589 1.00 9.08   ? 419  TYR D CB  1 
ATOM   11563 C  CG  . TYR D  1 332 ? 34.392  -20.275 102.859 1.00 10.43  ? 419  TYR D CG  1 
ATOM   11564 C  CD1 . TYR D  1 332 ? 34.930  -20.640 104.106 1.00 10.30  ? 419  TYR D CD1 1 
ATOM   11565 C  CD2 . TYR D  1 332 ? 33.444  -19.234 102.815 1.00 9.42   ? 419  TYR D CD2 1 
ATOM   11566 C  CE1 . TYR D  1 332 ? 34.557  -19.973 105.273 1.00 11.15  ? 419  TYR D CE1 1 
ATOM   11567 C  CE2 . TYR D  1 332 ? 33.074  -18.560 103.970 1.00 9.47   ? 419  TYR D CE2 1 
ATOM   11568 C  CZ  . TYR D  1 332 ? 33.630  -18.931 105.186 1.00 10.32  ? 419  TYR D CZ  1 
ATOM   11569 O  OH  . TYR D  1 332 ? 33.255  -18.261 106.320 1.00 8.58   ? 419  TYR D OH  1 
ATOM   11570 N  N   . TRP D  1 333 ? 36.811  -20.993 98.750  1.00 11.82  ? 420  TRP D N   1 
ATOM   11571 C  CA  . TRP D  1 333 ? 37.212  -21.799 97.577  1.00 12.31  ? 420  TRP D CA  1 
ATOM   11572 C  C   . TRP D  1 333 ? 38.656  -21.525 97.139  1.00 12.93  ? 420  TRP D C   1 
ATOM   11573 O  O   . TRP D  1 333 ? 39.090  -21.937 96.047  1.00 13.33  ? 420  TRP D O   1 
ATOM   11574 C  CB  . TRP D  1 333 ? 36.208  -21.571 96.440  1.00 12.71  ? 420  TRP D CB  1 
ATOM   11575 C  CG  . TRP D  1 333 ? 34.833  -21.989 96.868  1.00 12.21  ? 420  TRP D CG  1 
ATOM   11576 C  CD1 . TRP D  1 333 ? 34.273  -23.232 96.764  1.00 13.48  ? 420  TRP D CD1 1 
ATOM   11577 C  CD2 . TRP D  1 333 ? 33.869  -21.164 97.534  1.00 12.44  ? 420  TRP D CD2 1 
ATOM   11578 N  NE1 . TRP D  1 333 ? 32.996  -23.226 97.312  1.00 13.36  ? 420  TRP D NE1 1 
ATOM   11579 C  CE2 . TRP D  1 333 ? 32.731  -21.966 97.786  1.00 13.63  ? 420  TRP D CE2 1 
ATOM   11580 C  CE3 . TRP D  1 333 ? 33.852  -19.808 97.927  1.00 10.39  ? 420  TRP D CE3 1 
ATOM   11581 C  CZ2 . TRP D  1 333 ? 31.581  -21.461 98.419  1.00 12.63  ? 420  TRP D CZ2 1 
ATOM   11582 C  CZ3 . TRP D  1 333 ? 32.723  -19.318 98.565  1.00 12.16  ? 420  TRP D CZ3 1 
ATOM   11583 C  CH2 . TRP D  1 333 ? 31.600  -20.146 98.801  1.00 12.41  ? 420  TRP D CH2 1 
ATOM   11584 N  N   . ALA D  1 334 ? 39.412  -20.839 97.990  1.00 13.13  ? 421  ALA D N   1 
ATOM   11585 C  CA  . ALA D  1 334 ? 40.822  -20.580 97.692  1.00 13.87  ? 421  ALA D CA  1 
ATOM   11586 C  C   . ALA D  1 334 ? 41.628  -21.896 97.684  1.00 14.87  ? 421  ALA D C   1 
ATOM   11587 O  O   . ALA D  1 334 ? 41.289  -22.866 98.382  1.00 13.24  ? 421  ALA D O   1 
ATOM   11588 C  CB  . ALA D  1 334 ? 41.407  -19.611 98.694  1.00 13.57  ? 421  ALA D CB  1 
ATOM   11589 N  N   . ASN D  1 335 ? 42.708  -21.908 96.912  1.00 16.55  ? 422  ASN D N   1 
ATOM   11590 C  CA  . ASN D  1 335 ? 43.612  -23.061 96.886  1.00 18.31  ? 422  ASN D CA  1 
ATOM   11591 C  C   . ASN D  1 335 ? 44.603  -22.960 98.044  1.00 19.00  ? 422  ASN D C   1 
ATOM   11592 O  O   . ASN D  1 335 ? 45.781  -22.651 97.846  1.00 20.05  ? 422  ASN D O   1 
ATOM   11593 C  CB  . ASN D  1 335 ? 44.309  -23.133 95.517  1.00 18.72  ? 422  ASN D CB  1 
ATOM   11594 C  CG  . ASN D  1 335 ? 45.275  -24.309 95.396  1.00 22.08  ? 422  ASN D CG  1 
ATOM   11595 O  OD1 . ASN D  1 335 ? 46.325  -24.197 94.748  1.00 26.52  ? 422  ASN D OD1 1 
ATOM   11596 N  ND2 . ASN D  1 335 ? 44.939  -25.428 96.021  1.00 21.21  ? 422  ASN D ND2 1 
ATOM   11597 N  N   . LYS D  1 336 ? 44.100  -23.186 99.255  1.00 19.75  ? 423  LYS D N   1 
ATOM   11598 C  CA  . LYS D  1 336 ? 44.876  -23.087 100.493 1.00 20.36  ? 423  LYS D CA  1 
ATOM   11599 C  C   . LYS D  1 336 ? 44.432  -24.169 101.477 1.00 19.79  ? 423  LYS D C   1 
ATOM   11600 O  O   . LYS D  1 336 ? 43.277  -24.593 101.452 1.00 19.79  ? 423  LYS D O   1 
ATOM   11601 C  CB  . LYS D  1 336 ? 44.661  -21.720 101.162 1.00 20.78  ? 423  LYS D CB  1 
ATOM   11602 C  CG  . LYS D  1 336 ? 45.440  -20.541 100.627 1.00 23.84  ? 423  LYS D CG  1 
ATOM   11603 C  CD  . LYS D  1 336 ? 45.304  -19.387 101.641 1.00 27.22  ? 423  LYS D CD  1 
ATOM   11604 C  CE  . LYS D  1 336 ? 45.998  -18.082 101.225 1.00 29.52  ? 423  LYS D CE  1 
ATOM   11605 N  NZ  . LYS D  1 336 ? 45.589  -17.543 99.875  1.00 30.60  ? 423  LYS D NZ  1 
ATOM   11606 N  N   . GLU D  1 337 ? 45.352  -24.567 102.358 1.00 18.89  ? 424  GLU D N   1 
ATOM   11607 C  CA  . GLU D  1 337 ? 45.153  -25.536 103.454 1.00 19.17  ? 424  GLU D CA  1 
ATOM   11608 C  C   . GLU D  1 337 ? 44.205  -25.033 104.544 1.00 16.85  ? 424  GLU D C   1 
ATOM   11609 O  O   . GLU D  1 337 ? 43.680  -25.808 105.362 1.00 16.24  ? 424  GLU D O   1 
ATOM   11610 C  CB  . GLU D  1 337 ? 46.541  -25.838 104.094 1.00 20.07  ? 424  GLU D CB  1 
ATOM   11611 C  CG  . GLU D  1 337 ? 46.603  -26.059 105.641 1.00 26.31  ? 424  GLU D CG  1 
ATOM   11612 C  CD  . GLU D  1 337 ? 47.032  -24.811 106.479 1.00 32.95  ? 424  GLU D CD  1 
ATOM   11613 O  OE1 . GLU D  1 337 ? 46.619  -24.732 107.674 1.00 33.51  ? 424  GLU D OE1 1 
ATOM   11614 O  OE2 . GLU D  1 337 ? 47.785  -23.928 105.962 1.00 35.24  ? 424  GLU D OE2 1 
ATOM   11615 N  N   . CYS D  1 338 ? 44.025  -23.722 104.578 1.00 15.15  ? 425  CYS D N   1 
ATOM   11616 C  CA  . CYS D  1 338 ? 43.280  -23.093 105.644 1.00 13.81  ? 425  CYS D CA  1 
ATOM   11617 C  C   . CYS D  1 338 ? 42.347  -22.047 105.029 1.00 12.93  ? 425  CYS D C   1 
ATOM   11618 O  O   . CYS D  1 338 ? 42.573  -21.602 103.885 1.00 13.16  ? 425  CYS D O   1 
ATOM   11619 C  CB  . CYS D  1 338 ? 44.243  -22.445 106.646 1.00 13.54  ? 425  CYS D CB  1 
ATOM   11620 S  SG  . CYS D  1 338 ? 45.494  -21.331 105.944 1.00 15.29  ? 425  CYS D SG  1 
ATOM   11621 N  N   . PHE D  1 339 ? 41.325  -21.667 105.796 1.00 12.45  ? 426  PHE D N   1 
ATOM   11622 C  CA  . PHE D  1 339 ? 40.422  -20.562 105.459 1.00 11.93  ? 426  PHE D CA  1 
ATOM   11623 C  C   . PHE D  1 339 ? 41.009  -19.249 105.981 1.00 11.28  ? 426  PHE D C   1 
ATOM   11624 O  O   . PHE D  1 339 ? 41.190  -19.085 107.204 1.00 10.98  ? 426  PHE D O   1 
ATOM   11625 C  CB  . PHE D  1 339 ? 39.024  -20.772 106.097 1.00 11.71  ? 426  PHE D CB  1 
ATOM   11626 C  CG  . PHE D  1 339 ? 38.246  -21.956 105.552 1.00 12.27  ? 426  PHE D CG  1 
ATOM   11627 C  CD1 . PHE D  1 339 ? 38.320  -22.333 104.207 1.00 11.06  ? 426  PHE D CD1 1 
ATOM   11628 C  CD2 . PHE D  1 339 ? 37.389  -22.665 106.401 1.00 12.55  ? 426  PHE D CD2 1 
ATOM   11629 C  CE1 . PHE D  1 339 ? 37.573  -23.412 103.727 1.00 14.43  ? 426  PHE D CE1 1 
ATOM   11630 C  CE2 . PHE D  1 339 ? 36.640  -23.742 105.937 1.00 13.63  ? 426  PHE D CE2 1 
ATOM   11631 C  CZ  . PHE D  1 339 ? 36.728  -24.123 104.600 1.00 12.68  ? 426  PHE D CZ  1 
ATOM   11632 N  N   . ASN D  1 340 ? 41.293  -18.319 105.065 1.00 10.48  ? 427  ASN D N   1 
ATOM   11633 C  CA  . ASN D  1 340 ? 41.960  -17.064 105.401 1.00 10.08  ? 427  ASN D CA  1 
ATOM   11634 C  C   . ASN D  1 340 ? 40.923  -15.972 105.689 1.00 9.51   ? 427  ASN D C   1 
ATOM   11635 O  O   . ASN D  1 340 ? 40.134  -15.623 104.810 1.00 8.73   ? 427  ASN D O   1 
ATOM   11636 C  CB  . ASN D  1 340 ? 42.927  -16.644 104.281 1.00 10.73  ? 427  ASN D CB  1 
ATOM   11637 C  CG  . ASN D  1 340 ? 43.885  -15.532 104.703 1.00 10.50  ? 427  ASN D CG  1 
ATOM   11638 O  OD1 . ASN D  1 340 ? 44.208  -14.646 103.903 1.00 12.91  ? 427  ASN D OD1 1 
ATOM   11639 N  ND2 . ASN D  1 340 ? 44.349  -15.579 105.938 1.00 8.92   ? 427  ASN D ND2 1 
ATOM   11640 N  N   . PRO D  1 341 ? 40.903  -15.464 106.938 1.00 9.42   ? 428  PRO D N   1 
ATOM   11641 C  CA  . PRO D  1 341 ? 40.008  -14.350 107.292 1.00 9.15   ? 428  PRO D CA  1 
ATOM   11642 C  C   . PRO D  1 341 ? 40.115  -13.151 106.336 1.00 9.03   ? 428  PRO D C   1 
ATOM   11643 O  O   . PRO D  1 341 ? 41.231  -12.714 106.026 1.00 9.21   ? 428  PRO D O   1 
ATOM   11644 C  CB  . PRO D  1 341 ? 40.518  -13.927 108.671 1.00 8.06   ? 428  PRO D CB  1 
ATOM   11645 C  CG  . PRO D  1 341 ? 41.065  -15.212 109.283 1.00 9.41   ? 428  PRO D CG  1 
ATOM   11646 C  CD  . PRO D  1 341 ? 41.718  -15.904 108.096 1.00 9.61   ? 428  PRO D CD  1 
ATOM   11647 N  N   . CYS D  1 342 ? 38.965  -12.635 105.889 1.00 8.45   ? 429  CYS D N   1 
ATOM   11648 C  CA  . CYS D  1 342 ? 38.903  -11.302 105.242 1.00 7.97   ? 429  CYS D CA  1 
ATOM   11649 C  C   . CYS D  1 342 ? 37.864  -10.412 105.896 1.00 8.24   ? 429  CYS D C   1 
ATOM   11650 O  O   . CYS D  1 342 ? 36.951  -10.899 106.566 1.00 7.69   ? 429  CYS D O   1 
ATOM   11651 C  CB  . CYS D  1 342 ? 38.574  -11.384 103.748 1.00 8.08   ? 429  CYS D CB  1 
ATOM   11652 S  SG  . CYS D  1 342 ? 39.665  -12.464 102.767 1.00 9.66   ? 429  CYS D SG  1 
ATOM   11653 N  N   . PHE D  1 343 ? 37.988  -9.103  105.669 1.00 7.73   ? 430  PHE D N   1 
ATOM   11654 C  CA  . PHE D  1 343 ? 36.974  -8.156  106.140 1.00 8.15   ? 430  PHE D CA  1 
ATOM   11655 C  C   . PHE D  1 343 ? 36.872  -6.950  105.200 1.00 8.14   ? 430  PHE D C   1 
ATOM   11656 O  O   . PHE D  1 343 ? 37.780  -6.703  104.392 1.00 8.08   ? 430  PHE D O   1 
ATOM   11657 C  CB  . PHE D  1 343 ? 37.248  -7.703  107.593 1.00 8.30   ? 430  PHE D CB  1 
ATOM   11658 C  CG  . PHE D  1 343 ? 38.429  -6.781  107.753 1.00 8.37   ? 430  PHE D CG  1 
ATOM   11659 C  CD1 . PHE D  1 343 ? 38.252  -5.382  107.807 1.00 6.61   ? 430  PHE D CD1 1 
ATOM   11660 C  CD2 . PHE D  1 343 ? 39.727  -7.301  107.853 1.00 9.97   ? 430  PHE D CD2 1 
ATOM   11661 C  CE1 . PHE D  1 343 ? 39.352  -4.519  107.949 1.00 7.54   ? 430  PHE D CE1 1 
ATOM   11662 C  CE2 . PHE D  1 343 ? 40.827  -6.448  108.002 1.00 8.82   ? 430  PHE D CE2 1 
ATOM   11663 C  CZ  . PHE D  1 343 ? 40.644  -5.059  108.061 1.00 7.56   ? 430  PHE D CZ  1 
ATOM   11664 N  N   . TYR D  1 344 ? 35.771  -6.207  105.313 1.00 7.46   ? 431  TYR D N   1 
ATOM   11665 C  CA  . TYR D  1 344 ? 35.598  -4.940  104.593 1.00 7.57   ? 431  TYR D CA  1 
ATOM   11666 C  C   . TYR D  1 344 ? 35.278  -3.886  105.637 1.00 7.56   ? 431  TYR D C   1 
ATOM   11667 O  O   . TYR D  1 344 ? 34.819  -4.218  106.751 1.00 7.46   ? 431  TYR D O   1 
ATOM   11668 C  CB  . TYR D  1 344 ? 34.455  -4.992  103.548 1.00 7.60   ? 431  TYR D CB  1 
ATOM   11669 C  CG  . TYR D  1 344 ? 33.116  -5.203  104.204 1.00 6.41   ? 431  TYR D CG  1 
ATOM   11670 C  CD1 . TYR D  1 344 ? 32.652  -6.505  104.472 1.00 8.94   ? 431  TYR D CD1 1 
ATOM   11671 C  CD2 . TYR D  1 344 ? 32.347  -4.115  104.616 1.00 8.30   ? 431  TYR D CD2 1 
ATOM   11672 C  CE1 . TYR D  1 344 ? 31.431  -6.719  105.112 1.00 6.86   ? 431  TYR D CE1 1 
ATOM   11673 C  CE2 . TYR D  1 344 ? 31.143  -4.304  105.273 1.00 6.82   ? 431  TYR D CE2 1 
ATOM   11674 C  CZ  . TYR D  1 344 ? 30.692  -5.594  105.512 1.00 8.50   ? 431  TYR D CZ  1 
ATOM   11675 O  OH  . TYR D  1 344 ? 29.499  -5.718  106.163 1.00 8.54   ? 431  TYR D OH  1 
ATOM   11676 N  N   . VAL D  1 345 ? 35.550  -2.634  105.275 1.00 7.42   ? 432  VAL D N   1 
ATOM   11677 C  CA  . VAL D  1 345 ? 35.075  -1.475  106.012 1.00 7.78   ? 432  VAL D CA  1 
ATOM   11678 C  C   . VAL D  1 345 ? 34.293  -0.649  105.000 1.00 8.54   ? 432  VAL D C   1 
ATOM   11679 O  O   . VAL D  1 345 ? 34.797  -0.353  103.885 1.00 8.65   ? 432  VAL D O   1 
ATOM   11680 C  CB  . VAL D  1 345 ? 36.218  -0.599  106.601 1.00 7.17   ? 432  VAL D CB  1 
ATOM   11681 C  CG1 . VAL D  1 345 ? 35.656  0.590   107.463 1.00 7.84   ? 432  VAL D CG1 1 
ATOM   11682 C  CG2 . VAL D  1 345 ? 37.187  -1.434  107.399 1.00 7.93   ? 432  VAL D CG2 1 
ATOM   11683 N  N   . GLU D  1 346 ? 33.072  -0.303  105.400 1.00 7.14   ? 433  GLU D N   1 
ATOM   11684 C  CA  . GLU D  1 346 ? 32.234  0.654   104.691 1.00 7.53   ? 433  GLU D CA  1 
ATOM   11685 C  C   . GLU D  1 346 ? 32.718  2.081   104.997 1.00 7.65   ? 433  GLU D C   1 
ATOM   11686 O  O   . GLU D  1 346 ? 32.829  2.473   106.164 1.00 8.48   ? 433  GLU D O   1 
ATOM   11687 C  CB  . GLU D  1 346 ? 30.769  0.488   105.110 1.00 6.85   ? 433  GLU D CB  1 
ATOM   11688 C  CG  . GLU D  1 346 ? 29.823  1.567   104.533 1.00 6.83   ? 433  GLU D CG  1 
ATOM   11689 C  CD  . GLU D  1 346 ? 28.465  1.581   105.203 1.00 8.11   ? 433  GLU D CD  1 
ATOM   11690 O  OE1 . GLU D  1 346 ? 27.461  1.761   104.483 1.00 7.07   ? 433  GLU D OE1 1 
ATOM   11691 O  OE2 . GLU D  1 346 ? 28.402  1.439   106.442 1.00 10.44  ? 433  GLU D OE2 1 
ATOM   11692 N  N   . LEU D  1 347 ? 32.995  2.857   103.958 1.00 7.35   ? 434  LEU D N   1 
ATOM   11693 C  CA  . LEU D  1 347 ? 33.541  4.204   104.155 1.00 7.37   ? 434  LEU D CA  1 
ATOM   11694 C  C   . LEU D  1 347 ? 32.437  5.227   103.829 1.00 7.53   ? 434  LEU D C   1 
ATOM   11695 O  O   . LEU D  1 347 ? 32.232  5.589   102.656 1.00 6.09   ? 434  LEU D O   1 
ATOM   11696 C  CB  . LEU D  1 347 ? 34.814  4.391   103.293 1.00 7.69   ? 434  LEU D CB  1 
ATOM   11697 C  CG  . LEU D  1 347 ? 35.912  3.318   103.389 1.00 8.66   ? 434  LEU D CG  1 
ATOM   11698 C  CD1 . LEU D  1 347 ? 37.007  3.579   102.321 1.00 8.32   ? 434  LEU D CD1 1 
ATOM   11699 C  CD2 . LEU D  1 347 ? 36.552  3.246   104.793 1.00 8.73   ? 434  LEU D CD2 1 
ATOM   11700 N  N   . ILE D  1 348 ? 31.708  5.656   104.871 1.00 7.61   ? 435  ILE D N   1 
ATOM   11701 C  CA  . ILE D  1 348 ? 30.525  6.504   104.693 1.00 8.09   ? 435  ILE D CA  1 
ATOM   11702 C  C   . ILE D  1 348 ? 30.913  7.942   104.411 1.00 8.59   ? 435  ILE D C   1 
ATOM   11703 O  O   . ILE D  1 348 ? 31.685  8.539   105.160 1.00 9.21   ? 435  ILE D O   1 
ATOM   11704 C  CB  . ILE D  1 348 ? 29.561  6.466   105.934 1.00 8.43   ? 435  ILE D CB  1 
ATOM   11705 C  CG1 . ILE D  1 348 ? 29.021  5.045   106.167 1.00 9.35   ? 435  ILE D CG1 1 
ATOM   11706 C  CG2 . ILE D  1 348 ? 28.401  7.460   105.726 1.00 7.71   ? 435  ILE D CG2 1 
ATOM   11707 C  CD1 . ILE D  1 348 ? 28.350  4.833   107.574 1.00 9.02   ? 435  ILE D CD1 1 
ATOM   11708 N  N   . ARG D  1 349 ? 30.339  8.502   103.348 1.00 8.75   ? 436  ARG D N   1 
ATOM   11709 C  CA  . ARG D  1 349 ? 30.534  9.903   103.012 1.00 8.88   ? 436  ARG D CA  1 
ATOM   11710 C  C   . ARG D  1 349 ? 29.180  10.607  102.994 1.00 9.15   ? 436  ARG D C   1 
ATOM   11711 O  O   . ARG D  1 349 ? 28.159  9.980   102.682 1.00 9.76   ? 436  ARG D O   1 
ATOM   11712 C  CB  . ARG D  1 349 ? 31.239  10.032  101.651 1.00 8.49   ? 436  ARG D CB  1 
ATOM   11713 C  CG  . ARG D  1 349 ? 32.683  9.482   101.606 1.00 8.61   ? 436  ARG D CG  1 
ATOM   11714 C  CD  . ARG D  1 349 ? 33.566  9.973   102.789 1.00 9.09   ? 436  ARG D CD  1 
ATOM   11715 N  NE  . ARG D  1 349 ? 33.747  11.439  102.826 1.00 9.37   ? 436  ARG D NE  1 
ATOM   11716 C  CZ  . ARG D  1 349 ? 34.717  12.078  102.180 1.00 11.01  ? 436  ARG D CZ  1 
ATOM   11717 N  NH1 . ARG D  1 349 ? 35.573  11.389  101.426 1.00 9.77   ? 436  ARG D NH1 1 
ATOM   11718 N  NH2 . ARG D  1 349 ? 34.825  13.407  102.280 1.00 9.99   ? 436  ARG D NH2 1 
ATOM   11719 N  N   . GLY D  1 350 ? 29.162  11.899  103.332 1.00 9.07   ? 437  GLY D N   1 
ATOM   11720 C  CA  . GLY D  1 350 ? 27.905  12.655  103.315 1.00 8.80   ? 437  GLY D CA  1 
ATOM   11721 C  C   . GLY D  1 350 ? 27.206  12.644  104.668 1.00 9.14   ? 437  GLY D C   1 
ATOM   11722 O  O   . GLY D  1 350 ? 27.852  12.652  105.725 1.00 8.19   ? 437  GLY D O   1 
ATOM   11723 N  N   . ARG D  1 351 ? 25.880  12.675  104.644 1.00 9.97   ? 438  ARG D N   1 
ATOM   11724 C  CA  . ARG D  1 351 ? 25.118  12.854  105.897 1.00 11.54  ? 438  ARG D CA  1 
ATOM   11725 C  C   . ARG D  1 351 ? 25.154  11.638  106.826 1.00 12.04  ? 438  ARG D C   1 
ATOM   11726 O  O   . ARG D  1 351 ? 25.259  10.503  106.357 1.00 12.97  ? 438  ARG D O   1 
ATOM   11727 C  CB  . ARG D  1 351 ? 23.675  13.234  105.577 1.00 11.56  ? 438  ARG D CB  1 
ATOM   11728 C  CG  . ARG D  1 351 ? 23.619  14.497  104.792 1.00 14.00  ? 438  ARG D CG  1 
ATOM   11729 C  CD  . ARG D  1 351 ? 22.218  15.040  104.790 1.00 19.22  ? 438  ARG D CD  1 
ATOM   11730 N  NE  . ARG D  1 351 ? 22.267  16.441  104.424 1.00 23.39  ? 438  ARG D NE  1 
ATOM   11731 C  CZ  . ARG D  1 351 ? 22.070  17.458  105.249 1.00 25.30  ? 438  ARG D CZ  1 
ATOM   11732 N  NH1 . ARG D  1 351 ? 21.770  17.259  106.533 1.00 27.65  ? 438  ARG D NH1 1 
ATOM   11733 N  NH2 . ARG D  1 351 ? 22.150  18.686  104.767 1.00 25.41  ? 438  ARG D NH2 1 
ATOM   11734 N  N   . PRO D  1 352 ? 25.046  11.858  108.152 1.00 12.94  ? 439  PRO D N   1 
ATOM   11735 C  CA  . PRO D  1 352 ? 24.904  13.129  108.864 1.00 13.04  ? 439  PRO D CA  1 
ATOM   11736 C  C   . PRO D  1 352 ? 26.217  13.842  109.181 1.00 13.21  ? 439  PRO D C   1 
ATOM   11737 O  O   . PRO D  1 352 ? 26.187  15.023  109.496 1.00 13.02  ? 439  PRO D O   1 
ATOM   11738 C  CB  . PRO D  1 352 ? 24.238  12.696  110.179 1.00 13.10  ? 439  PRO D CB  1 
ATOM   11739 C  CG  . PRO D  1 352 ? 24.842  11.375  110.459 1.00 12.96  ? 439  PRO D CG  1 
ATOM   11740 C  CD  . PRO D  1 352 ? 24.989  10.712  109.087 1.00 12.74  ? 439  PRO D CD  1 
ATOM   11741 N  N   . LYS D  1 353 ? 27.347  13.142  109.112 1.00 12.82  ? 440  LYS D N   1 
ATOM   11742 C  CA  . LYS D  1 353 ? 28.644  13.734  109.507 1.00 12.85  ? 440  LYS D CA  1 
ATOM   11743 C  C   . LYS D  1 353 ? 29.126  14.870  108.598 1.00 13.05  ? 440  LYS D C   1 
ATOM   11744 O  O   . LYS D  1 353 ? 29.805  15.812  109.056 1.00 12.78  ? 440  LYS D O   1 
ATOM   11745 C  CB  . LYS D  1 353 ? 29.714  12.645  109.653 1.00 13.93  ? 440  LYS D CB  1 
ATOM   11746 C  CG  . LYS D  1 353 ? 29.484  11.702  110.846 1.00 13.33  ? 440  LYS D CG  1 
ATOM   11747 C  CD  . LYS D  1 353 ? 29.460  12.463  112.181 1.00 15.41  ? 440  LYS D CD  1 
ATOM   11748 C  CE  . LYS D  1 353 ? 29.281  11.544  113.391 1.00 15.20  ? 440  LYS D CE  1 
ATOM   11749 N  NZ  . LYS D  1 353 ? 27.880  11.071  113.500 1.00 18.42  ? 440  LYS D NZ  1 
ATOM   11750 N  N   . GLU D  1 354 ? 28.763  14.793  107.321 1.00 12.30  ? 441  GLU D N   1 
ATOM   11751 C  CA  . GLU D  1 354 ? 29.142  15.799  106.336 1.00 12.48  ? 441  GLU D CA  1 
ATOM   11752 C  C   . GLU D  1 354 ? 27.871  16.416  105.735 1.00 13.58  ? 441  GLU D C   1 
ATOM   11753 O  O   . GLU D  1 354 ? 27.350  15.958  104.708 1.00 13.59  ? 441  GLU D O   1 
ATOM   11754 C  CB  . GLU D  1 354 ? 30.050  15.179  105.257 1.00 12.62  ? 441  GLU D CB  1 
ATOM   11755 C  CG  . GLU D  1 354 ? 31.366  14.654  105.829 1.00 11.53  ? 441  GLU D CG  1 
ATOM   11756 C  CD  . GLU D  1 354 ? 32.204  13.862  104.825 1.00 12.63  ? 441  GLU D CD  1 
ATOM   11757 O  OE1 . GLU D  1 354 ? 33.361  14.262  104.560 1.00 13.29  ? 441  GLU D OE1 1 
ATOM   11758 O  OE2 . GLU D  1 354 ? 31.711  12.837  104.317 1.00 11.66  ? 441  GLU D OE2 1 
ATOM   11759 N  N   . SER D  1 355 ? 27.348  17.441  106.403 1.00 13.57  ? 442  SER D N   1 
ATOM   11760 C  CA  . SER D  1 355 ? 26.031  17.985  106.046 1.00 14.64  ? 442  SER D CA  1 
ATOM   11761 C  C   . SER D  1 355 ? 26.044  19.050  104.951 1.00 14.81  ? 442  SER D C   1 
ATOM   11762 O  O   . SER D  1 355 ? 24.988  19.625  104.653 1.00 15.24  ? 442  SER D O   1 
ATOM   11763 C  CB  . SER D  1 355 ? 25.328  18.552  107.278 1.00 15.05  ? 442  SER D CB  1 
ATOM   11764 O  OG  . SER D  1 355 ? 26.153  19.532  107.871 1.00 16.92  ? 442  SER D OG  1 
ATOM   11765 N  N   . SER D  1 356 ? 27.214  19.324  104.363 1.00 13.71  ? 443  SER D N   1 
ATOM   11766 C  CA  . SER D  1 356 ? 27.318  20.262  103.232 1.00 14.15  ? 443  SER D CA  1 
ATOM   11767 C  C   . SER D  1 356 ? 26.800  19.662  101.903 1.00 13.57  ? 443  SER D C   1 
ATOM   11768 O  O   . SER D  1 356 ? 26.701  20.365  100.899 1.00 13.69  ? 443  SER D O   1 
ATOM   11769 C  CB  . SER D  1 356 ? 28.761  20.735  103.060 1.00 13.97  ? 443  SER D CB  1 
ATOM   11770 O  OG  . SER D  1 356 ? 29.570  19.692  102.535 1.00 15.81  ? 443  SER D OG  1 
ATOM   11771 N  N   . VAL D  1 357 ? 26.523  18.359  101.908 1.00 13.06  ? 444  VAL D N   1 
ATOM   11772 C  CA  . VAL D  1 357 ? 25.888  17.655  100.787 1.00 12.59  ? 444  VAL D CA  1 
ATOM   11773 C  C   . VAL D  1 357 ? 24.507  17.121  101.231 1.00 12.64  ? 444  VAL D C   1 
ATOM   11774 O  O   . VAL D  1 357 ? 24.253  16.979  102.433 1.00 13.40  ? 444  VAL D O   1 
ATOM   11775 C  CB  . VAL D  1 357 ? 26.792  16.495  100.240 1.00 12.45  ? 444  VAL D CB  1 
ATOM   11776 C  CG1 . VAL D  1 357 ? 28.144  17.033  99.750  1.00 12.75  ? 444  VAL D CG1 1 
ATOM   11777 C  CG2 . VAL D  1 357 ? 27.001  15.378  101.299 1.00 11.91  ? 444  VAL D CG2 1 
ATOM   11778 N  N   . LEU D  1 358 ? 23.631  16.807  100.277 1.00 11.90  ? 445  LEU D N   1 
ATOM   11779 C  CA  . LEU D  1 358 ? 22.240  16.388  100.573 1.00 12.47  ? 445  LEU D CA  1 
ATOM   11780 C  C   . LEU D  1 358 ? 22.086  14.865  100.678 1.00 11.86  ? 445  LEU D C   1 
ATOM   11781 O  O   . LEU D  1 358 ? 21.001  14.357  101.007 1.00 11.03  ? 445  LEU D O   1 
ATOM   11782 C  CB  . LEU D  1 358 ? 21.303  16.902  99.472  1.00 12.63  ? 445  LEU D CB  1 
ATOM   11783 C  CG  . LEU D  1 358 ? 20.616  18.276  99.602  1.00 16.63  ? 445  LEU D CG  1 
ATOM   11784 C  CD1 . LEU D  1 358 ? 21.346  19.225  100.522 1.00 20.17  ? 445  LEU D CD1 1 
ATOM   11785 C  CD2 . LEU D  1 358 ? 20.302  18.903  98.235  1.00 14.19  ? 445  LEU D CD2 1 
ATOM   11786 N  N   . TRP D  1 359 ? 23.177  14.159  100.366 1.00 11.07  ? 446  TRP D N   1 
ATOM   11787 C  CA  . TRP D  1 359 ? 23.171  12.711  100.217 1.00 10.25  ? 446  TRP D CA  1 
ATOM   11788 C  C   . TRP D  1 359 ? 23.988  11.975  101.269 1.00 10.23  ? 446  TRP D C   1 
ATOM   11789 O  O   . TRP D  1 359 ? 24.744  12.588  102.018 1.00 11.19  ? 446  TRP D O   1 
ATOM   11790 C  CB  . TRP D  1 359 ? 23.677  12.330  98.807  1.00 9.88   ? 446  TRP D CB  1 
ATOM   11791 C  CG  . TRP D  1 359 ? 24.991  12.958  98.386  1.00 9.79   ? 446  TRP D CG  1 
ATOM   11792 C  CD1 . TRP D  1 359 ? 25.143  14.060  97.564  1.00 10.20  ? 446  TRP D CD1 1 
ATOM   11793 C  CD2 . TRP D  1 359 ? 26.323  12.524  98.719  1.00 10.58  ? 446  TRP D CD2 1 
ATOM   11794 N  NE1 . TRP D  1 359 ? 26.487  14.325  97.363  1.00 10.90  ? 446  TRP D NE1 1 
ATOM   11795 C  CE2 . TRP D  1 359 ? 27.230  13.411  98.070  1.00 11.17  ? 446  TRP D CE2 1 
ATOM   11796 C  CE3 . TRP D  1 359 ? 26.845  11.473  99.502  1.00 8.21   ? 446  TRP D CE3 1 
ATOM   11797 C  CZ2 . TRP D  1 359 ? 28.629  13.274  98.178  1.00 11.02  ? 446  TRP D CZ2 1 
ATOM   11798 C  CZ3 . TRP D  1 359 ? 28.235  11.345  99.615  1.00 10.30  ? 446  TRP D CZ3 1 
ATOM   11799 C  CH2 . TRP D  1 359 ? 29.110  12.245  98.957  1.00 10.04  ? 446  TRP D CH2 1 
ATOM   11800 N  N   . THR D  1 360 ? 23.826  10.650  101.293 1.00 9.49   ? 447  THR D N   1 
ATOM   11801 C  CA  . THR D  1 360 ? 24.641  9.729   102.087 1.00 8.98   ? 447  THR D CA  1 
ATOM   11802 C  C   . THR D  1 360 ? 24.986  8.551   101.162 1.00 8.63   ? 447  THR D C   1 
ATOM   11803 O  O   . THR D  1 360 ? 24.102  8.001   100.509 1.00 7.99   ? 447  THR D O   1 
ATOM   11804 C  CB  . THR D  1 360 ? 23.876  9.153   103.316 1.00 9.42   ? 447  THR D CB  1 
ATOM   11805 O  OG1 . THR D  1 360 ? 23.526  10.200  104.233 1.00 8.50   ? 447  THR D OG1 1 
ATOM   11806 C  CG2 . THR D  1 360 ? 24.716  8.076   104.049 1.00 8.88   ? 447  THR D CG2 1 
ATOM   11807 N  N   . SER D  1 361 ? 26.262  8.189   101.109 1.00 8.19   ? 448  SER D N   1 
ATOM   11808 C  CA  . SER D  1 361 ? 26.705  7.022   100.342 1.00 7.55   ? 448  SER D CA  1 
ATOM   11809 C  C   . SER D  1 361 ? 27.989  6.464   100.979 1.00 7.99   ? 448  SER D C   1 
ATOM   11810 O  O   . SER D  1 361 ? 28.346  6.834   102.109 1.00 8.05   ? 448  SER D O   1 
ATOM   11811 C  CB  . SER D  1 361 ? 26.889  7.378   98.856  1.00 7.67   ? 448  SER D CB  1 
ATOM   11812 O  OG  . SER D  1 361 ? 26.948  6.188   98.068  1.00 7.97   ? 448  SER D OG  1 
ATOM   11813 N  N   . ASN D  1 362 ? 28.650  5.534   100.297 1.00 7.72   ? 449  ASN D N   1 
ATOM   11814 C  CA  . ASN D  1 362 ? 29.895  4.968   100.805 1.00 7.23   ? 449  ASN D CA  1 
ATOM   11815 C  C   . ASN D  1 362 ? 30.798  4.514   99.681  1.00 7.49   ? 449  ASN D C   1 
ATOM   11816 O  O   . ASN D  1 362 ? 30.357  4.408   98.526  1.00 7.85   ? 449  ASN D O   1 
ATOM   11817 C  CB  . ASN D  1 362 ? 29.609  3.742   101.671 1.00 6.98   ? 449  ASN D CB  1 
ATOM   11818 C  CG  . ASN D  1 362 ? 29.119  2.577   100.855 1.00 7.35   ? 449  ASN D CG  1 
ATOM   11819 O  OD1 . ASN D  1 362 ? 29.887  1.655   100.511 1.00 12.01  ? 449  ASN D OD1 1 
ATOM   11820 N  ND2 . ASN D  1 362 ? 27.870  2.648   100.454 1.00 5.60   ? 449  ASN D ND2 1 
ATOM   11821 N  N   . SER D  1 363 ? 32.063  4.245   100.021 1.00 6.49   ? 450  SER D N   1 
ATOM   11822 C  CA  . SER D  1 363 ? 32.878  3.382   99.181  1.00 7.60   ? 450  SER D CA  1 
ATOM   11823 C  C   . SER D  1 363 ? 33.289  2.148   100.019 1.00 7.96   ? 450  SER D C   1 
ATOM   11824 O  O   . SER D  1 363 ? 32.881  2.008   101.173 1.00 9.14   ? 450  SER D O   1 
ATOM   11825 C  CB  . SER D  1 363 ? 34.082  4.131   98.584  1.00 7.38   ? 450  SER D CB  1 
ATOM   11826 O  OG  . SER D  1 363 ? 35.050  4.418   99.568  1.00 9.32   ? 450  SER D OG  1 
ATOM   11827 N  N   . ILE D  1 364 ? 34.094  1.270   99.444  1.00 8.73   ? 451  ILE D N   1 
ATOM   11828 C  CA  . ILE D  1 364 ? 34.490  0.027   100.119 1.00 9.26   ? 451  ILE D CA  1 
ATOM   11829 C  C   . ILE D  1 364 ? 36.014  -0.131  100.120 1.00 8.96   ? 451  ILE D C   1 
ATOM   11830 O  O   . ILE D  1 364 ? 36.692  0.223   99.149  1.00 9.14   ? 451  ILE D O   1 
ATOM   11831 C  CB  . ILE D  1 364 ? 33.855  -1.223  99.413  1.00 8.74   ? 451  ILE D CB  1 
ATOM   11832 C  CG1 . ILE D  1 364 ? 32.318  -1.086  99.284  1.00 9.66   ? 451  ILE D CG1 1 
ATOM   11833 C  CG2 . ILE D  1 364 ? 34.238  -2.548  100.130 1.00 10.45  ? 451  ILE D CG2 1 
ATOM   11834 C  CD1 . ILE D  1 364 ? 31.678  -2.152  98.370  1.00 9.15   ? 451  ILE D CD1 1 
ATOM   11835 N  N   . VAL D  1 365 ? 36.545  -0.663  101.215 1.00 9.03   ? 452  VAL D N   1 
ATOM   11836 C  CA  . VAL D  1 365 ? 37.889  -1.267  101.189 1.00 8.66   ? 452  VAL D CA  1 
ATOM   11837 C  C   . VAL D  1 365 ? 37.779  -2.650  101.817 1.00 8.33   ? 452  VAL D C   1 
ATOM   11838 O  O   . VAL D  1 365 ? 36.981  -2.850  102.757 1.00 8.02   ? 452  VAL D O   1 
ATOM   11839 C  CB  . VAL D  1 365 ? 38.964  -0.413  101.927 1.00 8.55   ? 452  VAL D CB  1 
ATOM   11840 C  CG1 . VAL D  1 365 ? 38.674  -0.307  103.435 1.00 9.43   ? 452  VAL D CG1 1 
ATOM   11841 C  CG2 . VAL D  1 365 ? 40.381  -0.973  101.658 1.00 9.45   ? 452  VAL D CG2 1 
ATOM   11842 N  N   . ALA D  1 366 ? 38.577  -3.587  101.311 1.00 8.15   ? 453  ALA D N   1 
ATOM   11843 C  CA  . ALA D  1 366 ? 38.584  -4.965  101.812 1.00 7.75   ? 453  ALA D CA  1 
ATOM   11844 C  C   . ALA D  1 366 ? 40.020  -5.457  101.973 1.00 8.54   ? 453  ALA D C   1 
ATOM   11845 O  O   . ALA D  1 366 ? 40.868  -5.138  101.124 1.00 7.33   ? 453  ALA D O   1 
ATOM   11846 C  CB  . ALA D  1 366 ? 37.846  -5.863  100.855 1.00 8.64   ? 453  ALA D CB  1 
ATOM   11847 N  N   . LEU D  1 367 ? 40.268  -6.236  103.041 1.00 7.94   ? 454  LEU D N   1 
ATOM   11848 C  CA  . LEU D  1 367 ? 41.596  -6.790  103.339 1.00 7.86   ? 454  LEU D CA  1 
ATOM   11849 C  C   . LEU D  1 367 ? 41.479  -8.264  103.764 1.00 7.87   ? 454  LEU D C   1 
ATOM   11850 O  O   . LEU D  1 367 ? 40.418  -8.699  104.211 1.00 7.41   ? 454  LEU D O   1 
ATOM   11851 C  CB  . LEU D  1 367 ? 42.284  -5.975  104.439 1.00 8.27   ? 454  LEU D CB  1 
ATOM   11852 C  CG  . LEU D  1 367 ? 42.663  -4.518  104.086 1.00 7.49   ? 454  LEU D CG  1 
ATOM   11853 C  CD1 . LEU D  1 367 ? 41.531  -3.516  104.408 1.00 9.16   ? 454  LEU D CD1 1 
ATOM   11854 C  CD2 . LEU D  1 367 ? 43.924  -4.119  104.794 1.00 8.74   ? 454  LEU D CD2 1 
ATOM   11855 N  N   . CYS D  1 368 ? 42.568  -9.016  103.621 1.00 7.50   ? 455  CYS D N   1 
ATOM   11856 C  CA  . CYS D  1 368 ? 42.626  -10.395 104.094 1.00 8.60   ? 455  CYS D CA  1 
ATOM   11857 C  C   . CYS D  1 368 ? 43.908  -10.611 104.896 1.00 8.76   ? 455  CYS D C   1 
ATOM   11858 O  O   . CYS D  1 368 ? 44.833  -9.777  104.873 1.00 9.16   ? 455  CYS D O   1 
ATOM   11859 C  CB  . CYS D  1 368 ? 42.539  -11.407 102.944 1.00 8.18   ? 455  CYS D CB  1 
ATOM   11860 S  SG  . CYS D  1 368 ? 41.043  -11.245 101.907 1.00 10.03  ? 455  CYS D SG  1 
ATOM   11861 N  N   . GLY D  1 369 ? 43.941  -11.728 105.611 1.00 8.55   ? 456  GLY D N   1 
ATOM   11862 C  CA  . GLY D  1 369 ? 45.058  -12.034 106.504 1.00 8.84   ? 456  GLY D CA  1 
ATOM   11863 C  C   . GLY D  1 369 ? 46.351  -12.327 105.768 1.00 8.86   ? 456  GLY D C   1 
ATOM   11864 O  O   . GLY D  1 369 ? 46.352  -12.797 104.624 1.00 7.81   ? 456  GLY D O   1 
ATOM   11865 N  N   . SER D  1 370 ? 47.454  -11.998 106.424 1.00 9.06   ? 457  SER D N   1 
ATOM   11866 C  CA  . SER D  1 370 ? 48.768  -12.473 106.001 1.00 10.54  ? 457  SER D CA  1 
ATOM   11867 C  C   . SER D  1 370 ? 49.472  -13.058 107.220 1.00 11.59  ? 457  SER D C   1 
ATOM   11868 O  O   . SER D  1 370 ? 49.336  -12.523 108.324 1.00 10.53  ? 457  SER D O   1 
ATOM   11869 C  CB  . SER D  1 370 ? 49.624  -11.349 105.458 1.00 11.01  ? 457  SER D CB  1 
ATOM   11870 O  OG  . SER D  1 370 ? 50.913  -11.858 105.101 1.00 11.38  ? 457  SER D OG  1 
ATOM   11871 N  N   . LYS D  1 371 ? 50.204  -14.155 107.010 1.00 12.32  ? 458  LYS D N   1 
ATOM   11872 C  CA  . LYS D  1 371 ? 51.141  -14.649 108.029 1.00 13.72  ? 458  LYS D CA  1 
ATOM   11873 C  C   . LYS D  1 371 ? 52.408  -13.767 108.159 1.00 14.21  ? 458  LYS D C   1 
ATOM   11874 O  O   . LYS D  1 371 ? 53.096  -13.799 109.185 1.00 13.55  ? 458  LYS D O   1 
ATOM   11875 C  CB  . LYS D  1 371 ? 51.521  -16.105 107.746 1.00 14.41  ? 458  LYS D CB  1 
ATOM   11876 C  CG  . LYS D  1 371 ? 52.009  -16.818 108.986 1.00 19.30  ? 458  LYS D CG  1 
ATOM   11877 C  CD  . LYS D  1 371 ? 52.564  -18.203 108.701 1.00 24.28  ? 458  LYS D CD  1 
ATOM   11878 C  CE  . LYS D  1 371 ? 53.586  -18.558 109.792 1.00 26.62  ? 458  LYS D CE  1 
ATOM   11879 N  NZ  . LYS D  1 371 ? 54.112  -19.942 109.610 1.00 31.29  ? 458  LYS D NZ  1 
ATOM   11880 N  N   . LYS D  1 372 ? 52.692  -12.967 107.134 1.00 14.23  ? 459  LYS D N   1 
ATOM   11881 C  CA  . LYS D  1 372 ? 53.797  -12.016 107.184 1.00 15.15  ? 459  LYS D CA  1 
ATOM   11882 C  C   . LYS D  1 372 ? 53.458  -10.806 108.073 1.00 15.06  ? 459  LYS D C   1 
ATOM   11883 O  O   . LYS D  1 372 ? 52.298  -10.576 108.433 1.00 14.14  ? 459  LYS D O   1 
ATOM   11884 C  CB  . LYS D  1 372 ? 54.170  -11.541 105.762 1.00 15.04  ? 459  LYS D CB  1 
ATOM   11885 C  CG  . LYS D  1 372 ? 54.249  -12.654 104.712 1.00 17.64  ? 459  LYS D CG  1 
ATOM   11886 C  CD  . LYS D  1 372 ? 55.622  -13.300 104.686 1.00 20.16  ? 459  LYS D CD  1 
ATOM   11887 C  CE  . LYS D  1 372 ? 55.665  -14.548 103.795 1.00 22.54  ? 459  LYS D CE  1 
ATOM   11888 N  NZ  . LYS D  1 372 ? 55.792  -14.236 102.331 1.00 23.26  ? 459  LYS D NZ  1 
ATOM   11889 N  N   . ARG D  1 373 ? 54.494  -10.041 108.403 1.00 15.58  ? 460  ARG D N   1 
ATOM   11890 C  CA  . ARG D  1 373 ? 54.361  -8.784  109.115 1.00 16.53  ? 460  ARG D CA  1 
ATOM   11891 C  C   . ARG D  1 373 ? 54.442  -7.687  108.061 1.00 15.31  ? 460  ARG D C   1 
ATOM   11892 O  O   . ARG D  1 373 ? 55.527  -7.178  107.756 1.00 15.00  ? 460  ARG D O   1 
ATOM   11893 C  CB  . ARG D  1 373 ? 55.506  -8.616  110.126 1.00 17.38  ? 460  ARG D CB  1 
ATOM   11894 C  CG  . ARG D  1 373 ? 56.026  -9.933  110.718 1.00 23.76  ? 460  ARG D CG  1 
ATOM   11895 C  CD  . ARG D  1 373 ? 55.497  -10.221 112.111 1.00 30.10  ? 460  ARG D CD  1 
ATOM   11896 N  NE  . ARG D  1 373 ? 54.104  -9.815  112.233 1.00 34.19  ? 460  ARG D NE  1 
ATOM   11897 C  CZ  . ARG D  1 373 ? 53.680  -8.787  112.965 1.00 36.66  ? 460  ARG D CZ  1 
ATOM   11898 N  NH1 . ARG D  1 373 ? 54.535  -8.065  113.682 1.00 37.42  ? 460  ARG D NH1 1 
ATOM   11899 N  NH2 . ARG D  1 373 ? 52.389  -8.492  112.989 1.00 36.91  ? 460  ARG D NH2 1 
ATOM   11900 N  N   . LEU D  1 374 ? 53.300  -7.347  107.476 1.00 13.31  ? 461  LEU D N   1 
ATOM   11901 C  CA  . LEU D  1 374 ? 53.292  -6.367  106.396 1.00 12.92  ? 461  LEU D CA  1 
ATOM   11902 C  C   . LEU D  1 374 ? 53.142  -4.953  106.924 1.00 12.46  ? 461  LEU D C   1 
ATOM   11903 O  O   . LEU D  1 374 ? 52.448  -4.734  107.925 1.00 13.14  ? 461  LEU D O   1 
ATOM   11904 C  CB  . LEU D  1 374 ? 52.137  -6.638  105.425 1.00 12.22  ? 461  LEU D CB  1 
ATOM   11905 C  CG  . LEU D  1 374 ? 52.056  -8.029  104.791 1.00 12.63  ? 461  LEU D CG  1 
ATOM   11906 C  CD1 . LEU D  1 374 ? 50.792  -8.116  103.959 1.00 12.20  ? 461  LEU D CD1 1 
ATOM   11907 C  CD2 . LEU D  1 374 ? 53.310  -8.311  103.954 1.00 14.44  ? 461  LEU D CD2 1 
ATOM   11908 N  N   . GLY D  1 375 ? 53.751  -3.991  106.227 1.00 12.24  ? 462  GLY D N   1 
ATOM   11909 C  CA  . GLY D  1 375 ? 53.536  -2.581  106.529 1.00 11.99  ? 462  GLY D CA  1 
ATOM   11910 C  C   . GLY D  1 375 ? 52.117  -2.143  106.203 1.00 12.35  ? 462  GLY D C   1 
ATOM   11911 O  O   . GLY D  1 375 ? 51.412  -2.800  105.444 1.00 12.19  ? 462  GLY D O   1 
ATOM   11912 N  N   . SER D  1 376 ? 51.694  -1.015  106.753 1.00 12.34  ? 463  SER D N   1 
ATOM   11913 C  CA  . SER D  1 376 ? 50.324  -0.563  106.488 1.00 12.46  ? 463  SER D CA  1 
ATOM   11914 C  C   . SER D  1 376 ? 50.204  0.930   106.195 1.00 12.46  ? 463  SER D C   1 
ATOM   11915 O  O   . SER D  1 376 ? 51.071  1.711   106.589 1.00 12.62  ? 463  SER D O   1 
ATOM   11916 C  CB  . SER D  1 376 ? 49.458  -0.908  107.693 1.00 12.60  ? 463  SER D CB  1 
ATOM   11917 O  OG  . SER D  1 376 ? 49.903  -0.190  108.833 1.00 14.60  ? 463  SER D OG  1 
ATOM   11918 N  N   . TRP D  1 377 ? 49.126  1.324   105.511 1.00 11.53  ? 464  TRP D N   1 
ATOM   11919 C  CA  . TRP D  1 377 ? 48.710  2.734   105.512 1.00 12.43  ? 464  TRP D CA  1 
ATOM   11920 C  C   . TRP D  1 377 ? 47.201  2.824   105.552 1.00 11.62  ? 464  TRP D C   1 
ATOM   11921 O  O   . TRP D  1 377 ? 46.508  1.799   105.542 1.00 12.52  ? 464  TRP D O   1 
ATOM   11922 C  CB  . TRP D  1 377 ? 49.321  3.587   104.378 1.00 12.74  ? 464  TRP D CB  1 
ATOM   11923 C  CG  . TRP D  1 377 ? 48.944  3.241   102.935 1.00 12.94  ? 464  TRP D CG  1 
ATOM   11924 C  CD1 . TRP D  1 377 ? 48.203  2.184   102.501 1.00 14.88  ? 464  TRP D CD1 1 
ATOM   11925 C  CD2 . TRP D  1 377 ? 49.375  3.941   101.759 1.00 14.00  ? 464  TRP D CD2 1 
ATOM   11926 N  NE1 . TRP D  1 377 ? 48.120  2.200   101.119 1.00 15.17  ? 464  TRP D NE1 1 
ATOM   11927 C  CE2 . TRP D  1 377 ? 48.828  3.267   100.642 1.00 14.38  ? 464  TRP D CE2 1 
ATOM   11928 C  CE3 . TRP D  1 377 ? 50.168  5.083   101.544 1.00 12.91  ? 464  TRP D CE3 1 
ATOM   11929 C  CZ2 . TRP D  1 377 ? 49.042  3.697   99.311  1.00 13.00  ? 464  TRP D CZ2 1 
ATOM   11930 C  CZ3 . TRP D  1 377 ? 50.378  5.517   100.217 1.00 14.49  ? 464  TRP D CZ3 1 
ATOM   11931 C  CH2 . TRP D  1 377 ? 49.826  4.807   99.124  1.00 12.34  ? 464  TRP D CH2 1 
ATOM   11932 N  N   . SER D  1 378 ? 46.712  4.053   105.622 1.00 11.09  ? 465  SER D N   1 
ATOM   11933 C  CA  . SER D  1 378 ? 45.297  4.309   105.728 1.00 10.57  ? 465  SER D CA  1 
ATOM   11934 C  C   . SER D  1 378 ? 44.618  4.174   104.367 1.00 10.25  ? 465  SER D C   1 
ATOM   11935 O  O   . SER D  1 378 ? 45.052  4.769   103.383 1.00 10.42  ? 465  SER D O   1 
ATOM   11936 C  CB  . SER D  1 378 ? 45.061  5.698   106.343 1.00 10.46  ? 465  SER D CB  1 
ATOM   11937 O  OG  . SER D  1 378 ? 43.674  5.988   106.363 1.00 8.95   ? 465  SER D OG  1 
ATOM   11938 N  N   . TRP D  1 379 ? 43.537  3.398   104.335 1.00 9.80   ? 466  TRP D N   1 
ATOM   11939 C  CA  . TRP D  1 379 ? 42.765  3.185   103.111 1.00 10.04  ? 466  TRP D CA  1 
ATOM   11940 C  C   . TRP D  1 379 ? 41.432  3.932   103.179 1.00 10.09  ? 466  TRP D C   1 
ATOM   11941 O  O   . TRP D  1 379 ? 40.365  3.359   102.957 1.00 10.34  ? 466  TRP D O   1 
ATOM   11942 C  CB  . TRP D  1 379 ? 42.537  1.683   102.915 1.00 10.21  ? 466  TRP D CB  1 
ATOM   11943 C  CG  . TRP D  1 379 ? 43.787  0.876   102.673 1.00 10.45  ? 466  TRP D CG  1 
ATOM   11944 C  CD1 . TRP D  1 379 ? 44.448  0.090   103.579 1.00 11.32  ? 466  TRP D CD1 1 
ATOM   11945 C  CD2 . TRP D  1 379 ? 44.517  0.767   101.444 1.00 9.59   ? 466  TRP D CD2 1 
ATOM   11946 N  NE1 . TRP D  1 379 ? 45.545  -0.499  102.991 1.00 8.46   ? 466  TRP D NE1 1 
ATOM   11947 C  CE2 . TRP D  1 379 ? 45.608  -0.107  101.680 1.00 10.00  ? 466  TRP D CE2 1 
ATOM   11948 C  CE3 . TRP D  1 379 ? 44.352  1.316   100.161 1.00 8.73   ? 466  TRP D CE3 1 
ATOM   11949 C  CZ2 . TRP D  1 379 ? 46.527  -0.452  100.677 1.00 8.12   ? 466  TRP D CZ2 1 
ATOM   11950 C  CZ3 . TRP D  1 379 ? 45.266  0.986   99.169  1.00 8.76   ? 466  TRP D CZ3 1 
ATOM   11951 C  CH2 . TRP D  1 379 ? 46.345  0.095   99.439  1.00 10.66  ? 466  TRP D CH2 1 
ATOM   11952 N  N   . HIS D  1 380 ? 41.511  5.234   103.488 1.00 10.25  ? 467  HIS D N   1 
ATOM   11953 C  CA  . HIS D  1 380 ? 40.333  6.080   103.594 1.00 10.07  ? 467  HIS D CA  1 
ATOM   11954 C  C   . HIS D  1 380 ? 39.680  6.297   102.222 1.00 9.95   ? 467  HIS D C   1 
ATOM   11955 O  O   . HIS D  1 380 ? 40.276  6.000   101.176 1.00 10.50  ? 467  HIS D O   1 
ATOM   11956 C  CB  . HIS D  1 380 ? 40.689  7.407   104.264 1.00 10.46  ? 467  HIS D CB  1 
ATOM   11957 C  CG  . HIS D  1 380 ? 41.939  8.036   103.731 1.00 10.22  ? 467  HIS D CG  1 
ATOM   11958 N  ND1 . HIS D  1 380 ? 43.192  7.656   104.154 1.00 10.73  ? 467  HIS D ND1 1 
ATOM   11959 C  CD2 . HIS D  1 380 ? 42.130  9.012   102.807 1.00 11.62  ? 467  HIS D CD2 1 
ATOM   11960 C  CE1 . HIS D  1 380 ? 44.106  8.383   103.527 1.00 10.42  ? 467  HIS D CE1 1 
ATOM   11961 N  NE2 . HIS D  1 380 ? 43.485  9.220   102.710 1.00 10.97  ? 467  HIS D NE2 1 
ATOM   11962 N  N   . ASP D  1 381 ? 38.451  6.795   102.232 1.00 9.44   ? 468  ASP D N   1 
ATOM   11963 C  CA  . ASP D  1 381 ? 37.661  6.958   101.009 1.00 8.67   ? 468  ASP D CA  1 
ATOM   11964 C  C   . ASP D  1 381 ? 38.379  7.764   99.917  1.00 9.16   ? 468  ASP D C   1 
ATOM   11965 O  O   . ASP D  1 381 ? 38.399  7.366   98.755  1.00 9.22   ? 468  ASP D O   1 
ATOM   11966 C  CB  . ASP D  1 381 ? 36.306  7.611   101.327 1.00 7.92   ? 468  ASP D CB  1 
ATOM   11967 C  CG  . ASP D  1 381 ? 35.526  7.969   100.055 1.00 7.86   ? 468  ASP D CG  1 
ATOM   11968 O  OD1 . ASP D  1 381 ? 34.996  7.039   99.400  1.00 9.48   ? 468  ASP D OD1 1 
ATOM   11969 O  OD2 . ASP D  1 381 ? 35.453  9.172   99.707  1.00 7.98   ? 468  ASP D OD2 1 
ATOM   11970 N  N   . GLY D  1 382 ? 38.936  8.912   100.293 1.00 10.35  ? 469  GLY D N   1 
ATOM   11971 C  CA  . GLY D  1 382 ? 39.731  9.708   99.365  1.00 10.00  ? 469  GLY D CA  1 
ATOM   11972 C  C   . GLY D  1 382 ? 39.037  10.780  98.532  1.00 9.78   ? 469  GLY D C   1 
ATOM   11973 O  O   . GLY D  1 382 ? 39.714  11.500  97.777  1.00 8.90   ? 469  GLY D O   1 
ATOM   11974 N  N   . ALA D  1 383 ? 37.709  10.887  98.638  1.00 10.36  ? 470  ALA D N   1 
ATOM   11975 C  CA  . ALA D  1 383 ? 36.984  11.963  97.959  1.00 10.32  ? 470  ALA D CA  1 
ATOM   11976 C  C   . ALA D  1 383 ? 37.080  13.273  98.724  1.00 11.13  ? 470  ALA D C   1 
ATOM   11977 O  O   . ALA D  1 383 ? 37.145  13.292  99.961  1.00 11.41  ? 470  ALA D O   1 
ATOM   11978 C  CB  . ALA D  1 383 ? 35.514  11.615  97.730  1.00 10.61  ? 470  ALA D CB  1 
ATOM   11979 N  N   . GLU D  1 384 ? 37.078  14.366  97.969  1.00 11.58  ? 471  GLU D N   1 
ATOM   11980 C  CA  . GLU D  1 384 ? 37.056  15.701  98.544  1.00 12.70  ? 471  GLU D CA  1 
ATOM   11981 C  C   . GLU D  1 384 ? 35.611  16.218  98.577  1.00 12.11  ? 471  GLU D C   1 
ATOM   11982 O  O   . GLU D  1 384 ? 34.998  16.428  97.547  1.00 11.45  ? 471  GLU D O   1 
ATOM   11983 C  CB  . GLU D  1 384 ? 37.992  16.612  97.733  1.00 13.68  ? 471  GLU D CB  1 
ATOM   11984 C  CG  . GLU D  1 384 ? 37.933  18.050  98.144  1.00 18.59  ? 471  GLU D CG  1 
ATOM   11985 C  CD  . GLU D  1 384 ? 38.295  18.240  99.611  1.00 21.75  ? 471  GLU D CD  1 
ATOM   11986 O  OE1 . GLU D  1 384 ? 39.448  17.856  99.969  1.00 23.17  ? 471  GLU D OE1 1 
ATOM   11987 O  OE2 . GLU D  1 384 ? 37.422  18.753  100.380 1.00 20.07  ? 471  GLU D OE2 1 
ATOM   11988 N  N   . ILE D  1 385 ? 35.063  16.422  99.769  1.00 12.21  ? 472  ILE D N   1 
ATOM   11989 C  CA  . ILE D  1 385 ? 33.656  16.825  99.899  1.00 12.83  ? 472  ILE D CA  1 
ATOM   11990 C  C   . ILE D  1 385 ? 33.384  18.177  99.203  1.00 13.49  ? 472  ILE D C   1 
ATOM   11991 O  O   . ILE D  1 385 ? 32.303  18.379  98.644  1.00 12.34  ? 472  ILE D O   1 
ATOM   11992 C  CB  . ILE D  1 385 ? 33.170  16.825  101.407 1.00 13.23  ? 472  ILE D CB  1 
ATOM   11993 C  CG1 . ILE D  1 385 ? 31.647  16.648  101.512 1.00 14.24  ? 472  ILE D CG1 1 
ATOM   11994 C  CG2 . ILE D  1 385 ? 33.625  18.096  102.170 1.00 14.46  ? 472  ILE D CG2 1 
ATOM   11995 C  CD1 . ILE D  1 385 ? 31.140  15.274  101.063 1.00 15.11  ? 472  ILE D CD1 1 
ATOM   11996 N  N   . ILE D  1 386 ? 34.390  19.063  99.192  1.00 13.82  ? 473  ILE D N   1 
ATOM   11997 C  CA  . ILE D  1 386 ? 34.216  20.394  98.587  1.00 15.01  ? 473  ILE D CA  1 
ATOM   11998 C  C   . ILE D  1 386 ? 33.845  20.294  97.091  1.00 14.35  ? 473  ILE D C   1 
ATOM   11999 O  O   . ILE D  1 386 ? 33.063  21.092  96.575  1.00 14.19  ? 473  ILE D O   1 
ATOM   12000 C  CB  . ILE D  1 386 ? 35.428  21.360  98.855  1.00 15.38  ? 473  ILE D CB  1 
ATOM   12001 C  CG1 . ILE D  1 386 ? 35.155  22.749  98.268  1.00 15.55  ? 473  ILE D CG1 1 
ATOM   12002 C  CG2 . ILE D  1 386 ? 36.696  20.857  98.245  1.00 16.53  ? 473  ILE D CG2 1 
ATOM   12003 C  CD1 . ILE D  1 386 ? 36.096  23.840  98.784  1.00 18.10  ? 473  ILE D CD1 1 
ATOM   12004 N  N   . TYR D  1 387 ? 34.377  19.292  96.404  1.00 13.05  ? 474  TYR D N   1 
ATOM   12005 C  CA  . TYR D  1 387 ? 34.016  19.075  94.999  1.00 12.67  ? 474  TYR D CA  1 
ATOM   12006 C  C   . TYR D  1 387 ? 32.522  18.799  94.775  1.00 12.07  ? 474  TYR D C   1 
ATOM   12007 O  O   . TYR D  1 387 ? 32.023  18.971  93.667  1.00 12.28  ? 474  TYR D O   1 
ATOM   12008 C  CB  . TYR D  1 387 ? 34.828  17.907  94.417  1.00 12.34  ? 474  TYR D CB  1 
ATOM   12009 C  CG  . TYR D  1 387 ? 36.323  18.164  94.268  1.00 12.47  ? 474  TYR D CG  1 
ATOM   12010 C  CD1 . TYR D  1 387 ? 37.206  17.094  94.148  1.00 11.84  ? 474  TYR D CD1 1 
ATOM   12011 C  CD2 . TYR D  1 387 ? 36.848  19.472  94.227  1.00 13.35  ? 474  TYR D CD2 1 
ATOM   12012 C  CE1 . TYR D  1 387 ? 38.580  17.289  94.001  1.00 10.94  ? 474  TYR D CE1 1 
ATOM   12013 C  CE2 . TYR D  1 387 ? 38.234  19.686  94.082  1.00 12.31  ? 474  TYR D CE2 1 
ATOM   12014 C  CZ  . TYR D  1 387 ? 39.086  18.582  93.959  1.00 12.72  ? 474  TYR D CZ  1 
ATOM   12015 O  OH  . TYR D  1 387 ? 40.445  18.736  93.802  1.00 11.42  ? 474  TYR D OH  1 
ATOM   12016 N  N   . PHE D  1 388 ? 31.826  18.346  95.812  1.00 11.98  ? 475  PHE D N   1 
ATOM   12017 C  CA  . PHE D  1 388 ? 30.411  18.030  95.703  1.00 12.75  ? 475  PHE D CA  1 
ATOM   12018 C  C   . PHE D  1 388 ? 29.525  19.177  96.170  1.00 13.74  ? 475  PHE D C   1 
ATOM   12019 O  O   . PHE D  1 388 ? 28.289  19.064  96.178  1.00 13.24  ? 475  PHE D O   1 
ATOM   12020 C  CB  . PHE D  1 388 ? 30.093  16.800  96.548  1.00 12.21  ? 475  PHE D CB  1 
ATOM   12021 C  CG  . PHE D  1 388 ? 30.562  15.499  95.953  1.00 11.04  ? 475  PHE D CG  1 
ATOM   12022 C  CD1 . PHE D  1 388 ? 29.740  14.790  95.070  1.00 10.24  ? 475  PHE D CD1 1 
ATOM   12023 C  CD2 . PHE D  1 388 ? 31.794  14.947  96.335  1.00 9.69   ? 475  PHE D CD2 1 
ATOM   12024 C  CE1 . PHE D  1 388 ? 30.151  13.531  94.544  1.00 12.10  ? 475  PHE D CE1 1 
ATOM   12025 C  CE2 . PHE D  1 388 ? 32.230  13.697  95.823  1.00 9.72   ? 475  PHE D CE2 1 
ATOM   12026 C  CZ  . PHE D  1 388 ? 31.394  12.982  94.927  1.00 9.61   ? 475  PHE D CZ  1 
ATOM   12027 N  N   . GLU D  1 389 ? 30.157  20.272  96.581  1.00 15.09  ? 476  GLU D N   1 
ATOM   12028 C  CA  . GLU D  1 389 ? 29.421  21.437  97.076  1.00 16.87  ? 476  GLU D CA  1 
ATOM   12029 C  C   . GLU D  1 389 ? 29.133  22.416  95.948  1.00 17.83  ? 476  GLU D C   1 
ATOM   12030 O  O   . GLU D  1 389 ? 29.490  22.187  94.793  1.00 18.12  ? 476  GLU D O   1 
ATOM   12031 C  CB  . GLU D  1 389 ? 30.198  22.129  98.207  1.00 16.57  ? 476  GLU D CB  1 
ATOM   12032 C  CG  . GLU D  1 389 ? 30.372  21.241  99.450  1.00 17.03  ? 476  GLU D CG  1 
ATOM   12033 C  CD  . GLU D  1 389 ? 31.318  21.831  100.496 1.00 18.42  ? 476  GLU D CD  1 
ATOM   12034 O  OE1 . GLU D  1 389 ? 31.903  22.909  100.263 1.00 20.24  ? 476  GLU D OE1 1 
ATOM   12035 O  OE2 . GLU D  1 389 ? 31.498  21.191  101.546 1.00 19.38  ? 476  GLU D OE2 1 
ATOM   12036 O  OXT . GLU D  1 389 ? 28.542  23.483  96.176  1.00 19.10  ? 476  GLU D OXT 1 
HETATM 12037 CA CA  . CA  E  2 .   ? 31.023  7.861   39.397  1.00 20.02  ? 501  CA  A CA  1 
HETATM 12038 C  C1  . GOL F  3 .   ? 39.400  15.303  64.323  1.00 31.60  ? 502  GOL A C1  1 
HETATM 12039 O  O1  . GOL F  3 .   ? 39.275  15.509  65.733  1.00 29.16  ? 502  GOL A O1  1 
HETATM 12040 C  C2  . GOL F  3 .   ? 40.193  14.058  63.864  1.00 30.69  ? 502  GOL A C2  1 
HETATM 12041 O  O2  . GOL F  3 .   ? 40.629  14.363  62.514  1.00 29.28  ? 502  GOL A O2  1 
HETATM 12042 C  C3  . GOL F  3 .   ? 39.399  12.704  64.059  1.00 30.78  ? 502  GOL A C3  1 
HETATM 12043 O  O3  . GOL F  3 .   ? 39.943  11.328  63.852  1.00 19.31  ? 502  GOL A O3  1 
HETATM 12044 C  C1  . NAG G  4 .   ? 29.219  -26.637 51.175  1.00 21.34  ? 503  NAG A C1  1 
HETATM 12045 C  C2  . NAG G  4 .   ? 29.795  -28.018 50.825  1.00 22.31  ? 503  NAG A C2  1 
HETATM 12046 C  C3  . NAG G  4 .   ? 28.779  -29.125 51.094  1.00 24.80  ? 503  NAG A C3  1 
HETATM 12047 C  C4  . NAG G  4 .   ? 28.130  -29.004 52.482  1.00 26.93  ? 503  NAG A C4  1 
HETATM 12048 C  C5  . NAG G  4 .   ? 27.664  -27.554 52.676  1.00 25.09  ? 503  NAG A C5  1 
HETATM 12049 C  C6  . NAG G  4 .   ? 26.997  -27.315 54.032  1.00 25.71  ? 503  NAG A C6  1 
HETATM 12050 C  C7  . NAG G  4 .   ? 31.519  -27.997 49.120  1.00 21.37  ? 503  NAG A C7  1 
HETATM 12051 C  C8  . NAG G  4 .   ? 31.874  -28.394 47.717  1.00 21.01  ? 503  NAG A C8  1 
HETATM 12052 N  N2  . NAG G  4 .   ? 30.227  -28.083 49.432  1.00 20.81  ? 503  NAG A N2  1 
HETATM 12053 O  O3  . NAG G  4 .   ? 29.436  -30.362 50.943  1.00 22.31  ? 503  NAG A O3  1 
HETATM 12054 O  O4  . NAG G  4 .   ? 26.967  -29.792 52.570  1.00 32.79  ? 503  NAG A O4  1 
HETATM 12055 O  O5  . NAG G  4 .   ? 28.746  -26.660 52.510  1.00 22.28  ? 503  NAG A O5  1 
HETATM 12056 O  O6  . NAG G  4 .   ? 27.898  -27.672 55.053  1.00 26.77  ? 503  NAG A O6  1 
HETATM 12057 O  O7  . NAG G  4 .   ? 32.391  -27.600 49.913  1.00 20.98  ? 503  NAG A O7  1 
HETATM 12058 C  C1  . NAG H  4 .   ? 27.186  -31.188 52.828  1.00 39.28  ? 504  NAG A C1  1 
HETATM 12059 C  C2  . NAG H  4 .   ? 26.095  -31.703 53.768  1.00 41.53  ? 504  NAG A C2  1 
HETATM 12060 C  C3  . NAG H  4 .   ? 26.216  -33.215 53.959  1.00 43.59  ? 504  NAG A C3  1 
HETATM 12061 C  C4  . NAG H  4 .   ? 26.288  -33.940 52.605  1.00 44.09  ? 504  NAG A C4  1 
HETATM 12062 C  C5  . NAG H  4 .   ? 27.350  -33.288 51.714  1.00 43.61  ? 504  NAG A C5  1 
HETATM 12063 C  C6  . NAG H  4 .   ? 27.356  -33.867 50.301  1.00 44.51  ? 504  NAG A C6  1 
HETATM 12064 C  C7  . NAG H  4 .   ? 25.151  -30.193 55.434  1.00 43.62  ? 504  NAG A C7  1 
HETATM 12065 C  C8  . NAG H  4 .   ? 25.110  -29.854 56.896  1.00 43.33  ? 504  NAG A C8  1 
HETATM 12066 N  N2  . NAG H  4 .   ? 26.136  -31.009 55.046  1.00 42.88  ? 504  NAG A N2  1 
HETATM 12067 O  O3  . NAG H  4 .   ? 25.121  -33.673 54.726  1.00 44.40  ? 504  NAG A O3  1 
HETATM 12068 O  O4  . NAG H  4 .   ? 26.621  -35.301 52.798  1.00 45.61  ? 504  NAG A O4  1 
HETATM 12069 O  O5  . NAG H  4 .   ? 27.112  -31.898 51.610  1.00 40.87  ? 504  NAG A O5  1 
HETATM 12070 O  O6  . NAG H  4 .   ? 28.356  -33.213 49.543  1.00 45.01  ? 504  NAG A O6  1 
HETATM 12071 O  O7  . NAG H  4 .   ? 24.307  -29.726 54.662  1.00 43.79  ? 504  NAG A O7  1 
HETATM 12072 C  C1  . NAG I  4 .   ? 37.189  23.703  65.597  1.00 19.74  ? 505  NAG A C1  1 
HETATM 12073 C  C2  . NAG I  4 .   ? 37.331  24.844  66.622  1.00 21.12  ? 505  NAG A C2  1 
HETATM 12074 C  C3  . NAG I  4 .   ? 37.916  26.098  65.973  1.00 24.27  ? 505  NAG A C3  1 
HETATM 12075 C  C4  . NAG I  4 .   ? 39.128  25.795  65.107  1.00 24.36  ? 505  NAG A C4  1 
HETATM 12076 C  C5  . NAG I  4 .   ? 38.929  24.549  64.232  1.00 23.25  ? 505  NAG A C5  1 
HETATM 12077 C  C6  . NAG I  4 .   ? 40.208  24.130  63.499  1.00 23.56  ? 505  NAG A C6  1 
HETATM 12078 C  C7  . NAG I  4 .   ? 35.689  24.817  68.455  1.00 20.87  ? 505  NAG A C7  1 
HETATM 12079 C  C8  . NAG I  4 .   ? 34.391  25.367  68.967  1.00 20.43  ? 505  NAG A C8  1 
HETATM 12080 N  N2  . NAG I  4 .   ? 36.051  25.195  67.229  1.00 21.49  ? 505  NAG A N2  1 
HETATM 12081 O  O3  . NAG I  4 .   ? 38.254  27.022  66.984  1.00 25.06  ? 505  NAG A O3  1 
HETATM 12082 O  O4  . NAG I  4 .   ? 39.315  26.915  64.262  1.00 28.31  ? 505  NAG A O4  1 
HETATM 12083 O  O5  . NAG I  4 .   ? 38.451  23.463  65.011  1.00 19.84  ? 505  NAG A O5  1 
HETATM 12084 O  O6  . NAG I  4 .   ? 41.213  23.833  64.457  1.00 27.36  ? 505  NAG A O6  1 
HETATM 12085 O  O7  . NAG I  4 .   ? 36.357  24.035  69.149  1.00 22.15  ? 505  NAG A O7  1 
HETATM 12086 C  C1  . NAG J  4 .   ? 0.712   -1.576  49.983  1.00 45.10  ? 506  NAG A C1  1 
HETATM 12087 C  C2  . NAG J  4 .   ? 1.021   -0.207  49.380  1.00 44.34  ? 506  NAG A C2  1 
HETATM 12088 C  C3  . NAG J  4 .   ? 1.586   -0.434  47.983  1.00 44.35  ? 506  NAG A C3  1 
HETATM 12089 C  C4  . NAG J  4 .   ? 2.827   -1.323  48.125  1.00 43.86  ? 506  NAG A C4  1 
HETATM 12090 C  C5  . NAG J  4 .   ? 2.559   -2.556  48.982  1.00 44.38  ? 506  NAG A C5  1 
HETATM 12091 C  C6  . NAG J  4 .   ? 3.833   -3.368  49.167  1.00 44.33  ? 506  NAG A C6  1 
HETATM 12092 C  C7  . NAG J  4 .   ? -0.246  1.598   50.341  1.00 45.06  ? 506  NAG A C7  1 
HETATM 12093 C  C8  . NAG J  4 .   ? -1.511  1.570   51.149  1.00 45.40  ? 506  NAG A C8  1 
HETATM 12094 N  N2  . NAG J  4 .   ? -0.133  0.661   49.405  1.00 44.72  ? 506  NAG A N2  1 
HETATM 12095 O  O3  . NAG J  4 .   ? 1.887   0.788   47.341  1.00 42.40  ? 506  NAG A O3  1 
HETATM 12096 O  O4  . NAG J  4 .   ? 3.197   -1.839  46.878  1.00 43.08  ? 506  NAG A O4  1 
HETATM 12097 O  O5  . NAG J  4 .   ? 1.975   -2.175  50.213  1.00 44.54  ? 506  NAG A O5  1 
HETATM 12098 O  O6  . NAG J  4 .   ? 4.945   -2.500  49.202  1.00 44.40  ? 506  NAG A O6  1 
HETATM 12099 O  O7  . NAG J  4 .   ? 0.627   2.443   50.548  1.00 44.70  ? 506  NAG A O7  1 
HETATM 12100 C  C1  . MAN K  5 .   ? 9.917   2.639   39.813  1.00 22.35  ? 507  MAN A C1  1 
HETATM 12101 C  C2  . MAN K  5 .   ? 9.850   3.965   40.582  1.00 24.05  ? 507  MAN A C2  1 
HETATM 12102 C  C3  . MAN K  5 .   ? 9.129   5.060   39.774  1.00 24.06  ? 507  MAN A C3  1 
HETATM 12103 C  C4  . MAN K  5 .   ? 9.697   5.189   38.379  1.00 24.78  ? 507  MAN A C4  1 
HETATM 12104 C  C5  . MAN K  5 .   ? 9.682   3.798   37.739  1.00 24.42  ? 507  MAN A C5  1 
HETATM 12105 C  C6  . MAN K  5 .   ? 10.269  3.847   36.352  1.00 24.08  ? 507  MAN A C6  1 
HETATM 12106 O  O2  . MAN K  5 .   ? 11.166  4.406   40.938  1.00 23.45  ? 507  MAN A O2  1 
HETATM 12107 O  O3  . MAN K  5 .   ? 9.241   6.358   40.367  1.00 24.00  ? 507  MAN A O3  1 
HETATM 12108 O  O4  . MAN K  5 .   ? 8.924   6.166   37.656  1.00 27.00  ? 507  MAN A O4  1 
HETATM 12109 O  O5  . MAN K  5 .   ? 10.498  2.918   38.535  1.00 23.74  ? 507  MAN A O5  1 
HETATM 12110 O  O6  . MAN K  5 .   ? 11.521  4.480   36.604  1.00 24.42  ? 507  MAN A O6  1 
HETATM 12111 C  C1  . BMA L  6 .   ? 5.314   0.172   40.795  1.00 24.94  ? 510  BMA A C1  1 
HETATM 12112 C  C2  . BMA L  6 .   ? 4.376   0.684   39.710  1.00 26.44  ? 510  BMA A C2  1 
HETATM 12113 C  C3  . BMA L  6 .   ? 4.904   0.391   38.306  1.00 26.78  ? 510  BMA A C3  1 
HETATM 12114 C  C4  . BMA L  6 .   ? 6.335   0.884   38.154  1.00 26.85  ? 510  BMA A C4  1 
HETATM 12115 C  C5  . BMA L  6 .   ? 7.191   0.248   39.241  1.00 25.20  ? 510  BMA A C5  1 
HETATM 12116 C  C6  . BMA L  6 .   ? 8.621   0.760   39.165  1.00 23.08  ? 510  BMA A C6  1 
HETATM 12117 O  O2  . BMA L  6 .   ? 4.237   2.093   39.891  1.00 24.98  ? 510  BMA A O2  1 
HETATM 12118 O  O3  . BMA L  6 .   ? 4.097   1.054   37.324  1.00 31.14  ? 510  BMA A O3  1 
HETATM 12119 O  O4  . BMA L  6 .   ? 6.832   0.529   36.863  1.00 26.45  ? 510  BMA A O4  1 
HETATM 12120 O  O5  . BMA L  6 .   ? 6.663   0.566   40.529  1.00 26.16  ? 510  BMA A O5  1 
HETATM 12121 O  O6  . BMA L  6 .   ? 8.695   2.103   39.666  1.00 21.71  ? 510  BMA A O6  1 
HETATM 12122 C  C1  . MAN M  5 .   ? 3.670   0.989   36.059  1.00 45.53  ? 511  MAN A C1  1 
HETATM 12123 C  C2  . MAN M  5 .   ? 2.390   1.823   35.982  1.00 48.89  ? 511  MAN A C2  1 
HETATM 12124 C  C3  . MAN M  5 .   ? 1.219   1.069   36.616  1.00 49.14  ? 511  MAN A C3  1 
HETATM 12125 C  C4  . MAN M  5 .   ? 1.129   -0.395  36.160  1.00 49.48  ? 511  MAN A C4  1 
HETATM 12126 C  C5  . MAN M  5 .   ? 2.491   -1.091  36.065  1.00 48.91  ? 511  MAN A C5  1 
HETATM 12127 C  C6  . MAN M  5 .   ? 2.397   -2.421  35.323  1.00 48.89  ? 511  MAN A C6  1 
HETATM 12128 O  O2  . MAN M  5 .   ? 2.102   2.161   34.616  1.00 49.12  ? 511  MAN A O2  1 
HETATM 12129 O  O3  . MAN M  5 .   ? 0.002   1.762   36.306  1.00 50.17  ? 511  MAN A O3  1 
HETATM 12130 O  O4  . MAN M  5 .   ? 0.319   -1.115  37.094  1.00 49.68  ? 511  MAN A O4  1 
HETATM 12131 O  O5  . MAN M  5 .   ? 3.444   -0.260  35.395  1.00 48.77  ? 511  MAN A O5  1 
HETATM 12132 O  O6  . MAN M  5 .   ? 2.071   -3.445  36.270  1.00 49.31  ? 511  MAN A O6  1 
HETATM 12133 C  C1  . NAG N  4 .   ? 4.353   -0.776  45.737  1.00 24.71  ? 512  NAG A C1  1 
HETATM 12134 C  C2  . NAG N  4 .   ? 5.319   -1.615  44.915  1.00 23.34  ? 512  NAG A C2  1 
HETATM 12135 C  C3  . NAG N  4 .   ? 5.736   -0.696  43.776  1.00 23.76  ? 512  NAG A C3  1 
HETATM 12136 C  C4  . NAG N  4 .   ? 4.512   -0.226  42.977  1.00 24.76  ? 512  NAG A C4  1 
HETATM 12137 C  C5  . NAG N  4 .   ? 3.462   0.399   43.900  1.00 25.02  ? 512  NAG A C5  1 
HETATM 12138 C  C6  . NAG N  4 .   ? 2.149   0.708   43.182  1.00 27.32  ? 512  NAG A C6  1 
HETATM 12139 C  C7  . NAG N  4 .   ? 6.639   -3.219  46.244  1.00 25.43  ? 512  NAG A C7  1 
HETATM 12140 C  C8  . NAG N  4 .   ? 7.808   -3.353  47.192  1.00 24.65  ? 512  NAG A C8  1 
HETATM 12141 N  N2  . NAG N  4 .   ? 6.465   -1.996  45.722  1.00 23.32  ? 512  NAG A N2  1 
HETATM 12142 O  O3  . NAG N  4 .   ? 6.611   -1.405  42.949  1.00 20.91  ? 512  NAG A O3  1 
HETATM 12143 O  O4  . NAG N  4 .   ? 4.914   0.758   42.053  1.00 24.22  ? 512  NAG A O4  1 
HETATM 12144 O  O5  . NAG N  4 .   ? 3.191   -0.475  44.971  1.00 23.55  ? 512  NAG A O5  1 
HETATM 12145 O  O6  . NAG N  4 .   ? 1.328   1.373   44.119  1.00 30.07  ? 512  NAG A O6  1 
HETATM 12146 O  O7  . NAG N  4 .   ? 5.909   -4.192  45.988  1.00 24.06  ? 512  NAG A O7  1 
HETATM 12147 C  C1  . MAN O  5 .   ? 12.980  4.693   35.494  1.00 30.04  ? 508  MAN A C1  1 
HETATM 12148 C  C2  . MAN O  5 .   ? 14.207  5.406   36.016  1.00 28.83  ? 508  MAN A C2  1 
HETATM 12149 C  C3  . MAN O  5 .   ? 13.826  6.796   36.527  1.00 28.90  ? 508  MAN A C3  1 
HETATM 12150 C  C4  . MAN O  5 .   ? 13.018  7.594   35.501  1.00 31.46  ? 508  MAN A C4  1 
HETATM 12151 C  C5  . MAN O  5 .   ? 11.849  6.795   34.900  1.00 33.12  ? 508  MAN A C5  1 
HETATM 12152 C  C6  . MAN O  5 .   ? 11.306  7.443   33.628  1.00 35.41  ? 508  MAN A C6  1 
HETATM 12153 O  O2  . MAN O  5 .   ? 15.111  5.436   34.914  1.00 26.63  ? 508  MAN A O2  1 
HETATM 12154 O  O3  . MAN O  5 .   ? 14.990  7.545   36.877  1.00 27.38  ? 508  MAN A O3  1 
HETATM 12155 O  O4  . MAN O  5 .   ? 12.525  8.779   36.136  1.00 32.07  ? 508  MAN A O4  1 
HETATM 12156 O  O5  . MAN O  5 .   ? 12.250  5.466   34.526  1.00 32.38  ? 508  MAN A O5  1 
HETATM 12157 O  O6  . MAN O  5 .   ? 11.060  8.829   33.865  1.00 38.35  ? 508  MAN A O6  1 
HETATM 12158 C  C1  . MAN P  5 .   ? 8.121   6.429   41.922  1.00 27.53  ? 509  MAN A C1  1 
HETATM 12159 C  C2  . MAN P  5 .   ? 7.668   7.839   42.258  1.00 27.45  ? 509  MAN A C2  1 
HETATM 12160 C  C3  . MAN P  5 .   ? 8.870   8.688   42.674  1.00 27.38  ? 509  MAN A C3  1 
HETATM 12161 C  C4  . MAN P  5 .   ? 9.724   7.993   43.745  1.00 27.94  ? 509  MAN A C4  1 
HETATM 12162 C  C5  . MAN P  5 .   ? 10.181  6.613   43.261  1.00 27.41  ? 509  MAN A C5  1 
HETATM 12163 C  C6  . MAN P  5 .   ? 10.994  5.824   44.303  1.00 27.19  ? 509  MAN A C6  1 
HETATM 12164 O  O2  . MAN P  5 .   ? 6.704   7.707   43.297  1.00 27.65  ? 509  MAN A O2  1 
HETATM 12165 O  O3  . MAN P  5 .   ? 8.419   9.975   43.112  1.00 28.90  ? 509  MAN A O3  1 
HETATM 12166 O  O4  . MAN P  5 .   ? 10.874  8.793   44.028  1.00 29.05  ? 509  MAN A O4  1 
HETATM 12167 O  O5  . MAN P  5 .   ? 9.036   5.838   42.875  1.00 27.29  ? 509  MAN A O5  1 
HETATM 12168 O  O6  . MAN P  5 .   ? 11.492  4.586   43.746  1.00 24.79  ? 509  MAN A O6  1 
HETATM 12169 C  C1  . NAG Q  4 .   ? 6.668   24.783  67.261  1.00 96.82  ? 513  NAG A C1  1 
HETATM 12170 C  C2  . NAG Q  4 .   ? 7.826   25.014  66.295  1.00 96.85  ? 513  NAG A C2  1 
HETATM 12171 C  C3  . NAG Q  4 .   ? 7.236   25.305  64.921  1.00 97.08  ? 513  NAG A C3  1 
HETATM 12172 C  C4  . NAG Q  4 .   ? 6.392   24.104  64.487  1.00 97.10  ? 513  NAG A C4  1 
HETATM 12173 C  C5  . NAG Q  4 .   ? 5.432   23.627  65.596  1.00 96.96  ? 513  NAG A C5  1 
HETATM 12174 C  C6  . NAG Q  4 .   ? 4.851   22.252  65.274  1.00 96.86  ? 513  NAG A C6  1 
HETATM 12175 C  C7  . NAG Q  4 .   ? 9.657   25.762  67.673  1.00 96.39  ? 513  NAG A C7  1 
HETATM 12176 C  C8  . NAG Q  4 .   ? 9.849   26.741  68.795  1.00 96.21  ? 513  NAG A C8  1 
HETATM 12177 N  N2  . NAG Q  4 .   ? 8.715   26.053  66.777  1.00 96.62  ? 513  NAG A N2  1 
HETATM 12178 O  O3  . NAG Q  4 .   ? 8.257   25.554  63.980  1.00 97.26  ? 513  NAG A O3  1 
HETATM 12179 O  O4  . NAG Q  4 .   ? 5.670   24.455  63.326  1.00 97.13  ? 513  NAG A O4  1 
HETATM 12180 O  O5  . NAG Q  4 .   ? 6.047   23.572  66.878  1.00 96.53  ? 513  NAG A O5  1 
HETATM 12181 O  O6  . NAG Q  4 .   ? 5.609   21.242  65.904  1.00 96.57  ? 513  NAG A O6  1 
HETATM 12182 O  O7  . NAG Q  4 .   ? 10.341  24.741  67.604  1.00 95.99  ? 513  NAG A O7  1 
HETATM 12183 C  C1  . MAN R  5 .   ? 73.665  7.687   65.068  1.00 33.97  ? 514  MAN A C1  1 
HETATM 12184 C  C2  . MAN R  5 .   ? 73.076  8.105   66.410  1.00 33.69  ? 514  MAN A C2  1 
HETATM 12185 C  C3  . MAN R  5 .   ? 72.476  9.513   66.354  1.00 33.21  ? 514  MAN A C3  1 
HETATM 12186 C  C4  . MAN R  5 .   ? 73.474  10.508  65.745  1.00 32.99  ? 514  MAN A C4  1 
HETATM 12187 C  C5  . MAN R  5 .   ? 73.941  10.044  64.363  1.00 34.45  ? 514  MAN A C5  1 
HETATM 12188 C  C6  . MAN R  5 .   ? 75.033  10.947  63.796  1.00 36.76  ? 514  MAN A C6  1 
HETATM 12189 O  O2  . MAN R  5 .   ? 74.120  8.021   67.381  1.00 32.26  ? 514  MAN A O2  1 
HETATM 12190 O  O3  . MAN R  5 .   ? 72.055  9.913   67.668  1.00 31.08  ? 514  MAN A O3  1 
HETATM 12191 O  O4  . MAN R  5 .   ? 72.872  11.791  65.610  1.00 30.30  ? 514  MAN A O4  1 
HETATM 12192 O  O5  . MAN R  5 .   ? 74.449  8.697   64.408  1.00 34.17  ? 514  MAN A O5  1 
HETATM 12193 O  O6  . MAN R  5 .   ? 75.763  10.200  62.810  1.00 38.32  ? 514  MAN A O6  1 
HETATM 12194 C  C1  . NAG S  4 .   ? 57.855  5.093   53.740  1.00 28.93  ? 515  NAG A C1  1 
HETATM 12195 C  C2  . NAG S  4 .   ? 58.997  6.117   53.555  1.00 29.79  ? 515  NAG A C2  1 
HETATM 12196 C  C3  . NAG S  4 .   ? 60.427  5.530   53.676  1.00 29.99  ? 515  NAG A C3  1 
HETATM 12197 C  C4  . NAG S  4 .   ? 60.542  4.532   54.840  1.00 29.08  ? 515  NAG A C4  1 
HETATM 12198 C  C5  . NAG S  4 .   ? 59.399  3.594   54.480  1.00 32.22  ? 515  NAG A C5  1 
HETATM 12199 C  C6  . NAG S  4 .   ? 59.536  2.166   54.961  1.00 33.82  ? 515  NAG A C6  1 
HETATM 12200 C  C7  . NAG S  4 .   ? 58.268  7.879   51.978  1.00 33.09  ? 515  NAG A C7  1 
HETATM 12201 C  C8  . NAG S  4 .   ? 58.126  8.855   53.106  1.00 32.06  ? 515  NAG A C8  1 
HETATM 12202 N  N2  . NAG S  4 .   ? 58.838  6.697   52.231  1.00 31.17  ? 515  NAG A N2  1 
HETATM 12203 O  O3  . NAG S  4 .   ? 61.408  6.558   53.721  1.00 29.88  ? 515  NAG A O3  1 
HETATM 12204 O  O4  . NAG S  4 .   ? 61.729  3.749   54.891  1.00 26.23  ? 515  NAG A O4  1 
HETATM 12205 O  O5  . NAG S  4 .   ? 58.176  4.229   54.808  1.00 31.06  ? 515  NAG A O5  1 
HETATM 12206 O  O6  . NAG S  4 .   ? 59.618  1.429   53.759  1.00 38.54  ? 515  NAG A O6  1 
HETATM 12207 O  O7  . NAG S  4 .   ? 57.877  8.186   50.846  1.00 35.50  ? 515  NAG A O7  1 
HETATM 12208 C  C1  . NAG T  4 .   ? 62.753  4.382   55.681  1.00 24.39  ? 516  NAG A C1  1 
HETATM 12209 C  C2  . NAG T  4 .   ? 63.639  3.337   56.382  1.00 21.22  ? 516  NAG A C2  1 
HETATM 12210 C  C3  . NAG T  4 .   ? 64.844  4.028   57.037  1.00 20.70  ? 516  NAG A C3  1 
HETATM 12211 C  C4  . NAG T  4 .   ? 65.603  4.900   56.024  1.00 20.14  ? 516  NAG A C4  1 
HETATM 12212 C  C5  . NAG T  4 .   ? 64.650  5.856   55.307  1.00 22.41  ? 516  NAG A C5  1 
HETATM 12213 C  C6  . NAG T  4 .   ? 65.326  6.581   54.142  1.00 23.45  ? 516  NAG A C6  1 
HETATM 12214 C  C7  . NAG T  4 .   ? 62.405  1.362   57.233  1.00 20.63  ? 516  NAG A C7  1 
HETATM 12215 C  C8  . NAG T  4 .   ? 61.680  0.806   58.426  1.00 18.73  ? 516  NAG A C8  1 
HETATM 12216 N  N2  . NAG T  4 .   ? 62.898  2.591   57.395  1.00 19.32  ? 516  NAG A N2  1 
HETATM 12217 O  O3  . NAG T  4 .   ? 65.672  3.042   57.645  1.00 14.77  ? 516  NAG A O3  1 
HETATM 12218 O  O4  . NAG T  4 .   ? 66.509  5.766   56.667  1.00 19.94  ? 516  NAG A O4  1 
HETATM 12219 O  O5  . NAG T  4 .   ? 63.510  5.191   54.791  1.00 22.70  ? 516  NAG A O5  1 
HETATM 12220 O  O6  . NAG T  4 .   ? 64.335  7.362   53.494  1.00 25.76  ? 516  NAG A O6  1 
HETATM 12221 O  O7  . NAG T  4 .   ? 62.504  0.684   56.191  1.00 19.17  ? 516  NAG A O7  1 
HETATM 12222 C  C1  . BMA U  6 .   ? 67.812  5.188   56.858  1.00 19.04  ? 517  BMA A C1  1 
HETATM 12223 C  C2  . BMA U  6 .   ? 68.858  6.044   56.148  1.00 18.28  ? 517  BMA A C2  1 
HETATM 12224 C  C3  . BMA U  6 .   ? 70.258  5.497   56.448  1.00 19.18  ? 517  BMA A C3  1 
HETATM 12225 C  C4  . BMA U  6 .   ? 70.515  5.464   57.952  1.00 18.87  ? 517  BMA A C4  1 
HETATM 12226 C  C5  . BMA U  6 .   ? 69.406  4.645   58.636  1.00 19.19  ? 517  BMA A C5  1 
HETATM 12227 C  C6  . BMA U  6 .   ? 69.514  4.718   60.153  1.00 16.95  ? 517  BMA A C6  1 
HETATM 12228 O  O2  . BMA U  6 .   ? 68.782  7.422   56.577  1.00 16.92  ? 517  BMA A O2  1 
HETATM 12229 O  O3  . BMA U  6 .   ? 71.248  6.280   55.768  1.00 21.63  ? 517  BMA A O3  1 
HETATM 12230 O  O4  . BMA U  6 .   ? 71.805  4.857   58.173  1.00 19.82  ? 517  BMA A O4  1 
HETATM 12231 O  O5  . BMA U  6 .   ? 68.086  5.104   58.263  1.00 19.05  ? 517  BMA A O5  1 
HETATM 12232 O  O6  . BMA U  6 .   ? 69.076  6.018   60.563  1.00 19.00  ? 517  BMA A O6  1 
HETATM 12233 C  C1  . MAN V  5 .   ? 71.634  5.790   54.577  1.00 24.10  ? 518  MAN A C1  1 
HETATM 12234 C  C2  . MAN V  5 .   ? 72.943  6.490   54.170  1.00 24.68  ? 518  MAN A C2  1 
HETATM 12235 C  C3  . MAN V  5 .   ? 72.672  7.917   53.681  1.00 26.03  ? 518  MAN A C3  1 
HETATM 12236 C  C4  . MAN V  5 .   ? 71.658  7.888   52.541  1.00 24.97  ? 518  MAN A C4  1 
HETATM 12237 C  C5  . MAN V  5 .   ? 70.394  7.147   52.988  1.00 26.14  ? 518  MAN A C5  1 
HETATM 12238 C  C6  . MAN V  5 .   ? 69.361  7.052   51.868  1.00 27.42  ? 518  MAN A C6  1 
HETATM 12239 O  O2  . MAN V  5 .   ? 73.563  5.762   53.113  1.00 27.10  ? 518  MAN A O2  1 
HETATM 12240 O  O3  . MAN V  5 .   ? 73.891  8.539   53.252  1.00 24.55  ? 518  MAN A O3  1 
HETATM 12241 O  O4  . MAN V  5 .   ? 71.350  9.224   52.137  1.00 27.03  ? 518  MAN A O4  1 
HETATM 12242 O  O5  . MAN V  5 .   ? 70.706  5.824   53.479  1.00 25.12  ? 518  MAN A O5  1 
HETATM 12243 O  O6  . MAN V  5 .   ? 68.278  6.235   52.335  1.00 27.49  ? 518  MAN A O6  1 
HETATM 12244 C  C1  . MAN W  5 .   ? 74.428  4.753   53.162  1.00 38.73  ? 519  MAN A C1  1 
HETATM 12245 C  C2  . MAN W  5 .   ? 75.237  4.492   51.894  1.00 42.29  ? 519  MAN A C2  1 
HETATM 12246 C  C3  . MAN W  5 .   ? 74.290  4.013   50.790  1.00 42.94  ? 519  MAN A C3  1 
HETATM 12247 C  C4  . MAN W  5 .   ? 73.413  2.833   51.221  1.00 43.17  ? 519  MAN A C4  1 
HETATM 12248 C  C5  . MAN W  5 .   ? 72.813  3.030   52.618  1.00 42.40  ? 519  MAN A C5  1 
HETATM 12249 C  C6  . MAN W  5 .   ? 72.223  1.734   53.178  1.00 43.00  ? 519  MAN A C6  1 
HETATM 12250 O  O2  . MAN W  5 .   ? 76.253  3.514   52.170  1.00 43.40  ? 519  MAN A O2  1 
HETATM 12251 O  O3  . MAN W  5 .   ? 75.039  3.655   49.624  1.00 44.36  ? 519  MAN A O3  1 
HETATM 12252 O  O4  . MAN W  5 .   ? 72.346  2.698   50.270  1.00 44.84  ? 519  MAN A O4  1 
HETATM 12253 O  O5  . MAN W  5 .   ? 73.783  3.536   53.552  1.00 41.71  ? 519  MAN A O5  1 
HETATM 12254 O  O6  . MAN W  5 .   ? 71.113  2.045   54.035  1.00 41.43  ? 519  MAN A O6  1 
HETATM 12255 C  C1  . MAN X  5 .   ? 69.161  6.192   61.886  1.00 16.25  ? 520  MAN A C1  1 
HETATM 12256 C  C2  . MAN X  5 .   ? 68.355  7.472   62.043  1.00 16.22  ? 520  MAN A C2  1 
HETATM 12257 C  C3  . MAN X  5 .   ? 69.102  8.664   61.427  1.00 15.14  ? 520  MAN A C3  1 
HETATM 12258 C  C4  . MAN X  5 .   ? 70.526  8.784   61.931  1.00 14.55  ? 520  MAN A C4  1 
HETATM 12259 C  C5  . MAN X  5 .   ? 71.228  7.458   61.654  1.00 15.23  ? 520  MAN A C5  1 
HETATM 12260 C  C6  . MAN X  5 .   ? 72.639  7.439   62.201  1.00 16.92  ? 520  MAN A C6  1 
HETATM 12261 O  O2  . MAN X  5 .   ? 68.083  7.687   63.436  1.00 15.45  ? 520  MAN A O2  1 
HETATM 12262 O  O3  . MAN X  5 .   ? 68.437  9.910   61.685  1.00 16.94  ? 520  MAN A O3  1 
HETATM 12263 O  O4  . MAN X  5 .   ? 71.166  9.858   61.246  1.00 15.84  ? 520  MAN A O4  1 
HETATM 12264 O  O5  . MAN X  5 .   ? 70.499  6.435   62.349  1.00 15.62  ? 520  MAN A O5  1 
HETATM 12265 O  O6  . MAN X  5 .   ? 72.425  7.690   63.596  1.00 19.29  ? 520  MAN A O6  1 
HETATM 12266 C  C1  . MAN Y  5 .   ? 66.944  10.007  60.658  1.00 21.09  ? 521  MAN A C1  1 
HETATM 12267 C  C2  . MAN Y  5 .   ? 66.674  11.502  60.547  1.00 21.32  ? 521  MAN A C2  1 
HETATM 12268 C  C3  . MAN Y  5 .   ? 66.138  12.127  61.840  1.00 20.99  ? 521  MAN A C3  1 
HETATM 12269 C  C4  . MAN Y  5 .   ? 65.026  11.258  62.466  1.00 20.96  ? 521  MAN A C4  1 
HETATM 12270 C  C5  . MAN Y  5 .   ? 65.552  9.842   62.688  1.00 20.43  ? 521  MAN A C5  1 
HETATM 12271 C  C6  . MAN Y  5 .   ? 64.498  8.906   63.297  1.00 19.59  ? 521  MAN A C6  1 
HETATM 12272 O  O2  . MAN Y  5 .   ? 65.730  11.603  59.488  1.00 19.32  ? 521  MAN A O2  1 
HETATM 12273 O  O3  . MAN Y  5 .   ? 65.672  13.457  61.538  1.00 21.91  ? 521  MAN A O3  1 
HETATM 12274 O  O4  . MAN Y  5 .   ? 64.531  11.807  63.707  1.00 20.21  ? 521  MAN A O4  1 
HETATM 12275 O  O5  . MAN Y  5 .   ? 65.984  9.274   61.444  1.00 21.16  ? 521  MAN A O5  1 
HETATM 12276 O  O6  . MAN Y  5 .   ? 65.186  7.811   63.914  1.00 19.07  ? 521  MAN A O6  1 
HETATM 12277 CA CA  . CA  Z  2 .   ? -12.553 -1.318  77.247  1.00 19.72  ? 501  CA  B CA  1 
HETATM 12278 C  C1  . GOL AA 3 .   ? 10.490  11.772  68.942  1.00 26.99  ? 502  GOL B C1  1 
HETATM 12279 O  O1  . GOL AA 3 .   ? 11.846  12.190  69.243  1.00 23.91  ? 502  GOL B O1  1 
HETATM 12280 C  C2  . GOL AA 3 .   ? 10.221  10.339  68.358  1.00 26.36  ? 502  GOL B C2  1 
HETATM 12281 O  O2  . GOL AA 3 .   ? 8.840   10.311  67.856  1.00 28.59  ? 502  GOL B O2  1 
HETATM 12282 C  C3  . GOL AA 3 .   ? 10.592  9.062   69.223  1.00 25.69  ? 502  GOL B C3  1 
HETATM 12283 O  O3  . GOL AA 3 .   ? 10.688  7.605   68.755  1.00 12.09  ? 502  GOL B O3  1 
HETATM 12284 C  C1  . NAG BA 4 .   ? 9.457   -32.962 76.422  1.00 99.08  ? 503  NAG B C1  1 
HETATM 12285 C  C2  . NAG BA 4 .   ? 9.436   -33.804 77.692  1.00 99.12  ? 503  NAG B C2  1 
HETATM 12286 C  C3  . NAG BA 4 .   ? 9.583   -35.264 77.276  1.00 99.18  ? 503  NAG B C3  1 
HETATM 12287 C  C4  . NAG BA 4 .   ? 8.461   -35.662 76.311  1.00 99.17  ? 503  NAG B C4  1 
HETATM 12288 C  C5  . NAG BA 4 .   ? 8.110   -34.593 75.263  1.00 99.15  ? 503  NAG B C5  1 
HETATM 12289 C  C6  . NAG BA 4 .   ? 6.662   -34.781 74.819  1.00 98.99  ? 503  NAG B C6  1 
HETATM 12290 C  C7  . NAG BA 4 .   ? 10.271  -32.431 79.528  1.00 98.58  ? 503  NAG B C7  1 
HETATM 12291 C  C8  . NAG BA 4 .   ? 9.832   -32.855 80.901  1.00 98.34  ? 503  NAG B C8  1 
HETATM 12292 N  N2  . NAG BA 4 .   ? 10.467  -33.396 78.631  1.00 98.89  ? 503  NAG B N2  1 
HETATM 12293 O  O3  . NAG BA 4 .   ? 9.562   -36.106 78.409  1.00 99.09  ? 503  NAG B O3  1 
HETATM 12294 O  O4  . NAG BA 4 .   ? 8.841   -36.844 75.640  1.00 99.24  ? 503  NAG B O4  1 
HETATM 12295 O  O5  . NAG BA 4 .   ? 8.264   -33.250 75.714  1.00 99.22  ? 503  NAG B O5  1 
HETATM 12296 O  O6  . NAG BA 4 .   ? 6.504   -34.305 73.502  1.00 98.92  ? 503  NAG B O6  1 
HETATM 12297 O  O7  . NAG BA 4 .   ? 10.441  -31.241 79.265  1.00 98.49  ? 503  NAG B O7  1 
HETATM 12298 C  C1  . NAG CA 4 .   ? 9.654   20.388  71.280  1.00 20.97  ? 504  NAG B C1  1 
HETATM 12299 C  C2  . NAG CA 4 .   ? 10.555  21.591  71.105  1.00 21.25  ? 504  NAG B C2  1 
HETATM 12300 C  C3  . NAG CA 4 .   ? 9.708   22.627  70.360  1.00 23.12  ? 504  NAG B C3  1 
HETATM 12301 C  C4  . NAG CA 4 .   ? 9.015   22.025  69.114  1.00 23.95  ? 504  NAG B C4  1 
HETATM 12302 C  C5  . NAG CA 4 .   ? 8.379   20.648  69.376  1.00 24.94  ? 504  NAG B C5  1 
HETATM 12303 C  C6  . NAG CA 4 .   ? 7.838   19.947  68.122  1.00 26.32  ? 504  NAG B C6  1 
HETATM 12304 C  C7  . NAG CA 4 .   ? 12.276  21.861  72.828  1.00 17.67  ? 504  NAG B C7  1 
HETATM 12305 C  C8  . NAG CA 4 .   ? 12.642  22.450  74.166  1.00 16.85  ? 504  NAG B C8  1 
HETATM 12306 N  N2  . NAG CA 4 .   ? 11.022  22.041  72.416  1.00 17.91  ? 504  NAG B N2  1 
HETATM 12307 O  O3  . NAG CA 4 .   ? 10.585  23.667  70.014  1.00 23.56  ? 504  NAG B O3  1 
HETATM 12308 O  O4  . NAG CA 4 .   ? 7.999   22.897  68.669  1.00 26.94  ? 504  NAG B O4  1 
HETATM 12309 O  O5  . NAG CA 4 .   ? 9.330   19.825  70.031  1.00 22.77  ? 504  NAG B O5  1 
HETATM 12310 O  O6  . NAG CA 4 .   ? 8.893   19.604  67.247  1.00 29.33  ? 504  NAG B O6  1 
HETATM 12311 O  O7  . NAG CA 4 .   ? 13.128  21.253  72.162  1.00 16.43  ? 504  NAG B O7  1 
HETATM 12312 C  C1  . MAN DA 5 .   ? -11.313 -5.454  98.428  1.00 37.30  ? 505  MAN B C1  1 
HETATM 12313 C  C2  . MAN DA 5 .   ? -10.887 -3.987  98.467  1.00 37.20  ? 505  MAN B C2  1 
HETATM 12314 C  C3  . MAN DA 5 .   ? -11.982 -3.121  99.108  1.00 37.20  ? 505  MAN B C3  1 
HETATM 12315 C  C4  . MAN DA 5 .   ? -13.346 -3.406  98.499  1.00 36.91  ? 505  MAN B C4  1 
HETATM 12316 C  C5  . MAN DA 5 .   ? -13.618 -4.905  98.542  1.00 36.93  ? 505  MAN B C5  1 
HETATM 12317 C  C6  . MAN DA 5 .   ? -14.926 -5.229  97.866  1.00 37.70  ? 505  MAN B C6  1 
HETATM 12318 O  O2  . MAN DA 5 .   ? -10.587 -3.553  97.129  1.00 37.78  ? 505  MAN B O2  1 
HETATM 12319 O  O3  . MAN DA 5 .   ? -11.742 -1.734  98.897  1.00 37.11  ? 505  MAN B O3  1 
HETATM 12320 O  O4  . MAN DA 5 .   ? -14.355 -2.633  99.165  1.00 37.41  ? 505  MAN B O4  1 
HETATM 12321 O  O5  . MAN DA 5 .   ? -12.590 -5.556  97.787  1.00 36.47  ? 505  MAN B O5  1 
HETATM 12322 O  O6  . MAN DA 5 .   ? -14.819 -4.562  96.603  1.00 35.76  ? 505  MAN B O6  1 
HETATM 12323 C  C1  . BMA EA 6 .   ? -10.150 -7.266  103.114 1.00 35.67  ? 507  BMA B C1  1 
HETATM 12324 C  C2  . BMA EA 6 .   ? -11.336 -6.698  103.866 1.00 36.27  ? 507  BMA B C2  1 
HETATM 12325 C  C3  . BMA EA 6 .   ? -12.629 -7.362  103.409 1.00 37.02  ? 507  BMA B C3  1 
HETATM 12326 C  C4  . BMA EA 6 .   ? -12.764 -7.393  101.881 1.00 37.36  ? 507  BMA B C4  1 
HETATM 12327 C  C5  . BMA EA 6 .   ? -11.490 -7.917  101.207 1.00 37.20  ? 507  BMA B C5  1 
HETATM 12328 C  C6  . BMA EA 6 .   ? -11.499 -7.638  99.715  1.00 36.58  ? 507  BMA B C6  1 
HETATM 12329 O  O2  . BMA EA 6 .   ? -11.389 -5.286  103.608 1.00 36.68  ? 507  BMA B O2  1 
HETATM 12330 O  O3  . BMA EA 6 .   ? -13.709 -6.619  103.973 1.00 37.94  ? 507  BMA B O3  1 
HETATM 12331 O  O4  . BMA EA 6 .   ? -13.877 -8.212  101.489 1.00 37.46  ? 507  BMA B O4  1 
HETATM 12332 O  O5  . BMA EA 6 .   ? -10.342 -7.246  101.708 1.00 36.89  ? 507  BMA B O5  1 
HETATM 12333 O  O6  . BMA EA 6 .   ? -11.377 -6.222  99.518  1.00 38.03  ? 507  BMA B O6  1 
HETATM 12334 C  C1  . NAG FA 4 .   ? -5.142  -6.998  103.700 1.00 34.49  ? 508  NAG B C1  1 
HETATM 12335 C  C2  . NAG FA 4 .   ? -5.866  -8.263  103.281 1.00 34.66  ? 508  NAG B C2  1 
HETATM 12336 C  C3  . NAG FA 4 .   ? -7.084  -7.677  102.596 1.00 33.13  ? 508  NAG B C3  1 
HETATM 12337 C  C4  . NAG FA 4 .   ? -7.941  -7.180  103.780 1.00 34.00  ? 508  NAG B C4  1 
HETATM 12338 C  C5  . NAG FA 4 .   ? -7.171  -6.228  104.714 1.00 35.47  ? 508  NAG B C5  1 
HETATM 12339 C  C6  . NAG FA 4 .   ? -7.843  -6.169  106.089 1.00 36.05  ? 508  NAG B C6  1 
HETATM 12340 C  C7  . NAG FA 4 .   ? -4.332  -9.287  101.555 1.00 38.99  ? 508  NAG B C7  1 
HETATM 12341 C  C8  . NAG FA 4 .   ? -3.912  -10.599 100.964 1.00 38.69  ? 508  NAG B C8  1 
HETATM 12342 N  N2  . NAG FA 4 .   ? -5.071  -9.330  102.650 1.00 37.29  ? 508  NAG B N2  1 
HETATM 12343 O  O3  . NAG FA 4 .   ? -7.711  -8.626  101.782 1.00 26.12  ? 508  NAG B O3  1 
HETATM 12344 O  O4  . NAG FA 4 .   ? -9.031  -6.416  103.350 1.00 35.56  ? 508  NAG B O4  1 
HETATM 12345 O  O5  . NAG FA 4 .   ? -5.807  -6.584  104.882 1.00 34.97  ? 508  NAG B O5  1 
HETATM 12346 O  O6  . NAG FA 4 .   ? -7.206  -5.180  106.870 1.00 39.01  ? 508  NAG B O6  1 
HETATM 12347 O  O7  . NAG FA 4 .   ? -3.987  -8.243  101.021 1.00 43.04  ? 508  NAG B O7  1 
HETATM 12348 C  C1  . MAN GA 5 .   ? -16.237 -4.395  95.356  1.00 33.96  ? 506  MAN B C1  1 
HETATM 12349 C  C2  . MAN GA 5 .   ? -15.784 -3.713  94.078  1.00 32.66  ? 506  MAN B C2  1 
HETATM 12350 C  C3  . MAN GA 5 .   ? -15.388 -2.261  94.358  1.00 33.55  ? 506  MAN B C3  1 
HETATM 12351 C  C4  . MAN GA 5 .   ? -16.484 -1.514  95.132  1.00 34.50  ? 506  MAN B C4  1 
HETATM 12352 C  C5  . MAN GA 5 .   ? -16.910 -2.284  96.379  1.00 35.15  ? 506  MAN B C5  1 
HETATM 12353 C  C6  . MAN GA 5 .   ? -18.134 -1.658  97.042  1.00 36.23  ? 506  MAN B C6  1 
HETATM 12354 O  O2  . MAN GA 5 .   ? -16.903 -3.785  93.203  1.00 32.67  ? 506  MAN B O2  1 
HETATM 12355 O  O3  . MAN GA 5 .   ? -15.103 -1.570  93.137  1.00 32.48  ? 506  MAN B O3  1 
HETATM 12356 O  O4  . MAN GA 5 .   ? -15.994 -0.222  95.513  1.00 36.54  ? 506  MAN B O4  1 
HETATM 12357 O  O5  . MAN GA 5 .   ? -17.240 -3.641  96.055  1.00 34.21  ? 506  MAN B O5  1 
HETATM 12358 O  O6  . MAN GA 5 .   ? -18.263 -2.280  98.324  1.00 38.78  ? 506  MAN B O6  1 
HETATM 12359 C  C1  . MAN HA 5 .   ? -9.579  -1.390  100.521 1.00 48.66  ? 509  MAN B C1  1 
HETATM 12360 C  C2  . MAN HA 5 .   ? -10.003 0.070   100.728 1.00 48.72  ? 509  MAN B C2  1 
HETATM 12361 C  C3  . MAN HA 5 .   ? -10.051 0.886   99.430  1.00 48.15  ? 509  MAN B C3  1 
HETATM 12362 C  C4  . MAN HA 5 .   ? -8.823  0.612   98.564  1.00 47.13  ? 509  MAN B C4  1 
HETATM 12363 C  C5  . MAN HA 5 .   ? -8.764  -0.880  98.235  1.00 47.10  ? 509  MAN B C5  1 
HETATM 12364 C  C6  . MAN HA 5 .   ? -7.589  -1.202  97.305  1.00 45.70  ? 509  MAN B C6  1 
HETATM 12365 O  O2  . MAN HA 5 .   ? -9.114  0.672   101.677 1.00 49.85  ? 509  MAN B O2  1 
HETATM 12366 O  O3  . MAN HA 5 .   ? -10.175 2.286   99.727  1.00 48.51  ? 509  MAN B O3  1 
HETATM 12367 O  O4  . MAN HA 5 .   ? -8.875  1.395   97.367  1.00 46.69  ? 509  MAN B O4  1 
HETATM 12368 O  O5  . MAN HA 5 .   ? -8.646  -1.640  99.450  1.00 47.68  ? 509  MAN B O5  1 
HETATM 12369 O  O6  . MAN HA 5 .   ? -7.617  -2.576  96.891  1.00 44.40  ? 509  MAN B O6  1 
HETATM 12370 C  C1  . NAG IA 4 .   ? 41.991  27.406  65.247  1.00 67.93  ? 501  NAG C C1  1 
HETATM 12371 C  C2  . NAG IA 4 .   ? 41.989  28.225  63.964  1.00 67.38  ? 501  NAG C C2  1 
HETATM 12372 C  C3  . NAG IA 4 .   ? 42.992  29.358  64.139  1.00 68.11  ? 501  NAG C C3  1 
HETATM 12373 C  C4  . NAG IA 4 .   ? 42.711  30.156  65.421  1.00 68.46  ? 501  NAG C C4  1 
HETATM 12374 C  C5  . NAG IA 4 .   ? 42.211  29.318  66.618  1.00 68.49  ? 501  NAG C C5  1 
HETATM 12375 C  C6  . NAG IA 4 .   ? 41.442  30.187  67.617  1.00 68.61  ? 501  NAG C C6  1 
HETATM 12376 C  C7  . NAG IA 4 .   ? 41.404  27.298  61.775  1.00 65.17  ? 501  NAG C C7  1 
HETATM 12377 C  C8  . NAG IA 4 .   ? 41.801  26.378  60.661  1.00 64.75  ? 501  NAG C C8  1 
HETATM 12378 N  N2  . NAG IA 4 .   ? 42.258  27.393  62.801  1.00 66.29  ? 501  NAG C N2  1 
HETATM 12379 O  O3  . NAG IA 4 .   ? 42.921  30.221  63.026  1.00 68.89  ? 501  NAG C O3  1 
HETATM 12380 O  O4  . NAG IA 4 .   ? 43.890  30.841  65.791  1.00 68.66  ? 501  NAG C O4  1 
HETATM 12381 O  O5  . NAG IA 4 .   ? 41.396  28.214  66.241  1.00 67.97  ? 501  NAG C O5  1 
HETATM 12382 O  O6  . NAG IA 4 .   ? 40.133  30.472  67.159  1.00 68.47  ? 501  NAG C O6  1 
HETATM 12383 O  O7  . NAG IA 4 .   ? 40.337  27.913  61.702  1.00 64.40  ? 501  NAG C O7  1 
HETATM 12384 CA CA  . CA  JA 2 .   ? 69.600  6.785   83.538  1.00 19.10  ? 502  CA  C CA  1 
HETATM 12385 C  C1  . PEG KA 7 .   ? 51.990  -9.985  66.408  1.00 28.83  ? 503  PEG C C1  1 
HETATM 12386 O  O1  . PEG KA 7 .   ? 51.517  -10.006 67.729  1.00 27.12  ? 503  PEG C O1  1 
HETATM 12387 C  C2  . PEG KA 7 .   ? 52.581  -9.594  65.119  1.00 20.42  ? 503  PEG C C2  1 
HETATM 12388 O  O2  . PEG KA 7 .   ? 52.328  -8.968  63.892  1.00 28.95  ? 503  PEG C O2  1 
HETATM 12389 C  C3  . PEG KA 7 .   ? 52.233  -10.269 63.342  1.00 24.52  ? 503  PEG C C3  1 
HETATM 12390 C  C4  . PEG KA 7 .   ? 52.619  -10.641 61.943  1.00 29.51  ? 503  PEG C C4  1 
HETATM 12391 O  O4  . PEG KA 7 .   ? 53.677  -10.006 61.215  1.00 21.02  ? 503  PEG C O4  1 
HETATM 12392 C  C1  . GOL LA 3 .   ? 44.783  12.695  93.582  1.00 28.50  ? 504  GOL C C1  1 
HETATM 12393 O  O1  . GOL LA 3 .   ? 43.383  13.040  93.588  1.00 26.05  ? 504  GOL C O1  1 
HETATM 12394 C  C2  . GOL LA 3 .   ? 45.284  11.263  93.928  1.00 26.31  ? 504  GOL C C2  1 
HETATM 12395 O  O2  . GOL LA 3 .   ? 46.673  11.349  94.445  1.00 26.35  ? 504  GOL C O2  1 
HETATM 12396 C  C3  . GOL LA 3 .   ? 45.026  10.121  92.862  1.00 29.09  ? 504  GOL C C3  1 
HETATM 12397 O  O3  . GOL LA 3 .   ? 45.181  8.627   93.081  1.00 13.49  ? 504  GOL C O3  1 
HETATM 12398 C  C1  . NAG MA 4 .   ? 54.720  -27.002 79.103  1.00 64.53  ? 505  NAG C C1  1 
HETATM 12399 C  C2  . NAG MA 4 .   ? 54.177  -27.943 78.040  1.00 63.99  ? 505  NAG C C2  1 
HETATM 12400 C  C3  . NAG MA 4 .   ? 53.492  -29.050 78.822  1.00 63.95  ? 505  NAG C C3  1 
HETATM 12401 C  C4  . NAG MA 4 .   ? 54.567  -29.798 79.623  1.00 64.20  ? 505  NAG C C4  1 
HETATM 12402 C  C5  . NAG MA 4 .   ? 55.626  -28.887 80.302  1.00 64.33  ? 505  NAG C C5  1 
HETATM 12403 C  C6  . NAG MA 4 .   ? 56.980  -29.599 80.399  1.00 64.11  ? 505  NAG C C6  1 
HETATM 12404 C  C7  . NAG MA 4 .   ? 53.505  -27.426 75.762  1.00 63.47  ? 505  NAG C C7  1 
HETATM 12405 C  C8  . NAG MA 4 .   ? 52.609  -26.644 74.847  1.00 62.78  ? 505  NAG C C8  1 
HETATM 12406 N  N2  . NAG MA 4 .   ? 53.322  -27.269 77.075  1.00 63.81  ? 505  NAG C N2  1 
HETATM 12407 O  O3  . NAG MA 4 .   ? 52.785  -29.919 77.964  1.00 63.48  ? 505  NAG C O3  1 
HETATM 12408 O  O4  . NAG MA 4 .   ? 53.921  -30.603 80.590  1.00 63.55  ? 505  NAG C O4  1 
HETATM 12409 O  O5  . NAG MA 4 .   ? 55.853  -27.620 79.684  1.00 64.29  ? 505  NAG C O5  1 
HETATM 12410 O  O6  . NAG MA 4 .   ? 57.710  -29.475 79.195  1.00 63.76  ? 505  NAG C O6  1 
HETATM 12411 O  O7  . NAG MA 4 .   ? 54.360  -28.173 75.281  1.00 63.42  ? 505  NAG C O7  1 
HETATM 12412 C  C1  . NAG NA 4 .   ? 43.305  21.714  93.057  1.00 18.08  ? 506  NAG C C1  1 
HETATM 12413 C  C2  . NAG NA 4 .   ? 42.105  22.586  93.376  1.00 17.89  ? 506  NAG C C2  1 
HETATM 12414 C  C3  . NAG NA 4 .   ? 42.546  23.630  94.392  1.00 21.25  ? 506  NAG C C3  1 
HETATM 12415 C  C4  . NAG NA 4 .   ? 43.195  22.927  95.592  1.00 21.65  ? 506  NAG C C4  1 
HETATM 12416 C  C5  . NAG NA 4 .   ? 44.255  21.891  95.145  1.00 21.34  ? 506  NAG C C5  1 
HETATM 12417 C  C6  . NAG NA 4 .   ? 44.895  21.036  96.234  1.00 21.74  ? 506  NAG C C6  1 
HETATM 12418 C  C7  . NAG NA 4 .   ? 40.396  22.866  91.684  1.00 18.00  ? 506  NAG C C7  1 
HETATM 12419 C  C8  . NAG NA 4 .   ? 39.951  23.682  90.504  1.00 15.56  ? 506  NAG C C8  1 
HETATM 12420 N  N2  . NAG NA 4 .   ? 41.603  23.157  92.146  1.00 16.52  ? 506  NAG C N2  1 
HETATM 12421 O  O3  . NAG NA 4 .   ? 41.401  24.358  94.757  1.00 19.16  ? 506  NAG C O3  1 
HETATM 12422 O  O4  . NAG NA 4 .   ? 43.770  23.941  96.396  1.00 26.50  ? 506  NAG C O4  1 
HETATM 12423 O  O5  . NAG NA 4 .   ? 43.695  20.989  94.200  1.00 17.96  ? 506  NAG C O5  1 
HETATM 12424 O  O6  . NAG NA 4 .   ? 43.913  20.685  97.170  1.00 25.28  ? 506  NAG C O6  1 
HETATM 12425 O  O7  . NAG NA 4 .   ? 39.667  21.987  92.173  1.00 18.86  ? 506  NAG C O7  1 
HETATM 12426 C  C1  . NAG OA 4 .   ? 55.008  -1.040  109.404 1.00 29.91  ? 507  NAG C C1  1 
HETATM 12427 C  C2  . NAG OA 4 .   ? 55.611  -0.286  110.578 1.00 30.33  ? 507  NAG C C2  1 
HETATM 12428 C  C3  . NAG OA 4 .   ? 55.457  -1.153  111.809 1.00 28.75  ? 507  NAG C C3  1 
HETATM 12429 C  C4  . NAG OA 4 .   ? 54.029  -1.717  111.909 1.00 27.54  ? 507  NAG C C4  1 
HETATM 12430 C  C5  . NAG OA 4 .   ? 53.437  -2.190  110.563 1.00 29.64  ? 507  NAG C C5  1 
HETATM 12431 C  C6  . NAG OA 4 .   ? 51.967  -2.653  110.584 1.00 28.64  ? 507  NAG C C6  1 
HETATM 12432 C  C7  . NAG OA 4 .   ? 57.337  1.345   110.195 1.00 32.41  ? 507  NAG C C7  1 
HETATM 12433 C  C8  . NAG OA 4 .   ? 58.801  1.619   109.997 1.00 32.26  ? 507  NAG C C8  1 
HETATM 12434 N  N2  . NAG OA 4 .   ? 57.002  0.068   110.345 1.00 31.73  ? 507  NAG C N2  1 
HETATM 12435 O  O3  . NAG OA 4 .   ? 55.779  -0.346  112.919 1.00 27.99  ? 507  NAG C O3  1 
HETATM 12436 O  O4  . NAG OA 4 .   ? 54.082  -2.797  112.814 1.00 25.96  ? 507  NAG C O4  1 
HETATM 12437 O  O5  . NAG OA 4 .   ? 53.614  -1.175  109.594 1.00 29.38  ? 507  NAG C O5  1 
HETATM 12438 O  O6  . NAG OA 4 .   ? 51.081  -1.588  110.867 1.00 28.28  ? 507  NAG C O6  1 
HETATM 12439 O  O7  . NAG OA 4 .   ? 56.504  2.262   110.215 1.00 34.13  ? 507  NAG C O7  1 
HETATM 12440 C  C1  . NAG PA 4 .   ? 53.502  -2.295  114.013 1.00 26.06  ? 508  NAG C C1  1 
HETATM 12441 C  C2  . NAG PA 4 .   ? 52.747  -3.388  114.765 1.00 24.03  ? 508  NAG C C2  1 
HETATM 12442 C  C3  . NAG PA 4 .   ? 52.127  -2.734  115.988 1.00 24.60  ? 508  NAG C C3  1 
HETATM 12443 C  C4  . NAG PA 4 .   ? 53.206  -2.001  116.795 1.00 26.37  ? 508  NAG C C4  1 
HETATM 12444 C  C5  . NAG PA 4 .   ? 53.957  -0.994  115.913 1.00 28.38  ? 508  NAG C C5  1 
HETATM 12445 C  C6  . NAG PA 4 .   ? 55.099  -0.302  116.653 1.00 29.06  ? 508  NAG C C6  1 
HETATM 12446 C  C7  . NAG PA 4 .   ? 51.798  -5.142  113.381 1.00 23.38  ? 508  NAG C C7  1 
HETATM 12447 C  C8  . NAG PA 4 .   ? 50.580  -5.670  112.661 1.00 21.90  ? 508  NAG C C8  1 
HETATM 12448 N  N2  . NAG PA 4 .   ? 51.694  -3.953  113.951 1.00 22.98  ? 508  NAG C N2  1 
HETATM 12449 O  O3  . NAG PA 4 .   ? 51.478  -3.704  116.765 1.00 18.94  ? 508  NAG C O3  1 
HETATM 12450 O  O4  . NAG PA 4 .   ? 52.598  -1.323  117.868 1.00 28.69  ? 508  NAG C O4  1 
HETATM 12451 O  O5  . NAG PA 4 .   ? 54.505  -1.721  114.836 1.00 28.14  ? 508  NAG C O5  1 
HETATM 12452 O  O6  . NAG PA 4 .   ? 56.024  -1.306  117.026 1.00 33.22  ? 508  NAG C O6  1 
HETATM 12453 O  O7  . NAG PA 4 .   ? 52.840  -5.783  113.420 1.00 23.01  ? 508  NAG C O7  1 
HETATM 12454 C  C1  . NAG QA 4 .   ? 42.602  23.856  98.912  1.00 77.26  ? 501  NAG D C1  1 
HETATM 12455 C  C2  . NAG QA 4 .   ? 43.459  25.043  99.331  1.00 76.78  ? 501  NAG D C2  1 
HETATM 12456 C  C3  . NAG QA 4 .   ? 42.793  25.713  100.531 1.00 77.14  ? 501  NAG D C3  1 
HETATM 12457 C  C4  . NAG QA 4 .   ? 41.333  26.073  100.213 1.00 77.52  ? 501  NAG D C4  1 
HETATM 12458 C  C5  . NAG QA 4 .   ? 40.587  24.927  99.500  1.00 77.44  ? 501  NAG D C5  1 
HETATM 12459 C  C6  . NAG QA 4 .   ? 39.246  25.382  98.933  1.00 77.06  ? 501  NAG D C6  1 
HETATM 12460 C  C7  . NAG QA 4 .   ? 45.809  24.646  98.705  1.00 74.95  ? 501  NAG D C7  1 
HETATM 12461 C  C8  . NAG QA 4 .   ? 46.032  25.893  97.894  1.00 74.93  ? 501  NAG D C8  1 
HETATM 12462 N  N2  . NAG QA 4 .   ? 44.826  24.636  99.611  1.00 75.95  ? 501  NAG D N2  1 
HETATM 12463 O  O3  . NAG QA 4 .   ? 43.507  26.872  100.896 1.00 77.26  ? 501  NAG D O3  1 
HETATM 12464 O  O4  . NAG QA 4 .   ? 40.663  26.429  101.408 1.00 77.65  ? 501  NAG D O4  1 
HETATM 12465 O  O5  . NAG QA 4 .   ? 41.366  24.369  98.450  1.00 77.44  ? 501  NAG D O5  1 
HETATM 12466 O  O6  . NAG QA 4 .   ? 39.435  26.040  97.700  1.00 76.93  ? 501  NAG D O6  1 
HETATM 12467 O  O7  . NAG QA 4 .   ? 46.539  23.676  98.532  1.00 74.73  ? 501  NAG D O7  1 
HETATM 12468 C  C1  . BMA RA 6 .   ? 52.717  -2.800  119.546 1.00 34.36  ? 502  BMA D C1  1 
HETATM 12469 C  C2  . BMA RA 6 .   ? 53.296  -1.894  120.618 1.00 34.73  ? 502  BMA D C2  1 
HETATM 12470 C  C3  . BMA RA 6 .   ? 52.819  -2.446  121.954 1.00 35.39  ? 502  BMA D C3  1 
HETATM 12471 C  C4  . BMA RA 6 .   ? 51.289  -2.625  121.999 1.00 35.76  ? 502  BMA D C4  1 
HETATM 12472 C  C5  . BMA RA 6 .   ? 50.728  -3.272  120.714 1.00 36.02  ? 502  BMA D C5  1 
HETATM 12473 C  C6  . BMA RA 6 .   ? 49.200  -3.297  120.626 1.00 36.63  ? 502  BMA D C6  1 
HETATM 12474 O  O2  . BMA RA 6 .   ? 52.836  -0.550  120.406 1.00 32.57  ? 502  BMA D O2  1 
HETATM 12475 O  O3  . BMA RA 6 .   ? 53.288  -1.591  123.000 1.00 35.77  ? 502  BMA D O3  1 
HETATM 12476 O  O4  . BMA RA 6 .   ? 50.969  -3.462  123.119 1.00 35.73  ? 502  BMA D O4  1 
HETATM 12477 O  O5  . BMA RA 6 .   ? 51.288  -2.686  119.534 1.00 35.85  ? 502  BMA D O5  1 
HETATM 12478 O  O6  . BMA RA 6 .   ? 48.588  -2.003  120.640 1.00 40.15  ? 502  BMA D O6  1 
HETATM 12479 C  C1  . MAN SA 5 .   ? 47.343  -1.556  120.866 1.00 45.64  ? 503  MAN D C1  1 
HETATM 12480 C  C2  . MAN SA 5 .   ? 47.128  -0.551  119.727 1.00 47.34  ? 503  MAN D C2  1 
HETATM 12481 C  C3  . MAN SA 5 .   ? 48.034  0.646   119.979 1.00 49.34  ? 503  MAN D C3  1 
HETATM 12482 C  C4  . MAN SA 5 .   ? 47.470  1.314   121.226 1.00 49.59  ? 503  MAN D C4  1 
HETATM 12483 C  C5  . MAN SA 5 .   ? 47.664  0.337   122.395 1.00 49.33  ? 503  MAN D C5  1 
HETATM 12484 C  C6  . MAN SA 5 .   ? 47.112  0.916   123.690 1.00 50.27  ? 503  MAN D C6  1 
HETATM 12485 O  O2  . MAN SA 5 .   ? 45.771  -0.078  119.660 1.00 45.55  ? 503  MAN D O2  1 
HETATM 12486 O  O3  . MAN SA 5 .   ? 48.132  1.524   118.844 1.00 50.44  ? 503  MAN D O3  1 
HETATM 12487 O  O4  . MAN SA 5 .   ? 48.101  2.581   121.438 1.00 51.98  ? 503  MAN D O4  1 
HETATM 12488 O  O5  . MAN SA 5 .   ? 47.031  -0.939  122.132 1.00 48.13  ? 503  MAN D O5  1 
HETATM 12489 O  O6  . MAN SA 5 .   ? 47.945  2.005   124.105 1.00 51.64  ? 503  MAN D O6  1 
HETATM 12490 CA CA  . CA  TA 2 .   ? 25.868  -1.427  121.409 1.00 19.83  ? 504  CA  D CA  1 
HETATM 12491 C  C1  . GOL UA 3 .   ? 15.427  9.160   98.313  1.00 30.52  ? 505  GOL D C1  1 
HETATM 12492 O  O1  . GOL UA 3 .   ? 15.486  9.586   96.941  1.00 29.28  ? 505  GOL D O1  1 
HETATM 12493 C  C2  . GOL UA 3 .   ? 14.996  7.691   98.578  1.00 30.94  ? 505  GOL D C2  1 
HETATM 12494 O  O2  . GOL UA 3 .   ? 14.444  7.603   99.933  1.00 26.46  ? 505  GOL D O2  1 
HETATM 12495 C  C3  . GOL UA 3 .   ? 16.138  6.642   98.226  1.00 29.67  ? 505  GOL D C3  1 
HETATM 12496 O  O3  . GOL UA 3 .   ? 15.988  5.171   97.998  1.00 17.66  ? 505  GOL D O3  1 
HETATM 12497 C  C1  . NAG VA 4 .   ? 31.313  -33.924 101.502 1.00 105.97 ? 506  NAG D C1  1 
HETATM 12498 C  C2  . NAG VA 4 .   ? 31.090  -34.167 102.993 1.00 105.82 ? 506  NAG D C2  1 
HETATM 12499 C  C3  . NAG VA 4 .   ? 29.953  -35.174 103.115 1.00 105.80 ? 506  NAG D C3  1 
HETATM 12500 C  C4  . NAG VA 4 .   ? 28.702  -34.560 102.487 1.00 105.86 ? 506  NAG D C4  1 
HETATM 12501 C  C5  . NAG VA 4 .   ? 28.974  -34.026 101.071 1.00 105.94 ? 506  NAG D C5  1 
HETATM 12502 C  C6  . NAG VA 4 .   ? 27.813  -33.173 100.568 1.00 105.96 ? 506  NAG D C6  1 
HETATM 12503 C  C7  . NAG VA 4 .   ? 33.116  -33.604 104.228 1.00 105.38 ? 506  NAG D C7  1 
HETATM 12504 C  C8  . NAG VA 4 .   ? 34.402  -33.308 103.509 1.00 105.18 ? 506  NAG D C8  1 
HETATM 12505 N  N2  . NAG VA 4 .   ? 32.318  -34.532 103.685 1.00 105.62 ? 506  NAG D N2  1 
HETATM 12506 O  O3  . NAG VA 4 .   ? 29.708  -35.509 104.460 1.00 105.79 ? 506  NAG D O3  1 
HETATM 12507 O  O4  . NAG VA 4 .   ? 27.681  -35.530 102.446 1.00 106.14 ? 506  NAG D O4  1 
HETATM 12508 O  O5  . NAG VA 4 .   ? 30.167  -33.252 101.005 1.00 105.80 ? 506  NAG D O5  1 
HETATM 12509 O  O6  . NAG VA 4 .   ? 27.802  -31.937 101.251 1.00 106.02 ? 506  NAG D O6  1 
HETATM 12510 O  O7  . NAG VA 4 .   ? 32.842  -33.001 105.267 1.00 105.21 ? 506  NAG D O7  1 
HETATM 12511 C  C1  . NAG WA 4 .   ? 15.935  18.409  98.899  1.00 21.26  ? 507  NAG D C1  1 
HETATM 12512 C  C2  . NAG WA 4 .   ? 15.556  19.480  97.892  1.00 21.20  ? 507  NAG D C2  1 
HETATM 12513 C  C3  . NAG WA 4 .   ? 14.536  20.404  98.563  1.00 22.92  ? 507  NAG D C3  1 
HETATM 12514 C  C4  . NAG WA 4 .   ? 13.388  19.603  99.199  1.00 24.39  ? 507  NAG D C4  1 
HETATM 12515 C  C5  . NAG WA 4 .   ? 13.935  18.410  100.008 1.00 24.57  ? 507  NAG D C5  1 
HETATM 12516 C  C6  . NAG WA 4 .   ? 12.848  17.549  100.650 1.00 25.95  ? 507  NAG D C6  1 
HETATM 12517 C  C7  . NAG WA 4 .   ? 17.228  20.013  96.174  1.00 18.12  ? 507  NAG D C7  1 
HETATM 12518 C  C8  . NAG WA 4 .   ? 18.462  20.806  95.824  1.00 18.23  ? 507  NAG D C8  1 
HETATM 12519 N  N2  . NAG WA 4 .   ? 16.773  20.133  97.421  1.00 17.25  ? 507  NAG D N2  1 
HETATM 12520 O  O3  . NAG WA 4 .   ? 14.033  21.277  97.585  1.00 25.45  ? 507  NAG D O3  1 
HETATM 12521 O  O4  . NAG WA 4 .   ? 12.545  20.437  100.002 1.00 26.82  ? 507  NAG D O4  1 
HETATM 12522 O  O5  . NAG WA 4 .   ? 14.812  17.616  99.208  1.00 22.46  ? 507  NAG D O5  1 
HETATM 12523 O  O6  . NAG WA 4 .   ? 12.140  16.820  99.674  1.00 26.17  ? 507  NAG D O6  1 
HETATM 12524 O  O7  . NAG WA 4 .   ? 16.687  19.305  95.312  1.00 17.05  ? 507  NAG D O7  1 
HETATM 12525 C  C1  . NAG XA 4 .   ? -0.323  -6.364  105.818 1.00 26.49  ? 508  NAG D C1  1 
HETATM 12526 C  C2  . NAG XA 4 .   ? -1.464  -5.646  106.516 1.00 26.57  ? 508  NAG D C2  1 
HETATM 12527 C  C3  . NAG XA 4 .   ? -2.711  -6.471  106.244 1.00 26.52  ? 508  NAG D C3  1 
HETATM 12528 C  C4  . NAG XA 4 .   ? -2.786  -6.905  104.760 1.00 26.71  ? 508  NAG D C4  1 
HETATM 12529 C  C5  . NAG XA 4 .   ? -1.448  -7.182  104.043 1.00 26.99  ? 508  NAG D C5  1 
HETATM 12530 C  C6  . NAG XA 4 .   ? -1.509  -7.254  102.513 1.00 26.49  ? 508  NAG D C6  1 
HETATM 12531 C  C7  . NAG XA 4 .   ? -0.948  -4.255  108.431 1.00 26.99  ? 508  NAG D C7  1 
HETATM 12532 C  C8  . NAG XA 4 .   ? -0.611  -4.182  109.896 1.00 26.89  ? 508  NAG D C8  1 
HETATM 12533 N  N2  . NAG XA 4 .   ? -1.182  -5.474  107.935 1.00 26.52  ? 508  NAG D N2  1 
HETATM 12534 O  O3  . NAG XA 4 .   ? -3.839  -5.689  106.595 1.00 23.99  ? 508  NAG D O3  1 
HETATM 12535 O  O4  . NAG XA 4 .   ? -3.578  -8.083  104.706 1.00 27.24  ? 508  NAG D O4  1 
HETATM 12536 O  O5  . NAG XA 4 .   ? -0.504  -6.214  104.425 1.00 26.84  ? 508  NAG D O5  1 
HETATM 12537 O  O6  . NAG XA 4 .   ? -1.745  -5.991  101.915 1.00 27.45  ? 508  NAG D O6  1 
HETATM 12538 O  O7  . NAG XA 4 .   ? -0.985  -3.232  107.742 1.00 26.08  ? 508  NAG D O7  1 
HETATM 12539 C  C1  . MAN YA 5 .   ? 46.752  3.564   117.436 1.00 68.18  ? 509  MAN D C1  1 
HETATM 12540 C  C2  . MAN YA 5 .   ? 46.889  4.050   118.879 1.00 68.49  ? 509  MAN D C2  1 
HETATM 12541 C  C3  . MAN YA 5 .   ? 46.050  5.293   119.194 1.00 68.61  ? 509  MAN D C3  1 
HETATM 12542 C  C4  . MAN YA 5 .   ? 44.806  5.443   118.296 1.00 68.24  ? 509  MAN D C4  1 
HETATM 12543 C  C5  . MAN YA 5 .   ? 45.049  5.104   116.809 1.00 67.97  ? 509  MAN D C5  1 
HETATM 12544 C  C6  . MAN YA 5 .   ? 44.800  6.260   115.836 1.00 67.59  ? 509  MAN D C6  1 
HETATM 12545 O  O2  . MAN YA 5 .   ? 48.281  4.268   119.160 1.00 68.30  ? 509  MAN D O2  1 
HETATM 12546 O  O3  . MAN YA 5 .   ? 46.874  6.469   119.122 1.00 68.86  ? 509  MAN D O3  1 
HETATM 12547 O  O4  . MAN YA 5 .   ? 43.748  4.630   118.834 1.00 67.30  ? 509  MAN D O4  1 
HETATM 12548 O  O5  . MAN YA 5 .   ? 46.374  4.628   116.568 1.00 68.20  ? 509  MAN D O5  1 
HETATM 12549 O  O6  . MAN YA 5 .   ? 44.809  7.550   116.464 1.00 67.46  ? 509  MAN D O6  1 
HETATM 12550 O  O   . HOH ZA 8 .   ? 27.033  14.117  45.899  1.00 20.75  ? 2301 HOH A O   1 
HETATM 12551 O  O   . HOH ZA 8 .   ? 41.439  2.439   33.061  1.00 26.79  ? 2302 HOH A O   1 
HETATM 12552 O  O   . HOH ZA 8 .   ? 10.760  13.737  47.696  1.00 35.96  ? 2303 HOH A O   1 
HETATM 12553 O  O   . HOH ZA 8 .   ? 41.764  -13.222 36.747  1.00 17.58  ? 2304 HOH A O   1 
HETATM 12554 O  O   . HOH ZA 8 .   ? 6.094   -0.417  49.737  1.00 44.64  ? 2305 HOH A O   1 
HETATM 12555 O  O   . HOH ZA 8 .   ? 24.922  18.202  45.482  1.00 40.39  ? 2306 HOH A O   1 
HETATM 12556 O  O   . HOH ZA 8 .   ? 28.931  -6.344  25.921  1.00 26.53  ? 2307 HOH A O   1 
HETATM 12557 O  O   . HOH ZA 8 .   ? 66.189  13.693  58.265  1.00 14.07  ? 2308 HOH A O   1 
HETATM 12558 O  O   . HOH ZA 8 .   ? 19.278  19.663  58.602  1.00 24.26  ? 2309 HOH A O   1 
HETATM 12559 O  O   . HOH ZA 8 .   ? 10.951  10.369  45.964  1.00 29.73  ? 2310 HOH A O   1 
HETATM 12560 O  O   . HOH ZA 8 .   ? 19.682  24.914  61.499  1.00 33.83  ? 2311 HOH A O   1 
HETATM 12561 O  O   . HOH ZA 8 .   ? 26.049  4.177   63.603  1.00 9.42   ? 2312 HOH A O   1 
HETATM 12562 O  O   . HOH ZA 8 .   ? 23.261  -22.462 43.513  1.00 30.67  ? 2313 HOH A O   1 
HETATM 12563 O  O   . HOH ZA 8 .   ? 55.359  9.614   54.203  1.00 29.52  ? 2314 HOH A O   1 
HETATM 12564 O  O   . HOH ZA 8 .   ? 35.206  9.694   56.442  1.00 11.75  ? 2315 HOH A O   1 
HETATM 12565 O  O   . HOH ZA 8 .   ? 10.706  -10.176 35.634  1.00 32.26  ? 2316 HOH A O   1 
HETATM 12566 O  O   . HOH ZA 8 .   ? 26.152  20.895  40.190  1.00 43.89  ? 2317 HOH A O   1 
HETATM 12567 O  O   . HOH ZA 8 .   ? 28.099  -11.844 56.466  1.00 9.98   ? 2318 HOH A O   1 
HETATM 12568 O  O   . HOH ZA 8 .   ? 37.111  5.034   68.969  1.00 10.27  ? 2319 HOH A O   1 
HETATM 12569 O  O   . HOH ZA 8 .   ? 36.976  4.693   51.165  1.00 30.79  ? 2320 HOH A O   1 
HETATM 12570 O  O   . HOH ZA 8 .   ? 66.031  11.172  65.675  1.00 21.57  ? 2321 HOH A O   1 
HETATM 12571 O  O   . HOH ZA 8 .   ? 56.241  7.348   55.837  1.00 25.59  ? 2322 HOH A O   1 
HETATM 12572 O  O   . HOH ZA 8 .   ? 19.117  16.874  45.239  1.00 33.53  ? 2323 HOH A O   1 
HETATM 12573 O  O   . HOH ZA 8 .   ? 41.436  -5.567  69.395  1.00 47.99  ? 2324 HOH A O   1 
HETATM 12574 O  O   . HOH ZA 8 .   ? 25.176  -9.095  67.320  1.00 21.63  ? 2325 HOH A O   1 
HETATM 12575 O  O   . HOH ZA 8 .   ? 44.881  -6.389  33.782  1.00 28.42  ? 2326 HOH A O   1 
HETATM 12576 O  O   . HOH ZA 8 .   ? 17.944  -17.140 42.546  1.00 39.61  ? 2327 HOH A O   1 
HETATM 12577 O  O   . HOH ZA 8 .   ? 25.101  1.867   24.988  1.00 21.72  ? 2328 HOH A O   1 
HETATM 12578 O  O   . HOH ZA 8 .   ? 30.321  1.868   54.093  1.00 9.06   ? 2329 HOH A O   1 
HETATM 12579 O  O   . HOH ZA 8 .   ? 37.294  -9.844  65.022  1.00 36.60  ? 2330 HOH A O   1 
HETATM 12580 O  O   . HOH ZA 8 .   ? 23.050  -0.079  42.224  1.00 12.28  ? 2331 HOH A O   1 
HETATM 12581 O  O   . HOH ZA 8 .   ? 25.045  4.846   48.376  1.00 10.90  ? 2332 HOH A O   1 
HETATM 12582 O  O   . HOH ZA 8 .   ? 19.796  8.684   64.742  1.00 11.91  ? 2333 HOH A O   1 
HETATM 12583 O  O   . HOH ZA 8 .   ? 30.655  -0.200  25.178  1.00 21.03  ? 2334 HOH A O   1 
HETATM 12584 O  O   . HOH ZA 8 .   ? 74.303  5.450   57.678  1.00 26.83  ? 2335 HOH A O   1 
HETATM 12585 O  O   . HOH ZA 8 .   ? 28.993  -2.910  25.674  1.00 26.50  ? 2336 HOH A O   1 
HETATM 12586 O  O   . HOH ZA 8 .   ? 24.569  -20.882 62.852  1.00 33.74  ? 2337 HOH A O   1 
HETATM 12587 O  O   . HOH ZA 8 .   ? 21.195  17.566  75.637  1.00 25.65  ? 2338 HOH A O   1 
HETATM 12588 O  O   . HOH ZA 8 .   ? 19.111  -5.054  65.652  1.00 12.32  ? 2339 HOH A O   1 
HETATM 12589 O  O   . HOH ZA 8 .   ? 27.060  20.011  67.936  1.00 13.80  ? 2340 HOH A O   1 
HETATM 12590 O  O   . HOH ZA 8 .   ? 12.351  15.802  69.754  1.00 16.46  ? 2341 HOH A O   1 
HETATM 12591 O  O   . HOH ZA 8 .   ? 19.504  8.940   36.898  1.00 14.03  ? 2342 HOH A O   1 
HETATM 12592 O  O   . HOH ZA 8 .   ? 28.647  -11.987 36.816  1.00 20.60  ? 2343 HOH A O   1 
HETATM 12593 O  O   . HOH ZA 8 .   ? 38.855  18.797  67.120  1.00 15.41  ? 2344 HOH A O   1 
HETATM 12594 O  O   . HOH ZA 8 .   ? 71.834  1.859   56.574  1.00 32.99  ? 2345 HOH A O   1 
HETATM 12595 O  O   . HOH ZA 8 .   ? 20.140  1.659   69.186  1.00 12.27  ? 2346 HOH A O   1 
HETATM 12596 O  O   . HOH ZA 8 .   ? 14.513  -5.258  27.138  1.00 35.21  ? 2347 HOH A O   1 
HETATM 12597 O  O   . HOH ZA 8 .   ? 20.185  -11.349 32.747  1.00 21.97  ? 2348 HOH A O   1 
HETATM 12598 O  O   . HOH ZA 8 .   ? 38.748  7.293   55.215  1.00 26.66  ? 2349 HOH A O   1 
HETATM 12599 O  O   . HOH ZA 8 .   ? 46.230  -1.216  60.061  1.00 11.01  ? 2350 HOH A O   1 
HETATM 12600 O  O   . HOH ZA 8 .   ? 29.512  -13.018 66.878  1.00 37.75  ? 2351 HOH A O   1 
HETATM 12601 O  O   . HOH ZA 8 .   ? 49.592  -13.351 64.984  1.00 15.46  ? 2352 HOH A O   1 
HETATM 12602 O  O   . HOH ZA 8 .   ? 24.708  -7.927  27.316  1.00 23.26  ? 2353 HOH A O   1 
HETATM 12603 O  O   . HOH ZA 8 .   ? 27.946  -10.377 51.210  1.00 10.75  ? 2354 HOH A O   1 
HETATM 12604 O  O   . HOH ZA 8 .   ? 32.662  -12.439 64.050  1.00 18.75  ? 2355 HOH A O   1 
HETATM 12605 O  O   . HOH ZA 8 .   ? 27.082  -9.439  71.329  1.00 25.93  ? 2356 HOH A O   1 
HETATM 12606 O  O   . HOH ZA 8 .   ? 15.105  -7.730  30.044  1.00 34.70  ? 2357 HOH A O   1 
HETATM 12607 O  O   . HOH ZA 8 .   ? 25.576  11.251  29.754  1.00 35.17  ? 2358 HOH A O   1 
HETATM 12608 O  O   . HOH ZA 8 .   ? 15.071  -19.484 58.379  1.00 33.75  ? 2359 HOH A O   1 
HETATM 12609 O  O   . HOH ZA 8 .   ? 66.589  8.896   56.209  1.00 26.07  ? 2360 HOH A O   1 
HETATM 12610 O  O   . HOH ZA 8 .   ? 48.525  -0.025  58.836  1.00 11.60  ? 2361 HOH A O   1 
HETATM 12611 O  O   . HOH ZA 8 .   ? 19.648  -9.715  28.662  1.00 30.71  ? 2362 HOH A O   1 
HETATM 12612 O  O   . HOH ZA 8 .   ? 33.389  -21.332 42.663  1.00 25.27  ? 2363 HOH A O   1 
HETATM 12613 O  O   . HOH ZA 8 .   ? 23.163  0.659   35.719  1.00 14.26  ? 2364 HOH A O   1 
HETATM 12614 O  O   . HOH ZA 8 .   ? 23.274  6.464   44.089  1.00 12.90  ? 2365 HOH A O   1 
HETATM 12615 O  O   . HOH ZA 8 .   ? 40.167  -17.527 55.435  1.00 13.31  ? 2366 HOH A O   1 
HETATM 12616 O  O   . HOH ZA 8 .   ? 30.136  -5.909  50.857  1.00 18.90  ? 2367 HOH A O   1 
HETATM 12617 O  O   . HOH ZA 8 .   ? 45.216  12.897  39.094  1.00 26.14  ? 2368 HOH A O   1 
HETATM 12618 O  O   . HOH ZA 8 .   ? 30.558  17.894  69.532  1.00 12.93  ? 2369 HOH A O   1 
HETATM 12619 O  O   . HOH ZA 8 .   ? 9.243   -3.129  54.881  1.00 15.34  ? 2370 HOH A O   1 
HETATM 12620 O  O   . HOH ZA 8 .   ? 19.182  24.503  69.890  1.00 25.91  ? 2371 HOH A O   1 
HETATM 12621 O  O   . HOH ZA 8 .   ? 12.339  -12.170 41.843  1.00 18.74  ? 2372 HOH A O   1 
HETATM 12622 O  O   . HOH ZA 8 .   ? 46.925  -17.831 59.970  1.00 19.52  ? 2373 HOH A O   1 
HETATM 12623 O  O   . HOH ZA 8 .   ? 14.432  -13.986 56.670  1.00 31.47  ? 2374 HOH A O   1 
HETATM 12624 O  O   . HOH ZA 8 .   ? 53.617  8.535   46.217  1.00 36.23  ? 2375 HOH A O   1 
HETATM 12625 O  O   . HOH ZA 8 .   ? 16.947  -13.872 32.923  1.00 29.98  ? 2376 HOH A O   1 
HETATM 12626 O  O   . HOH ZA 8 .   ? 21.849  -15.485 38.291  1.00 42.49  ? 2377 HOH A O   1 
HETATM 12627 O  O   . HOH ZA 8 .   ? 31.942  -7.732  28.396  1.00 25.67  ? 2378 HOH A O   1 
HETATM 12628 O  O   . HOH ZA 8 .   ? 21.538  -5.551  70.115  1.00 12.71  ? 2379 HOH A O   1 
HETATM 12629 O  O   . HOH ZA 8 .   ? 34.892  -22.717 39.471  1.00 27.85  ? 2380 HOH A O   1 
HETATM 12630 O  O   . HOH ZA 8 .   ? 18.533  13.244  72.596  1.00 9.76   ? 2381 HOH A O   1 
HETATM 12631 O  O   . HOH ZA 8 .   ? 24.399  12.434  52.963  1.00 12.15  ? 2382 HOH A O   1 
HETATM 12632 O  O   . HOH ZA 8 .   ? 34.945  -19.997 53.724  1.00 12.52  ? 2383 HOH A O   1 
HETATM 12633 O  O   . HOH ZA 8 .   ? 35.836  0.185   29.271  1.00 19.51  ? 2384 HOH A O   1 
HETATM 12634 O  O   . HOH ZA 8 .   ? 33.932  11.776  58.103  1.00 13.30  ? 2385 HOH A O   1 
HETATM 12635 O  O   . HOH ZA 8 .   ? 11.243  -18.496 45.420  1.00 23.63  ? 2386 HOH A O   1 
HETATM 12636 O  O   . HOH ZA 8 .   ? 14.769  9.222   38.991  1.00 33.34  ? 2387 HOH A O   1 
HETATM 12637 O  O   . HOH ZA 8 .   ? 40.882  1.532   39.799  1.00 14.47  ? 2388 HOH A O   1 
HETATM 12638 O  O   . HOH ZA 8 .   ? 8.988   7.304   58.136  1.00 14.46  ? 2389 HOH A O   1 
HETATM 12639 O  O   . HOH ZA 8 .   ? 5.324   -3.676  37.520  1.00 42.58  ? 2390 HOH A O   1 
HETATM 12640 O  O   . HOH ZA 8 .   ? 27.915  9.122   66.046  1.00 8.76   ? 2391 HOH A O   1 
HETATM 12641 O  O   . HOH ZA 8 .   ? 27.132  -6.139  33.944  1.00 19.25  ? 2392 HOH A O   1 
HETATM 12642 O  O   . HOH ZA 8 .   ? 21.600  -15.090 66.030  1.00 29.54  ? 2393 HOH A O   1 
HETATM 12643 O  O   . HOH ZA 8 .   ? 20.024  -25.256 49.012  1.00 39.29  ? 2394 HOH A O   1 
HETATM 12644 O  O   . HOH ZA 8 .   ? 52.758  -3.910  47.787  1.00 22.50  ? 2395 HOH A O   1 
HETATM 12645 O  O   . HOH ZA 8 .   ? 34.984  12.495  73.342  1.00 10.11  ? 2396 HOH A O   1 
HETATM 12646 O  O   . HOH ZA 8 .   ? 9.453   14.175  54.427  1.00 35.30  ? 2397 HOH A O   1 
HETATM 12647 O  O   . HOH ZA 8 .   ? 45.261  -10.191 69.742  1.00 19.11  ? 2398 HOH A O   1 
HETATM 12648 O  O   . HOH ZA 8 .   ? 40.197  -10.983 63.210  1.00 17.28  ? 2399 HOH A O   1 
HETATM 12649 O  O   . HOH ZA 8 .   ? 27.490  -7.523  27.708  1.00 28.01  ? 2400 HOH A O   1 
HETATM 12650 O  O   . HOH ZA 8 .   ? 32.530  -25.684 52.860  1.00 22.79  ? 2401 HOH A O   1 
HETATM 12651 O  O   . HOH ZA 8 .   ? 21.538  10.865  30.182  1.00 25.13  ? 2402 HOH A O   1 
HETATM 12652 O  O   . HOH ZA 8 .   ? 22.602  -20.443 54.895  1.00 17.20  ? 2403 HOH A O   1 
HETATM 12653 O  O   . HOH ZA 8 .   ? 45.132  -9.881  36.135  1.00 23.66  ? 2404 HOH A O   1 
HETATM 12654 O  O   . HOH ZA 8 .   ? 25.020  1.211   32.089  1.00 12.51  ? 2405 HOH A O   1 
HETATM 12655 O  O   . HOH ZA 8 .   ? 29.870  13.089  80.083  1.00 29.60  ? 2406 HOH A O   1 
HETATM 12656 O  O   . HOH ZA 8 .   ? 5.726   -2.356  56.647  1.00 16.54  ? 2407 HOH A O   1 
HETATM 12657 O  O   . HOH ZA 8 .   ? 2.785   -4.785  54.805  1.00 15.55  ? 2408 HOH A O   1 
HETATM 12658 O  O   . HOH ZA 8 .   ? 35.129  21.638  69.657  1.00 14.59  ? 2409 HOH A O   1 
HETATM 12659 O  O   . HOH ZA 8 .   ? 8.845   -6.716  43.606  1.00 20.98  ? 2410 HOH A O   1 
HETATM 12660 O  O   . HOH ZA 8 .   ? 19.645  4.958   62.395  1.00 8.86   ? 2411 HOH A O   1 
HETATM 12661 O  O   . HOH ZA 8 .   ? 26.748  -8.829  31.240  1.00 20.83  ? 2412 HOH A O   1 
HETATM 12662 O  O   . HOH ZA 8 .   ? 36.214  0.759   71.109  1.00 15.38  ? 2413 HOH A O   1 
HETATM 12663 O  O   . HOH ZA 8 .   ? 12.633  9.512   42.045  1.00 29.73  ? 2414 HOH A O   1 
HETATM 12664 O  O   . HOH ZA 8 .   ? 31.644  -1.764  79.072  1.00 27.42  ? 2415 HOH A O   1 
HETATM 12665 O  O   . HOH ZA 8 .   ? 0.673   -6.643  51.260  1.00 29.34  ? 2416 HOH A O   1 
HETATM 12666 O  O   . HOH ZA 8 .   ? 17.575  1.176   67.806  1.00 17.73  ? 2417 HOH A O   1 
HETATM 12667 O  O   . HOH ZA 8 .   ? 32.986  10.928  60.595  1.00 10.48  ? 2418 HOH A O   1 
HETATM 12668 O  O   . HOH ZA 8 .   ? 29.559  12.882  38.454  1.00 24.36  ? 2419 HOH A O   1 
HETATM 12669 O  O   . HOH ZA 8 .   ? 29.306  9.399   39.005  1.00 23.75  ? 2420 HOH A O   1 
HETATM 12670 O  O   . HOH ZA 8 .   ? 66.738  1.277   55.824  1.00 28.32  ? 2421 HOH A O   1 
HETATM 12671 O  O   . HOH ZA 8 .   ? 55.489  7.067   47.913  1.00 42.64  ? 2422 HOH A O   1 
HETATM 12672 O  O   . HOH ZA 8 .   ? 45.096  8.107   32.204  1.00 35.87  ? 2423 HOH A O   1 
HETATM 12673 O  O   . HOH ZA 8 .   ? 35.010  0.810   56.645  1.00 9.23   ? 2424 HOH A O   1 
HETATM 12674 O  O   . HOH ZA 8 .   ? 28.346  -4.805  71.546  1.00 14.81  ? 2425 HOH A O   1 
HETATM 12675 O  O   . HOH ZA 8 .   ? 8.935   -12.464 41.841  1.00 29.22  ? 2426 HOH A O   1 
HETATM 12676 O  O   . HOH ZA 8 .   ? 23.869  15.213  38.475  1.00 15.65  ? 2427 HOH A O   1 
HETATM 12677 O  O   . HOH ZA 8 .   ? 20.664  -9.084  36.111  1.00 14.03  ? 2428 HOH A O   1 
HETATM 12678 O  O   . HOH ZA 8 .   ? 15.269  8.822   41.786  1.00 14.25  ? 2429 HOH A O   1 
HETATM 12679 O  O   . HOH ZA 8 .   ? 27.514  6.556   64.880  1.00 13.71  ? 2430 HOH A O   1 
HETATM 12680 O  O   . HOH ZA 8 .   ? 32.001  12.164  45.709  1.00 18.74  ? 2431 HOH A O   1 
HETATM 12681 O  O   . HOH ZA 8 .   ? 40.221  -8.213  64.337  1.00 21.61  ? 2432 HOH A O   1 
HETATM 12682 O  O   . HOH ZA 8 .   ? 44.317  -16.133 65.209  1.00 27.48  ? 2433 HOH A O   1 
HETATM 12683 O  O   . HOH ZA 8 .   ? 10.018  1.052   34.016  1.00 31.97  ? 2434 HOH A O   1 
HETATM 12684 O  O   . HOH ZA 8 .   ? 40.738  -21.648 60.350  1.00 26.37  ? 2435 HOH A O   1 
HETATM 12685 O  O   . HOH ZA 8 .   ? 23.604  -17.309 68.234  1.00 34.23  ? 2436 HOH A O   1 
HETATM 12686 O  O   . HOH ZA 8 .   ? 24.191  5.500   27.003  1.00 33.33  ? 2437 HOH A O   1 
HETATM 12687 O  O   . HOH ZA 8 .   ? 34.216  18.654  60.387  1.00 12.86  ? 2438 HOH A O   1 
HETATM 12688 O  O   . HOH ZA 8 .   ? 13.587  -12.904 50.367  1.00 13.26  ? 2439 HOH A O   1 
HETATM 12689 O  O   . HOH ZA 8 .   ? 44.039  8.799   45.823  1.00 21.47  ? 2440 HOH A O   1 
HETATM 12690 O  O   . HOH ZA 8 .   ? 26.614  -5.524  45.683  1.00 9.80   ? 2441 HOH A O   1 
HETATM 12691 O  O   . HOH ZA 8 .   ? 22.931  22.598  59.324  1.00 23.63  ? 2442 HOH A O   1 
HETATM 12692 O  O   . HOH ZA 8 .   ? 37.877  -21.448 47.298  1.00 14.21  ? 2443 HOH A O   1 
HETATM 12693 O  O   . HOH ZA 8 .   ? 31.625  19.313  74.341  1.00 37.17  ? 2444 HOH A O   1 
HETATM 12694 O  O   . HOH ZA 8 .   ? 26.162  1.675   73.278  1.00 15.49  ? 2445 HOH A O   1 
HETATM 12695 O  O   . HOH ZA 8 .   ? 11.323  1.089   53.257  1.00 10.98  ? 2446 HOH A O   1 
HETATM 12696 O  O   . HOH ZA 8 .   ? 49.058  -20.004 53.118  1.00 26.96  ? 2447 HOH A O   1 
HETATM 12697 O  O   . HOH ZA 8 .   ? 43.554  5.132   66.206  1.00 9.50   ? 2448 HOH A O   1 
HETATM 12698 O  O   . HOH ZA 8 .   ? 38.386  2.985   49.774  1.00 18.40  ? 2449 HOH A O   1 
HETATM 12699 O  O   . HOH ZA 8 .   ? 22.788  21.510  52.428  1.00 35.30  ? 2450 HOH A O   1 
HETATM 12700 O  O   . HOH ZA 8 .   ? 22.168  -11.272 36.198  1.00 14.87  ? 2451 HOH A O   1 
HETATM 12701 O  O   . HOH ZA 8 .   ? 44.883  -3.246  36.371  1.00 23.65  ? 2452 HOH A O   1 
HETATM 12702 O  O   . HOH ZA 8 .   ? 34.821  13.463  54.072  1.00 25.05  ? 2453 HOH A O   1 
HETATM 12703 O  O   . HOH ZA 8 .   ? 39.903  12.067  60.689  1.00 21.77  ? 2454 HOH A O   1 
HETATM 12704 O  O   . HOH ZA 8 .   ? 8.653   3.738   51.910  1.00 22.21  ? 2455 HOH A O   1 
HETATM 12705 O  O   . HOH ZA 8 .   ? 37.124  12.261  39.633  1.00 30.38  ? 2456 HOH A O   1 
HETATM 12706 O  O   . HOH ZA 8 .   ? 31.308  -8.601  35.930  1.00 12.18  ? 2457 HOH A O   1 
HETATM 12707 O  O   . HOH ZA 8 .   ? 24.134  21.857  71.459  1.00 16.01  ? 2458 HOH A O   1 
HETATM 12708 O  O   . HOH ZA 8 .   ? 39.932  12.486  51.343  1.00 36.81  ? 2459 HOH A O   1 
HETATM 12709 O  O   . HOH ZA 8 .   ? 46.880  -3.146  39.619  1.00 20.77  ? 2460 HOH A O   1 
HETATM 12710 O  O   . HOH ZA 8 .   ? 16.125  12.527  59.943  1.00 16.89  ? 2461 HOH A O   1 
HETATM 12711 O  O   . HOH ZA 8 .   ? 55.707  -9.980  58.348  1.00 20.85  ? 2462 HOH A O   1 
HETATM 12712 O  O   . HOH ZA 8 .   ? 18.779  27.002  63.363  1.00 38.19  ? 2463 HOH A O   1 
HETATM 12713 O  O   . HOH ZA 8 .   ? 16.333  9.425   35.230  1.00 27.19  ? 2464 HOH A O   1 
HETATM 12714 O  O   . HOH ZA 8 .   ? 17.549  -18.766 59.971  1.00 16.97  ? 2465 HOH A O   1 
HETATM 12715 O  O   . HOH ZA 8 .   ? 32.317  -9.801  33.847  1.00 29.25  ? 2466 HOH A O   1 
HETATM 12716 O  O   . HOH ZA 8 .   ? 28.748  -5.326  54.417  1.00 10.42  ? 2467 HOH A O   1 
HETATM 12717 O  O   . HOH ZA 8 .   ? 20.666  -12.983 54.950  1.00 15.81  ? 2468 HOH A O   1 
HETATM 12718 O  O   . HOH ZA 8 .   ? 44.195  5.331   62.003  1.00 9.93   ? 2469 HOH A O   1 
HETATM 12719 O  O   . HOH ZA 8 .   ? 14.025  -4.889  33.376  1.00 24.11  ? 2470 HOH A O   1 
HETATM 12720 O  O   . HOH ZA 8 .   ? 27.696  20.189  50.261  1.00 26.84  ? 2471 HOH A O   1 
HETATM 12721 O  O   . HOH ZA 8 .   ? 51.281  -16.829 51.972  1.00 41.63  ? 2472 HOH A O   1 
HETATM 12722 O  O   . HOH ZA 8 .   ? 46.545  9.315   55.283  1.00 13.47  ? 2473 HOH A O   1 
HETATM 12723 O  O   . HOH ZA 8 .   ? 49.770  4.712   50.209  1.00 14.21  ? 2474 HOH A O   1 
HETATM 12724 O  O   . HOH ZA 8 .   ? 15.366  9.342   32.431  1.00 31.47  ? 2475 HOH A O   1 
HETATM 12725 O  O   . HOH ZA 8 .   ? 7.326   5.457   45.065  1.00 30.88  ? 2476 HOH A O   1 
HETATM 12726 O  O   . HOH ZA 8 .   ? 18.542  10.496  57.323  1.00 12.96  ? 2477 HOH A O   1 
HETATM 12727 O  O   . HOH ZA 8 .   ? 22.590  1.496   72.068  1.00 11.38  ? 2478 HOH A O   1 
HETATM 12728 O  O   . HOH ZA 8 .   ? 68.313  3.610   53.333  1.00 43.20  ? 2479 HOH A O   1 
HETATM 12729 O  O   . HOH ZA 8 .   ? 48.510  13.610  49.647  1.00 30.33  ? 2480 HOH A O   1 
HETATM 12730 O  O   . HOH ZA 8 .   ? 24.167  1.973   44.753  1.00 12.90  ? 2481 HOH A O   1 
HETATM 12731 O  O   . HOH ZA 8 .   ? 30.360  0.742   45.464  1.00 11.08  ? 2482 HOH A O   1 
HETATM 12732 O  O   . HOH ZA 8 .   ? 76.560  7.310   65.639  1.00 49.34  ? 2483 HOH A O   1 
HETATM 12733 O  O   . HOH ZA 8 .   ? 17.431  -5.243  24.965  1.00 17.84  ? 2484 HOH A O   1 
HETATM 12734 O  O   . HOH ZA 8 .   ? 39.702  17.917  56.095  1.00 37.25  ? 2485 HOH A O   1 
HETATM 12735 O  O   . HOH ZA 8 .   ? 34.244  -16.610 65.357  1.00 38.38  ? 2486 HOH A O   1 
HETATM 12736 O  O   . HOH ZA 8 .   ? 28.609  -8.384  35.048  1.00 14.36  ? 2487 HOH A O   1 
HETATM 12737 O  O   . HOH ZA 8 .   ? 30.736  -22.592 60.964  1.00 20.58  ? 2488 HOH A O   1 
HETATM 12738 O  O   . HOH ZA 8 .   ? 62.866  13.935  64.511  1.00 29.83  ? 2489 HOH A O   1 
HETATM 12739 O  O   . HOH ZA 8 .   ? 31.176  -11.542 70.853  1.00 42.13  ? 2490 HOH A O   1 
HETATM 12740 O  O   . HOH ZA 8 .   ? 20.876  6.074   24.891  1.00 30.69  ? 2491 HOH A O   1 
HETATM 12741 O  O   . HOH ZA 8 .   ? 30.208  4.066   39.446  1.00 14.81  ? 2492 HOH A O   1 
HETATM 12742 O  O   . HOH ZA 8 .   ? 43.410  11.340  43.989  1.00 35.75  ? 2493 HOH A O   1 
HETATM 12743 O  O   . HOH ZA 8 .   ? 27.943  11.505  46.008  1.00 13.58  ? 2494 HOH A O   1 
HETATM 12744 O  O   . HOH ZA 8 .   ? 24.827  1.822   37.729  1.00 14.77  ? 2495 HOH A O   1 
HETATM 12745 O  O   . HOH ZA 8 .   ? 41.537  -3.450  32.929  1.00 24.34  ? 2496 HOH A O   1 
HETATM 12746 O  O   . HOH ZA 8 .   ? 24.473  -14.874 37.581  1.00 39.53  ? 2497 HOH A O   1 
HETATM 12747 O  O   . HOH ZA 8 .   ? 30.334  -21.987 57.843  1.00 14.78  ? 2498 HOH A O   1 
HETATM 12748 O  O   . HOH ZA 8 .   ? 29.778  10.318  36.119  1.00 25.86  ? 2499 HOH A O   1 
HETATM 12749 O  O   . HOH ZA 8 .   ? 33.492  -0.422  25.428  1.00 19.59  ? 2500 HOH A O   1 
HETATM 12750 O  O   . HOH ZA 8 .   ? 9.718   -0.456  55.865  1.00 12.80  ? 2501 HOH A O   1 
HETATM 12751 O  O   . HOH ZA 8 .   ? 32.097  -14.772 54.186  1.00 15.14  ? 2502 HOH A O   1 
HETATM 12752 O  O   . HOH ZA 8 .   ? 49.194  9.185   42.163  1.00 34.76  ? 2503 HOH A O   1 
HETATM 12753 O  O   . HOH ZA 8 .   ? 13.607  -17.966 47.110  1.00 24.04  ? 2504 HOH A O   1 
HETATM 12754 O  O   . HOH ZA 8 .   ? 19.192  -14.137 58.655  1.00 22.19  ? 2505 HOH A O   1 
HETATM 12755 O  O   . HOH ZA 8 .   ? 41.137  -1.000  34.249  1.00 27.67  ? 2506 HOH A O   1 
HETATM 12756 O  O   . HOH ZA 8 .   ? 31.128  -12.523 56.969  1.00 12.90  ? 2507 HOH A O   1 
HETATM 12757 O  O   . HOH ZA 8 .   ? 20.200  16.584  37.992  1.00 29.86  ? 2508 HOH A O   1 
HETATM 12758 O  O   . HOH ZA 8 .   ? 34.502  26.926  65.595  1.00 21.92  ? 2509 HOH A O   1 
HETATM 12759 O  O   . HOH ZA 8 .   ? 29.891  20.287  37.085  1.00 42.27  ? 2510 HOH A O   1 
HETATM 12760 O  O   . HOH ZA 8 .   ? 30.664  -12.394 54.183  1.00 12.13  ? 2511 HOH A O   1 
HETATM 12761 O  O   . HOH ZA 8 .   ? 50.755  3.118   59.141  1.00 11.68  ? 2512 HOH A O   1 
HETATM 12762 O  O   . HOH ZA 8 .   ? 24.523  -13.440 41.917  1.00 18.93  ? 2513 HOH A O   1 
HETATM 12763 O  O   . HOH ZA 8 .   ? 37.164  -15.912 36.227  1.00 21.68  ? 2514 HOH A O   1 
HETATM 12764 O  O   . HOH ZA 8 .   ? 13.354  6.225   40.561  1.00 20.75  ? 2515 HOH A O   1 
HETATM 12765 O  O   . HOH ZA 8 .   ? 21.096  -18.453 53.930  1.00 15.95  ? 2516 HOH A O   1 
HETATM 12766 O  O   . HOH ZA 8 .   ? 22.738  -10.955 65.480  1.00 17.93  ? 2517 HOH A O   1 
HETATM 12767 O  O   . HOH ZA 8 .   ? 36.707  2.794   74.213  1.00 9.82   ? 2518 HOH A O   1 
HETATM 12768 O  O   . HOH ZA 8 .   ? 32.646  9.995   38.020  1.00 23.44  ? 2519 HOH A O   1 
HETATM 12769 O  O   . HOH ZA 8 .   ? 9.743   -4.419  57.450  1.00 13.85  ? 2520 HOH A O   1 
HETATM 12770 O  O   . HOH ZA 8 .   ? 38.289  2.055   47.303  1.00 12.23  ? 2521 HOH A O   1 
HETATM 12771 O  O   . HOH ZA 8 .   ? 10.689  12.961  56.629  1.00 33.32  ? 2522 HOH A O   1 
HETATM 12772 O  O   . HOH ZA 8 .   ? 33.376  -9.006  65.313  1.00 31.95  ? 2523 HOH A O   1 
HETATM 12773 O  O   . HOH ZA 8 .   ? 39.388  5.041   67.182  1.00 12.93  ? 2524 HOH A O   1 
HETATM 12774 O  O   . HOH ZA 8 .   ? 34.999  -9.244  48.841  1.00 15.48  ? 2525 HOH A O   1 
HETATM 12775 O  O   . HOH ZA 8 .   ? 28.140  11.879  72.273  1.00 10.62  ? 2526 HOH A O   1 
HETATM 12776 O  O   . HOH ZA 8 .   ? 29.268  21.227  66.563  1.00 13.03  ? 2527 HOH A O   1 
HETATM 12777 O  O   . HOH ZA 8 .   ? 16.034  -15.108 36.288  1.00 26.59  ? 2528 HOH A O   1 
HETATM 12778 O  O   . HOH ZA 8 .   ? 20.024  19.074  43.913  1.00 36.83  ? 2529 HOH A O   1 
HETATM 12779 O  O   . HOH ZA 8 .   ? 37.176  12.717  37.025  1.00 41.91  ? 2530 HOH A O   1 
HETATM 12780 O  O   . HOH ZA 8 .   ? 41.889  2.398   37.256  1.00 16.58  ? 2531 HOH A O   1 
HETATM 12781 O  O   . HOH ZA 8 .   ? 70.008  10.783  54.146  1.00 8.42   ? 2532 HOH A O   1 
HETATM 12782 O  O   . HOH ZA 8 .   ? 69.990  9.966   49.714  1.00 20.55  ? 2533 HOH A O   1 
HETATM 12783 O  O   . HOH ZA 8 .   ? 50.696  -13.901 53.608  1.00 21.62  ? 2534 HOH A O   1 
HETATM 12784 O  O   . HOH ZA 8 .   ? 37.141  -25.590 40.939  1.00 42.67  ? 2535 HOH A O   1 
HETATM 12785 O  O   . HOH ZA 8 .   ? 26.051  14.826  48.357  1.00 16.64  ? 2536 HOH A O   1 
HETATM 12786 O  O   . HOH ZA 8 .   ? 27.938  -12.092 64.898  1.00 32.54  ? 2537 HOH A O   1 
HETATM 12787 O  O   . HOH ZA 8 .   ? 20.253  -15.832 54.198  1.00 12.92  ? 2538 HOH A O   1 
HETATM 12788 O  O   . HOH ZA 8 .   ? 12.225  19.973  67.830  1.00 24.58  ? 2539 HOH A O   1 
HETATM 12789 O  O   . HOH ZA 8 .   ? 26.965  17.496  46.564  1.00 31.38  ? 2540 HOH A O   1 
HETATM 12790 O  O   . HOH ZA 8 .   ? 15.011  14.470  61.521  1.00 32.61  ? 2541 HOH A O   1 
HETATM 12791 O  O   . HOH ZA 8 .   ? 13.937  -22.154 56.000  1.00 43.63  ? 2542 HOH A O   1 
HETATM 12792 O  O   . HOH ZA 8 .   ? 53.302  -9.728  56.022  1.00 17.87  ? 2543 HOH A O   1 
HETATM 12793 O  O   . HOH ZA 8 .   ? 8.433   -18.140 42.735  1.00 46.40  ? 2544 HOH A O   1 
HETATM 12794 O  O   . HOH ZA 8 .   ? 16.851  -6.145  65.213  1.00 19.36  ? 2545 HOH A O   1 
HETATM 12795 O  O   . HOH ZA 8 .   ? 29.174  12.872  52.493  1.00 17.50  ? 2546 HOH A O   1 
HETATM 12796 O  O   . HOH ZA 8 .   ? 27.586  -9.836  68.596  1.00 16.61  ? 2547 HOH A O   1 
HETATM 12797 O  O   . HOH ZA 8 .   ? 36.099  22.657  61.676  1.00 37.15  ? 2548 HOH A O   1 
HETATM 12798 O  O   . HOH ZA 8 .   ? 41.863  -7.634  30.793  1.00 29.59  ? 2549 HOH A O   1 
HETATM 12799 O  O   . HOH ZA 8 .   ? 21.494  -17.237 42.598  1.00 26.65  ? 2550 HOH A O   1 
HETATM 12800 O  O   . HOH ZA 8 .   ? 21.550  16.253  79.946  1.00 32.35  ? 2551 HOH A O   1 
HETATM 12801 O  O   . HOH ZA 8 .   ? 15.937  -19.085 45.060  1.00 28.64  ? 2552 HOH A O   1 
HETATM 12802 O  O   . HOH ZA 8 .   ? 42.153  15.840  65.453  1.00 50.32  ? 2553 HOH A O   1 
HETATM 12803 O  O   . HOH ZA 8 .   ? 29.474  -7.301  71.442  1.00 25.86  ? 2554 HOH A O   1 
HETATM 12804 O  O   . HOH ZA 8 .   ? 26.158  -21.935 55.854  1.00 26.88  ? 2555 HOH A O   1 
HETATM 12805 O  O   . HOH ZA 8 .   ? 29.643  -10.932 62.921  1.00 14.30  ? 2556 HOH A O   1 
HETATM 12806 O  O   . HOH ZA 8 .   ? 16.064  17.127  32.216  1.00 31.02  ? 2557 HOH A O   1 
HETATM 12807 O  O   . HOH ZA 8 .   ? 33.599  10.519  48.521  1.00 16.81  ? 2558 HOH A O   1 
HETATM 12808 O  O   . HOH ZA 8 .   ? 20.895  14.694  32.564  1.00 30.81  ? 2559 HOH A O   1 
HETATM 12809 O  O   . HOH ZA 8 .   ? 43.914  -1.233  37.962  1.00 20.23  ? 2560 HOH A O   1 
HETATM 12810 O  O   . HOH ZA 8 .   ? 18.212  13.576  57.499  1.00 9.85   ? 2561 HOH A O   1 
HETATM 12811 O  O   . HOH ZA 8 .   ? 47.393  -20.289 58.673  1.00 33.52  ? 2562 HOH A O   1 
HETATM 12812 O  O   . HOH ZA 8 .   ? 7.950   2.853   48.613  1.00 17.05  ? 2563 HOH A O   1 
HETATM 12813 O  O   . HOH ZA 8 .   ? 45.826  13.801  57.783  1.00 32.77  ? 2564 HOH A O   1 
HETATM 12814 O  O   . HOH ZA 8 .   ? 28.847  8.739   28.298  1.00 27.13  ? 2565 HOH A O   1 
HETATM 12815 O  O   . HOH ZA 8 .   ? 31.516  11.994  34.096  1.00 33.11  ? 2566 HOH A O   1 
HETATM 12816 O  O   . HOH ZA 8 .   ? 42.721  -13.344 69.505  1.00 22.71  ? 2567 HOH A O   1 
HETATM 12817 O  O   . HOH ZA 8 .   ? 47.798  -10.077 37.734  1.00 29.34  ? 2568 HOH A O   1 
HETATM 12818 O  O   . HOH ZA 8 .   ? 46.481  -20.341 54.953  1.00 30.81  ? 2569 HOH A O   1 
HETATM 12819 O  O   . HOH ZA 8 .   ? 23.702  16.944  75.596  1.00 37.66  ? 2570 HOH A O   1 
HETATM 12820 O  O   . HOH ZA 8 .   ? 26.524  -23.156 52.300  1.00 24.36  ? 2571 HOH A O   1 
HETATM 12821 O  O   . HOH ZA 8 .   ? 17.399  18.088  61.405  1.00 14.12  ? 2572 HOH A O   1 
HETATM 12822 O  O   . HOH ZA 8 .   ? 10.903  10.632  48.757  1.00 19.75  ? 2573 HOH A O   1 
HETATM 12823 O  O   . HOH ZA 8 .   ? 34.773  -14.834 37.280  1.00 24.51  ? 2574 HOH A O   1 
HETATM 12824 O  O   . HOH ZA 8 .   ? 7.378   2.758   35.016  1.00 43.68  ? 2575 HOH A O   1 
HETATM 12825 O  O   . HOH ZA 8 .   ? 41.945  12.881  55.105  1.00 20.66  ? 2576 HOH A O   1 
HETATM 12826 O  O   . HOH ZA 8 .   ? 4.982   -17.448 55.863  1.00 24.34  ? 2577 HOH A O   1 
HETATM 12827 O  O   . HOH ZA 8 .   ? 27.534  15.250  50.599  1.00 15.94  ? 2578 HOH A O   1 
HETATM 12828 O  O   . HOH ZA 8 .   ? 32.723  9.927   51.180  1.00 20.03  ? 2579 HOH A O   1 
HETATM 12829 O  O   . HOH ZA 8 .   ? 8.330   9.423   53.953  1.00 27.99  ? 2580 HOH A O   1 
HETATM 12830 O  O   . HOH ZA 8 .   ? 15.496  12.698  41.635  1.00 33.85  ? 2581 HOH A O   1 
HETATM 12831 O  O   . HOH ZA 8 .   ? 28.815  -23.830 53.878  1.00 20.39  ? 2582 HOH A O   1 
HETATM 12832 O  O   . HOH ZA 8 .   ? 17.466  14.468  41.323  1.00 15.91  ? 2583 HOH A O   1 
HETATM 12833 O  O   . HOH ZA 8 .   ? 15.306  5.628   30.802  1.00 35.62  ? 2584 HOH A O   1 
HETATM 12834 O  O   . HOH ZA 8 .   ? 51.743  -2.754  41.404  1.00 33.72  ? 2585 HOH A O   1 
HETATM 12835 O  O   . HOH ZA 8 .   ? 29.395  6.222   27.312  1.00 41.77  ? 2586 HOH A O   1 
HETATM 12836 O  O   . HOH ZA 8 .   ? 39.070  -0.459  46.351  1.00 20.11  ? 2587 HOH A O   1 
HETATM 12837 O  O   . HOH ZA 8 .   ? 32.554  19.539  41.046  1.00 46.15  ? 2588 HOH A O   1 
HETATM 12838 O  O   . HOH ZA 8 .   ? 28.276  3.669   62.114  1.00 8.52   ? 2589 HOH A O   1 
HETATM 12839 O  O   . HOH ZA 8 .   ? 16.063  -12.072 56.324  1.00 19.68  ? 2590 HOH A O   1 
HETATM 12840 O  O   . HOH ZA 8 .   ? 74.929  13.956  65.657  1.00 27.78  ? 2591 HOH A O   1 
HETATM 12841 O  O   . HOH ZA 8 .   ? 73.808  11.694  69.304  1.00 21.63  ? 2592 HOH A O   1 
HETATM 12842 O  O   . HOH ZA 8 .   ? 32.916  12.574  55.504  1.00 16.24  ? 2593 HOH A O   1 
HETATM 12843 O  O   . HOH ZA 8 .   ? 41.836  -8.203  68.423  1.00 25.69  ? 2594 HOH A O   1 
HETATM 12844 O  O   . HOH ZA 8 .   ? 37.145  -2.118  47.005  1.00 11.03  ? 2595 HOH A O   1 
HETATM 12845 O  O   . HOH ZA 8 .   ? 17.407  9.395   39.133  1.00 22.88  ? 2596 HOH A O   1 
HETATM 12846 O  O   . HOH ZA 8 .   ? 24.454  15.429  56.169  1.00 15.35  ? 2597 HOH A O   1 
HETATM 12847 O  O   . HOH ZA 8 .   ? 26.827  15.812  55.081  1.00 14.54  ? 2598 HOH A O   1 
HETATM 12848 O  O   . HOH ZA 8 .   ? 64.592  9.001   58.517  1.00 37.08  ? 2599 HOH A O   1 
HETATM 12849 O  O   . HOH ZA 8 .   ? 8.336   -8.797  41.192  1.00 31.67  ? 2600 HOH A O   1 
HETATM 12850 O  O   . HOH ZA 8 .   ? 26.789  -4.808  74.501  1.00 51.76  ? 2601 HOH A O   1 
HETATM 12851 O  O   . HOH ZA 8 .   ? 19.081  17.056  48.090  1.00 28.55  ? 2602 HOH A O   1 
HETATM 12852 O  O   . HOH ZA 8 .   ? 44.723  13.420  54.065  1.00 25.07  ? 2603 HOH A O   1 
HETATM 12853 O  O   . HOH ZA 8 .   ? 5.505   -3.878  41.642  1.00 38.78  ? 2604 HOH A O   1 
HETATM 12854 O  O   . HOH ZA 8 .   ? 33.368  -18.630 37.120  1.00 30.03  ? 2605 HOH A O   1 
HETATM 12855 O  O   . HOH ZA 8 .   ? 24.085  23.886  55.931  1.00 33.42  ? 2606 HOH A O   1 
HETATM 12856 O  O   . HOH ZA 8 .   ? 16.387  20.435  63.581  1.00 22.74  ? 2607 HOH A O   1 
HETATM 12857 O  O   . HOH ZA 8 .   ? 4.885   5.280   53.685  1.00 27.61  ? 2608 HOH A O   1 
HETATM 12858 O  O   . HOH ZA 8 .   ? 41.395  -15.102 55.285  1.00 14.91  ? 2609 HOH A O   1 
HETATM 12859 O  O   . HOH ZA 8 .   ? 28.128  -28.868 47.399  1.00 29.51  ? 2610 HOH A O   1 
HETATM 12860 O  O   . HOH ZA 8 .   ? 51.766  -13.984 56.217  1.00 33.86  ? 2611 HOH A O   1 
HETATM 12861 O  O   . HOH ZA 8 .   ? 54.941  1.455   50.491  1.00 23.64  ? 2612 HOH A O   1 
HETATM 12862 O  O   . HOH ZA 8 .   ? 31.144  3.584   24.771  1.00 36.03  ? 2613 HOH A O   1 
HETATM 12863 O  O   . HOH ZA 8 .   ? 51.652  11.574  52.308  1.00 20.43  ? 2614 HOH A O   1 
HETATM 12864 O  O   . HOH ZA 8 .   ? 39.637  14.300  54.072  1.00 22.18  ? 2615 HOH A O   1 
HETATM 12865 O  O   . HOH ZA 8 .   ? 31.620  -5.671  71.134  1.00 19.79  ? 2616 HOH A O   1 
HETATM 12866 O  O   . HOH ZA 8 .   ? 19.987  27.314  67.161  1.00 42.68  ? 2617 HOH A O   1 
HETATM 12867 O  O   . HOH ZA 8 .   ? 37.246  -14.592 65.020  1.00 11.16  ? 2618 HOH A O   1 
HETATM 12868 O  O   . HOH ZA 8 .   ? 37.321  -17.400 66.159  1.00 38.32  ? 2619 HOH A O   1 
HETATM 12869 O  O   . HOH ZA 8 .   ? 12.202  -2.712  31.232  1.00 41.38  ? 2620 HOH A O   1 
HETATM 12870 O  O   . HOH ZA 8 .   ? 40.161  7.486   52.882  1.00 26.62  ? 2621 HOH A O   1 
HETATM 12871 O  O   . HOH ZA 8 .   ? 12.489  -6.346  62.573  1.00 12.13  ? 2622 HOH A O   1 
HETATM 12872 O  O   . HOH ZA 8 .   ? 32.690  24.015  73.467  1.00 43.45  ? 2623 HOH A O   1 
HETATM 12873 O  O   . HOH ZA 8 .   ? 2.420   -10.789 50.461  1.00 18.49  ? 2624 HOH A O   1 
HETATM 12874 O  O   . HOH ZA 8 .   ? 6.496   -2.183  35.403  1.00 38.88  ? 2625 HOH A O   1 
HETATM 12875 O  O   . HOH ZA 8 .   ? 6.677   1.783   46.931  1.00 25.50  ? 2626 HOH A O   1 
HETATM 12876 O  O   . HOH ZA 8 .   ? 49.354  12.197  54.548  1.00 17.02  ? 2627 HOH A O   1 
HETATM 12877 O  O   . HOH ZA 8 .   ? 50.169  10.492  47.935  1.00 30.18  ? 2628 HOH A O   1 
HETATM 12878 O  O   . HOH ZA 8 .   ? 7.528   7.471   55.408  1.00 25.89  ? 2629 HOH A O   1 
HETATM 12879 O  O   . HOH ZA 8 .   ? 24.189  4.483   45.804  1.00 10.83  ? 2630 HOH A O   1 
HETATM 12880 O  O   . HOH ZA 8 .   ? 19.680  8.687   25.959  1.00 28.38  ? 2631 HOH A O   1 
HETATM 12881 O  O   . HOH ZA 8 .   ? 19.430  19.678  55.869  1.00 35.00  ? 2632 HOH A O   1 
HETATM 12882 O  O   . HOH ZA 8 .   ? 15.422  17.733  49.640  1.00 46.01  ? 2633 HOH A O   1 
HETATM 12883 O  O   . HOH ZA 8 .   ? 56.830  11.559  53.302  1.00 40.68  ? 2634 HOH A O   1 
HETATM 12884 O  O   . HOH ZA 8 .   ? 20.459  -12.356 60.670  1.00 27.91  ? 2635 HOH A O   1 
HETATM 12885 O  O   . HOH ZA 8 .   ? 35.201  5.133   27.631  1.00 31.09  ? 2636 HOH A O   1 
HETATM 12886 O  O   . HOH ZA 8 .   ? 15.858  -21.722 62.568  1.00 23.43  ? 2637 HOH A O   1 
HETATM 12887 O  O   . HOH ZA 8 .   ? 42.349  -17.199 70.307  1.00 48.24  ? 2638 HOH A O   1 
HETATM 12888 O  O   . HOH ZA 8 .   ? 36.894  7.173   47.993  1.00 45.97  ? 2639 HOH A O   1 
HETATM 12889 O  O   . HOH ZA 8 .   ? 33.253  -14.575 35.004  1.00 36.26  ? 2640 HOH A O   1 
HETATM 12890 O  O   . HOH ZA 8 .   ? 28.362  19.299  70.340  1.00 12.10  ? 2641 HOH A O   1 
HETATM 12891 O  O   . HOH ZA 8 .   ? 30.509  13.752  54.697  1.00 18.07  ? 2642 HOH A O   1 
HETATM 12892 O  O   . HOH ZA 8 .   ? 1.900   -13.979 55.561  1.00 35.28  ? 2643 HOH A O   1 
HETATM 12893 O  O   . HOH ZA 8 .   ? 35.809  24.211  72.292  1.00 25.43  ? 2644 HOH A O   1 
HETATM 12894 O  O   . HOH ZA 8 .   ? 36.995  -9.290  32.015  1.00 24.31  ? 2645 HOH A O   1 
HETATM 12895 O  O   . HOH ZA 8 .   ? 71.043  1.978   54.188  1.00 34.17  ? 2646 HOH A O   1 
HETATM 12896 O  O   . HOH ZA 8 .   ? 26.437  4.426   25.563  1.00 31.92  ? 2647 HOH A O   1 
HETATM 12897 O  O   . HOH ZA 8 .   ? 5.410   -6.703  42.126  1.00 38.67  ? 2648 HOH A O   1 
HETATM 12898 O  O   . HOH ZA 8 .   ? 23.382  -15.240 40.528  1.00 29.60  ? 2649 HOH A O   1 
HETATM 12899 O  O   . HOH ZA 8 .   ? 51.378  -0.081  41.309  1.00 36.12  ? 2650 HOH A O   1 
HETATM 12900 O  O   . HOH ZA 8 .   ? 39.413  15.887  40.623  1.00 29.86  ? 2651 HOH A O   1 
HETATM 12901 O  O   . HOH ZA 8 .   ? 2.639   -4.547  45.160  1.00 37.78  ? 2652 HOH A O   1 
HETATM 12902 O  O   . HOH ZA 8 .   ? 40.411  12.886  33.293  1.00 26.73  ? 2653 HOH A O   1 
HETATM 12903 O  O   . HOH ZA 8 .   ? 55.302  -2.252  47.230  1.00 38.80  ? 2654 HOH A O   1 
HETATM 12904 O  O   . HOH ZA 8 .   ? 16.569  15.957  44.122  1.00 45.51  ? 2655 HOH A O   1 
HETATM 12905 O  O   . HOH ZA 8 .   ? 18.029  16.221  57.948  1.00 35.33  ? 2656 HOH A O   1 
HETATM 12906 O  O   . HOH ZA 8 .   ? 17.098  -10.231 29.032  1.00 43.35  ? 2657 HOH A O   1 
HETATM 12907 O  O   . HOH ZA 8 .   ? 17.595  16.646  50.866  1.00 44.98  ? 2658 HOH A O   1 
HETATM 12908 O  O   . HOH ZA 8 .   ? 43.819  14.887  61.849  1.00 31.31  ? 2659 HOH A O   1 
HETATM 12909 O  O   . HOH ZA 8 .   ? 12.350  14.408  58.117  1.00 35.33  ? 2660 HOH A O   1 
HETATM 12910 O  O   . HOH ZA 8 .   ? 45.770  12.299  43.327  1.00 34.88  ? 2661 HOH A O   1 
HETATM 12911 O  O   . HOH ZA 8 .   ? 30.462  13.734  48.116  1.00 33.64  ? 2662 HOH A O   1 
HETATM 12912 O  O   . HOH ZA 8 .   ? 16.639  17.941  52.362  1.00 43.73  ? 2663 HOH A O   1 
HETATM 12913 O  O   . HOH ZA 8 .   ? 14.559  -24.761 57.632  1.00 57.83  ? 2664 HOH A O   1 
HETATM 12914 O  O   . HOH ZA 8 .   ? 32.399  21.355  55.490  1.00 25.55  ? 2665 HOH A O   1 
HETATM 12915 O  O   . HOH ZA 8 .   ? 45.009  15.119  51.012  1.00 43.54  ? 2666 HOH A O   1 
HETATM 12916 O  O   . HOH ZA 8 .   ? 53.473  -12.567 56.980  1.00 52.01  ? 2667 HOH A O   1 
HETATM 12917 O  O   . HOH ZA 8 .   ? 18.211  -15.253 55.862  1.00 24.74  ? 2668 HOH A O   1 
HETATM 12918 O  O   . HOH ZA 8 .   ? 23.098  -6.838  75.298  1.00 30.53  ? 2669 HOH A O   1 
HETATM 12919 O  O   . HOH ZA 8 .   ? 32.281  14.865  39.107  1.00 37.59  ? 2670 HOH A O   1 
HETATM 12920 O  O   . HOH ZA 8 .   ? 39.576  -8.216  67.365  1.00 40.12  ? 2671 HOH A O   1 
HETATM 12921 O  O   . HOH ZA 8 .   ? 31.451  20.638  72.161  1.00 33.15  ? 2672 HOH A O   1 
HETATM 12922 O  O   . HOH ZA 8 .   ? 45.848  13.324  60.489  1.00 26.84  ? 2673 HOH A O   1 
HETATM 12923 O  O   . HOH ZA 8 .   ? 12.667  -15.207 51.967  1.00 31.49  ? 2674 HOH A O   1 
HETATM 12924 O  O   . HOH ZA 8 .   ? 46.384  11.917  55.989  1.00 20.21  ? 2675 HOH A O   1 
HETATM 12925 O  O   . HOH ZA 8 .   ? 42.817  0.086   35.761  1.00 23.94  ? 2676 HOH A O   1 
HETATM 12926 O  O   . HOH ZA 8 .   ? 15.462  15.944  37.852  1.00 31.86  ? 2677 HOH A O   1 
HETATM 12927 O  O   . HOH ZA 8 .   ? 42.260  -12.212 34.679  1.00 41.98  ? 2678 HOH A O   1 
HETATM 12928 O  O   . HOH ZA 8 .   ? 38.455  12.941  43.307  1.00 40.17  ? 2679 HOH A O   1 
HETATM 12929 O  O   . HOH ZA 8 .   ? 34.486  16.590  40.849  1.00 48.53  ? 2680 HOH A O   1 
HETATM 12930 O  O   . HOH ZA 8 .   ? 34.440  12.747  46.252  1.00 33.59  ? 2681 HOH A O   1 
HETATM 12931 O  O   . HOH ZA 8 .   ? 41.967  -18.346 65.477  1.00 41.22  ? 2682 HOH A O   1 
HETATM 12932 O  O   . HOH ZA 8 .   ? 19.965  -8.018  26.037  1.00 24.59  ? 2683 HOH A O   1 
HETATM 12933 O  O   . HOH ZA 8 .   ? 47.840  -20.968 45.722  1.00 42.83  ? 2684 HOH A O   1 
HETATM 12934 O  O   . HOH ZA 8 .   ? 9.975   11.574  61.227  1.00 29.70  ? 2685 HOH A O   1 
HETATM 12935 O  O   . HOH ZA 8 .   ? 76.294  5.641   63.577  1.00 37.42  ? 2686 HOH A O   1 
HETATM 12936 O  O   . HOH ZA 8 .   ? 22.933  25.094  57.794  1.00 44.84  ? 2687 HOH A O   1 
HETATM 12937 O  O   . HOH ZA 8 .   ? 20.602  -15.374 35.473  1.00 36.49  ? 2688 HOH A O   1 
HETATM 12938 O  O   . HOH ZA 8 .   ? 39.572  18.837  58.232  1.00 38.79  ? 2689 HOH A O   1 
HETATM 12939 O  O   . HOH ZA 8 .   ? 37.444  2.301   25.931  1.00 35.94  ? 2690 HOH A O   1 
HETATM 12940 O  O   . HOH ZA 8 .   ? 11.747  2.233   32.371  1.00 34.72  ? 2691 HOH A O   1 
HETATM 12941 O  O   . HOH ZA 8 .   ? 40.448  -21.435 62.825  1.00 43.75  ? 2692 HOH A O   1 
HETATM 12942 O  O   . HOH ZA 8 .   ? 34.683  21.868  56.706  1.00 34.94  ? 2693 HOH A O   1 
HETATM 12943 O  O   . HOH ZA 8 .   ? 28.958  -4.341  75.954  1.00 26.75  ? 2694 HOH A O   1 
HETATM 12944 O  O   . HOH ZA 8 .   ? 21.886  -13.030 34.448  1.00 33.69  ? 2695 HOH A O   1 
HETATM 12945 O  O   . HOH ZA 8 .   ? 31.563  -21.311 39.313  1.00 40.24  ? 2696 HOH A O   1 
HETATM 12946 O  O   . HOH ZA 8 .   ? 21.629  -8.978  67.378  1.00 33.38  ? 2697 HOH A O   1 
HETATM 12947 O  O   . HOH ZA 8 .   ? 37.596  -11.764 66.131  1.00 39.99  ? 2698 HOH A O   1 
HETATM 12948 O  O   . HOH ZA 8 .   ? 49.208  14.815  53.105  1.00 43.26  ? 2699 HOH A O   1 
HETATM 12949 O  O   . HOH ZA 8 .   ? 33.432  12.368  51.388  1.00 39.29  ? 2700 HOH A O   1 
HETATM 12950 O  O   . HOH ZA 8 .   ? 12.098  21.483  64.483  1.00 42.80  ? 2701 HOH A O   1 
HETATM 12951 O  O   . HOH ZA 8 .   ? 53.778  12.831  53.755  1.00 35.77  ? 2702 HOH A O   1 
HETATM 12952 O  O   . HOH ZA 8 .   ? 31.406  12.332  36.935  1.00 37.45  ? 2703 HOH A O   1 
HETATM 12953 O  O   . HOH ZA 8 .   ? 42.445  -22.878 49.312  1.00 32.94  ? 2704 HOH A O   1 
HETATM 12954 O  O   . HOH ZA 8 .   ? 14.750  -16.383 42.319  1.00 35.49  ? 2705 HOH A O   1 
HETATM 12955 O  O   . HOH ZA 8 .   ? 18.066  17.653  35.091  1.00 41.55  ? 2706 HOH A O   1 
HETATM 12956 O  O   . HOH ZA 8 .   ? 50.865  12.489  49.808  1.00 42.25  ? 2707 HOH A O   1 
HETATM 12957 O  O   . HOH ZA 8 .   ? 27.712  -10.695 32.818  1.00 39.44  ? 2708 HOH A O   1 
HETATM 12958 O  O   . HOH ZA 8 .   ? 31.169  21.247  39.581  1.00 57.82  ? 2709 HOH A O   1 
HETATM 12959 O  O   . HOH ZA 8 .   ? 23.486  16.481  35.752  1.00 50.41  ? 2710 HOH A O   1 
HETATM 12960 O  O   . HOH ZA 8 .   ? 23.727  20.100  43.403  1.00 44.09  ? 2711 HOH A O   1 
HETATM 12961 O  O   . HOH ZA 8 .   ? 30.104  14.872  50.229  1.00 24.94  ? 2712 HOH A O   1 
HETATM 12962 O  O   . HOH ZA 8 .   ? 12.423  -14.024 40.007  1.00 39.44  ? 2713 HOH A O   1 
HETATM 12963 O  O   . HOH ZA 8 .   ? 28.466  21.814  71.441  1.00 23.36  ? 2714 HOH A O   1 
HETATM 12964 O  O   . HOH ZA 8 .   ? 26.950  19.008  75.016  1.00 43.05  ? 2715 HOH A O   1 
HETATM 12965 O  O   . HOH ZA 8 .   ? 45.643  -8.711  34.142  1.00 46.42  ? 2716 HOH A O   1 
HETATM 12966 O  O   . HOH ZA 8 .   ? 35.350  21.038  59.702  1.00 26.95  ? 2717 HOH A O   1 
HETATM 12967 O  O   . HOH ZA 8 .   ? 47.533  -1.965  37.293  1.00 35.56  ? 2718 HOH A O   1 
HETATM 12968 O  O   . HOH ZA 8 .   ? 31.345  19.943  67.844  1.00 14.88  ? 2719 HOH A O   1 
HETATM 12969 O  O   . HOH ZA 8 .   ? 28.191  -14.538 36.681  1.00 27.29  ? 2720 HOH A O   1 
HETATM 12970 O  O   . HOH ZA 8 .   ? 26.206  -16.469 38.510  1.00 40.30  ? 2721 HOH A O   1 
HETATM 12971 O  O   . HOH ZA 8 .   ? 7.808   8.863   60.114  1.00 23.51  ? 2722 HOH A O   1 
HETATM 12972 O  O   . HOH ZA 8 .   ? 22.644  -19.902 41.740  1.00 31.09  ? 2723 HOH A O   1 
HETATM 12973 O  O   . HOH ZA 8 .   ? 21.962  -25.465 47.775  1.00 42.63  ? 2724 HOH A O   1 
HETATM 12974 O  O   . HOH ZA 8 .   ? 44.265  13.304  48.345  1.00 41.58  ? 2725 HOH A O   1 
HETATM 12975 O  O   . HOH ZA 8 .   ? 51.018  -19.872 50.148  1.00 48.70  ? 2726 HOH A O   1 
HETATM 12976 O  O   . HOH ZA 8 .   ? 17.698  -20.008 62.358  1.00 27.11  ? 2727 HOH A O   1 
HETATM 12977 O  O   . HOH ZA 8 .   ? 8.481   7.316   51.918  1.00 32.31  ? 2728 HOH A O   1 
HETATM 12978 O  O   . HOH ZA 8 .   ? 29.466  -12.607 34.022  1.00 51.41  ? 2729 HOH A O   1 
HETATM 12979 O  O   . HOH ZA 8 .   ? 51.406  -14.662 46.314  1.00 44.96  ? 2730 HOH A O   1 
HETATM 12980 O  O   . HOH ZA 8 .   ? 28.128  -23.187 56.545  1.00 21.68  ? 2731 HOH A O   1 
HETATM 12981 O  O   . HOH ZA 8 .   ? 24.554  19.223  75.863  1.00 43.74  ? 2732 HOH A O   1 
HETATM 12982 O  O   . HOH ZA 8 .   ? 39.236  6.309   51.223  1.00 31.26  ? 2733 HOH A O   1 
HETATM 12983 O  O   . HOH ZA 8 .   ? 30.508  21.279  74.847  1.00 42.27  ? 2734 HOH A O   1 
HETATM 12984 O  O   . HOH ZA 8 .   ? 23.109  1.399   22.024  1.00 32.92  ? 2735 HOH A O   1 
HETATM 12985 O  O   . HOH ZA 8 .   ? 31.912  14.435  52.209  1.00 33.06  ? 2736 HOH A O   1 
HETATM 12986 O  O   . HOH ZA 8 .   ? 36.848  3.362   71.307  1.00 11.79  ? 2737 HOH A O   1 
HETATM 12987 O  O   . HOH ZA 8 .   ? 32.392  21.454  69.861  1.00 18.47  ? 2738 HOH A O   1 
HETATM 12988 O  O   . HOH ZA 8 .   ? 20.420  -10.878 58.667  1.00 25.34  ? 2739 HOH A O   1 
HETATM 12989 O  O   . HOH ZA 8 .   ? 32.833  -16.541 37.496  1.00 49.93  ? 2740 HOH A O   1 
HETATM 12990 O  O   . HOH ZA 8 .   ? 16.435  -23.408 64.756  1.00 35.52  ? 2741 HOH A O   1 
HETATM 12991 O  O   . HOH ZA 8 .   ? 27.458  -12.065 67.545  1.00 38.48  ? 2742 HOH A O   1 
HETATM 12992 O  O   . HOH ZA 8 .   ? 20.665  22.262  58.377  1.00 38.41  ? 2743 HOH A O   1 
HETATM 12993 O  O   . HOH ZA 8 .   ? 28.695  -23.534 62.603  1.00 40.31  ? 2744 HOH A O   1 
HETATM 12994 O  O   . HOH ZA 8 .   ? 38.055  17.482  54.030  1.00 38.05  ? 2745 HOH A O   1 
HETATM 12995 O  O   . HOH ZA 8 .   ? 18.950  -12.259 56.918  1.00 18.58  ? 2746 HOH A O   1 
HETATM 12996 O  O   . HOH ZA 8 .   ? 1.303   -13.277 52.345  1.00 36.39  ? 2747 HOH A O   1 
HETATM 12997 O  O   . HOH ZA 8 .   ? 15.901  -21.489 46.594  1.00 41.81  ? 2748 HOH A O   1 
HETATM 12998 O  O   . HOH ZA 8 .   ? 28.961  23.961  67.450  1.00 26.52  ? 2749 HOH A O   1 
HETATM 12999 O  O   . HOH ZA 8 .   ? 37.374  14.184  41.295  1.00 32.02  ? 2750 HOH A O   1 
HETATM 13000 O  O   . HOH ZA 8 .   ? 24.329  8.069   27.294  1.00 26.54  ? 2751 HOH A O   1 
HETATM 13001 O  O   . HOH ZA 8 .   ? 50.461  12.366  57.041  1.00 27.11  ? 2752 HOH A O   1 
HETATM 13002 O  O   . HOH ZA 8 .   ? 37.733  20.976  58.496  1.00 41.62  ? 2753 HOH A O   1 
HETATM 13003 O  O   . HOH ZA 8 .   ? 4.944   6.985   55.451  1.00 25.20  ? 2754 HOH A O   1 
HETATM 13004 O  O   . HOH ZA 8 .   ? 51.551  -5.585  46.019  1.00 42.38  ? 2755 HOH A O   1 
HETATM 13005 O  O   . HOH ZA 8 .   ? 26.705  14.080  52.973  1.00 12.86  ? 2756 HOH A O   1 
HETATM 13006 O  O   . HOH ZA 8 .   ? 0.455   -16.936 55.169  1.00 45.97  ? 2757 HOH A O   1 
HETATM 13007 O  O   . HOH ZA 8 .   ? 8.680   9.264   49.460  1.00 45.94  ? 2758 HOH A O   1 
HETATM 13008 O  O   . HOH ZA 8 .   ? 31.000  23.904  69.677  1.00 34.47  ? 2759 HOH A O   1 
HETATM 13009 O  O   . HOH ZA 8 .   ? 33.451  17.474  51.182  1.00 42.64  ? 2760 HOH A O   1 
HETATM 13010 O  O   . HOH AB 8 .   ? -17.323 -8.332  66.898  1.00 28.18  ? 601  HOH B O   1 
HETATM 13011 O  O   . HOH AB 8 .   ? 6.321   8.158   92.225  1.00 14.29  ? 602  HOH B O   1 
HETATM 13012 O  O   . HOH AB 8 .   ? -4.316  -17.946 103.357 1.00 39.61  ? 603  HOH B O   1 
HETATM 13013 O  O   . HOH AB 8 .   ? -23.788 -15.676 78.867  1.00 33.04  ? 604  HOH B O   1 
HETATM 13014 O  O   . HOH AB 8 .   ? -11.563 -19.278 63.699  1.00 22.55  ? 605  HOH B O   1 
HETATM 13015 O  O   . HOH AB 8 .   ? -7.588  6.275   81.335  1.00 18.51  ? 606  HOH B O   1 
HETATM 13016 O  O   . HOH AB 8 .   ? 0.258   -2.184  99.759  1.00 16.92  ? 607  HOH B O   1 
HETATM 13017 O  O   . HOH AB 8 .   ? -2.650  15.221  85.418  1.00 30.41  ? 608  HOH B O   1 
HETATM 13018 O  O   . HOH AB 8 .   ? -8.125  -24.320 86.637  1.00 40.61  ? 609  HOH B O   1 
HETATM 13019 O  O   . HOH AB 8 .   ? -14.745 -21.389 88.130  1.00 27.34  ? 610  HOH B O   1 
HETATM 13020 O  O   . HOH AB 8 .   ? -23.748 -9.109  93.015  1.00 39.88  ? 611  HOH B O   1 
HETATM 13021 O  O   . HOH AB 8 .   ? 20.316  -7.372  87.268  1.00 9.73   ? 612  HOH B O   1 
HETATM 13022 O  O   . HOH AB 8 .   ? 15.487  22.545  87.154  1.00 34.26  ? 613  HOH B O   1 
HETATM 13023 O  O   . HOH AB 8 .   ? 11.877  0.742   82.609  1.00 11.57  ? 614  HOH B O   1 
HETATM 13024 O  O   . HOH AB 8 .   ? 3.700   1.436   51.989  1.00 24.42  ? 615  HOH B O   1 
HETATM 13025 O  O   . HOH AB 8 .   ? -10.772 -21.071 79.747  1.00 22.01  ? 616  HOH B O   1 
HETATM 13026 O  O   . HOH AB 8 .   ? -15.291 5.750   84.306  1.00 14.08  ? 617  HOH B O   1 
HETATM 13027 O  O   . HOH AB 8 .   ? 8.925   -25.148 86.256  1.00 15.69  ? 618  HOH B O   1 
HETATM 13028 O  O   . HOH AB 8 .   ? 18.421  -11.736 83.651  1.00 33.15  ? 619  HOH B O   1 
HETATM 13029 O  O   . HOH AB 8 .   ? 19.286  17.596  77.382  1.00 27.26  ? 620  HOH B O   1 
HETATM 13030 O  O   . HOH AB 8 .   ? 9.800   -5.413  62.437  1.00 14.05  ? 621  HOH B O   1 
HETATM 13031 O  O   . HOH AB 8 .   ? -3.118  -2.025  83.359  1.00 9.93   ? 622  HOH B O   1 
HETATM 13032 O  O   . HOH AB 8 .   ? 5.171   20.211  88.757  1.00 30.29  ? 623  HOH B O   1 
HETATM 13033 O  O   . HOH AB 8 .   ? 16.111  -15.267 76.167  1.00 21.41  ? 624  HOH B O   1 
HETATM 13034 O  O   . HOH AB 8 .   ? 3.085   -16.355 80.618  1.00 12.57  ? 625  HOH B O   1 
HETATM 13035 O  O   . HOH AB 8 .   ? -18.310 -5.962  93.374  1.00 42.44  ? 626  HOH B O   1 
HETATM 13036 O  O   . HOH AB 8 .   ? 7.465   7.648   68.815  1.00 21.21  ? 627  HOH B O   1 
HETATM 13037 O  O   . HOH AB 8 .   ? -14.022 -19.901 76.033  1.00 20.00  ? 628  HOH B O   1 
HETATM 13038 O  O   . HOH AB 8 .   ? 3.960   17.667  85.342  1.00 23.09  ? 629  HOH B O   1 
HETATM 13039 O  O   . HOH AB 8 .   ? 8.847   -22.398 68.566  1.00 15.55  ? 630  HOH B O   1 
HETATM 13040 O  O   . HOH AB 8 .   ? 5.669   13.784  69.035  1.00 39.92  ? 631  HOH B O   1 
HETATM 13041 O  O   . HOH AB 8 .   ? 20.810  -19.428 85.435  1.00 40.75  ? 632  HOH B O   1 
HETATM 13042 O  O   . HOH AB 8 .   ? 13.127  -18.092 56.938  1.00 32.66  ? 633  HOH B O   1 
HETATM 13043 O  O   . HOH AB 8 .   ? 8.376   -4.530  60.081  1.00 11.78  ? 634  HOH B O   1 
HETATM 13044 O  O   . HOH AB 8 .   ? -10.623 0.558   92.715  1.00 17.43  ? 635  HOH B O   1 
HETATM 13045 O  O   . HOH AB 8 .   ? 8.529   -16.597 80.670  1.00 14.10  ? 636  HOH B O   1 
HETATM 13046 O  O   . HOH AB 8 .   ? 3.175   -3.778  78.198  1.00 9.27   ? 637  HOH B O   1 
HETATM 13047 O  O   . HOH AB 8 .   ? 22.518  -10.853 81.829  1.00 24.86  ? 638  HOH B O   1 
HETATM 13048 O  O   . HOH AB 8 .   ? 8.074   -16.766 93.705  1.00 21.97  ? 639  HOH B O   1 
HETATM 13049 O  O   . HOH AB 8 .   ? -6.460  -31.155 73.676  1.00 32.75  ? 640  HOH B O   1 
HETATM 13050 O  O   . HOH AB 8 .   ? 1.679   -12.012 78.376  1.00 9.87   ? 641  HOH B O   1 
HETATM 13051 O  O   . HOH AB 8 .   ? -7.724  -1.347  85.028  1.00 10.64  ? 642  HOH B O   1 
HETATM 13052 O  O   . HOH AB 8 .   ? -6.020  -20.096 99.584  1.00 26.30  ? 643  HOH B O   1 
HETATM 13053 O  O   . HOH AB 8 .   ? 3.026   1.660   69.881  1.00 26.07  ? 644  HOH B O   1 
HETATM 13054 O  O   . HOH AB 8 .   ? 15.704  -7.984  89.679  1.00 16.15  ? 645  HOH B O   1 
HETATM 13055 O  O   . HOH AB 8 .   ? -3.887  -24.926 89.886  1.00 28.67  ? 646  HOH B O   1 
HETATM 13056 O  O   . HOH AB 8 .   ? -6.014  -19.851 96.146  1.00 19.17  ? 647  HOH B O   1 
HETATM 13057 O  O   . HOH AB 8 .   ? -6.852  3.089   97.495  1.00 37.85  ? 648  HOH B O   1 
HETATM 13058 O  O   . HOH AB 8 .   ? 8.935   -29.109 79.683  1.00 31.21  ? 649  HOH B O   1 
HETATM 13059 O  O   . HOH AB 8 .   ? -5.859  -28.842 82.120  1.00 37.14  ? 650  HOH B O   1 
HETATM 13060 O  O   . HOH AB 8 .   ? 3.854   4.546   73.340  1.00 11.67  ? 651  HOH B O   1 
HETATM 13061 O  O   . HOH AB 8 .   ? 20.846  16.281  87.523  1.00 25.38  ? 652  HOH B O   1 
HETATM 13062 O  O   . HOH AB 8 .   ? -13.841 -21.758 68.168  1.00 29.48  ? 653  HOH B O   1 
HETATM 13063 O  O   . HOH AB 8 .   ? 0.666   7.706   73.481  1.00 26.98  ? 654  HOH B O   1 
HETATM 13064 O  O   . HOH AB 8 .   ? -2.216  6.242   72.293  1.00 35.18  ? 655  HOH B O   1 
HETATM 13065 O  O   . HOH AB 8 .   ? -13.558 0.597   93.198  1.00 23.32  ? 656  HOH B O   1 
HETATM 13066 O  O   . HOH AB 8 .   ? -23.040 -0.558  90.746  1.00 43.31  ? 657  HOH B O   1 
HETATM 13067 O  O   . HOH AB 8 .   ? -21.077 -5.245  92.439  1.00 28.07  ? 658  HOH B O   1 
HETATM 13068 O  O   . HOH AB 8 .   ? 15.369  13.444  96.179  1.00 15.65  ? 659  HOH B O   1 
HETATM 13069 O  O   . HOH AB 8 .   ? 2.791   7.760   97.765  1.00 33.40  ? 660  HOH B O   1 
HETATM 13070 O  O   . HOH AB 8 .   ? -22.566 1.963   76.208  1.00 19.30  ? 661  HOH B O   1 
HETATM 13071 O  O   . HOH AB 8 .   ? -11.386 -20.603 86.129  1.00 20.09  ? 662  HOH B O   1 
HETATM 13072 O  O   . HOH AB 8 .   ? 13.106  5.918   80.806  1.00 10.81  ? 663  HOH B O   1 
HETATM 13073 O  O   . HOH AB 8 .   ? -1.368  -10.844 55.816  1.00 25.68  ? 664  HOH B O   1 
HETATM 13074 O  O   . HOH AB 8 .   ? 7.006   -17.909 88.078  1.00 11.29  ? 665  HOH B O   1 
HETATM 13075 O  O   . HOH AB 8 .   ? -12.813 -12.757 63.487  1.00 20.16  ? 666  HOH B O   1 
HETATM 13076 O  O   . HOH AB 8 .   ? -7.431  4.200   76.268  1.00 14.32  ? 667  HOH B O   1 
HETATM 13077 O  O   . HOH AB 8 .   ? -11.605 -4.882  78.144  1.00 9.80   ? 668  HOH B O   1 
HETATM 13078 O  O   . HOH AB 8 .   ? 13.272  -21.627 61.743  1.00 24.66  ? 669  HOH B O   1 
HETATM 13079 O  O   . HOH AB 8 .   ? -14.737 -16.143 63.307  1.00 31.23  ? 670  HOH B O   1 
HETATM 13080 O  O   . HOH AB 8 .   ? 18.684  11.374  90.111  1.00 10.91  ? 671  HOH B O   1 
HETATM 13081 O  O   . HOH AB 8 .   ? 7.560   6.629   75.587  1.00 9.02   ? 672  HOH B O   1 
HETATM 13082 O  O   . HOH AB 8 .   ? 2.501   -18.785 94.982  1.00 14.07  ? 673  HOH B O   1 
HETATM 13083 O  O   . HOH AB 8 .   ? -8.083  -8.152  85.435  1.00 11.88  ? 674  HOH B O   1 
HETATM 13084 O  O   . HOH AB 8 .   ? 16.444  -1.214  91.102  1.00 16.06  ? 675  HOH B O   1 
HETATM 13085 O  O   . HOH AB 8 .   ? -7.461  10.123  80.957  1.00 28.74  ? 676  HOH B O   1 
HETATM 13086 O  O   . HOH AB 8 .   ? 20.984  -11.884 63.353  1.00 19.65  ? 677  HOH B O   1 
HETATM 13087 O  O   . HOH AB 8 .   ? 11.986  5.327   88.886  1.00 9.56   ? 678  HOH B O   1 
HETATM 13088 O  O   . HOH AB 8 .   ? -14.588 -9.073  85.127  1.00 15.89  ? 679  HOH B O   1 
HETATM 13089 O  O   . HOH AB 8 .   ? 3.278   14.832  89.145  1.00 25.38  ? 680  HOH B O   1 
HETATM 13090 O  O   . HOH AB 8 .   ? -9.584  -23.670 62.882  1.00 28.91  ? 681  HOH B O   1 
HETATM 13091 O  O   . HOH AB 8 .   ? -16.792 -15.831 94.063  1.00 32.09  ? 682  HOH B O   1 
HETATM 13092 O  O   . HOH AB 8 .   ? 17.743  -0.588  88.581  1.00 9.54   ? 683  HOH B O   1 
HETATM 13093 O  O   . HOH AB 8 .   ? 16.458  -11.921 75.200  1.00 29.48  ? 684  HOH B O   1 
HETATM 13094 O  O   . HOH AB 8 .   ? 14.730  15.274  78.012  1.00 11.59  ? 685  HOH B O   1 
HETATM 13095 O  O   . HOH AB 8 .   ? 17.355  -16.005 59.076  1.00 21.51  ? 686  HOH B O   1 
HETATM 13096 O  O   . HOH AB 8 .   ? -19.951 -1.307  63.745  1.00 34.12  ? 687  HOH B O   1 
HETATM 13097 O  O   . HOH AB 8 .   ? 17.125  2.602   71.523  1.00 13.79  ? 688  HOH B O   1 
HETATM 13098 O  O   . HOH AB 8 .   ? -20.506 -10.868 72.513  1.00 21.69  ? 689  HOH B O   1 
HETATM 13099 O  O   . HOH AB 8 .   ? -14.664 -16.057 81.299  1.00 18.69  ? 690  HOH B O   1 
HETATM 13100 O  O   . HOH AB 8 .   ? 16.632  -24.224 83.885  1.00 28.11  ? 691  HOH B O   1 
HETATM 13101 O  O   . HOH AB 8 .   ? -14.876 -2.181  61.279  1.00 25.93  ? 692  HOH B O   1 
HETATM 13102 O  O   . HOH AB 8 .   ? -18.691 5.032   77.881  1.00 26.81  ? 693  HOH B O   1 
HETATM 13103 O  O   . HOH AB 8 .   ? 11.256  -18.093 89.344  1.00 32.06  ? 694  HOH B O   1 
HETATM 13104 O  O   . HOH AB 8 .   ? 4.636   -9.715  105.971 1.00 15.04  ? 695  HOH B O   1 
HETATM 13105 O  O   . HOH AB 8 .   ? 12.588  3.278   81.217  1.00 10.76  ? 696  HOH B O   1 
HETATM 13106 O  O   . HOH AB 8 .   ? 1.658   -27.902 70.955  1.00 13.57  ? 697  HOH B O   1 
HETATM 13107 O  O   . HOH AB 8 .   ? -6.132  -5.669  84.335  1.00 11.71  ? 698  HOH B O   1 
HETATM 13108 O  O   . HOH AB 8 .   ? -11.833 -23.643 74.952  1.00 26.87  ? 699  HOH B O   1 
HETATM 13109 O  O   . HOH AB 8 .   ? 6.427   18.628  72.218  1.00 32.43  ? 700  HOH B O   1 
HETATM 13110 O  O   . HOH AB 8 .   ? 2.189   -4.387  97.200  1.00 14.39  ? 701  HOH B O   1 
HETATM 13111 O  O   . HOH AB 8 .   ? 10.357  1.202   88.965  1.00 9.63   ? 702  HOH B O   1 
HETATM 13112 O  O   . HOH AB 8 .   ? 5.772   14.167  74.232  1.00 14.68  ? 703  HOH B O   1 
HETATM 13113 O  O   . HOH AB 8 .   ? 8.135   22.880  83.041  1.00 34.40  ? 704  HOH B O   1 
HETATM 13114 O  O   . HOH AB 8 .   ? -8.740  -10.884 102.925 1.00 36.86  ? 705  HOH B O   1 
HETATM 13115 O  O   . HOH AB 8 .   ? -11.230 -2.270  94.801  1.00 17.91  ? 706  HOH B O   1 
HETATM 13116 O  O   . HOH AB 8 .   ? 15.199  -26.226 77.924  1.00 23.57  ? 707  HOH B O   1 
HETATM 13117 O  O   . HOH AB 8 .   ? 20.117  -1.015  72.512  1.00 13.14  ? 708  HOH B O   1 
HETATM 13118 O  O   . HOH AB 8 .   ? -18.325 -9.476  83.216  1.00 10.18  ? 709  HOH B O   1 
HETATM 13119 O  O   . HOH AB 8 .   ? -10.226 -25.214 71.477  1.00 23.37  ? 710  HOH B O   1 
HETATM 13120 O  O   . HOH AB 8 .   ? 2.759   3.757   62.075  1.00 15.59  ? 711  HOH B O   1 
HETATM 13121 O  O   . HOH AB 8 .   ? 10.255  1.417   64.438  1.00 11.31  ? 712  HOH B O   1 
HETATM 13122 O  O   . HOH AB 8 .   ? -13.047 -17.964 79.757  1.00 15.20  ? 713  HOH B O   1 
HETATM 13123 O  O   . HOH AB 8 .   ? -22.347 -0.132  86.176  1.00 17.72  ? 714  HOH B O   1 
HETATM 13124 O  O   . HOH AB 8 .   ? -10.634 -22.721 66.774  1.00 20.11  ? 715  HOH B O   1 
HETATM 13125 O  O   . HOH AB 8 .   ? 12.670  16.569  96.477  1.00 33.44  ? 716  HOH B O   1 
HETATM 13126 O  O   . HOH AB 8 .   ? 1.952   4.194   53.321  1.00 24.75  ? 717  HOH B O   1 
HETATM 13127 O  O   . HOH AB 8 .   ? 15.370  -9.017  91.896  1.00 21.37  ? 718  HOH B O   1 
HETATM 13128 O  O   . HOH AB 8 .   ? 15.298  2.345   69.227  1.00 11.92  ? 719  HOH B O   1 
HETATM 13129 O  O   . HOH AB 8 .   ? 21.531  -6.318  80.497  1.00 12.18  ? 720  HOH B O   1 
HETATM 13130 O  O   . HOH AB 8 .   ? 6.356   -17.596 77.987  1.00 11.42  ? 721  HOH B O   1 
HETATM 13131 O  O   . HOH AB 8 .   ? -3.958  0.146   53.183  1.00 34.52  ? 722  HOH B O   1 
HETATM 13132 O  O   . HOH AB 8 .   ? 4.632   -8.172  99.387  1.00 11.83  ? 723  HOH B O   1 
HETATM 13133 O  O   . HOH AB 8 .   ? 14.312  2.035   65.156  1.00 11.60  ? 724  HOH B O   1 
HETATM 13134 O  O   . HOH AB 8 .   ? -12.898 -7.534  83.645  1.00 12.10  ? 725  HOH B O   1 
HETATM 13135 O  O   . HOH AB 8 .   ? 1.556   12.151  68.760  1.00 28.50  ? 726  HOH B O   1 
HETATM 13136 O  O   . HOH AB 8 .   ? 10.994  9.987   95.823  1.00 37.56  ? 727  HOH B O   1 
HETATM 13137 O  O   . HOH AB 8 .   ? 5.956   -4.115  73.563  1.00 10.08  ? 728  HOH B O   1 
HETATM 13138 O  O   . HOH AB 8 .   ? -12.241 -18.080 77.093  1.00 13.67  ? 729  HOH B O   1 
HETATM 13139 O  O   . HOH AB 8 .   ? -4.802  4.242   61.159  1.00 34.10  ? 730  HOH B O   1 
HETATM 13140 O  O   . HOH AB 8 .   ? -4.768  -5.039  101.362 1.00 62.10  ? 731  HOH B O   1 
HETATM 13141 O  O   . HOH AB 8 .   ? -23.962 -2.309  76.973  1.00 14.28  ? 732  HOH B O   1 
HETATM 13142 O  O   . HOH AB 8 .   ? 19.657  10.690  73.751  1.00 11.00  ? 733  HOH B O   1 
HETATM 13143 O  O   . HOH AB 8 .   ? 7.274   -25.220 59.775  1.00 36.38  ? 734  HOH B O   1 
HETATM 13144 O  O   . HOH AB 8 .   ? 4.940   6.847   74.612  1.00 9.81   ? 735  HOH B O   1 
HETATM 13145 O  O   . HOH AB 8 .   ? 19.890  -23.945 79.179  1.00 48.77  ? 736  HOH B O   1 
HETATM 13146 O  O   . HOH AB 8 .   ? 18.752  9.920   80.647  1.00 9.24   ? 737  HOH B O   1 
HETATM 13147 O  O   . HOH AB 8 .   ? -13.353 0.011   78.947  1.00 15.38  ? 738  HOH B O   1 
HETATM 13148 O  O   . HOH AB 8 .   ? -6.841  3.858   80.370  1.00 9.98   ? 739  HOH B O   1 
HETATM 13149 O  O   . HOH AB 8 .   ? 18.168  -17.752 87.209  1.00 26.06  ? 740  HOH B O   1 
HETATM 13150 O  O   . HOH AB 8 .   ? -22.874 -1.425  81.560  1.00 20.24  ? 741  HOH B O   1 
HETATM 13151 O  O   . HOH AB 8 .   ? 24.048  -5.917  81.936  1.00 41.78  ? 742  HOH B O   1 
HETATM 13152 O  O   . HOH AB 8 .   ? 15.775  19.653  84.503  1.00 14.69  ? 743  HOH B O   1 
HETATM 13153 O  O   . HOH AB 8 .   ? 6.881   12.780  93.758  1.00 38.28  ? 744  HOH B O   1 
HETATM 13154 O  O   . HOH AB 8 .   ? -16.050 0.276   78.628  1.00 21.64  ? 745  HOH B O   1 
HETATM 13155 O  O   . HOH AB 8 .   ? 14.107  19.001  73.491  1.00 14.12  ? 746  HOH B O   1 
HETATM 13156 O  O   . HOH AB 8 .   ? 14.121  21.749  89.080  1.00 34.59  ? 747  HOH B O   1 
HETATM 13157 O  O   . HOH AB 8 .   ? -11.058 1.497   95.625  1.00 30.15  ? 748  HOH B O   1 
HETATM 13158 O  O   . HOH AB 8 .   ? -16.905 -19.549 81.752  1.00 25.80  ? 749  HOH B O   1 
HETATM 13159 O  O   . HOH AB 8 .   ? 8.552   -20.101 90.729  1.00 20.83  ? 750  HOH B O   1 
HETATM 13160 O  O   . HOH AB 8 .   ? -5.403  7.763   82.421  1.00 13.92  ? 751  HOH B O   1 
HETATM 13161 O  O   . HOH AB 8 .   ? 5.013   -10.549 79.889  1.00 9.35   ? 752  HOH B O   1 
HETATM 13162 O  O   . HOH AB 8 .   ? -5.099  -6.710  78.015  1.00 9.59   ? 753  HOH B O   1 
HETATM 13163 O  O   . HOH AB 8 .   ? -1.133  -3.552  70.261  1.00 17.74  ? 754  HOH B O   1 
HETATM 13164 O  O   . HOH AB 8 .   ? -19.027 1.224   72.110  1.00 23.62  ? 755  HOH B O   1 
HETATM 13165 O  O   . HOH AB 8 .   ? 6.899   -19.902 76.509  1.00 12.06  ? 756  HOH B O   1 
HETATM 13166 O  O   . HOH AB 8 .   ? -12.060 -18.380 87.721  1.00 13.91  ? 757  HOH B O   1 
HETATM 13167 O  O   . HOH AB 8 .   ? 21.760  0.415   82.639  1.00 21.52  ? 758  HOH B O   1 
HETATM 13168 O  O   . HOH AB 8 .   ? -15.522 -10.877 67.189  1.00 22.74  ? 759  HOH B O   1 
HETATM 13169 O  O   . HOH AB 8 .   ? 14.550  -25.174 68.232  1.00 24.03  ? 760  HOH B O   1 
HETATM 13170 O  O   . HOH AB 8 .   ? -6.351  -8.730  53.289  1.00 30.96  ? 761  HOH B O   1 
HETATM 13171 O  O   . HOH AB 8 .   ? 19.067  -19.841 71.027  1.00 34.18  ? 762  HOH B O   1 
HETATM 13172 O  O   . HOH AB 8 .   ? -14.159 -0.005  75.587  1.00 20.69  ? 763  HOH B O   1 
HETATM 13173 O  O   . HOH AB 8 .   ? -15.369 -0.431  88.518  1.00 13.87  ? 764  HOH B O   1 
HETATM 13174 O  O   . HOH AB 8 .   ? -6.387  -24.280 92.166  1.00 40.45  ? 765  HOH B O   1 
HETATM 13175 O  O   . HOH AB 8 .   ? 8.402   16.502  92.107  1.00 19.96  ? 766  HOH B O   1 
HETATM 13176 O  O   . HOH AB 8 .   ? 5.080   -32.046 84.718  1.00 40.43  ? 767  HOH B O   1 
HETATM 13177 O  O   . HOH AB 8 .   ? -9.289  -1.986  58.781  1.00 28.82  ? 768  HOH B O   1 
HETATM 13178 O  O   . HOH AB 8 .   ? -21.029 -18.691 79.409  1.00 31.89  ? 769  HOH B O   1 
HETATM 13179 O  O   . HOH AB 8 .   ? -13.338 -7.074  66.377  1.00 18.79  ? 770  HOH B O   1 
HETATM 13180 O  O   . HOH AB 8 .   ? -28.780 -3.762  89.837  1.00 51.03  ? 771  HOH B O   1 
HETATM 13181 O  O   . HOH AB 8 .   ? 15.008  -14.102 68.486  1.00 14.41  ? 772  HOH B O   1 
HETATM 13182 O  O   . HOH AB 8 .   ? 10.533  23.716  82.805  1.00 34.94  ? 773  HOH B O   1 
HETATM 13183 O  O   . HOH AB 8 .   ? -9.636  -11.976 61.478  1.00 24.04  ? 774  HOH B O   1 
HETATM 13184 O  O   . HOH AB 8 .   ? 9.179   -17.046 77.581  1.00 12.03  ? 775  HOH B O   1 
HETATM 13185 O  O   . HOH AB 8 .   ? 3.531   -28.001 64.314  1.00 39.28  ? 776  HOH B O   1 
HETATM 13186 O  O   . HOH AB 8 .   ? 9.823   -26.532 82.692  1.00 29.64  ? 777  HOH B O   1 
HETATM 13187 O  O   . HOH AB 8 .   ? -0.375  6.429   83.967  1.00 10.75  ? 778  HOH B O   1 
HETATM 13188 O  O   . HOH AB 8 .   ? 7.398   -23.480 87.803  1.00 19.72  ? 779  HOH B O   1 
HETATM 13189 O  O   . HOH AB 8 .   ? 7.677   -25.054 73.871  1.00 11.03  ? 780  HOH B O   1 
HETATM 13190 O  O   . HOH AB 8 .   ? -3.381  -12.750 81.912  1.00 13.97  ? 781  HOH B O   1 
HETATM 13191 O  O   . HOH AB 8 .   ? 15.968  -24.375 86.127  1.00 43.27  ? 782  HOH B O   1 
HETATM 13192 O  O   . HOH AB 8 .   ? -13.558 3.078   71.358  1.00 31.40  ? 783  HOH B O   1 
HETATM 13193 O  O   . HOH AB 8 .   ? 26.653  12.756  79.616  1.00 31.90  ? 784  HOH B O   1 
HETATM 13194 O  O   . HOH AB 8 .   ? 9.132   23.456  74.001  1.00 23.68  ? 785  HOH B O   1 
HETATM 13195 O  O   . HOH AB 8 .   ? -1.067  -1.805  58.775  1.00 10.80  ? 786  HOH B O   1 
HETATM 13196 O  O   . HOH AB 8 .   ? -9.832  0.547   59.122  1.00 24.64  ? 787  HOH B O   1 
HETATM 13197 O  O   . HOH AB 8 .   ? 10.176  -14.253 52.680  1.00 16.76  ? 788  HOH B O   1 
HETATM 13198 O  O   . HOH AB 8 .   ? -25.622 -10.523 83.051  1.00 32.89  ? 789  HOH B O   1 
HETATM 13199 O  O   . HOH AB 8 .   ? -1.940  5.720   68.793  1.00 40.92  ? 790  HOH B O   1 
HETATM 13200 O  O   . HOH AB 8 .   ? -3.321  -5.142  70.175  1.00 14.93  ? 791  HOH B O   1 
HETATM 13201 O  O   . HOH AB 8 .   ? -5.407  -21.312 83.849  1.00 15.47  ? 792  HOH B O   1 
HETATM 13202 O  O   . HOH AB 8 .   ? 5.511   2.733   99.631  1.00 14.21  ? 793  HOH B O   1 
HETATM 13203 O  O   . HOH AB 8 .   ? 7.989   -16.989 91.819  1.00 22.70  ? 794  HOH B O   1 
HETATM 13204 O  O   . HOH AB 8 .   ? 4.334   5.604   89.791  1.00 10.60  ? 795  HOH B O   1 
HETATM 13205 O  O   . HOH AB 8 .   ? 0.465   -15.902 73.611  1.00 13.73  ? 796  HOH B O   1 
HETATM 13206 O  O   . HOH AB 8 .   ? 1.391   -13.944 107.648 1.00 41.48  ? 797  HOH B O   1 
HETATM 13207 O  O   . HOH AB 8 .   ? 4.909   -5.296  98.916  1.00 13.88  ? 798  HOH B O   1 
HETATM 13208 O  O   . HOH AB 8 .   ? 12.254  -26.334 78.544  1.00 17.95  ? 799  HOH B O   1 
HETATM 13209 O  O   . HOH AB 8 .   ? -3.407  -22.819 102.220 1.00 37.14  ? 800  HOH B O   1 
HETATM 13210 O  O   . HOH AB 8 .   ? 14.544  -14.151 79.126  1.00 10.76  ? 801  HOH B O   1 
HETATM 13211 O  O   . HOH AB 8 .   ? 2.248   9.989   84.096  1.00 11.79  ? 802  HOH B O   1 
HETATM 13212 O  O   . HOH AB 8 .   ? 10.939  -15.459 55.242  1.00 53.23  ? 803  HOH B O   1 
HETATM 13213 O  O   . HOH AB 8 .   ? -16.274 -13.912 66.700  1.00 28.72  ? 804  HOH B O   1 
HETATM 13214 O  O   . HOH AB 8 .   ? -1.328  -10.879 103.082 1.00 31.18  ? 805  HOH B O   1 
HETATM 13215 O  O   . HOH AB 8 .   ? -4.866  3.118   58.162  1.00 30.67  ? 806  HOH B O   1 
HETATM 13216 O  O   . HOH AB 8 .   ? -20.791 4.755   82.196  1.00 24.00  ? 807  HOH B O   1 
HETATM 13217 O  O   . HOH AB 8 .   ? 9.187   -25.125 62.302  1.00 27.79  ? 808  HOH B O   1 
HETATM 13218 O  O   . HOH AB 8 .   ? 19.589  -10.568 66.862  1.00 27.75  ? 809  HOH B O   1 
HETATM 13219 O  O   . HOH AB 8 .   ? 21.151  11.049  78.785  1.00 28.29  ? 810  HOH B O   1 
HETATM 13220 O  O   . HOH AB 8 .   ? 13.292  -22.287 91.245  1.00 21.55  ? 811  HOH B O   1 
HETATM 13221 O  O   . HOH AB 8 .   ? 12.725  16.926  81.406  1.00 10.85  ? 812  HOH B O   1 
HETATM 13222 O  O   . HOH AB 8 .   ? 3.749   8.561   90.209  1.00 8.57   ? 813  HOH B O   1 
HETATM 13223 O  O   . HOH AB 8 .   ? 0.490   -24.504 95.075  1.00 18.74  ? 814  HOH B O   1 
HETATM 13224 O  O   . HOH AB 8 .   ? -12.215 5.887   90.603  1.00 19.29  ? 815  HOH B O   1 
HETATM 13225 O  O   . HOH AB 8 .   ? 7.397   -8.852  98.936  1.00 13.92  ? 816  HOH B O   1 
HETATM 13226 O  O   . HOH AB 8 .   ? 7.028   -20.760 88.547  1.00 13.09  ? 817  HOH B O   1 
HETATM 13227 O  O   . HOH AB 8 .   ? -17.280 -0.253  91.780  1.00 17.18  ? 818  HOH B O   1 
HETATM 13228 O  O   . HOH AB 8 .   ? -0.166  -5.097  53.686  1.00 26.01  ? 819  HOH B O   1 
HETATM 13229 O  O   . HOH AB 8 .   ? 10.618  -0.023  80.389  1.00 8.55   ? 820  HOH B O   1 
HETATM 13230 O  O   . HOH AB 8 .   ? 15.415  -11.430 68.586  1.00 19.30  ? 821  HOH B O   1 
HETATM 13231 O  O   . HOH AB 8 .   ? -3.801  -7.713  69.354  1.00 14.30  ? 822  HOH B O   1 
HETATM 13232 O  O   . HOH AB 8 .   ? -3.037  -3.707  100.373 1.00 21.05  ? 823  HOH B O   1 
HETATM 13233 O  O   . HOH AB 8 .   ? 12.425  -16.297 88.289  1.00 25.26  ? 824  HOH B O   1 
HETATM 13234 O  O   . HOH AB 8 .   ? 8.323   -19.910 67.257  1.00 13.15  ? 825  HOH B O   1 
HETATM 13235 O  O   . HOH AB 8 .   ? -13.362 0.446   90.671  1.00 24.34  ? 826  HOH B O   1 
HETATM 13236 O  O   . HOH AB 8 .   ? -9.355  -23.880 73.821  1.00 22.43  ? 827  HOH B O   1 
HETATM 13237 O  O   . HOH AB 8 .   ? 21.273  -7.286  77.232  1.00 22.28  ? 828  HOH B O   1 
HETATM 13238 O  O   . HOH AB 8 .   ? -6.255  1.194   64.502  1.00 20.85  ? 829  HOH B O   1 
HETATM 13239 O  O   . HOH AB 8 .   ? -9.314  -23.786 84.102  1.00 42.40  ? 830  HOH B O   1 
HETATM 13240 O  O   . HOH AB 8 .   ? -22.305 -17.197 86.052  1.00 17.87  ? 831  HOH B O   1 
HETATM 13241 O  O   . HOH AB 8 .   ? -14.778 3.604   78.592  1.00 19.13  ? 832  HOH B O   1 
HETATM 13242 O  O   . HOH AB 8 .   ? -20.106 -0.823  92.459  1.00 30.72  ? 833  HOH B O   1 
HETATM 13243 O  O   . HOH AB 8 .   ? 1.925   7.364   66.581  1.00 22.55  ? 834  HOH B O   1 
HETATM 13244 O  O   . HOH AB 8 .   ? -18.274 1.708   76.624  1.00 25.62  ? 835  HOH B O   1 
HETATM 13245 O  O   . HOH AB 8 .   ? 20.865  -18.308 65.357  1.00 28.15  ? 836  HOH B O   1 
HETATM 13246 O  O   . HOH AB 8 .   ? -3.744  -21.810 58.562  1.00 23.57  ? 837  HOH B O   1 
HETATM 13247 O  O   . HOH AB 8 .   ? -11.747 -10.482 64.528  1.00 16.94  ? 838  HOH B O   1 
HETATM 13248 O  O   . HOH AB 8 .   ? -17.632 -17.624 66.298  1.00 21.85  ? 839  HOH B O   1 
HETATM 13249 O  O   . HOH AB 8 .   ? 0.174   5.775   51.837  1.00 45.67  ? 840  HOH B O   1 
HETATM 13250 O  O   . HOH AB 8 .   ? 19.735  -12.069 81.216  1.00 20.06  ? 841  HOH B O   1 
HETATM 13251 O  O   . HOH AB 8 .   ? 13.106  -13.364 54.351  1.00 26.81  ? 842  HOH B O   1 
HETATM 13252 O  O   . HOH AB 8 .   ? 18.312  -18.968 64.846  1.00 26.88  ? 843  HOH B O   1 
HETATM 13253 O  O   . HOH AB 8 .   ? -10.661 -7.086  67.411  1.00 15.22  ? 844  HOH B O   1 
HETATM 13254 O  O   . HOH AB 8 .   ? -19.104 -20.827 88.974  1.00 26.90  ? 845  HOH B O   1 
HETATM 13255 O  O   . HOH AB 8 .   ? 6.179   -19.083 57.908  1.00 15.75  ? 846  HOH B O   1 
HETATM 13256 O  O   . HOH AB 8 .   ? -20.856 3.973   86.876  1.00 16.20  ? 847  HOH B O   1 
HETATM 13257 O  O   . HOH AB 8 .   ? -9.436  3.702   62.404  1.00 38.87  ? 848  HOH B O   1 
HETATM 13258 O  O   . HOH AB 8 .   ? -15.112 6.291   77.423  1.00 37.99  ? 849  HOH B O   1 
HETATM 13259 O  O   . HOH AB 8 .   ? -0.895  6.565   79.209  1.00 18.59  ? 850  HOH B O   1 
HETATM 13260 O  O   . HOH AB 8 .   ? -3.976  -24.822 87.038  1.00 21.21  ? 851  HOH B O   1 
HETATM 13261 O  O   . HOH AB 8 .   ? 11.198  18.056  79.280  1.00 12.58  ? 852  HOH B O   1 
HETATM 13262 O  O   . HOH AB 8 .   ? -23.790 -4.346  71.593  1.00 23.50  ? 853  HOH B O   1 
HETATM 13263 O  O   . HOH AB 8 .   ? -1.263  3.478   75.662  1.00 15.95  ? 854  HOH B O   1 
HETATM 13264 O  O   . HOH AB 8 .   ? -4.122  3.397   74.770  1.00 19.41  ? 855  HOH B O   1 
HETATM 13265 O  O   . HOH AB 8 .   ? 7.432   10.373  93.584  1.00 27.72  ? 856  HOH B O   1 
HETATM 13266 O  O   . HOH AB 8 .   ? 7.942   -14.733 55.299  1.00 20.19  ? 857  HOH B O   1 
HETATM 13267 O  O   . HOH AB 8 .   ? -2.802  -9.222  71.399  1.00 10.98  ? 858  HOH B O   1 
HETATM 13268 O  O   . HOH AB 8 .   ? 16.885  -13.677 86.265  1.00 27.17  ? 859  HOH B O   1 
HETATM 13269 O  O   . HOH AB 8 .   ? 6.696   13.810  91.178  1.00 11.91  ? 860  HOH B O   1 
HETATM 13270 O  O   . HOH AB 8 .   ? -5.789  -27.122 75.726  1.00 24.48  ? 861  HOH B O   1 
HETATM 13271 O  O   . HOH AB 8 .   ? -0.715  5.328   56.939  1.00 16.70  ? 862  HOH B O   1 
HETATM 13272 O  O   . HOH AB 8 .   ? 2.284   7.128   75.601  1.00 11.66  ? 863  HOH B O   1 
HETATM 13273 O  O   . HOH AB 8 .   ? 21.386  11.418  81.060  1.00 17.91  ? 864  HOH B O   1 
HETATM 13274 O  O   . HOH AB 8 .   ? -20.078 -19.984 83.239  1.00 33.68  ? 865  HOH B O   1 
HETATM 13275 O  O   . HOH AB 8 .   ? -13.356 6.843   68.858  1.00 46.70  ? 866  HOH B O   1 
HETATM 13276 O  O   . HOH AB 8 .   ? 0.644   8.578   68.992  1.00 22.63  ? 867  HOH B O   1 
HETATM 13277 O  O   . HOH AB 8 .   ? 7.091   -27.991 82.613  1.00 29.38  ? 868  HOH B O   1 
HETATM 13278 O  O   . HOH AB 8 .   ? 27.114  11.292  87.373  1.00 21.85  ? 869  HOH B O   1 
HETATM 13279 O  O   . HOH AB 8 .   ? 1.590   -16.625 106.125 1.00 21.08  ? 870  HOH B O   1 
HETATM 13280 O  O   . HOH AB 8 .   ? -8.955  3.468   64.914  1.00 32.94  ? 871  HOH B O   1 
HETATM 13281 O  O   . HOH AB 8 .   ? -6.075  9.896   89.686  1.00 31.90  ? 872  HOH B O   1 
HETATM 13282 O  O   . HOH AB 8 .   ? 8.472   -21.974 103.834 1.00 21.40  ? 873  HOH B O   1 
HETATM 13283 O  O   . HOH AB 8 .   ? 18.447  -19.473 74.393  1.00 33.83  ? 874  HOH B O   1 
HETATM 13284 O  O   . HOH AB 8 .   ? 13.564  20.909  81.698  1.00 36.71  ? 875  HOH B O   1 
HETATM 13285 O  O   . HOH AB 8 .   ? -8.212  11.346  77.460  1.00 35.97  ? 876  HOH B O   1 
HETATM 13286 O  O   . HOH AB 8 .   ? -4.495  13.467  80.421  1.00 28.70  ? 877  HOH B O   1 
HETATM 13287 O  O   . HOH AB 8 .   ? 1.031   10.097  81.679  1.00 13.57  ? 878  HOH B O   1 
HETATM 13288 O  O   . HOH AB 8 .   ? -10.804 -24.119 92.514  1.00 24.02  ? 879  HOH B O   1 
HETATM 13289 O  O   . HOH AB 8 .   ? -2.884  -29.234 74.982  1.00 38.11  ? 880  HOH B O   1 
HETATM 13290 O  O   . HOH AB 8 .   ? -4.288  3.891   97.501  1.00 19.26  ? 881  HOH B O   1 
HETATM 13291 O  O   . HOH AB 8 .   ? 4.319   8.710   62.609  1.00 24.01  ? 882  HOH B O   1 
HETATM 13292 O  O   . HOH AB 8 .   ? -23.304 -14.507 81.619  1.00 21.79  ? 883  HOH B O   1 
HETATM 13293 O  O   . HOH AB 8 .   ? -25.828 -11.062 77.012  1.00 24.82  ? 884  HOH B O   1 
HETATM 13294 O  O   . HOH AB 8 .   ? 1.383   6.355   59.241  1.00 12.68  ? 885  HOH B O   1 
HETATM 13295 O  O   . HOH AB 8 .   ? -0.570  12.747  93.628  1.00 41.62  ? 886  HOH B O   1 
HETATM 13296 O  O   . HOH AB 8 .   ? -12.329 -24.549 69.851  1.00 43.18  ? 887  HOH B O   1 
HETATM 13297 O  O   . HOH AB 8 .   ? 0.006   18.163  84.480  1.00 30.09  ? 888  HOH B O   1 
HETATM 13298 O  O   . HOH AB 8 .   ? 7.971   -1.351  57.794  1.00 15.56  ? 889  HOH B O   1 
HETATM 13299 O  O   . HOH AB 8 .   ? -5.658  -24.700 82.997  1.00 37.85  ? 890  HOH B O   1 
HETATM 13300 O  O   . HOH AB 8 .   ? 17.477  -17.369 71.614  1.00 16.31  ? 891  HOH B O   1 
HETATM 13301 O  O   . HOH AB 8 .   ? 5.553   2.946   104.625 1.00 26.68  ? 892  HOH B O   1 
HETATM 13302 O  O   . HOH AB 8 .   ? 8.350   -31.646 73.099  1.00 41.74  ? 893  HOH B O   1 
HETATM 13303 O  O   . HOH AB 8 .   ? -9.986  -19.429 60.697  1.00 29.20  ? 894  HOH B O   1 
HETATM 13304 O  O   . HOH AB 8 .   ? -2.861  -13.093 56.656  1.00 45.75  ? 895  HOH B O   1 
HETATM 13305 O  O   . HOH AB 8 .   ? -17.622 6.891   85.119  1.00 33.22  ? 896  HOH B O   1 
HETATM 13306 O  O   . HOH AB 8 .   ? 22.323  -9.009  79.234  1.00 29.11  ? 897  HOH B O   1 
HETATM 13307 O  O   . HOH AB 8 .   ? 15.290  16.802  80.335  1.00 11.34  ? 898  HOH B O   1 
HETATM 13308 O  O   . HOH AB 8 .   ? 1.058   3.936   100.164 1.00 26.09  ? 899  HOH B O   1 
HETATM 13309 O  O   . HOH AB 8 .   ? -26.126 -2.863  88.859  1.00 26.38  ? 900  HOH B O   1 
HETATM 13310 O  O   . HOH AB 8 .   ? -17.318 -10.465 97.753  1.00 36.01  ? 901  HOH B O   1 
HETATM 13311 O  O   . HOH AB 8 .   ? -12.241 4.120   92.022  1.00 30.10  ? 902  HOH B O   1 
HETATM 13312 O  O   . HOH AB 8 .   ? -8.005  4.283   71.233  1.00 33.02  ? 903  HOH B O   1 
HETATM 13313 O  O   . HOH AB 8 .   ? -5.602  -2.940  84.135  1.00 14.89  ? 904  HOH B O   1 
HETATM 13314 O  O   . HOH AB 8 .   ? 26.008  -6.338  84.052  1.00 47.26  ? 905  HOH B O   1 
HETATM 13315 O  O   . HOH AB 8 .   ? -9.686  7.825   91.532  1.00 35.40  ? 906  HOH B O   1 
HETATM 13316 O  O   . HOH AB 8 .   ? 1.123   8.133   77.898  1.00 19.55  ? 907  HOH B O   1 
HETATM 13317 O  O   . HOH AB 8 .   ? 1.530   -0.076  103.383 1.00 42.36  ? 908  HOH B O   1 
HETATM 13318 O  O   . HOH AB 8 .   ? -15.859 -19.582 71.455  1.00 23.94  ? 909  HOH B O   1 
HETATM 13319 O  O   . HOH AB 8 .   ? 0.563   1.254   68.404  1.00 28.04  ? 910  HOH B O   1 
HETATM 13320 O  O   . HOH AB 8 .   ? -2.045  -2.955  53.683  1.00 32.25  ? 911  HOH B O   1 
HETATM 13321 O  O   . HOH AB 8 .   ? 19.085  -24.619 72.385  1.00 44.34  ? 912  HOH B O   1 
HETATM 13322 O  O   . HOH AB 8 .   ? -7.171  -18.030 58.442  1.00 30.81  ? 913  HOH B O   1 
HETATM 13323 O  O   . HOH AB 8 .   ? -0.463  16.805  77.814  1.00 50.05  ? 914  HOH B O   1 
HETATM 13324 O  O   . HOH AB 8 .   ? 16.495  -24.739 93.283  1.00 31.63  ? 915  HOH B O   1 
HETATM 13325 O  O   . HOH AB 8 .   ? 0.898   14.062  89.328  1.00 24.55  ? 916  HOH B O   1 
HETATM 13326 O  O   . HOH AB 8 .   ? -3.170  8.571   80.812  1.00 14.05  ? 917  HOH B O   1 
HETATM 13327 O  O   . HOH AB 8 .   ? -17.234 -13.887 96.140  1.00 39.64  ? 918  HOH B O   1 
HETATM 13328 O  O   . HOH AB 8 .   ? 18.403  -24.212 75.964  1.00 40.56  ? 919  HOH B O   1 
HETATM 13329 O  O   . HOH AB 8 .   ? -22.898 -4.262  75.066  1.00 19.90  ? 920  HOH B O   1 
HETATM 13330 O  O   . HOH AB 8 .   ? -16.994 -8.885  101.235 1.00 48.45  ? 921  HOH B O   1 
HETATM 13331 O  O   . HOH AB 8 .   ? -6.585  -11.844 55.135  1.00 43.11  ? 922  HOH B O   1 
HETATM 13332 O  O   . HOH AB 8 .   ? 6.014   21.892  78.945  1.00 53.87  ? 923  HOH B O   1 
HETATM 13333 O  O   . HOH AB 8 .   ? 0.811   7.357   63.687  1.00 18.69  ? 924  HOH B O   1 
HETATM 13334 O  O   . HOH AB 8 .   ? -5.303  -30.187 78.567  1.00 36.64  ? 925  HOH B O   1 
HETATM 13335 O  O   . HOH AB 8 .   ? 4.627   22.260  75.860  1.00 40.38  ? 926  HOH B O   1 
HETATM 13336 O  O   . HOH AB 8 .   ? -7.055  4.542   73.499  1.00 29.73  ? 927  HOH B O   1 
HETATM 13337 O  O   . HOH AB 8 .   ? 7.735   10.436  64.783  1.00 24.32  ? 928  HOH B O   1 
HETATM 13338 O  O   . HOH AB 8 .   ? 19.966  -13.798 77.201  1.00 32.87  ? 929  HOH B O   1 
HETATM 13339 O  O   . HOH AB 8 .   ? 26.955  13.391  86.130  1.00 31.96  ? 930  HOH B O   1 
HETATM 13340 O  O   . HOH AB 8 .   ? 7.297   -18.485 107.029 1.00 23.17  ? 931  HOH B O   1 
HETATM 13341 O  O   . HOH AB 8 .   ? -8.827  -8.557  57.070  1.00 35.74  ? 932  HOH B O   1 
HETATM 13342 O  O   . HOH AB 8 .   ? -14.018 5.677   75.426  1.00 33.21  ? 933  HOH B O   1 
HETATM 13343 O  O   . HOH AB 8 .   ? 19.230  -15.607 86.561  1.00 33.54  ? 934  HOH B O   1 
HETATM 13344 O  O   . HOH AB 8 .   ? 3.289   1.824   103.448 1.00 31.09  ? 935  HOH B O   1 
HETATM 13345 O  O   . HOH AB 8 .   ? -8.317  -11.223 56.906  1.00 38.67  ? 936  HOH B O   1 
HETATM 13346 O  O   . HOH AB 8 .   ? -18.910 -9.352  96.384  1.00 33.26  ? 937  HOH B O   1 
HETATM 13347 O  O   . HOH AB 8 .   ? 7.432   8.959   95.904  1.00 38.32  ? 938  HOH B O   1 
HETATM 13348 O  O   . HOH AB 8 .   ? -5.362  6.659   77.887  1.00 32.54  ? 939  HOH B O   1 
HETATM 13349 O  O   . HOH AB 8 .   ? -5.605  -23.394 85.377  1.00 42.36  ? 940  HOH B O   1 
HETATM 13350 O  O   . HOH AB 8 .   ? 16.811  18.280  77.306  1.00 41.84  ? 941  HOH B O   1 
HETATM 13351 O  O   . HOH AB 8 .   ? -2.365  11.580  91.657  1.00 31.57  ? 942  HOH B O   1 
HETATM 13352 O  O   . HOH AB 8 .   ? -0.287  9.782   71.789  1.00 51.03  ? 943  HOH B O   1 
HETATM 13353 O  O   . HOH AB 8 .   ? -18.697 2.625   67.297  1.00 40.96  ? 944  HOH B O   1 
HETATM 13354 O  O   . HOH AB 8 .   ? 4.235   9.458   96.236  1.00 29.73  ? 945  HOH B O   1 
HETATM 13355 O  O   . HOH AB 8 .   ? 0.288   15.634  75.784  1.00 23.67  ? 946  HOH B O   1 
HETATM 13356 O  O   . HOH AB 8 .   ? 3.022   2.601   100.858 1.00 20.62  ? 947  HOH B O   1 
HETATM 13357 O  O   . HOH AB 8 .   ? -3.937  10.492  90.873  1.00 41.06  ? 948  HOH B O   1 
HETATM 13358 O  O   . HOH AB 8 .   ? 8.723   16.471  68.610  1.00 33.59  ? 949  HOH B O   1 
HETATM 13359 O  O   . HOH AB 8 .   ? -7.320  -15.636 58.245  1.00 40.49  ? 950  HOH B O   1 
HETATM 13360 O  O   . HOH AB 8 .   ? -20.871 -10.744 97.066  1.00 36.06  ? 951  HOH B O   1 
HETATM 13361 O  O   . HOH AB 8 .   ? 25.080  -5.523  76.323  1.00 44.64  ? 952  HOH B O   1 
HETATM 13362 O  O   . HOH AB 8 .   ? 12.450  15.050  67.317  1.00 42.20  ? 953  HOH B O   1 
HETATM 13363 O  O   . HOH AB 8 .   ? 7.034   8.820   62.721  1.00 21.71  ? 954  HOH B O   1 
HETATM 13364 O  O   . HOH AB 8 .   ? -14.355 -9.586  65.350  1.00 23.54  ? 955  HOH B O   1 
HETATM 13365 O  O   . HOH AB 8 .   ? 2.874   6.480   62.217  1.00 17.26  ? 956  HOH B O   1 
HETATM 13366 O  O   . HOH AB 8 .   ? -18.447 -6.966  96.076  1.00 33.80  ? 957  HOH B O   1 
HETATM 13367 O  O   . HOH AB 8 .   ? 7.813   7.324   98.606  1.00 34.99  ? 958  HOH B O   1 
HETATM 13368 O  O   . HOH AB 8 .   ? 4.638   7.474   99.544  1.00 38.98  ? 959  HOH B O   1 
HETATM 13369 O  O   . HOH AB 8 .   ? -2.266  2.817   72.381  1.00 35.03  ? 960  HOH B O   1 
HETATM 13370 O  O   . HOH AB 8 .   ? 21.075  -13.455 79.322  1.00 52.18  ? 961  HOH B O   1 
HETATM 13371 O  O   . HOH AB 8 .   ? -18.947 -12.314 96.634  1.00 52.29  ? 962  HOH B O   1 
HETATM 13372 O  O   . HOH AB 8 .   ? 25.826  -5.052  79.668  1.00 31.63  ? 963  HOH B O   1 
HETATM 13373 O  O   . HOH AB 8 .   ? 18.400  -11.336 87.125  1.00 34.42  ? 964  HOH B O   1 
HETATM 13374 O  O   . HOH AB 8 .   ? 20.424  -14.310 70.843  1.00 53.85  ? 965  HOH B O   1 
HETATM 13375 O  O   . HOH AB 8 .   ? 22.470  13.604  81.286  1.00 36.49  ? 966  HOH B O   1 
HETATM 13376 O  O   . HOH AB 8 .   ? 6.367   -23.411 57.500  1.00 43.31  ? 967  HOH B O   1 
HETATM 13377 O  O   . HOH AB 8 .   ? -7.644  -21.901 95.961  1.00 40.45  ? 968  HOH B O   1 
HETATM 13378 O  O   . HOH AB 8 .   ? -2.132  6.008   75.143  1.00 32.81  ? 969  HOH B O   1 
HETATM 13379 O  O   . HOH AB 8 .   ? -8.295  -24.624 82.140  1.00 40.32  ? 970  HOH B O   1 
HETATM 13380 O  O   . HOH AB 8 .   ? -4.776  1.285   66.964  1.00 25.94  ? 971  HOH B O   1 
HETATM 13381 O  O   . HOH AB 8 .   ? -8.952  10.334  83.040  1.00 22.91  ? 972  HOH B O   1 
HETATM 13382 O  O   . HOH AB 8 .   ? -0.754  -31.253 80.479  1.00 47.40  ? 973  HOH B O   1 
HETATM 13383 O  O   . HOH AB 8 .   ? 16.217  19.409  80.295  1.00 32.90  ? 974  HOH B O   1 
HETATM 13384 O  O   . HOH AB 8 .   ? 11.046  -27.607 80.625  1.00 30.24  ? 975  HOH B O   1 
HETATM 13385 O  O   . HOH AB 8 .   ? -5.155  6.246   63.000  1.00 41.57  ? 976  HOH B O   1 
HETATM 13386 O  O   . HOH AB 8 .   ? -5.173  10.651  78.055  1.00 60.37  ? 977  HOH B O   1 
HETATM 13387 O  O   . HOH AB 8 .   ? 25.655  16.143  87.563  1.00 41.91  ? 978  HOH B O   1 
HETATM 13388 O  O   . HOH AB 8 .   ? -15.671 2.258   76.322  1.00 32.85  ? 979  HOH B O   1 
HETATM 13389 O  O   . HOH AB 8 .   ? -8.284  2.278   57.203  1.00 46.84  ? 980  HOH B O   1 
HETATM 13390 O  O   . HOH AB 8 .   ? -8.043  -25.361 75.795  1.00 23.92  ? 981  HOH B O   1 
HETATM 13391 O  O   . HOH AB 8 .   ? -4.974  0.526   70.558  1.00 44.44  ? 982  HOH B O   1 
HETATM 13392 O  O   . HOH AB 8 .   ? -13.387 -22.892 83.371  1.00 39.40  ? 983  HOH B O   1 
HETATM 13393 O  O   . HOH AB 8 .   ? 17.512  -13.516 71.752  1.00 43.61  ? 984  HOH B O   1 
HETATM 13394 O  O   . HOH AB 8 .   ? 6.700   -22.691 101.683 1.00 40.69  ? 985  HOH B O   1 
HETATM 13395 O  O   . HOH AB 8 .   ? -12.997 -22.748 86.642  1.00 24.64  ? 986  HOH B O   1 
HETATM 13396 O  O   . HOH AB 8 .   ? -14.588 -21.465 81.495  1.00 49.11  ? 987  HOH B O   1 
HETATM 13397 O  O   . HOH AB 8 .   ? -13.847 -5.800  60.084  1.00 40.13  ? 988  HOH B O   1 
HETATM 13398 O  O   . HOH AB 8 .   ? 19.040  -14.529 81.093  1.00 42.17  ? 989  HOH B O   1 
HETATM 13399 O  O   . HOH AB 8 .   ? -10.430 5.077   70.216  1.00 42.86  ? 990  HOH B O   1 
HETATM 13400 O  O   . HOH AB 8 .   ? -10.005 -23.773 80.354  1.00 30.38  ? 991  HOH B O   1 
HETATM 13401 O  O   . HOH AB 8 .   ? -19.864 5.577   84.633  1.00 42.70  ? 992  HOH B O   1 
HETATM 13402 O  O   . HOH AB 8 .   ? -13.777 -12.130 103.650 1.00 41.39  ? 993  HOH B O   1 
HETATM 13403 O  O   . HOH AB 8 .   ? -25.415 -13.098 82.213  1.00 41.88  ? 994  HOH B O   1 
HETATM 13404 O  O   . HOH AB 8 .   ? -18.006 -20.146 67.397  1.00 33.36  ? 995  HOH B O   1 
HETATM 13405 O  O   . HOH AB 8 .   ? -13.202 7.144   73.221  1.00 38.49  ? 996  HOH B O   1 
HETATM 13406 O  O   . HOH AB 8 .   ? -21.108 5.780   79.110  1.00 31.59  ? 997  HOH B O   1 
HETATM 13407 O  O   . HOH AB 8 .   ? 12.632  17.030  77.223  1.00 11.02  ? 998  HOH B O   1 
HETATM 13408 O  O   . HOH AB 8 .   ? -11.338 -4.253  59.659  1.00 39.58  ? 999  HOH B O   1 
HETATM 13409 O  O   . HOH AB 8 .   ? -11.773 -11.598 104.991 1.00 35.74  ? 1000 HOH B O   1 
HETATM 13410 O  O   . HOH AB 8 .   ? 17.627  -14.911 74.505  1.00 46.55  ? 1001 HOH B O   1 
HETATM 13411 O  O   . HOH AB 8 .   ? -4.247  -27.194 85.810  1.00 36.90  ? 1002 HOH B O   1 
HETATM 13412 O  O   . HOH AB 8 .   ? 4.642   -20.411 95.903  1.00 32.48  ? 1003 HOH B O   1 
HETATM 13413 O  O   . HOH AB 8 .   ? -3.209  8.260   78.379  1.00 31.47  ? 1004 HOH B O   1 
HETATM 13414 O  O   . HOH AB 8 .   ? -0.349  1.863   99.502  1.00 30.25  ? 1005 HOH B O   1 
HETATM 13415 O  O   . HOH AB 8 .   ? -0.735  -21.765 57.268  1.00 40.43  ? 1006 HOH B O   1 
HETATM 13416 O  O   . HOH AB 8 .   ? 4.438   16.115  73.011  1.00 23.80  ? 1007 HOH B O   1 
HETATM 13417 O  O   . HOH AB 8 .   ? 28.925  -1.290  79.797  1.00 23.35  ? 1008 HOH B O   1 
HETATM 13418 O  O   . HOH AB 8 .   ? 19.469  18.193  81.006  1.00 44.65  ? 1009 HOH B O   1 
HETATM 13419 O  O   . HOH AB 8 .   ? 18.852  -25.766 92.149  1.00 32.42  ? 1010 HOH B O   1 
HETATM 13420 O  O   . HOH AB 8 .   ? 7.217   4.686   100.846 1.00 27.95  ? 1011 HOH B O   1 
HETATM 13421 O  O   . HOH AB 8 .   ? 19.713  1.486   71.918  1.00 12.80  ? 1012 HOH B O   1 
HETATM 13422 O  O   . HOH AB 8 .   ? 11.168  18.712  95.501  1.00 46.16  ? 1013 HOH B O   1 
HETATM 13423 O  O   . HOH AB 8 .   ? 9.170   15.326  66.496  1.00 43.37  ? 1014 HOH B O   1 
HETATM 13424 O  O   . HOH AB 8 .   ? -17.397 -14.497 64.396  1.00 31.75  ? 1015 HOH B O   1 
HETATM 13425 O  O   . HOH AB 8 .   ? 2.190   -30.007 69.347  1.00 24.68  ? 1016 HOH B O   1 
HETATM 13426 O  O   . HOH AB 8 .   ? 14.098  18.974  76.262  1.00 20.48  ? 1017 HOH B O   1 
HETATM 13427 O  O   . HOH AB 8 .   ? 4.461   15.105  91.501  1.00 31.52  ? 1018 HOH B O   1 
HETATM 13428 O  O   . HOH AB 8 .   ? 11.307  20.795  79.596  1.00 21.52  ? 1019 HOH B O   1 
HETATM 13429 O  O   . HOH AB 8 .   ? 2.629   -22.298 102.198 1.00 47.07  ? 1020 HOH B O   1 
HETATM 13430 O  O   . HOH AB 8 .   ? -22.449 5.370   94.316  1.00 41.82  ? 1021 HOH B O   1 
HETATM 13431 O  O   . HOH AB 8 .   ? 4.727   18.909  90.852  1.00 29.38  ? 1022 HOH B O   1 
HETATM 13432 O  O   . HOH AB 8 .   ? 9.025   -16.687 89.502  1.00 21.81  ? 1023 HOH B O   1 
HETATM 13433 O  O   . HOH AB 8 .   ? 2.888   17.382  87.874  1.00 38.63  ? 1024 HOH B O   1 
HETATM 13434 O  O   . HOH AB 8 .   ? 4.861   -21.812 100.474 1.00 36.98  ? 1025 HOH B O   1 
HETATM 13435 O  O   . HOH AB 8 .   ? -1.300  8.244   76.519  1.00 30.14  ? 1026 HOH B O   1 
HETATM 13436 O  O   . HOH AB 8 .   ? 4.211   -18.087 107.522 1.00 33.78  ? 1027 HOH B O   1 
HETATM 13437 O  O   . HOH AB 8 .   ? 12.450  -20.110 55.282  1.00 45.04  ? 1028 HOH B O   1 
HETATM 13438 O  O   . HOH AB 8 .   ? 6.448   22.261  73.121  1.00 38.74  ? 1029 HOH B O   1 
HETATM 13439 O  O   . HOH AB 8 .   ? -23.033 2.362   85.598  1.00 25.14  ? 1030 HOH B O   1 
HETATM 13440 O  O   . HOH AB 8 .   ? -5.093  13.409  78.000  1.00 50.36  ? 1031 HOH B O   1 
HETATM 13441 O  O   . HOH AB 8 .   ? -23.525 -16.876 83.320  1.00 28.64  ? 1032 HOH B O   1 
HETATM 13442 O  O   . HOH AB 8 .   ? -25.966 -17.313 80.102  1.00 37.77  ? 1033 HOH B O   1 
HETATM 13443 O  O   . HOH AB 8 .   ? -22.571 -19.027 81.840  1.00 32.63  ? 1034 HOH B O   1 
HETATM 13444 O  O   . HOH AB 8 .   ? 2.333   -24.935 102.027 1.00 45.47  ? 1035 HOH B O   1 
HETATM 13445 O  O   . HOH AB 8 .   ? 3.737   7.232   58.250  1.00 24.97  ? 1036 HOH B O   1 
HETATM 13446 O  O   . HOH AB 8 .   ? 3.447   10.904  60.852  1.00 34.57  ? 1037 HOH B O   1 
HETATM 13447 O  O   . HOH AB 8 .   ? -0.637  8.007   81.818  1.00 13.66  ? 1038 HOH B O   1 
HETATM 13448 O  O   . HOH AB 8 .   ? -0.769  12.331  71.355  1.00 47.59  ? 1039 HOH B O   1 
HETATM 13449 O  O   . HOH AB 8 .   ? -3.556  15.489  76.492  1.00 48.21  ? 1040 HOH B O   1 
HETATM 13450 O  O   . HOH AB 8 .   ? 13.956  21.536  77.513  1.00 32.80  ? 1041 HOH B O   1 
HETATM 13451 O  O   . HOH AB 8 .   ? -9.510  -25.429 78.110  1.00 29.34  ? 1042 HOH B O   1 
HETATM 13452 O  O   . HOH BB 8 .   ? 56.125  -23.402 64.877  1.00 46.92  ? 601  HOH C O   1 
HETATM 13453 O  O   . HOH BB 8 .   ? 42.796  21.019  66.900  1.00 55.52  ? 602  HOH C O   1 
HETATM 13454 O  O   . HOH BB 8 .   ? 64.653  -1.216  56.149  1.00 39.56  ? 603  HOH C O   1 
HETATM 13455 O  O   . HOH BB 8 .   ? 41.586  -8.173  74.398  1.00 31.56  ? 604  HOH C O   1 
HETATM 13456 O  O   . HOH BB 8 .   ? 70.119  18.984  84.769  1.00 39.38  ? 605  HOH C O   1 
HETATM 13457 O  O   . HOH BB 8 .   ? 75.798  -0.903  92.517  1.00 28.23  ? 606  HOH C O   1 
HETATM 13458 O  O   . HOH BB 8 .   ? 71.007  16.107  84.501  1.00 44.90  ? 607  HOH C O   1 
HETATM 13459 O  O   . HOH BB 8 .   ? 86.107  1.029   69.736  1.00 43.07  ? 608  HOH C O   1 
HETATM 13460 O  O   . HOH BB 8 .   ? 78.971  -5.785  64.978  1.00 40.82  ? 609  HOH C O   1 
HETATM 13461 O  O   . HOH BB 8 .   ? 50.085  -4.062  99.096  1.00 9.05   ? 610  HOH C O   1 
HETATM 13462 O  O   . HOH BB 8 .   ? 78.796  -10.802 79.132  1.00 39.56  ? 611  HOH C O   1 
HETATM 13463 O  O   . HOH BB 8 .   ? 61.302  6.661   100.366 1.00 36.73  ? 612  HOH C O   1 
HETATM 13464 O  O   . HOH BB 8 .   ? 37.338  -8.681  76.205  1.00 32.62  ? 613  HOH C O   1 
HETATM 13465 O  O   . HOH BB 8 .   ? 75.858  -9.838  68.756  1.00 21.88  ? 614  HOH C O   1 
HETATM 13466 O  O   . HOH BB 8 .   ? 71.837  -12.028 76.860  1.00 22.41  ? 615  HOH C O   1 
HETATM 13467 O  O   . HOH BB 8 .   ? 71.578  -20.567 92.160  1.00 31.94  ? 616  HOH C O   1 
HETATM 13468 O  O   . HOH BB 8 .   ? 67.446  11.110  69.144  1.00 31.60  ? 617  HOH C O   1 
HETATM 13469 O  O   . HOH BB 8 .   ? 41.876  16.341  93.586  1.00 15.02  ? 618  HOH C O   1 
HETATM 13470 O  O   . HOH BB 8 .   ? 80.948  -7.652  76.960  1.00 34.39  ? 619  HOH C O   1 
HETATM 13471 O  O   . HOH BB 8 .   ? 57.305  -10.174 76.747  1.00 8.61   ? 620  HOH C O   1 
HETATM 13472 O  O   . HOH BB 8 .   ? 59.035  -23.594 65.719  1.00 36.53  ? 621  HOH C O   1 
HETATM 13473 O  O   . HOH BB 8 .   ? 52.814  15.019  94.040  1.00 33.26  ? 622  HOH C O   1 
HETATM 13474 O  O   . HOH BB 8 .   ? 65.757  -14.681 65.285  1.00 36.27  ? 623  HOH C O   1 
HETATM 13475 O  O   . HOH BB 8 .   ? 52.152  -11.505 76.497  1.00 12.63  ? 624  HOH C O   1 
HETATM 13476 O  O   . HOH BB 8 .   ? 66.497  -8.194  57.448  1.00 28.34  ? 625  HOH C O   1 
HETATM 13477 O  O   . HOH BB 8 .   ? 71.465  -18.297 92.877  1.00 30.48  ? 626  HOH C O   1 
HETATM 13478 O  O   . HOH BB 8 .   ? 78.678  11.558  74.703  1.00 21.43  ? 627  HOH C O   1 
HETATM 13479 O  O   . HOH BB 8 .   ? 50.517  21.207  74.692  1.00 25.10  ? 628  HOH C O   1 
HETATM 13480 O  O   . HOH BB 8 .   ? 52.589  -12.803 66.076  1.00 18.78  ? 629  HOH C O   1 
HETATM 13481 O  O   . HOH BB 8 .   ? 43.861  -17.347 97.573  1.00 20.11  ? 630  HOH C O   1 
HETATM 13482 O  O   . HOH BB 8 .   ? 41.694  -13.005 78.312  1.00 27.17  ? 631  HOH C O   1 
HETATM 13483 O  O   . HOH BB 8 .   ? 57.797  -6.257  79.732  1.00 10.81  ? 632  HOH C O   1 
HETATM 13484 O  O   . HOH BB 8 .   ? 54.791  11.891  88.538  1.00 27.38  ? 633  HOH C O   1 
HETATM 13485 O  O   . HOH BB 8 .   ? 39.587  3.429   71.804  1.00 12.91  ? 634  HOH C O   1 
HETATM 13486 O  O   . HOH BB 8 .   ? 72.355  -16.192 89.303  1.00 17.48  ? 635  HOH C O   1 
HETATM 13487 O  O   . HOH BB 8 .   ? 47.804  25.774  76.130  1.00 26.38  ? 636  HOH C O   1 
HETATM 13488 O  O   . HOH BB 8 .   ? 53.400  -18.734 69.342  1.00 17.18  ? 637  HOH C O   1 
HETATM 13489 O  O   . HOH BB 8 .   ? 53.795  4.905   90.936  1.00 21.91  ? 638  HOH C O   1 
HETATM 13490 O  O   . HOH BB 8 .   ? 80.206  -8.677  81.394  1.00 20.59  ? 639  HOH C O   1 
HETATM 13491 O  O   . HOH BB 8 .   ? 49.487  23.239  78.854  1.00 20.66  ? 640  HOH C O   1 
HETATM 13492 O  O   . HOH BB 8 .   ? 78.264  0.114   92.905  1.00 34.79  ? 641  HOH C O   1 
HETATM 13493 O  O   . HOH BB 8 .   ? 48.838  -4.936  96.559  1.00 11.46  ? 642  HOH C O   1 
HETATM 13494 O  O   . HOH BB 8 .   ? 53.938  5.400   98.966  1.00 10.65  ? 643  HOH C O   1 
HETATM 13495 O  O   . HOH BB 8 .   ? 43.087  -2.975  69.212  1.00 17.05  ? 644  HOH C O   1 
HETATM 13496 O  O   . HOH BB 8 .   ? 69.172  9.713   90.231  1.00 29.81  ? 645  HOH C O   1 
HETATM 13497 O  O   . HOH BB 8 .   ? 39.883  3.132   89.126  1.00 12.77  ? 646  HOH C O   1 
HETATM 13498 O  O   . HOH BB 8 .   ? 72.294  3.229   99.048  1.00 30.85  ? 647  HOH C O   1 
HETATM 13499 O  O   . HOH BB 8 .   ? 54.739  1.306   81.678  1.00 7.75   ? 648  HOH C O   1 
HETATM 13500 O  O   . HOH BB 8 .   ? 64.127  2.592   75.507  1.00 10.70  ? 649  HOH C O   1 
HETATM 13501 O  O   . HOH BB 8 .   ? 45.153  4.756   78.087  1.00 9.80   ? 650  HOH C O   1 
HETATM 13502 O  O   . HOH BB 8 .   ? 83.763  -3.419  67.427  1.00 19.71  ? 651  HOH C O   1 
HETATM 13503 O  O   . HOH BB 8 .   ? 72.608  -7.124  94.667  1.00 19.78  ? 652  HOH C O   1 
HETATM 13504 O  O   . HOH BB 8 .   ? 44.051  10.443  72.849  1.00 10.53  ? 653  HOH C O   1 
HETATM 13505 O  O   . HOH BB 8 .   ? 48.290  -23.534 86.971  1.00 20.11  ? 654  HOH C O   1 
HETATM 13506 O  O   . HOH BB 8 .   ? 56.657  22.088  78.783  1.00 37.30  ? 655  HOH C O   1 
HETATM 13507 O  O   . HOH BB 8 .   ? 51.987  2.538   56.683  1.00 14.91  ? 656  HOH C O   1 
HETATM 13508 O  O   . HOH BB 8 .   ? 66.643  -12.396 72.927  1.00 22.15  ? 657  HOH C O   1 
HETATM 13509 O  O   . HOH BB 8 .   ? 64.790  7.063   75.659  1.00 10.04  ? 658  HOH C O   1 
HETATM 13510 O  O   . HOH BB 8 .   ? 61.486  -6.922  53.629  1.00 33.56  ? 659  HOH C O   1 
HETATM 13511 O  O   . HOH BB 8 .   ? 50.583  -15.236 104.372 1.00 17.15  ? 660  HOH C O   1 
HETATM 13512 O  O   . HOH BB 8 .   ? 69.638  -24.047 81.282  1.00 34.45  ? 661  HOH C O   1 
HETATM 13513 O  O   . HOH BB 8 .   ? 72.820  -13.532 93.338  1.00 23.03  ? 662  HOH C O   1 
HETATM 13514 O  O   . HOH BB 8 .   ? 48.601  17.169  89.033  1.00 10.75  ? 663  HOH C O   1 
HETATM 13515 O  O   . HOH BB 8 .   ? 75.004  -9.901  94.305  1.00 27.67  ? 664  HOH C O   1 
HETATM 13516 O  O   . HOH BB 8 .   ? 33.104  18.860  76.364  1.00 20.88  ? 665  HOH C O   1 
HETATM 13517 O  O   . HOH BB 8 .   ? 60.420  5.297   77.045  1.00 10.85  ? 666  HOH C O   1 
HETATM 13518 O  O   . HOH BB 8 .   ? 61.111  -8.997  102.459 1.00 24.04  ? 667  HOH C O   1 
HETATM 13519 O  O   . HOH BB 8 .   ? 57.478  2.968   88.708  1.00 32.40  ? 668  HOH C O   1 
HETATM 13520 O  O   . HOH BB 8 .   ? 79.518  -1.974  86.593  1.00 18.23  ? 669  HOH C O   1 
HETATM 13521 O  O   . HOH BB 8 .   ? 52.201  -0.598  86.154  1.00 9.09   ? 670  HOH C O   1 
HETATM 13522 O  O   . HOH BB 8 .   ? 66.662  -8.805  61.047  1.00 18.95  ? 671  HOH C O   1 
HETATM 13523 O  O   . HOH BB 8 .   ? 36.173  15.102  72.719  1.00 12.62  ? 672  HOH C O   1 
HETATM 13524 O  O   . HOH BB 8 .   ? 48.811  -21.290 93.901  1.00 18.82  ? 673  HOH C O   1 
HETATM 13525 O  O   . HOH BB 8 .   ? 75.275  -1.861  64.015  1.00 24.65  ? 674  HOH C O   1 
HETATM 13526 O  O   . HOH BB 8 .   ? 52.431  8.062   88.096  1.00 13.54  ? 675  HOH C O   1 
HETATM 13527 O  O   . HOH BB 8 .   ? 55.740  -22.091 72.710  1.00 37.29  ? 676  HOH C O   1 
HETATM 13528 O  O   . HOH BB 8 .   ? 81.263  -2.530  64.645  1.00 34.09  ? 677  HOH C O   1 
HETATM 13529 O  O   . HOH BB 8 .   ? 40.935  3.611   69.267  1.00 15.38  ? 678  HOH C O   1 
HETATM 13530 O  O   . HOH BB 8 .   ? 58.206  -9.654  62.136  1.00 15.07  ? 679  HOH C O   1 
HETATM 13531 O  O   . HOH BB 8 .   ? 65.037  -2.584  58.931  1.00 18.52  ? 680  HOH C O   1 
HETATM 13532 O  O   . HOH BB 8 .   ? 52.527  24.143  80.154  1.00 27.11  ? 681  HOH C O   1 
HETATM 13533 O  O   . HOH BB 8 .   ? 38.535  -3.918  71.563  1.00 10.11  ? 682  HOH C O   1 
HETATM 13534 O  O   . HOH BB 8 .   ? 44.538  -10.343 89.354  1.00 23.97  ? 683  HOH C O   1 
HETATM 13535 O  O   . HOH BB 8 .   ? 69.914  8.702   82.179  1.00 17.46  ? 684  HOH C O   1 
HETATM 13536 O  O   . HOH BB 8 .   ? 43.996  6.657   79.858  1.00 12.12  ? 685  HOH C O   1 
HETATM 13537 O  O   . HOH BB 8 .   ? 47.472  -22.738 77.174  1.00 21.75  ? 686  HOH C O   1 
HETATM 13538 O  O   . HOH BB 8 .   ? 53.602  -11.024 69.125  1.00 11.17  ? 687  HOH C O   1 
HETATM 13539 O  O   . HOH BB 8 .   ? 37.234  -4.524  78.480  1.00 11.21  ? 688  HOH C O   1 
HETATM 13540 O  O   . HOH BB 8 .   ? 53.089  -19.747 87.251  1.00 16.14  ? 689  HOH C O   1 
HETATM 13541 O  O   . HOH BB 8 .   ? 42.854  9.047   80.899  1.00 7.12   ? 690  HOH C O   1 
HETATM 13542 O  O   . HOH BB 8 .   ? 35.613  2.248   77.756  1.00 17.18  ? 691  HOH C O   1 
HETATM 13543 O  O   . HOH BB 8 .   ? 54.817  4.457   107.597 1.00 25.95  ? 692  HOH C O   1 
HETATM 13544 O  O   . HOH BB 8 .   ? 46.408  6.675   71.899  1.00 9.06   ? 693  HOH C O   1 
HETATM 13545 O  O   . HOH BB 8 .   ? 54.365  -12.577 79.064  1.00 10.50  ? 694  HOH C O   1 
HETATM 13546 O  O   . HOH BB 8 .   ? 44.471  -12.885 81.033  1.00 20.03  ? 695  HOH C O   1 
HETATM 13547 O  O   . HOH BB 8 .   ? 63.082  -25.151 87.041  1.00 24.79  ? 696  HOH C O   1 
HETATM 13548 O  O   . HOH BB 8 .   ? 70.498  15.530  77.936  1.00 23.28  ? 697  HOH C O   1 
HETATM 13549 O  O   . HOH BB 8 .   ? 62.879  10.963  81.196  1.00 11.51  ? 698  HOH C O   1 
HETATM 13550 O  O   . HOH BB 8 .   ? 75.887  -6.707  91.262  1.00 24.86  ? 699  HOH C O   1 
HETATM 13551 O  O   . HOH BB 8 .   ? 48.350  -18.881 99.438  1.00 25.94  ? 700  HOH C O   1 
HETATM 13552 O  O   . HOH BB 8 .   ? 39.336  -7.760  91.419  1.00 35.81  ? 701  HOH C O   1 
HETATM 13553 O  O   . HOH BB 8 .   ? 51.529  -12.862 79.492  1.00 12.16  ? 702  HOH C O   1 
HETATM 13554 O  O   . HOH BB 8 .   ? 53.739  0.994   59.948  1.00 12.35  ? 703  HOH C O   1 
HETATM 13555 O  O   . HOH BB 8 .   ? 61.794  -24.157 94.989  1.00 46.06  ? 704  HOH C O   1 
HETATM 13556 O  O   . HOH BB 8 .   ? 76.608  1.397   76.175  1.00 14.85  ? 705  HOH C O   1 
HETATM 13557 O  O   . HOH BB 8 .   ? 72.748  -9.504  80.273  1.00 14.04  ? 706  HOH C O   1 
HETATM 13558 O  O   . HOH BB 8 .   ? 74.813  -10.885 81.019  1.00 24.85  ? 707  HOH C O   1 
HETATM 13559 O  O   . HOH BB 8 .   ? 78.771  10.904  79.340  1.00 29.46  ? 708  HOH C O   1 
HETATM 13560 O  O   . HOH BB 8 .   ? 41.108  19.856  82.380  1.00 12.33  ? 709  HOH C O   1 
HETATM 13561 O  O   . HOH BB 8 .   ? 64.947  -28.558 80.401  1.00 36.11  ? 710  HOH C O   1 
HETATM 13562 O  O   . HOH BB 8 .   ? 48.373  9.635   93.159  1.00 18.99  ? 711  HOH C O   1 
HETATM 13563 O  O   . HOH BB 8 .   ? 54.869  -21.016 81.534  1.00 16.35  ? 712  HOH C O   1 
HETATM 13564 O  O   . HOH BB 8 .   ? 45.715  -10.859 78.413  1.00 13.31  ? 713  HOH C O   1 
HETATM 13565 O  O   . HOH BB 8 .   ? 41.978  27.249  81.998  1.00 36.83  ? 714  HOH C O   1 
HETATM 13566 O  O   . HOH BB 8 .   ? 58.496  19.473  82.867  1.00 31.67  ? 715  HOH C O   1 
HETATM 13567 O  O   . HOH BB 8 .   ? 54.213  -5.308  78.642  1.00 7.28   ? 716  HOH C O   1 
HETATM 13568 O  O   . HOH BB 8 .   ? 47.495  -14.926 102.487 1.00 32.88  ? 717  HOH C O   1 
HETATM 13569 O  O   . HOH BB 8 .   ? 42.168  28.475  77.077  1.00 34.27  ? 718  HOH C O   1 
HETATM 13570 O  O   . HOH BB 8 .   ? 71.024  2.221   76.190  1.00 11.78  ? 719  HOH C O   1 
HETATM 13571 O  O   . HOH BB 8 .   ? 81.883  5.628   76.269  1.00 25.09  ? 720  HOH C O   1 
HETATM 13572 O  O   . HOH BB 8 .   ? 39.311  19.794  90.489  1.00 15.08  ? 721  HOH C O   1 
HETATM 13573 O  O   . HOH BB 8 .   ? 72.851  -21.572 85.932  1.00 27.89  ? 722  HOH C O   1 
HETATM 13574 O  O   . HOH BB 8 .   ? 55.406  4.625   62.905  1.00 15.70  ? 723  HOH C O   1 
HETATM 13575 O  O   . HOH BB 8 .   ? 63.116  3.643   105.531 1.00 31.26  ? 724  HOH C O   1 
HETATM 13576 O  O   . HOH BB 8 .   ? 72.199  -20.447 82.270  1.00 29.16  ? 725  HOH C O   1 
HETATM 13577 O  O   . HOH BB 8 .   ? 64.118  -8.070  66.700  1.00 34.41  ? 726  HOH C O   1 
HETATM 13578 O  O   . HOH BB 8 .   ? 72.772  -6.742  59.445  1.00 32.13  ? 727  HOH C O   1 
HETATM 13579 O  O   . HOH BB 8 .   ? 49.987  -23.948 93.504  1.00 26.96  ? 728  HOH C O   1 
HETATM 13580 O  O   . HOH BB 8 .   ? 46.966  2.037   96.021  1.00 11.94  ? 729  HOH C O   1 
HETATM 13581 O  O   . HOH BB 8 .   ? 60.024  19.616  69.723  1.00 26.25  ? 730  HOH C O   1 
HETATM 13582 O  O   . HOH BB 8 .   ? 66.572  0.831   73.945  1.00 9.54   ? 731  HOH C O   1 
HETATM 13583 O  O   . HOH BB 8 .   ? 48.301  9.654   86.188  1.00 10.31  ? 732  HOH C O   1 
HETATM 13584 O  O   . HOH BB 8 .   ? 66.267  -22.218 79.819  1.00 30.21  ? 733  HOH C O   1 
HETATM 13585 O  O   . HOH BB 8 .   ? 46.611  3.732   80.110  1.00 7.74   ? 734  HOH C O   1 
HETATM 13586 O  O   . HOH BB 8 .   ? 40.485  22.849  67.579  1.00 26.12  ? 735  HOH C O   1 
HETATM 13587 O  O   . HOH BB 8 .   ? 72.245  -17.966 84.201  1.00 16.89  ? 736  HOH C O   1 
HETATM 13588 O  O   . HOH BB 8 .   ? 61.252  -22.948 83.879  1.00 14.04  ? 737  HOH C O   1 
HETATM 13589 O  O   . HOH BB 8 .   ? 71.991  10.288  72.508  1.00 15.23  ? 738  HOH C O   1 
HETATM 13590 O  O   . HOH BB 8 .   ? 36.446  -10.054 84.539  1.00 43.23  ? 739  HOH C O   1 
HETATM 13591 O  O   . HOH BB 8 .   ? 46.617  -19.439 68.598  1.00 33.45  ? 740  HOH C O   1 
HETATM 13592 O  O   . HOH BB 8 .   ? 82.835  9.848   72.137  1.00 28.46  ? 741  HOH C O   1 
HETATM 13593 O  O   . HOH BB 8 .   ? 54.377  -16.413 68.096  1.00 15.97  ? 742  HOH C O   1 
HETATM 13594 O  O   . HOH BB 8 .   ? 59.358  4.370   57.955  1.00 35.63  ? 743  HOH C O   1 
HETATM 13595 O  O   . HOH BB 8 .   ? 51.249  9.823   98.987  1.00 24.30  ? 744  HOH C O   1 
HETATM 13596 O  O   . HOH BB 8 .   ? 70.797  8.686   85.544  1.00 29.03  ? 745  HOH C O   1 
HETATM 13597 O  O   . HOH BB 8 .   ? 63.207  5.076   96.398  1.00 18.61  ? 746  HOH C O   1 
HETATM 13598 O  O   . HOH BB 8 .   ? 39.467  17.150  85.346  1.00 11.53  ? 747  HOH C O   1 
HETATM 13599 O  O   . HOH BB 8 .   ? 73.515  -8.453  77.682  1.00 16.40  ? 748  HOH C O   1 
HETATM 13600 O  O   . HOH BB 8 .   ? 39.175  -13.119 94.160  1.00 19.39  ? 749  HOH C O   1 
HETATM 13601 O  O   . HOH BB 8 .   ? 42.805  -17.085 81.461  1.00 35.53  ? 750  HOH C O   1 
HETATM 13602 O  O   . HOH BB 8 .   ? 44.166  16.552  67.118  1.00 32.28  ? 751  HOH C O   1 
HETATM 13603 O  O   . HOH BB 8 .   ? 53.757  0.858   53.305  1.00 14.56  ? 752  HOH C O   1 
HETATM 13604 O  O   . HOH BB 8 .   ? 72.265  -3.642  97.298  1.00 35.50  ? 753  HOH C O   1 
HETATM 13605 O  O   . HOH BB 8 .   ? 60.623  14.615  80.160  1.00 14.25  ? 754  HOH C O   1 
HETATM 13606 O  O   . HOH BB 8 .   ? 56.698  7.912   61.032  1.00 23.99  ? 755  HOH C O   1 
HETATM 13607 O  O   . HOH BB 8 .   ? 71.666  -0.777  92.939  1.00 16.56  ? 756  HOH C O   1 
HETATM 13608 O  O   . HOH BB 8 .   ? 54.392  -15.226 79.874  1.00 10.13  ? 757  HOH C O   1 
HETATM 13609 O  O   . HOH BB 8 .   ? 50.881  10.380  87.199  1.00 10.58  ? 758  HOH C O   1 
HETATM 13610 O  O   . HOH BB 8 .   ? 73.599  -15.373 81.090  1.00 18.55  ? 759  HOH C O   1 
HETATM 13611 O  O   . HOH BB 8 .   ? 42.564  -18.922 84.991  1.00 32.62  ? 760  HOH C O   1 
HETATM 13612 O  O   . HOH BB 8 .   ? 69.110  -7.415  96.751  1.00 21.91  ? 761  HOH C O   1 
HETATM 13613 O  O   . HOH BB 8 .   ? 35.577  10.874  88.626  1.00 7.73   ? 762  HOH C O   1 
HETATM 13614 O  O   . HOH BB 8 .   ? 70.859  -4.911  94.197  1.00 15.73  ? 763  HOH C O   1 
HETATM 13615 O  O   . HOH BB 8 .   ? 43.316  -19.028 91.332  1.00 22.17  ? 764  HOH C O   1 
HETATM 13616 O  O   . HOH BB 8 .   ? 80.010  -8.367  68.640  1.00 28.10  ? 765  HOH C O   1 
HETATM 13617 O  O   . HOH BB 8 .   ? 62.899  -5.302  76.360  1.00 9.20   ? 766  HOH C O   1 
HETATM 13618 O  O   . HOH BB 8 .   ? 28.497  13.761  77.470  1.00 33.52  ? 767  HOH C O   1 
HETATM 13619 O  O   . HOH BB 8 .   ? 69.149  -1.282  91.776  1.00 15.63  ? 768  HOH C O   1 
HETATM 13620 O  O   . HOH BB 8 .   ? 54.332  -23.786 75.023  1.00 26.25  ? 769  HOH C O   1 
HETATM 13621 O  O   . HOH BB 8 .   ? 75.381  -11.621 65.077  1.00 35.44  ? 770  HOH C O   1 
HETATM 13622 O  O   . HOH BB 8 .   ? 51.461  12.380  72.136  1.00 11.72  ? 771  HOH C O   1 
HETATM 13623 O  O   . HOH BB 8 .   ? 73.091  1.269   74.338  1.00 14.03  ? 772  HOH C O   1 
HETATM 13624 O  O   . HOH BB 8 .   ? 63.067  10.964  85.306  1.00 18.72  ? 773  HOH C O   1 
HETATM 13625 O  O   . HOH BB 8 .   ? 57.925  10.489  97.935  1.00 50.32  ? 774  HOH C O   1 
HETATM 13626 O  O   . HOH BB 8 .   ? 55.855  13.017  78.016  1.00 10.27  ? 775  HOH C O   1 
HETATM 13627 O  O   . HOH BB 8 .   ? 45.484  -13.032 88.895  1.00 12.51  ? 776  HOH C O   1 
HETATM 13628 O  O   . HOH BB 8 .   ? 43.369  25.137  91.183  1.00 22.77  ? 777  HOH C O   1 
HETATM 13629 O  O   . HOH BB 8 .   ? 62.772  -14.702 58.669  1.00 31.33  ? 778  HOH C O   1 
HETATM 13630 O  O   . HOH BB 8 .   ? 42.487  20.706  84.806  1.00 13.87  ? 779  HOH C O   1 
HETATM 13631 O  O   . HOH BB 8 .   ? 62.288  17.132  81.353  1.00 27.83  ? 780  HOH C O   1 
HETATM 13632 O  O   . HOH BB 8 .   ? 55.057  13.297  61.724  1.00 29.87  ? 781  HOH C O   1 
HETATM 13633 O  O   . HOH BB 8 .   ? 63.342  0.077   81.365  1.00 9.66   ? 782  HOH C O   1 
HETATM 13634 O  O   . HOH BB 8 .   ? 48.975  14.746  70.040  1.00 15.03  ? 783  HOH C O   1 
HETATM 13635 O  O   . HOH BB 8 .   ? 57.594  8.514   85.633  1.00 15.47  ? 784  HOH C O   1 
HETATM 13636 O  O   . HOH BB 8 .   ? 41.675  -8.426  91.862  1.00 27.29  ? 785  HOH C O   1 
HETATM 13637 O  O   . HOH BB 8 .   ? 77.497  -8.801  75.685  1.00 27.26  ? 786  HOH C O   1 
HETATM 13638 O  O   . HOH BB 8 .   ? 69.468  3.332   81.861  1.00 12.74  ? 787  HOH C O   1 
HETATM 13639 O  O   . HOH BB 8 .   ? 81.342  -7.752  74.034  1.00 21.52  ? 788  HOH C O   1 
HETATM 13640 O  O   . HOH BB 8 .   ? 74.694  -3.969  91.493  1.00 21.75  ? 789  HOH C O   1 
HETATM 13641 O  O   . HOH BB 8 .   ? 59.156  0.791   89.690  1.00 21.43  ? 790  HOH C O   1 
HETATM 13642 O  O   . HOH BB 8 .   ? 36.557  11.802  81.720  1.00 10.45  ? 791  HOH C O   1 
HETATM 13643 O  O   . HOH BB 8 .   ? 37.353  22.421  80.031  1.00 16.28  ? 792  HOH C O   1 
HETATM 13644 O  O   . HOH BB 8 .   ? 72.272  -10.120 70.727  1.00 16.85  ? 793  HOH C O   1 
HETATM 13645 O  O   . HOH BB 8 .   ? 61.519  -0.374  89.413  1.00 11.17  ? 794  HOH C O   1 
HETATM 13646 O  O   . HOH BB 8 .   ? 50.633  11.330  61.941  1.00 11.51  ? 795  HOH C O   1 
HETATM 13647 O  O   . HOH BB 8 .   ? 29.643  -2.449  82.442  1.00 27.23  ? 796  HOH C O   1 
HETATM 13648 O  O   . HOH BB 8 .   ? 58.291  14.956  81.708  1.00 16.29  ? 797  HOH C O   1 
HETATM 13649 O  O   . HOH BB 8 .   ? 58.726  -4.308  105.600 1.00 22.99  ? 798  HOH C O   1 
HETATM 13650 O  O   . HOH BB 8 .   ? 59.565  9.082   101.763 1.00 31.38  ? 799  HOH C O   1 
HETATM 13651 O  O   . HOH BB 8 .   ? 43.479  -9.919  82.468  1.00 25.51  ? 800  HOH C O   1 
HETATM 13652 O  O   . HOH BB 8 .   ? 60.989  5.983   108.047 1.00 41.97  ? 801  HOH C O   1 
HETATM 13653 O  O   . HOH BB 8 .   ? 52.653  15.829  78.676  1.00 13.48  ? 802  HOH C O   1 
HETATM 13654 O  O   . HOH BB 8 .   ? 68.201  -26.142 82.182  1.00 29.06  ? 803  HOH C O   1 
HETATM 13655 O  O   . HOH BB 8 .   ? 59.936  -10.564 83.846  1.00 13.84  ? 804  HOH C O   1 
HETATM 13656 O  O   . HOH BB 8 .   ? 37.636  -5.967  81.499  1.00 19.91  ? 805  HOH C O   1 
HETATM 13657 O  O   . HOH BB 8 .   ? 42.764  1.922   95.285  1.00 9.20   ? 806  HOH C O   1 
HETATM 13658 O  O   . HOH BB 8 .   ? 56.701  -20.986 98.386  1.00 43.43  ? 807  HOH C O   1 
HETATM 13659 O  O   . HOH BB 8 .   ? 43.412  -3.500  66.784  1.00 11.84  ? 808  HOH C O   1 
HETATM 13660 O  O   . HOH BB 8 .   ? 51.298  -27.522 81.577  1.00 27.12  ? 809  HOH C O   1 
HETATM 13661 O  O   . HOH BB 8 .   ? 58.846  0.138   101.242 1.00 14.66  ? 810  HOH C O   1 
HETATM 13662 O  O   . HOH BB 8 .   ? 60.187  6.952   60.060  1.00 17.60  ? 811  HOH C O   1 
HETATM 13663 O  O   . HOH BB 8 .   ? 50.432  -22.088 76.575  1.00 16.98  ? 812  HOH C O   1 
HETATM 13664 O  O   . HOH BB 8 .   ? 55.653  22.829  63.397  1.00 21.70  ? 813  HOH C O   1 
HETATM 13665 O  O   . HOH BB 8 .   ? 37.677  -0.821  87.450  1.00 17.25  ? 814  HOH C O   1 
HETATM 13666 O  O   . HOH BB 8 .   ? 66.927  4.000   101.425 1.00 26.55  ? 815  HOH C O   1 
HETATM 13667 O  O   . HOH BB 8 .   ? 51.370  15.460  72.275  1.00 10.39  ? 816  HOH C O   1 
HETATM 13668 O  O   . HOH BB 8 .   ? 73.701  10.334  94.405  1.00 29.43  ? 817  HOH C O   1 
HETATM 13669 O  O   . HOH BB 8 .   ? 75.859  8.938   93.955  1.00 23.20  ? 818  HOH C O   1 
HETATM 13670 O  O   . HOH BB 8 .   ? 78.213  7.427   67.673  1.00 28.01  ? 819  HOH C O   1 
HETATM 13671 O  O   . HOH BB 8 .   ? 55.217  -18.080 98.226  1.00 13.24  ? 820  HOH C O   1 
HETATM 13672 O  O   . HOH BB 8 .   ? 52.797  -12.028 52.755  1.00 21.95  ? 821  HOH C O   1 
HETATM 13673 O  O   . HOH BB 8 .   ? 45.600  -20.015 71.611  1.00 33.16  ? 822  HOH C O   1 
HETATM 13674 O  O   . HOH BB 8 .   ? 54.221  -13.753 68.022  1.00 11.06  ? 823  HOH C O   1 
HETATM 13675 O  O   . HOH BB 8 .   ? 48.646  15.653  94.435  1.00 35.92  ? 824  HOH C O   1 
HETATM 13676 O  O   . HOH BB 8 .   ? 74.569  -6.235  76.709  1.00 15.99  ? 825  HOH C O   1 
HETATM 13677 O  O   . HOH BB 8 .   ? 40.116  -9.417  76.686  1.00 16.98  ? 826  HOH C O   1 
HETATM 13678 O  O   . HOH BB 8 .   ? 52.780  3.417   60.975  1.00 17.10  ? 827  HOH C O   1 
HETATM 13679 O  O   . HOH BB 8 .   ? 34.788  1.070   88.236  1.00 13.16  ? 828  HOH C O   1 
HETATM 13680 O  O   . HOH BB 8 .   ? 27.961  12.726  75.157  1.00 20.88  ? 829  HOH C O   1 
HETATM 13681 O  O   . HOH BB 8 .   ? 72.578  -7.604  69.848  1.00 15.13  ? 830  HOH C O   1 
HETATM 13682 O  O   . HOH BB 8 .   ? 38.970  26.285  75.967  1.00 37.14  ? 831  HOH C O   1 
HETATM 13683 O  O   . HOH BB 8 .   ? 68.354  -19.768 79.711  1.00 21.82  ? 832  HOH C O   1 
HETATM 13684 O  O   . HOH BB 8 .   ? 52.903  -14.935 101.512 1.00 21.20  ? 833  HOH C O   1 
HETATM 13685 O  O   . HOH BB 8 .   ? 41.761  2.644   91.303  1.00 10.91  ? 834  HOH C O   1 
HETATM 13686 O  O   . HOH BB 8 .   ? 39.264  -15.780 90.906  1.00 28.55  ? 835  HOH C O   1 
HETATM 13687 O  O   . HOH BB 8 .   ? 40.575  -18.968 90.756  1.00 28.91  ? 836  HOH C O   1 
HETATM 13688 O  O   . HOH BB 8 .   ? 65.551  -18.498 97.558  1.00 22.27  ? 837  HOH C O   1 
HETATM 13689 O  O   . HOH BB 8 .   ? 55.505  -24.135 95.053  1.00 31.68  ? 838  HOH C O   1 
HETATM 13690 O  O   . HOH BB 8 .   ? 52.535  -21.003 72.519  1.00 24.86  ? 839  HOH C O   1 
HETATM 13691 O  O   . HOH BB 8 .   ? 81.718  4.776   81.730  1.00 33.68  ? 840  HOH C O   1 
HETATM 13692 O  O   . HOH BB 8 .   ? 66.093  7.626   98.962  1.00 38.49  ? 841  HOH C O   1 
HETATM 13693 O  O   . HOH BB 8 .   ? 65.257  7.847   96.452  1.00 34.39  ? 842  HOH C O   1 
HETATM 13694 O  O   . HOH BB 8 .   ? 60.152  14.274  64.674  1.00 20.44  ? 843  HOH C O   1 
HETATM 13695 O  O   . HOH BB 8 .   ? 57.944  9.675   93.107  1.00 37.82  ? 844  HOH C O   1 
HETATM 13696 O  O   . HOH BB 8 .   ? 49.542  -17.418 60.735  1.00 37.50  ? 845  HOH C O   1 
HETATM 13697 O  O   . HOH BB 8 .   ? 58.810  -26.209 85.969  1.00 31.29  ? 846  HOH C O   1 
HETATM 13698 O  O   . HOH BB 8 .   ? 83.080  -3.233  79.148  1.00 26.09  ? 847  HOH C O   1 
HETATM 13699 O  O   . HOH BB 8 .   ? 54.310  -21.608 71.122  1.00 41.00  ? 848  HOH C O   1 
HETATM 13700 O  O   . HOH BB 8 .   ? 77.977  -10.657 90.947  1.00 33.58  ? 849  HOH C O   1 
HETATM 13701 O  O   . HOH BB 8 .   ? 62.518  -2.817  89.627  1.00 10.17  ? 850  HOH C O   1 
HETATM 13702 O  O   . HOH BB 8 .   ? 61.772  -4.066  87.337  1.00 10.90  ? 851  HOH C O   1 
HETATM 13703 O  O   . HOH BB 8 .   ? 53.397  11.283  86.442  1.00 15.23  ? 852  HOH C O   1 
HETATM 13704 O  O   . HOH BB 8 .   ? 49.827  -1.355  101.989 1.00 12.17  ? 853  HOH C O   1 
HETATM 13705 O  O   . HOH BB 8 .   ? 43.185  -9.462  71.432  1.00 20.07  ? 854  HOH C O   1 
HETATM 13706 O  O   . HOH BB 8 .   ? 47.361  19.936  72.365  1.00 12.82  ? 855  HOH C O   1 
HETATM 13707 O  O   . HOH BB 8 .   ? 51.152  -0.231  60.139  1.00 13.84  ? 856  HOH C O   1 
HETATM 13708 O  O   . HOH BB 8 .   ? 57.312  0.549   51.264  1.00 49.41  ? 857  HOH C O   1 
HETATM 13709 O  O   . HOH BB 8 .   ? 71.278  -16.306 82.332  1.00 20.02  ? 858  HOH C O   1 
HETATM 13710 O  O   . HOH BB 8 .   ? 67.389  16.794  73.192  1.00 24.71  ? 859  HOH C O   1 
HETATM 13711 O  O   . HOH BB 8 .   ? 78.429  -9.664  83.581  1.00 40.64  ? 860  HOH C O   1 
HETATM 13712 O  O   . HOH BB 8 .   ? 68.212  -23.210 91.907  1.00 35.01  ? 861  HOH C O   1 
HETATM 13713 O  O   . HOH BB 8 .   ? 38.531  19.013  83.372  1.00 13.41  ? 862  HOH C O   1 
HETATM 13714 O  O   . HOH BB 8 .   ? 46.711  25.037  85.733  1.00 43.12  ? 863  HOH C O   1 
HETATM 13715 O  O   . HOH BB 8 .   ? 40.331  -10.782 90.924  1.00 29.49  ? 864  HOH C O   1 
HETATM 13716 O  O   . HOH BB 8 .   ? 58.156  -4.902  51.714  1.00 22.30  ? 865  HOH C O   1 
HETATM 13717 O  O   . HOH BB 8 .   ? 67.636  -16.094 66.772  1.00 56.29  ? 866  HOH C O   1 
HETATM 13718 O  O   . HOH BB 8 .   ? 83.487  -1.806  84.201  1.00 16.79  ? 867  HOH C O   1 
HETATM 13719 O  O   . HOH BB 8 .   ? 47.384  16.838  69.504  1.00 40.53  ? 868  HOH C O   1 
HETATM 13720 O  O   . HOH BB 8 .   ? 53.066  20.894  74.591  1.00 30.14  ? 869  HOH C O   1 
HETATM 13721 O  O   . HOH BB 8 .   ? 77.458  0.250   62.970  1.00 39.23  ? 870  HOH C O   1 
HETATM 13722 O  O   . HOH BB 8 .   ? 76.054  6.740   99.718  1.00 27.79  ? 871  HOH C O   1 
HETATM 13723 O  O   . HOH BB 8 .   ? 56.173  4.952   92.417  1.00 22.04  ? 872  HOH C O   1 
HETATM 13724 O  O   . HOH BB 8 .   ? 55.010  9.562   98.080  1.00 26.88  ? 873  HOH C O   1 
HETATM 13725 O  O   . HOH BB 8 .   ? 48.346  -15.808 64.797  1.00 21.94  ? 874  HOH C O   1 
HETATM 13726 O  O   . HOH BB 8 .   ? 80.605  8.178   81.598  1.00 24.10  ? 875  HOH C O   1 
HETATM 13727 O  O   . HOH BB 8 .   ? 71.294  -14.567 95.706  1.00 29.70  ? 876  HOH C O   1 
HETATM 13728 O  O   . HOH BB 8 .   ? 56.407  12.272  82.700  1.00 13.23  ? 877  HOH C O   1 
HETATM 13729 O  O   . HOH BB 8 .   ? 68.452  8.963   66.150  1.00 34.17  ? 878  HOH C O   1 
HETATM 13730 O  O   . HOH BB 8 .   ? 53.177  -7.946  50.527  1.00 33.18  ? 879  HOH C O   1 
HETATM 13731 O  O   . HOH BB 8 .   ? 60.414  9.083   86.619  1.00 21.41  ? 880  HOH C O   1 
HETATM 13732 O  O   . HOH BB 8 .   ? 53.725  22.670  76.600  1.00 39.48  ? 881  HOH C O   1 
HETATM 13733 O  O   . HOH BB 8 .   ? 72.043  -12.606 64.045  1.00 24.71  ? 882  HOH C O   1 
HETATM 13734 O  O   . HOH BB 8 .   ? 66.919  1.727   101.353 1.00 34.58  ? 883  HOH C O   1 
HETATM 13735 O  O   . HOH BB 8 .   ? 53.274  -17.519 88.902  1.00 13.30  ? 884  HOH C O   1 
HETATM 13736 O  O   . HOH BB 8 .   ? 76.189  15.629  75.043  1.00 29.92  ? 885  HOH C O   1 
HETATM 13737 O  O   . HOH BB 8 .   ? 28.078  12.652  82.934  1.00 34.72  ? 886  HOH C O   1 
HETATM 13738 O  O   . HOH BB 8 .   ? 57.051  6.529   104.468 1.00 19.12  ? 887  HOH C O   1 
HETATM 13739 O  O   . HOH BB 8 .   ? 36.683  22.248  91.792  1.00 27.33  ? 888  HOH C O   1 
HETATM 13740 O  O   . HOH BB 8 .   ? 54.958  11.568  93.209  1.00 23.67  ? 889  HOH C O   1 
HETATM 13741 O  O   . HOH BB 8 .   ? 85.982  1.365   63.558  1.00 36.33  ? 890  HOH C O   1 
HETATM 13742 O  O   . HOH BB 8 .   ? 61.463  -14.794 60.991  1.00 17.81  ? 891  HOH C O   1 
HETATM 13743 O  O   . HOH BB 8 .   ? 65.879  -15.733 68.939  1.00 21.13  ? 892  HOH C O   1 
HETATM 13744 O  O   . HOH BB 8 .   ? 43.650  -15.997 84.934  1.00 13.50  ? 893  HOH C O   1 
HETATM 13745 O  O   . HOH BB 8 .   ? 46.401  -6.304  96.148  1.00 13.82  ? 894  HOH C O   1 
HETATM 13746 O  O   . HOH BB 8 .   ? 54.025  9.857   95.224  1.00 16.80  ? 895  HOH C O   1 
HETATM 13747 O  O   . HOH BB 8 .   ? 70.670  11.801  83.263  1.00 42.52  ? 896  HOH C O   1 
HETATM 13748 O  O   . HOH BB 8 .   ? 60.844  4.944   89.048  1.00 28.76  ? 897  HOH C O   1 
HETATM 13749 O  O   . HOH BB 8 .   ? 66.848  -4.076  57.734  1.00 43.44  ? 898  HOH C O   1 
HETATM 13750 O  O   . HOH BB 8 .   ? 46.049  -2.662  62.491  1.00 11.01  ? 899  HOH C O   1 
HETATM 13751 O  O   . HOH BB 8 .   ? 71.229  -13.656 71.593  1.00 42.77  ? 900  HOH C O   1 
HETATM 13752 O  O   . HOH BB 8 .   ? 53.862  15.616  81.016  1.00 10.80  ? 901  HOH C O   1 
HETATM 13753 O  O   . HOH BB 8 .   ? 68.079  -22.093 76.408  1.00 34.49  ? 902  HOH C O   1 
HETATM 13754 O  O   . HOH BB 8 .   ? 56.473  -11.280 60.957  1.00 27.17  ? 903  HOH C O   1 
HETATM 13755 O  O   . HOH BB 8 .   ? 38.926  22.872  95.843  1.00 27.90  ? 904  HOH C O   1 
HETATM 13756 O  O   . HOH BB 8 .   ? 67.634  -13.982 70.856  1.00 44.17  ? 905  HOH C O   1 
HETATM 13757 O  O   . HOH BB 8 .   ? 45.270  22.343  71.897  1.00 21.06  ? 906  HOH C O   1 
HETATM 13758 O  O   . HOH BB 8 .   ? 37.088  -7.362  78.996  1.00 28.32  ? 907  HOH C O   1 
HETATM 13759 O  O   . HOH BB 8 .   ? 82.511  0.383   88.503  1.00 28.34  ? 908  HOH C O   1 
HETATM 13760 O  O   . HOH BB 8 .   ? 62.976  -11.021 100.854 1.00 45.60  ? 909  HOH C O   1 
HETATM 13761 O  O   . HOH BB 8 .   ? 60.951  18.716  73.176  1.00 39.56  ? 910  HOH C O   1 
HETATM 13762 O  O   . HOH BB 8 .   ? 63.964  9.970   89.958  1.00 34.12  ? 911  HOH C O   1 
HETATM 13763 O  O   . HOH BB 8 .   ? 63.011  5.050   76.163  1.00 11.24  ? 912  HOH C O   1 
HETATM 13764 O  O   . HOH BB 8 .   ? 53.161  11.829  60.738  1.00 19.97  ? 913  HOH C O   1 
HETATM 13765 O  O   . HOH BB 8 .   ? 76.613  -11.333 85.775  1.00 20.04  ? 914  HOH C O   1 
HETATM 13766 O  O   . HOH BB 8 .   ? 69.977  11.198  70.799  1.00 37.53  ? 915  HOH C O   1 
HETATM 13767 O  O   . HOH BB 8 .   ? 47.539  22.131  68.477  1.00 43.77  ? 916  HOH C O   1 
HETATM 13768 O  O   . HOH BB 8 .   ? 63.362  18.272  72.632  1.00 32.77  ? 917  HOH C O   1 
HETATM 13769 O  O   . HOH BB 8 .   ? 58.768  -25.468 69.031  1.00 31.18  ? 918  HOH C O   1 
HETATM 13770 O  O   . HOH BB 8 .   ? 34.529  18.776  86.620  1.00 40.05  ? 919  HOH C O   1 
HETATM 13771 O  O   . HOH BB 8 .   ? 50.882  17.923  72.820  1.00 32.29  ? 920  HOH C O   1 
HETATM 13772 O  O   . HOH BB 8 .   ? 70.195  21.792  80.917  1.00 26.96  ? 921  HOH C O   1 
HETATM 13773 O  O   . HOH BB 8 .   ? 54.594  7.618   102.202 1.00 13.44  ? 922  HOH C O   1 
HETATM 13774 O  O   . HOH BB 8 .   ? 39.816  -12.019 79.853  1.00 33.25  ? 923  HOH C O   1 
HETATM 13775 O  O   . HOH BB 8 .   ? 34.374  -4.669  77.084  1.00 40.50  ? 924  HOH C O   1 
HETATM 13776 O  O   . HOH BB 8 .   ? 77.527  3.758   63.221  1.00 38.79  ? 925  HOH C O   1 
HETATM 13777 O  O   . HOH BB 8 .   ? 42.970  -21.006 71.960  1.00 42.84  ? 926  HOH C O   1 
HETATM 13778 O  O   . HOH BB 8 .   ? 61.654  5.690   102.700 1.00 34.18  ? 927  HOH C O   1 
HETATM 13779 O  O   . HOH BB 8 .   ? 50.795  17.317  66.589  1.00 37.18  ? 928  HOH C O   1 
HETATM 13780 O  O   . HOH BB 8 .   ? 52.348  16.600  64.825  1.00 29.09  ? 929  HOH C O   1 
HETATM 13781 O  O   . HOH BB 8 .   ? 56.814  -26.271 93.786  1.00 41.64  ? 930  HOH C O   1 
HETATM 13782 O  O   . HOH BB 8 .   ? 43.775  -20.676 88.743  1.00 46.21  ? 931  HOH C O   1 
HETATM 13783 O  O   . HOH BB 8 .   ? 77.037  -6.779  60.770  1.00 50.74  ? 932  HOH C O   1 
HETATM 13784 O  O   . HOH BB 8 .   ? 47.426  11.389  97.543  1.00 27.57  ? 933  HOH C O   1 
HETATM 13785 O  O   . HOH BB 8 .   ? 83.154  4.369   78.252  1.00 28.63  ? 934  HOH C O   1 
HETATM 13786 O  O   . HOH BB 8 .   ? 43.212  -22.831 83.697  1.00 39.68  ? 935  HOH C O   1 
HETATM 13787 O  O   . HOH BB 8 .   ? 45.896  -18.233 62.253  1.00 26.24  ? 936  HOH C O   1 
HETATM 13788 O  O   . HOH BB 8 .   ? 52.379  -18.859 99.174  1.00 36.26  ? 937  HOH C O   1 
HETATM 13789 O  O   . HOH BB 8 .   ? 55.084  4.011   89.461  1.00 61.02  ? 938  HOH C O   1 
HETATM 13790 O  O   . HOH BB 8 .   ? 54.308  12.970  84.352  1.00 20.62  ? 939  HOH C O   1 
HETATM 13791 O  O   . HOH BB 8 .   ? 77.397  -3.856  64.070  1.00 48.38  ? 940  HOH C O   1 
HETATM 13792 O  O   . HOH BB 8 .   ? 83.766  6.934   73.456  1.00 35.45  ? 941  HOH C O   1 
HETATM 13793 O  O   . HOH BB 8 .   ? 82.330  -6.950  69.676  1.00 30.93  ? 942  HOH C O   1 
HETATM 13794 O  O   . HOH BB 8 .   ? 79.806  6.401   92.986  1.00 33.10  ? 943  HOH C O   1 
HETATM 13795 O  O   . HOH BB 8 .   ? 60.822  13.011  83.970  1.00 32.31  ? 944  HOH C O   1 
HETATM 13796 O  O   . HOH BB 8 .   ? 57.939  -1.698  50.176  1.00 38.16  ? 945  HOH C O   1 
HETATM 13797 O  O   . HOH BB 8 .   ? 83.763  3.124   82.818  1.00 22.72  ? 946  HOH C O   1 
HETATM 13798 O  O   . HOH BB 8 .   ? 69.027  20.880  73.723  1.00 41.75  ? 947  HOH C O   1 
HETATM 13799 O  O   . HOH BB 8 .   ? 86.016  5.445   74.059  1.00 44.21  ? 948  HOH C O   1 
HETATM 13800 O  O   . HOH BB 8 .   ? 53.292  7.923   99.361  1.00 20.00  ? 949  HOH C O   1 
HETATM 13801 O  O   . HOH BB 8 .   ? 47.286  15.896  66.323  1.00 37.53  ? 950  HOH C O   1 
HETATM 13802 O  O   . HOH BB 8 .   ? 70.099  13.670  85.153  1.00 46.82  ? 951  HOH C O   1 
HETATM 13803 O  O   . HOH BB 8 .   ? 33.649  -5.172  82.647  1.00 40.12  ? 952  HOH C O   1 
HETATM 13804 O  O   . HOH BB 8 .   ? 47.795  -10.128 69.063  1.00 31.73  ? 953  HOH C O   1 
HETATM 13805 O  O   . HOH BB 8 .   ? 50.608  16.028  63.171  1.00 41.68  ? 954  HOH C O   1 
HETATM 13806 O  O   . HOH BB 8 .   ? 73.340  -3.220  93.425  1.00 21.19  ? 955  HOH C O   1 
HETATM 13807 O  O   . HOH BB 8 .   ? 59.242  -25.354 95.849  1.00 50.27  ? 956  HOH C O   1 
HETATM 13808 O  O   . HOH BB 8 .   ? 62.605  10.742  87.906  1.00 31.43  ? 957  HOH C O   1 
HETATM 13809 O  O   . HOH BB 8 .   ? 67.794  -12.211 99.265  1.00 40.19  ? 958  HOH C O   1 
HETATM 13810 O  O   . HOH BB 8 .   ? 81.134  3.464   86.898  1.00 26.24  ? 959  HOH C O   1 
HETATM 13811 O  O   . HOH BB 8 .   ? 71.283  13.225  70.780  1.00 33.94  ? 960  HOH C O   1 
HETATM 13812 O  O   . HOH BB 8 .   ? 33.535  -5.705  72.902  1.00 31.00  ? 961  HOH C O   1 
HETATM 13813 O  O   . HOH BB 8 .   ? 44.447  -20.415 61.756  1.00 35.05  ? 962  HOH C O   1 
HETATM 13814 O  O   . HOH BB 8 .   ? 50.151  -21.304 70.963  1.00 42.80  ? 963  HOH C O   1 
HETATM 13815 O  O   . HOH BB 8 .   ? 80.384  -0.556  63.291  1.00 42.21  ? 964  HOH C O   1 
HETATM 13816 O  O   . HOH BB 8 .   ? 48.641  9.441   99.197  1.00 20.70  ? 965  HOH C O   1 
HETATM 13817 O  O   . HOH BB 8 .   ? 52.266  19.939  89.992  1.00 33.26  ? 966  HOH C O   1 
HETATM 13818 O  O   . HOH BB 8 .   ? 66.245  -27.619 77.843  1.00 64.20  ? 967  HOH C O   1 
HETATM 13819 O  O   . HOH BB 8 .   ? 32.290  14.711  81.503  1.00 38.43  ? 968  HOH C O   1 
HETATM 13820 O  O   . HOH BB 8 .   ? 83.149  -6.005  73.412  1.00 32.81  ? 969  HOH C O   1 
HETATM 13821 O  O   . HOH BB 8 .   ? 58.876  7.233   88.835  1.00 32.71  ? 970  HOH C O   1 
HETATM 13822 O  O   . HOH BB 8 .   ? 56.859  17.363  72.619  1.00 28.94  ? 971  HOH C O   1 
HETATM 13823 O  O   . HOH BB 8 .   ? 63.150  -27.509 83.045  1.00 34.07  ? 972  HOH C O   1 
HETATM 13824 O  O   . HOH BB 8 .   ? 62.792  5.694   90.356  1.00 41.64  ? 973  HOH C O   1 
HETATM 13825 O  O   . HOH BB 8 .   ? 75.621  -4.853  60.548  1.00 33.88  ? 974  HOH C O   1 
HETATM 13826 O  O   . HOH BB 8 .   ? 47.631  15.250  63.984  1.00 31.10  ? 975  HOH C O   1 
HETATM 13827 O  O   . HOH BB 8 .   ? 33.041  -4.325  79.581  1.00 31.57  ? 976  HOH C O   1 
HETATM 13828 O  O   . HOH BB 8 .   ? 43.062  27.253  93.443  1.00 49.20  ? 977  HOH C O   1 
HETATM 13829 O  O   . HOH BB 8 .   ? 62.058  -25.731 76.087  1.00 34.19  ? 978  HOH C O   1 
HETATM 13830 O  O   . HOH BB 8 .   ? 58.651  16.546  63.964  1.00 32.18  ? 979  HOH C O   1 
HETATM 13831 O  O   . HOH BB 8 .   ? 53.261  -22.627 100.058 1.00 42.39  ? 980  HOH C O   1 
HETATM 13832 O  O   . HOH BB 8 .   ? 56.032  9.846   102.898 1.00 36.29  ? 981  HOH C O   1 
HETATM 13833 O  O   . HOH BB 8 .   ? 41.323  -7.380  71.106  1.00 29.22  ? 982  HOH C O   1 
HETATM 13834 O  O   . HOH BB 8 .   ? 73.160  -13.739 68.711  1.00 39.94  ? 983  HOH C O   1 
HETATM 13835 O  O   . HOH BB 8 .   ? 66.276  -17.923 69.899  1.00 25.37  ? 984  HOH C O   1 
HETATM 13836 O  O   . HOH BB 8 .   ? 71.181  5.879   100.481 1.00 44.04  ? 985  HOH C O   1 
HETATM 13837 O  O   . HOH BB 8 .   ? 55.586  7.361   106.453 1.00 30.68  ? 986  HOH C O   1 
HETATM 13838 O  O   . HOH BB 8 .   ? 41.919  15.540  96.059  1.00 37.76  ? 987  HOH C O   1 
HETATM 13839 O  O   . HOH BB 8 .   ? 74.050  -3.859  95.903  1.00 31.65  ? 988  HOH C O   1 
HETATM 13840 O  O   . HOH BB 8 .   ? 56.903  20.103  71.794  1.00 33.40  ? 989  HOH C O   1 
HETATM 13841 O  O   . HOH BB 8 .   ? 69.684  -12.583 62.932  1.00 41.11  ? 990  HOH C O   1 
HETATM 13842 O  O   . HOH BB 8 .   ? 38.948  -20.694 89.437  1.00 48.56  ? 991  HOH C O   1 
HETATM 13843 O  O   . HOH BB 8 .   ? 28.554  15.667  79.672  1.00 40.11  ? 992  HOH C O   1 
HETATM 13844 O  O   . HOH BB 8 .   ? 53.602  19.986  87.694  1.00 32.74  ? 993  HOH C O   1 
HETATM 13845 O  O   . HOH BB 8 .   ? 44.203  -19.943 93.261  1.00 31.89  ? 994  HOH C O   1 
HETATM 13846 O  O   . HOH BB 8 .   ? 58.804  14.019  84.063  1.00 30.01  ? 995  HOH C O   1 
HETATM 13847 O  O   . HOH BB 8 .   ? 61.669  5.638   93.939  1.00 20.88  ? 996  HOH C O   1 
HETATM 13848 O  O   . HOH BB 8 .   ? 39.586  -15.275 86.580  1.00 42.94  ? 997  HOH C O   1 
HETATM 13849 O  O   . HOH BB 8 .   ? 74.362  -11.715 70.068  1.00 35.62  ? 998  HOH C O   1 
HETATM 13850 O  O   . HOH BB 8 .   ? 37.402  21.436  84.112  1.00 28.74  ? 999  HOH C O   1 
HETATM 13851 O  O   . HOH BB 8 .   ? 27.050  14.669  76.706  1.00 33.68  ? 1000 HOH C O   1 
HETATM 13852 O  O   . HOH BB 8 .   ? 70.314  -17.464 79.915  1.00 24.78  ? 1001 HOH C O   1 
HETATM 13853 O  O   . HOH BB 8 .   ? 69.635  -14.476 98.713  1.00 47.95  ? 1002 HOH C O   1 
HETATM 13854 O  O   . HOH BB 8 .   ? 66.193  -13.663 62.744  1.00 46.08  ? 1003 HOH C O   1 
HETATM 13855 O  O   . HOH BB 8 .   ? 58.496  21.454  82.249  1.00 41.09  ? 1004 HOH C O   1 
HETATM 13856 O  O   . HOH BB 8 .   ? 67.567  -11.963 60.204  1.00 62.93  ? 1005 HOH C O   1 
HETATM 13857 O  O   . HOH BB 8 .   ? 74.847  -12.365 78.053  1.00 39.07  ? 1006 HOH C O   1 
HETATM 13858 O  O   . HOH BB 8 .   ? 41.102  -11.611 76.492  1.00 40.72  ? 1007 HOH C O   1 
HETATM 13859 O  O   . HOH BB 8 .   ? 86.375  2.137   74.443  1.00 27.10  ? 1008 HOH C O   1 
HETATM 13860 O  O   . HOH BB 8 .   ? 65.904  -20.718 69.236  1.00 32.87  ? 1009 HOH C O   1 
HETATM 13861 O  O   . HOH BB 8 .   ? 41.193  18.990  86.525  1.00 13.83  ? 1010 HOH C O   1 
HETATM 13862 O  O   . HOH BB 8 .   ? 51.893  -22.680 74.382  1.00 22.20  ? 1011 HOH C O   1 
HETATM 13863 O  O   . HOH BB 8 .   ? 55.988  -23.330 97.424  1.00 39.10  ? 1012 HOH C O   1 
HETATM 13864 O  O   . HOH BB 8 .   ? 71.569  -14.759 75.879  1.00 26.84  ? 1013 HOH C O   1 
HETATM 13865 O  O   . HOH BB 8 .   ? 49.637  19.149  90.486  1.00 26.09  ? 1014 HOH C O   1 
HETATM 13866 O  O   . HOH BB 8 .   ? 52.392  2.631   110.712 1.00 41.19  ? 1015 HOH C O   1 
HETATM 13867 O  O   . HOH BB 8 .   ? 64.889  -24.316 76.042  1.00 47.96  ? 1016 HOH C O   1 
HETATM 13868 O  O   . HOH BB 8 .   ? 56.789  11.435  61.641  1.00 31.30  ? 1017 HOH C O   1 
HETATM 13869 O  O   . HOH BB 8 .   ? 48.543  13.072  61.091  1.00 30.23  ? 1018 HOH C O   1 
HETATM 13870 O  O   . HOH BB 8 .   ? 57.964  3.623   91.287  1.00 34.76  ? 1019 HOH C O   1 
HETATM 13871 O  O   . HOH BB 8 .   ? 49.172  21.598  72.437  1.00 32.07  ? 1020 HOH C O   1 
HETATM 13872 O  O   . HOH BB 8 .   ? 39.195  20.286  87.938  1.00 17.51  ? 1021 HOH C O   1 
HETATM 13873 O  O   . HOH BB 8 .   ? 80.798  12.152  72.956  1.00 37.42  ? 1022 HOH C O   1 
HETATM 13874 O  O   . HOH BB 8 .   ? 31.430  -6.221  82.273  1.00 60.66  ? 1023 HOH C O   1 
HETATM 13875 O  O   . HOH BB 8 .   ? 61.564  -25.526 85.013  1.00 18.45  ? 1024 HOH C O   1 
HETATM 13876 O  O   . HOH BB 8 .   ? 37.513  1.610   88.537  1.00 11.86  ? 1025 HOH C O   1 
HETATM 13877 O  O   . HOH BB 8 .   ? 79.316  9.747   76.657  1.00 30.94  ? 1026 HOH C O   1 
HETATM 13878 O  O   . HOH BB 8 .   ? 56.289  -27.009 67.305  1.00 33.90  ? 1027 HOH C O   1 
HETATM 13879 O  O   . HOH BB 8 .   ? 59.826  7.972   104.150 1.00 31.10  ? 1028 HOH C O   1 
HETATM 13880 O  O   . HOH BB 8 .   ? 41.645  23.355  84.955  1.00 22.13  ? 1029 HOH C O   1 
HETATM 13881 O  O   . HOH BB 8 .   ? 77.552  -8.339  93.585  1.00 45.79  ? 1030 HOH C O   1 
HETATM 13882 O  O   . HOH BB 8 .   ? 53.140  -10.118 48.746  1.00 62.29  ? 1031 HOH C O   1 
HETATM 13883 O  O   . HOH BB 8 .   ? 43.296  -20.309 63.520  1.00 44.49  ? 1032 HOH C O   1 
HETATM 13884 O  O   . HOH BB 8 .   ? 56.413  13.381  85.858  1.00 38.08  ? 1033 HOH C O   1 
HETATM 13885 O  O   . HOH BB 8 .   ? 81.376  8.137   76.820  1.00 25.87  ? 1034 HOH C O   1 
HETATM 13886 O  O   . HOH BB 8 .   ? 78.852  14.034  78.578  1.00 42.46  ? 1035 HOH C O   1 
HETATM 13887 O  O   . HOH BB 8 .   ? 56.207  -11.850 56.212  1.00 36.98  ? 1036 HOH C O   1 
HETATM 13888 O  O   . HOH BB 8 .   ? 77.336  10.432  91.015  1.00 36.13  ? 1037 HOH C O   1 
HETATM 13889 O  O   . HOH BB 8 .   ? 63.064  9.731   92.485  1.00 47.72  ? 1038 HOH C O   1 
HETATM 13890 O  O   . HOH BB 8 .   ? 42.540  26.149  88.633  1.00 36.93  ? 1039 HOH C O   1 
HETATM 13891 O  O   . HOH BB 8 .   ? 74.053  -15.652 78.632  1.00 35.77  ? 1040 HOH C O   1 
HETATM 13892 O  O   . HOH BB 8 .   ? 56.130  -6.623  50.052  1.00 34.91  ? 1041 HOH C O   1 
HETATM 13893 O  O   . HOH BB 8 .   ? 50.730  23.542  76.396  1.00 42.61  ? 1042 HOH C O   1 
HETATM 13894 O  O   . HOH BB 8 .   ? 53.170  -12.403 49.502  1.00 40.90  ? 1043 HOH C O   1 
HETATM 13895 O  O   . HOH BB 8 .   ? 56.821  13.973  88.167  1.00 38.68  ? 1044 HOH C O   1 
HETATM 13896 O  O   . HOH BB 8 .   ? 47.561  -21.916 72.715  1.00 31.49  ? 1045 HOH C O   1 
HETATM 13897 O  O   . HOH BB 8 .   ? 52.087  7.683   103.608 1.00 30.18  ? 1046 HOH C O   1 
HETATM 13898 O  O   . HOH BB 8 .   ? 55.968  13.956  80.607  1.00 14.51  ? 1047 HOH C O   1 
HETATM 13899 O  O   . HOH BB 8 .   ? 59.326  13.369  62.238  1.00 38.49  ? 1048 HOH C O   1 
HETATM 13900 O  O   . HOH BB 8 .   ? 52.935  12.159  57.765  1.00 30.44  ? 1049 HOH C O   1 
HETATM 13901 O  O   . HOH BB 8 .   ? 39.366  23.023  86.867  1.00 28.93  ? 1050 HOH C O   1 
HETATM 13902 O  O   . HOH BB 8 .   ? 71.721  -16.755 77.886  1.00 23.52  ? 1051 HOH C O   1 
HETATM 13903 O  O   . HOH BB 8 .   ? 61.096  -9.934  106.205 1.00 38.00  ? 1052 HOH C O   1 
HETATM 13904 O  O   . HOH BB 8 .   ? 60.930  -11.927 104.640 1.00 49.25  ? 1053 HOH C O   1 
HETATM 13905 O  O   . HOH BB 8 .   ? 49.655  14.245  58.742  1.00 44.00  ? 1054 HOH C O   1 
HETATM 13906 O  O   . HOH CB 8 .   ? 43.316  4.636   119.655 1.00 38.81  ? 601  HOH D O   1 
HETATM 13907 O  O   . HOH CB 8 .   ? 34.047  11.814  83.815  1.00 27.97  ? 602  HOH D O   1 
HETATM 13908 O  O   . HOH CB 8 .   ? 32.627  -10.061 86.500  1.00 26.29  ? 603  HOH D O   1 
HETATM 13909 O  O   . HOH CB 8 .   ? 34.421  -10.618 90.817  1.00 24.60  ? 604  HOH D O   1 
HETATM 13910 O  O   . HOH CB 8 .   ? 45.372  1.294   116.669 1.00 30.42  ? 605  HOH D O   1 
HETATM 13911 O  O   . HOH CB 8 .   ? 21.259  -22.716 123.033 1.00 44.85  ? 606  HOH D O   1 
HETATM 13912 O  O   . HOH CB 8 .   ? 32.619  17.505  88.160  1.00 21.76  ? 607  HOH D O   1 
HETATM 13913 O  O   . HOH CB 8 .   ? 29.699  10.990  117.621 1.00 45.13  ? 608  HOH D O   1 
HETATM 13914 O  O   . HOH CB 8 .   ? 30.870  -33.714 98.623  1.00 47.40  ? 609  HOH D O   1 
HETATM 13915 O  O   . HOH CB 8 .   ? 34.471  -28.902 114.957 1.00 43.71  ? 610  HOH D O   1 
HETATM 13916 O  O   . HOH CB 8 .   ? 0.819   -3.183  104.702 1.00 34.83  ? 611  HOH D O   1 
HETATM 13917 O  O   . HOH CB 8 .   ? 34.371  16.471  105.322 1.00 23.64  ? 612  HOH D O   1 
HETATM 13918 O  O   . HOH CB 8 .   ? 30.931  1.225   97.025  1.00 13.42  ? 613  HOH D O   1 
HETATM 13919 O  O   . HOH CB 8 .   ? 20.356  -2.943  108.936 1.00 37.09  ? 614  HOH D O   1 
HETATM 13920 O  O   . HOH CB 8 .   ? 28.457  6.767   116.458 1.00 16.35  ? 615  HOH D O   1 
HETATM 13921 O  O   . HOH CB 8 .   ? 32.443  -20.197 119.781 1.00 26.45  ? 616  HOH D O   1 
HETATM 13922 O  O   . HOH CB 8 .   ? 26.326  -2.672  80.762  1.00 28.88  ? 617  HOH D O   1 
HETATM 13923 O  O   . HOH CB 8 .   ? 31.605  -17.209 122.244 1.00 17.08  ? 618  HOH D O   1 
HETATM 13924 O  O   . HOH CB 8 .   ? 19.264  1.525   122.113 1.00 25.00  ? 619  HOH D O   1 
HETATM 13925 O  O   . HOH CB 8 .   ? 21.047  3.261   104.962 1.00 12.56  ? 620  HOH D O   1 
HETATM 13926 O  O   . HOH CB 8 .   ? 33.614  -0.203  116.621 1.00 12.10  ? 621  HOH D O   1 
HETATM 13927 O  O   . HOH CB 8 .   ? 32.516  -15.914 100.650 1.00 11.00  ? 622  HOH D O   1 
HETATM 13928 O  O   . HOH CB 8 .   ? 44.558  -20.159 123.397 1.00 30.18  ? 623  HOH D O   1 
HETATM 13929 O  O   . HOH CB 8 .   ? 19.839  -24.365 119.844 1.00 17.66  ? 624  HOH D O   1 
HETATM 13930 O  O   . HOH CB 8 .   ? 27.962  -23.854 121.077 1.00 21.52  ? 625  HOH D O   1 
HETATM 13931 O  O   . HOH CB 8 .   ? 27.504  -3.997  105.786 1.00 9.81   ? 626  HOH D O   1 
HETATM 13932 O  O   . HOH CB 8 .   ? 36.552  -25.231 99.569  1.00 18.35  ? 627  HOH D O   1 
HETATM 13933 O  O   . HOH CB 8 .   ? 17.652  -9.854  89.070  1.00 28.14  ? 628  HOH D O   1 
HETATM 13934 O  O   . HOH CB 8 .   ? 41.295  19.688  96.100  1.00 28.19  ? 629  HOH D O   1 
HETATM 13935 O  O   . HOH CB 8 .   ? 32.336  -15.811 106.056 1.00 12.69  ? 630  HOH D O   1 
HETATM 13936 O  O   . HOH CB 8 .   ? 27.843  -15.872 92.880  1.00 17.79  ? 631  HOH D O   1 
HETATM 13937 O  O   . HOH CB 8 .   ? 41.493  -16.228 98.072  1.00 29.89  ? 632  HOH D O   1 
HETATM 13938 O  O   . HOH CB 8 .   ? 33.267  -8.141  127.350 1.00 13.54  ? 633  HOH D O   1 
HETATM 13939 O  O   . HOH CB 8 .   ? 32.581  -15.176 123.974 1.00 22.04  ? 634  HOH D O   1 
HETATM 13940 O  O   . HOH CB 8 .   ? 48.275  -16.049 115.174 1.00 17.77  ? 635  HOH D O   1 
HETATM 13941 O  O   . HOH CB 8 .   ? 32.157  -1.115  112.055 1.00 9.87   ? 636  HOH D O   1 
HETATM 13942 O  O   . HOH CB 8 .   ? 37.168  1.107   91.177  1.00 10.96  ? 637  HOH D O   1 
HETATM 13943 O  O   . HOH CB 8 .   ? 16.718  -21.704 91.438  1.00 35.09  ? 638  HOH D O   1 
HETATM 13944 O  O   . HOH CB 8 .   ? 19.870  0.939   91.596  1.00 13.43  ? 639  HOH D O   1 
HETATM 13945 O  O   . HOH CB 8 .   ? 23.518  14.522  93.913  1.00 12.23  ? 640  HOH D O   1 
HETATM 13946 O  O   . HOH CB 8 .   ? 39.517  -23.291 100.457 1.00 13.23  ? 641  HOH D O   1 
HETATM 13947 O  O   . HOH CB 8 .   ? 9.923   -8.397  100.359 1.00 13.46  ? 642  HOH D O   1 
HETATM 13948 O  O   . HOH CB 8 .   ? 15.922  -21.856 120.918 1.00 25.08  ? 643  HOH D O   1 
HETATM 13949 O  O   . HOH CB 8 .   ? 31.394  6.942   123.917 1.00 14.17  ? 644  HOH D O   1 
HETATM 13950 O  O   . HOH CB 8 .   ? 27.855  -31.688 116.586 1.00 20.40  ? 645  HOH D O   1 
HETATM 13951 O  O   . HOH CB 8 .   ? 28.043  5.963   95.646  1.00 9.01   ? 646  HOH D O   1 
HETATM 13952 O  O   . HOH CB 8 .   ? 31.373  -17.750 130.341 1.00 27.78  ? 647  HOH D O   1 
HETATM 13953 O  O   . HOH CB 8 .   ? 40.787  3.310   119.587 1.00 11.98  ? 648  HOH D O   1 
HETATM 13954 O  O   . HOH CB 8 .   ? 15.109  -18.454 123.962 1.00 34.93  ? 649  HOH D O   1 
HETATM 13955 O  O   . HOH CB 8 .   ? 21.614  -2.698  88.821  1.00 16.49  ? 650  HOH D O   1 
HETATM 13956 O  O   . HOH CB 8 .   ? 15.288  -24.903 95.613  1.00 18.15  ? 651  HOH D O   1 
HETATM 13957 O  O   . HOH CB 8 .   ? 18.357  17.221  94.429  1.00 10.95  ? 652  HOH D O   1 
HETATM 13958 O  O   . HOH CB 8 .   ? 34.413  -2.080  85.009  1.00 23.77  ? 653  HOH D O   1 
HETATM 13959 O  O   . HOH CB 8 .   ? 27.334  0.311   122.159 1.00 19.73  ? 654  HOH D O   1 
HETATM 13960 O  O   . HOH CB 8 .   ? 36.821  1.452   124.325 1.00 14.34  ? 655  HOH D O   1 
HETATM 13961 O  O   . HOH CB 8 .   ? 23.075  -11.557 129.487 1.00 22.72  ? 656  HOH D O   1 
HETATM 13962 O  O   . HOH CB 8 .   ? 21.830  -24.126 100.303 1.00 12.62  ? 657  HOH D O   1 
HETATM 13963 O  O   . HOH CB 8 .   ? 31.126  7.116   109.228 1.00 12.77  ? 658  HOH D O   1 
HETATM 13964 O  O   . HOH CB 8 .   ? 20.525  6.432   108.085 1.00 25.10  ? 659  HOH D O   1 
HETATM 13965 O  O   . HOH CB 8 .   ? 39.872  -15.975 102.156 1.00 11.32  ? 660  HOH D O   1 
HETATM 13966 O  O   . HOH CB 8 .   ? 40.779  -21.337 101.898 1.00 12.10  ? 661  HOH D O   1 
HETATM 13967 O  O   . HOH CB 8 .   ? 29.346  -11.954 107.368 1.00 10.97  ? 662  HOH D O   1 
HETATM 13968 O  O   . HOH CB 8 .   ? 15.048  -15.159 87.736  1.00 23.55  ? 663  HOH D O   1 
HETATM 13969 O  O   . HOH CB 8 .   ? 18.222  -0.174  105.740 1.00 25.07  ? 664  HOH D O   1 
HETATM 13970 O  O   . HOH CB 8 .   ? 37.219  -5.767  88.747  1.00 12.35  ? 665  HOH D O   1 
HETATM 13971 O  O   . HOH CB 8 .   ? 52.314  -2.272  102.960 1.00 11.52  ? 666  HOH D O   1 
HETATM 13972 O  O   . HOH CB 8 .   ? 13.063  -25.307 116.236 1.00 40.61  ? 667  HOH D O   1 
HETATM 13973 O  O   . HOH CB 8 .   ? 50.592  -9.520  114.721 1.00 20.28  ? 668  HOH D O   1 
HETATM 13974 O  O   . HOH CB 8 .   ? 41.999  12.900  98.103  1.00 32.32  ? 669  HOH D O   1 
HETATM 13975 O  O   . HOH CB 8 .   ? 35.133  -7.453  123.643 1.00 17.70  ? 670  HOH D O   1 
HETATM 13976 O  O   . HOH CB 8 .   ? 39.599  -5.843  93.225  1.00 16.64  ? 671  HOH D O   1 
HETATM 13977 O  O   . HOH CB 8 .   ? 37.099  -21.758 118.784 1.00 38.68  ? 672  HOH D O   1 
HETATM 13978 O  O   . HOH CB 8 .   ? 22.160  9.946   122.140 1.00 39.38  ? 673  HOH D O   1 
HETATM 13979 O  O   . HOH CB 8 .   ? 10.606  -25.684 103.986 1.00 27.29  ? 674  HOH D O   1 
HETATM 13980 O  O   . HOH CB 8 .   ? 33.017  21.563  103.757 1.00 37.63  ? 675  HOH D O   1 
HETATM 13981 O  O   . HOH CB 8 .   ? 49.075  -4.093  104.441 1.00 11.94  ? 676  HOH D O   1 
HETATM 13982 O  O   . HOH CB 8 .   ? 39.345  1.487   132.480 1.00 50.13  ? 677  HOH D O   1 
HETATM 13983 O  O   . HOH CB 8 .   ? 30.203  18.550  104.910 1.00 17.83  ? 678  HOH D O   1 
HETATM 13984 O  O   . HOH CB 8 .   ? 8.580   -19.171 113.556 1.00 38.83  ? 679  HOH D O   1 
HETATM 13985 O  O   . HOH CB 8 .   ? 10.522  -5.099  123.672 1.00 21.67  ? 680  HOH D O   1 
HETATM 13986 O  O   . HOH CB 8 .   ? 37.043  2.916   98.507  1.00 9.98   ? 681  HOH D O   1 
HETATM 13987 O  O   . HOH CB 8 .   ? 47.944  -21.447 96.736  1.00 35.05  ? 682  HOH D O   1 
HETATM 13988 O  O   . HOH CB 8 .   ? 42.486  -0.900  125.276 1.00 34.73  ? 683  HOH D O   1 
HETATM 13989 O  O   . HOH CB 8 .   ? 12.379  -8.771  99.125  1.00 14.43  ? 684  HOH D O   1 
HETATM 13990 O  O   . HOH CB 8 .   ? 27.518  10.398  116.238 1.00 27.58  ? 685  HOH D O   1 
HETATM 13991 O  O   . HOH CB 8 .   ? 39.021  10.478  102.513 1.00 15.75  ? 686  HOH D O   1 
HETATM 13992 O  O   . HOH CB 8 .   ? 43.840  -21.869 113.213 1.00 32.85  ? 687  HOH D O   1 
HETATM 13993 O  O   . HOH CB 8 .   ? 26.593  16.943  96.022  1.00 11.81  ? 688  HOH D O   1 
HETATM 13994 O  O   . HOH CB 8 .   ? 46.964  -15.349 106.751 1.00 13.29  ? 689  HOH D O   1 
HETATM 13995 O  O   . HOH CB 8 .   ? 28.979  -17.873 121.345 1.00 15.70  ? 690  HOH D O   1 
HETATM 13996 O  O   . HOH CB 8 .   ? 43.066  -5.552  132.796 1.00 44.16  ? 691  HOH D O   1 
HETATM 13997 O  O   . HOH CB 8 .   ? 31.869  -26.054 94.094  1.00 24.79  ? 692  HOH D O   1 
HETATM 13998 O  O   . HOH CB 8 .   ? 16.569  16.049  101.964 1.00 32.96  ? 693  HOH D O   1 
HETATM 13999 O  O   . HOH CB 8 .   ? 20.085  12.807  103.053 1.00 11.08  ? 694  HOH D O   1 
HETATM 14000 O  O   . HOH CB 8 .   ? 45.188  -12.957 130.711 1.00 34.77  ? 695  HOH D O   1 
HETATM 14001 O  O   . HOH CB 8 .   ? 2.950   -7.535  110.748 1.00 34.59  ? 696  HOH D O   1 
HETATM 14002 O  O   . HOH CB 8 .   ? 37.426  -15.108 131.292 1.00 20.54  ? 697  HOH D O   1 
HETATM 14003 O  O   . HOH CB 8 .   ? 29.828  -29.199 111.650 1.00 19.64  ? 698  HOH D O   1 
HETATM 14004 O  O   . HOH CB 8 .   ? 15.836  5.326   101.247 1.00 14.99  ? 699  HOH D O   1 
HETATM 14005 O  O   . HOH CB 8 .   ? 30.783  -15.407 90.031  1.00 32.13  ? 700  HOH D O   1 
HETATM 14006 O  O   . HOH CB 8 .   ? 10.080  0.167   105.807 1.00 16.62  ? 701  HOH D O   1 
HETATM 14007 O  O   . HOH CB 8 .   ? 33.079  -9.760  134.341 1.00 44.19  ? 702  HOH D O   1 
HETATM 14008 O  O   . HOH CB 8 .   ? 25.811  -2.281  132.993 1.00 17.98  ? 703  HOH D O   1 
HETATM 14009 O  O   . HOH CB 8 .   ? 35.649  11.145  117.753 1.00 34.74  ? 704  HOH D O   1 
HETATM 14010 O  O   . HOH CB 8 .   ? 51.769  -15.607 115.197 1.00 25.47  ? 705  HOH D O   1 
HETATM 14011 O  O   . HOH CB 8 .   ? 27.497  -4.814  120.542 1.00 11.63  ? 706  HOH D O   1 
HETATM 14012 O  O   . HOH CB 8 .   ? 36.235  7.069   96.954  1.00 9.16   ? 707  HOH D O   1 
HETATM 14013 O  O   . HOH CB 8 .   ? 28.376  -19.725 123.158 1.00 17.33  ? 708  HOH D O   1 
HETATM 14014 O  O   . HOH CB 8 .   ? 34.494  1.638   131.239 1.00 22.98  ? 709  HOH D O   1 
HETATM 14015 O  O   . HOH CB 8 .   ? 28.888  20.263  92.931  1.00 16.93  ? 710  HOH D O   1 
HETATM 14016 O  O   . HOH CB 8 .   ? 36.507  -19.692 114.608 1.00 21.58  ? 711  HOH D O   1 
HETATM 14017 O  O   . HOH CB 8 .   ? 48.165  2.123   108.780 1.00 23.09  ? 712  HOH D O   1 
HETATM 14018 O  O   . HOH CB 8 .   ? 14.619  -15.453 121.865 1.00 18.14  ? 713  HOH D O   1 
HETATM 14019 O  O   . HOH CB 8 .   ? 6.143   -6.992  102.917 1.00 13.69  ? 714  HOH D O   1 
HETATM 14020 O  O   . HOH CB 8 .   ? 11.444  -20.179 91.608  1.00 20.42  ? 715  HOH D O   1 
HETATM 14021 O  O   . HOH CB 8 .   ? 21.944  -27.093 94.669  1.00 20.75  ? 716  HOH D O   1 
HETATM 14022 O  O   . HOH CB 8 .   ? 30.015  -17.608 102.731 1.00 12.43  ? 717  HOH D O   1 
HETATM 14023 O  O   . HOH CB 8 .   ? 27.402  -25.732 101.545 1.00 14.29  ? 718  HOH D O   1 
HETATM 14024 O  O   . HOH CB 8 .   ? 16.932  -28.648 118.307 1.00 35.57  ? 719  HOH D O   1 
HETATM 14025 O  O   . HOH CB 8 .   ? 23.988  -0.173  123.058 1.00 24.56  ? 720  HOH D O   1 
HETATM 14026 O  O   . HOH CB 8 .   ? 26.451  -12.581 92.718  1.00 28.73  ? 721  HOH D O   1 
HETATM 14027 O  O   . HOH CB 8 .   ? 27.540  8.778   112.013 1.00 17.58  ? 722  HOH D O   1 
HETATM 14028 O  O   . HOH CB 8 .   ? 19.463  -31.072 116.529 1.00 27.51  ? 723  HOH D O   1 
HETATM 14029 O  O   . HOH CB 8 .   ? 35.299  -6.503  117.135 1.00 10.23  ? 724  HOH D O   1 
HETATM 14030 O  O   . HOH CB 8 .   ? 53.333  1.933   108.155 1.00 29.97  ? 725  HOH D O   1 
HETATM 14031 O  O   . HOH CB 8 .   ? 22.851  5.657   101.260 1.00 10.97  ? 726  HOH D O   1 
HETATM 14032 O  O   . HOH CB 8 .   ? 12.839  -1.729  114.922 1.00 20.98  ? 727  HOH D O   1 
HETATM 14033 O  O   . HOH CB 8 .   ? 17.479  -9.182  119.480 1.00 13.87  ? 728  HOH D O   1 
HETATM 14034 O  O   . HOH CB 8 .   ? 43.281  1.103   120.150 1.00 18.98  ? 729  HOH D O   1 
HETATM 14035 O  O   . HOH CB 8 .   ? 23.007  -5.213  102.953 1.00 8.09   ? 730  HOH D O   1 
HETATM 14036 O  O   . HOH CB 8 .   ? 30.465  -6.131  87.422  1.00 11.79  ? 731  HOH D O   1 
HETATM 14037 O  O   . HOH CB 8 .   ? 39.663  6.507   120.831 1.00 39.07  ? 732  HOH D O   1 
HETATM 14038 O  O   . HOH CB 8 .   ? 22.185  -31.569 108.999 1.00 29.20  ? 733  HOH D O   1 
HETATM 14039 O  O   . HOH CB 8 .   ? 26.785  0.556   124.976 1.00 29.51  ? 734  HOH D O   1 
HETATM 14040 O  O   . HOH CB 8 .   ? 25.156  -29.009 107.609 1.00 14.56  ? 735  HOH D O   1 
HETATM 14041 O  O   . HOH CB 8 .   ? 37.089  7.472   104.616 1.00 11.60  ? 736  HOH D O   1 
HETATM 14042 O  O   . HOH CB 8 .   ? 20.227  9.340   89.035  1.00 11.15  ? 737  HOH D O   1 
HETATM 14043 O  O   . HOH CB 8 .   ? 19.776  -6.744  112.239 1.00 11.95  ? 738  HOH D O   1 
HETATM 14044 O  O   . HOH CB 8 .   ? 19.542  2.388   116.371 1.00 43.01  ? 739  HOH D O   1 
HETATM 14045 O  O   . HOH CB 8 .   ? 33.310  -6.287  121.831 1.00 14.56  ? 740  HOH D O   1 
HETATM 14046 O  O   . HOH CB 8 .   ? 20.241  0.339   127.683 1.00 29.44  ? 741  HOH D O   1 
HETATM 14047 O  O   . HOH CB 8 .   ? 42.159  -6.443  93.671  1.00 20.28  ? 742  HOH D O   1 
HETATM 14048 O  O   . HOH CB 8 .   ? 12.628  -14.919 118.593 1.00 28.96  ? 743  HOH D O   1 
HETATM 14049 O  O   . HOH CB 8 .   ? 23.125  -29.761 119.443 1.00 23.66  ? 744  HOH D O   1 
HETATM 14050 O  O   . HOH CB 8 .   ? 39.379  -15.892 121.174 1.00 14.76  ? 745  HOH D O   1 
HETATM 14051 O  O   . HOH CB 8 .   ? 41.288  -18.061 127.917 1.00 34.47  ? 746  HOH D O   1 
HETATM 14052 O  O   . HOH CB 8 .   ? 32.270  -26.087 97.018  1.00 16.96  ? 747  HOH D O   1 
HETATM 14053 O  O   . HOH CB 8 .   ? 32.755  -11.996 112.516 1.00 12.11  ? 748  HOH D O   1 
HETATM 14054 O  O   . HOH CB 8 .   ? 40.525  -19.027 123.797 1.00 32.85  ? 749  HOH D O   1 
HETATM 14055 O  O   . HOH CB 8 .   ? 4.950   -19.348 98.542  1.00 20.18  ? 750  HOH D O   1 
HETATM 14056 O  O   . HOH CB 8 .   ? 19.711  -13.428 93.605  1.00 20.54  ? 751  HOH D O   1 
HETATM 14057 O  O   . HOH CB 8 .   ? 33.724  -4.453  115.069 1.00 14.84  ? 752  HOH D O   1 
HETATM 14058 O  O   . HOH CB 8 .   ? 33.426  24.156  102.245 1.00 43.97  ? 753  HOH D O   1 
HETATM 14059 O  O   . HOH CB 8 .   ? 7.940   -5.801  109.772 1.00 13.59  ? 754  HOH D O   1 
HETATM 14060 O  O   . HOH CB 8 .   ? 21.796  5.695   103.868 1.00 12.10  ? 755  HOH D O   1 
HETATM 14061 O  O   . HOH CB 8 .   ? 27.915  4.205   115.702 1.00 12.08  ? 756  HOH D O   1 
HETATM 14062 O  O   . HOH CB 8 .   ? 27.583  -33.118 114.041 1.00 35.01  ? 757  HOH D O   1 
HETATM 14063 O  O   . HOH CB 8 .   ? 23.581  2.609   110.063 1.00 15.89  ? 758  HOH D O   1 
HETATM 14064 O  O   . HOH CB 8 .   ? 40.696  1.963   129.081 1.00 32.89  ? 759  HOH D O   1 
HETATM 14065 O  O   . HOH CB 8 .   ? 49.067  0.519   111.959 1.00 22.84  ? 760  HOH D O   1 
HETATM 14066 O  O   . HOH CB 8 .   ? 38.428  -18.497 120.645 1.00 17.99  ? 761  HOH D O   1 
HETATM 14067 O  O   . HOH CB 8 .   ? 19.556  -5.317  110.111 1.00 20.47  ? 762  HOH D O   1 
HETATM 14068 O  O   . HOH CB 8 .   ? 47.155  6.624   103.413 1.00 14.53  ? 763  HOH D O   1 
HETATM 14069 O  O   . HOH CB 8 .   ? 31.099  0.891   87.070  1.00 18.83  ? 764  HOH D O   1 
HETATM 14070 O  O   . HOH CB 8 .   ? 40.408  -22.667 113.115 1.00 22.84  ? 765  HOH D O   1 
HETATM 14071 O  O   . HOH CB 8 .   ? 26.328  3.638   123.452 1.00 20.64  ? 766  HOH D O   1 
HETATM 14072 O  O   . HOH CB 8 .   ? 19.563  5.224   110.993 1.00 34.25  ? 767  HOH D O   1 
HETATM 14073 O  O   . HOH CB 8 .   ? 39.656  1.168   92.450  1.00 13.95  ? 768  HOH D O   1 
HETATM 14074 O  O   . HOH CB 8 .   ? 27.803  -6.791  113.985 1.00 8.70   ? 769  HOH D O   1 
HETATM 14075 O  O   . HOH CB 8 .   ? 55.870  -4.390  104.421 1.00 12.07  ? 770  HOH D O   1 
HETATM 14076 O  O   . HOH CB 8 .   ? 26.660  -28.503 118.947 1.00 22.54  ? 771  HOH D O   1 
HETATM 14077 O  O   . HOH CB 8 .   ? 25.212  4.678   127.303 1.00 36.17  ? 772  HOH D O   1 
HETATM 14078 O  O   . HOH CB 8 .   ? 29.104  -20.089 102.286 1.00 11.73  ? 773  HOH D O   1 
HETATM 14079 O  O   . HOH CB 8 .   ? 6.954   -15.464 110.135 1.00 23.26  ? 774  HOH D O   1 
HETATM 14080 O  O   . HOH CB 8 .   ? 36.313  13.156  90.259  1.00 7.08   ? 775  HOH D O   1 
HETATM 14081 O  O   . HOH CB 8 .   ? 29.084  3.435   96.205  1.00 11.55  ? 776  HOH D O   1 
HETATM 14082 O  O   . HOH CB 8 .   ? 16.447  -9.280  122.182 1.00 16.86  ? 777  HOH D O   1 
HETATM 14083 O  O   . HOH CB 8 .   ? 33.782  -18.028 126.308 1.00 38.95  ? 778  HOH D O   1 
HETATM 14084 O  O   . HOH CB 8 .   ? 34.254  5.421   129.842 1.00 19.75  ? 779  HOH D O   1 
HETATM 14085 O  O   . HOH CB 8 .   ? 30.511  -10.293 104.050 1.00 10.19  ? 780  HOH D O   1 
HETATM 14086 O  O   . HOH CB 8 .   ? 12.469  -5.182  128.260 1.00 37.02  ? 781  HOH D O   1 
HETATM 14087 O  O   . HOH CB 8 .   ? 16.102  3.616   110.616 1.00 32.99  ? 782  HOH D O   1 
HETATM 14088 O  O   . HOH CB 8 .   ? 44.693  7.557   113.147 1.00 23.70  ? 783  HOH D O   1 
HETATM 14089 O  O   . HOH CB 8 .   ? 32.099  17.378  108.532 1.00 33.88  ? 784  HOH D O   1 
HETATM 14090 O  O   . HOH CB 8 .   ? 30.731  -14.927 133.271 1.00 38.26  ? 785  HOH D O   1 
HETATM 14091 O  O   . HOH CB 8 .   ? 36.628  -26.962 102.458 1.00 27.99  ? 786  HOH D O   1 
HETATM 14092 O  O   . HOH CB 8 .   ? 29.564  -27.172 115.008 1.00 20.31  ? 787  HOH D O   1 
HETATM 14093 O  O   . HOH CB 8 .   ? 13.000  -1.780  98.423  1.00 10.75  ? 788  HOH D O   1 
HETATM 14094 O  O   . HOH CB 8 .   ? 13.676  -0.996  94.371  1.00 8.32   ? 789  HOH D O   1 
HETATM 14095 O  O   . HOH CB 8 .   ? 25.128  -26.192 119.328 1.00 18.09  ? 790  HOH D O   1 
HETATM 14096 O  O   . HOH CB 8 .   ? 46.183  -0.837  106.750 1.00 11.99  ? 791  HOH D O   1 
HETATM 14097 O  O   . HOH CB 8 .   ? 48.790  -4.814  101.658 1.00 13.33  ? 792  HOH D O   1 
HETATM 14098 O  O   . HOH CB 8 .   ? 24.825  1.535   127.177 1.00 27.03  ? 793  HOH D O   1 
HETATM 14099 O  O   . HOH CB 8 .   ? 7.059   -5.625  100.632 1.00 14.06  ? 794  HOH D O   1 
HETATM 14100 O  O   . HOH CB 8 .   ? 37.320  -22.836 92.787  1.00 24.30  ? 795  HOH D O   1 
HETATM 14101 O  O   . HOH CB 8 .   ? 34.075  -28.407 100.657 1.00 24.42  ? 796  HOH D O   1 
HETATM 14102 O  O   . HOH CB 8 .   ? 42.855  -17.339 100.641 1.00 19.40  ? 797  HOH D O   1 
HETATM 14103 O  O   . HOH CB 8 .   ? 16.238  -28.201 100.076 1.00 34.86  ? 798  HOH D O   1 
HETATM 14104 O  O   . HOH CB 8 .   ? 1.392   -0.851  106.606 1.00 23.20  ? 799  HOH D O   1 
HETATM 14105 O  O   . HOH CB 8 .   ? 7.410   -19.294 100.960 1.00 18.50  ? 800  HOH D O   1 
HETATM 14106 O  O   . HOH CB 8 .   ? 7.267   2.970   111.979 1.00 34.33  ? 801  HOH D O   1 
HETATM 14107 O  O   . HOH CB 8 .   ? 15.430  -0.174  127.577 1.00 28.44  ? 802  HOH D O   1 
HETATM 14108 O  O   . HOH CB 8 .   ? 17.906  21.820  99.422  1.00 24.85  ? 803  HOH D O   1 
HETATM 14109 O  O   . HOH CB 8 .   ? 30.549  -14.157 94.629  1.00 12.43  ? 804  HOH D O   1 
HETATM 14110 O  O   . HOH CB 8 .   ? 29.606  -17.212 99.955  1.00 11.33  ? 805  HOH D O   1 
HETATM 14111 O  O   . HOH CB 8 .   ? 37.342  -12.369 92.207  1.00 17.85  ? 806  HOH D O   1 
HETATM 14112 O  O   . HOH CB 8 .   ? 50.499  -21.158 110.224 1.00 25.82  ? 807  HOH D O   1 
HETATM 14113 O  O   . HOH CB 8 .   ? 26.921  -24.208 118.651 1.00 15.08  ? 808  HOH D O   1 
HETATM 14114 O  O   . HOH CB 8 .   ? 12.848  20.547  95.080  1.00 35.66  ? 809  HOH D O   1 
HETATM 14115 O  O   . HOH CB 8 .   ? 37.137  -17.124 87.544  1.00 37.71  ? 810  HOH D O   1 
HETATM 14116 O  O   . HOH CB 8 .   ? 20.044  -16.149 94.075  1.00 18.33  ? 811  HOH D O   1 
HETATM 14117 O  O   . HOH CB 8 .   ? 9.480   -22.546 95.799  1.00 31.15  ? 812  HOH D O   1 
HETATM 14118 O  O   . HOH CB 8 .   ? 15.372  -12.990 120.599 1.00 17.69  ? 813  HOH D O   1 
HETATM 14119 O  O   . HOH CB 8 .   ? 18.550  -19.630 126.800 1.00 31.16  ? 814  HOH D O   1 
HETATM 14120 O  O   . HOH CB 8 .   ? 12.830  0.450   117.450 1.00 30.58  ? 815  HOH D O   1 
HETATM 14121 O  O   . HOH CB 8 .   ? 46.179  26.433  101.871 1.00 50.53  ? 816  HOH D O   1 
HETATM 14122 O  O   . HOH CB 8 .   ? 8.725   0.571   113.465 1.00 37.44  ? 817  HOH D O   1 
HETATM 14123 O  O   . HOH CB 8 .   ? 27.176  9.935   90.044  1.00 9.25   ? 818  HOH D O   1 
HETATM 14124 O  O   . HOH CB 8 .   ? 35.837  11.736  114.964 1.00 27.75  ? 819  HOH D O   1 
HETATM 14125 O  O   . HOH CB 8 .   ? 13.838  4.529   106.738 1.00 21.73  ? 820  HOH D O   1 
HETATM 14126 O  O   . HOH CB 8 .   ? 45.443  -20.758 120.000 1.00 25.27  ? 821  HOH D O   1 
HETATM 14127 O  O   . HOH CB 8 .   ? 17.925  -13.076 124.666 1.00 29.33  ? 822  HOH D O   1 
HETATM 14128 O  O   . HOH CB 8 .   ? 43.994  -19.534 95.895  1.00 17.00  ? 823  HOH D O   1 
HETATM 14129 O  O   . HOH CB 8 .   ? 23.808  3.855   116.140 1.00 14.06  ? 824  HOH D O   1 
HETATM 14130 O  O   . HOH CB 8 .   ? 27.292  -20.157 90.782  1.00 32.16  ? 825  HOH D O   1 
HETATM 14131 O  O   . HOH CB 8 .   ? 20.624  -0.080  86.177  1.00 11.70  ? 826  HOH D O   1 
HETATM 14132 O  O   . HOH CB 8 .   ? 32.150  -11.534 89.259  1.00 16.12  ? 827  HOH D O   1 
HETATM 14133 O  O   . HOH CB 8 .   ? 44.893  -14.685 127.025 1.00 33.72  ? 828  HOH D O   1 
HETATM 14134 O  O   . HOH CB 8 .   ? 24.287  17.549  97.554  1.00 9.66   ? 829  HOH D O   1 
HETATM 14135 O  O   . HOH CB 8 .   ? 39.562  12.930  101.522 1.00 27.60  ? 830  HOH D O   1 
HETATM 14136 O  O   . HOH CB 8 .   ? 45.069  11.111  101.185 1.00 31.19  ? 831  HOH D O   1 
HETATM 14137 O  O   . HOH CB 8 .   ? 40.917  -18.504 102.195 1.00 15.12  ? 832  HOH D O   1 
HETATM 14138 O  O   . HOH CB 8 .   ? 19.144  -21.221 85.776  1.00 42.34  ? 833  HOH D O   1 
HETATM 14139 O  O   . HOH CB 8 .   ? 11.677  -25.433 112.686 1.00 20.01  ? 834  HOH D O   1 
HETATM 14140 O  O   . HOH CB 8 .   ? 22.672  2.441   112.882 1.00 23.62  ? 835  HOH D O   1 
HETATM 14141 O  O   . HOH CB 8 .   ? 20.053  -22.156 100.772 1.00 12.94  ? 836  HOH D O   1 
HETATM 14142 O  O   . HOH CB 8 .   ? 32.400  -14.422 91.971  1.00 36.55  ? 837  HOH D O   1 
HETATM 14143 O  O   . HOH CB 8 .   ? 41.682  -26.848 98.334  1.00 51.24  ? 838  HOH D O   1 
HETATM 14144 O  O   . HOH CB 8 .   ? 10.752  -23.066 102.781 1.00 17.22  ? 839  HOH D O   1 
HETATM 14145 O  O   . HOH CB 8 .   ? 55.542  -22.443 109.133 1.00 46.50  ? 840  HOH D O   1 
HETATM 14146 O  O   . HOH CB 8 .   ? 18.000  -15.726 125.126 1.00 26.11  ? 841  HOH D O   1 
HETATM 14147 O  O   . HOH CB 8 .   ? 25.371  -16.564 108.581 1.00 15.27  ? 842  HOH D O   1 
HETATM 14148 O  O   . HOH CB 8 .   ? 6.363   -0.955  113.533 1.00 28.21  ? 843  HOH D O   1 
HETATM 14149 O  O   . HOH CB 8 .   ? 23.625  -20.296 124.788 1.00 19.15  ? 844  HOH D O   1 
HETATM 14150 O  O   . HOH CB 8 .   ? 29.635  -9.142  86.853  1.00 30.26  ? 845  HOH D O   1 
HETATM 14151 O  O   . HOH CB 8 .   ? 41.699  -2.024  130.090 1.00 25.89  ? 846  HOH D O   1 
HETATM 14152 O  O   . HOH CB 8 .   ? 48.108  -1.499  104.022 1.00 11.70  ? 847  HOH D O   1 
HETATM 14153 O  O   . HOH CB 8 .   ? 38.832  2.927   122.257 1.00 23.09  ? 848  HOH D O   1 
HETATM 14154 O  O   . HOH CB 8 .   ? 27.600  -10.756 134.856 1.00 25.78  ? 849  HOH D O   1 
HETATM 14155 O  O   . HOH CB 8 .   ? 46.089  -5.587  128.370 1.00 40.86  ? 850  HOH D O   1 
HETATM 14156 O  O   . HOH CB 8 .   ? 26.057  13.362  113.192 1.00 29.18  ? 851  HOH D O   1 
HETATM 14157 O  O   . HOH CB 8 .   ? 29.077  8.231   114.041 1.00 10.16  ? 852  HOH D O   1 
HETATM 14158 O  O   . HOH CB 8 .   ? 22.306  17.182  91.499  1.00 41.48  ? 853  HOH D O   1 
HETATM 14159 O  O   . HOH CB 8 .   ? 36.799  10.534  105.144 1.00 8.57   ? 854  HOH D O   1 
HETATM 14160 O  O   . HOH CB 8 .   ? 27.353  -7.772  87.679  1.00 19.65  ? 855  HOH D O   1 
HETATM 14161 O  O   . HOH CB 8 .   ? 17.709  -0.059  93.406  1.00 13.36  ? 856  HOH D O   1 
HETATM 14162 O  O   . HOH CB 8 .   ? 42.732  10.637  116.848 1.00 36.36  ? 857  HOH D O   1 
HETATM 14163 O  O   . HOH CB 8 .   ? 33.347  -7.047  84.057  1.00 40.80  ? 858  HOH D O   1 
HETATM 14164 O  O   . HOH CB 8 .   ? 28.963  0.013   98.235  1.00 7.37   ? 859  HOH D O   1 
HETATM 14165 O  O   . HOH CB 8 .   ? 27.705  -31.919 97.317  1.00 26.61  ? 860  HOH D O   1 
HETATM 14166 O  O   . HOH CB 8 .   ? 19.563  -9.456  112.751 1.00 13.01  ? 861  HOH D O   1 
HETATM 14167 O  O   . HOH CB 8 .   ? 49.226  2.672   115.899 1.00 39.75  ? 862  HOH D O   1 
HETATM 14168 O  O   . HOH CB 8 .   ? 53.615  -20.123 113.635 1.00 32.79  ? 863  HOH D O   1 
HETATM 14169 O  O   . HOH CB 8 .   ? 42.539  0.979   123.920 1.00 38.00  ? 864  HOH D O   1 
HETATM 14170 O  O   . HOH CB 8 .   ? 46.115  -22.883 110.719 1.00 30.62  ? 865  HOH D O   1 
HETATM 14171 O  O   . HOH CB 8 .   ? 30.394  10.877  106.458 1.00 19.27  ? 866  HOH D O   1 
HETATM 14172 O  O   . HOH CB 8 .   ? 14.968  10.201  106.799 1.00 34.98  ? 867  HOH D O   1 
HETATM 14173 O  O   . HOH CB 8 .   ? 10.480  0.531   117.721 1.00 28.20  ? 868  HOH D O   1 
HETATM 14174 O  O   . HOH CB 8 .   ? 48.104  -20.960 108.807 1.00 22.31  ? 869  HOH D O   1 
HETATM 14175 O  O   . HOH CB 8 .   ? 44.224  -13.681 101.077 1.00 26.22  ? 870  HOH D O   1 
HETATM 14176 O  O   . HOH CB 8 .   ? 36.681  15.804  102.192 1.00 17.76  ? 871  HOH D O   1 
HETATM 14177 O  O   . HOH CB 8 .   ? 26.239  6.540   109.646 1.00 14.24  ? 872  HOH D O   1 
HETATM 14178 O  O   . HOH CB 8 .   ? 17.204  20.219  92.516  1.00 26.61  ? 873  HOH D O   1 
HETATM 14179 O  O   . HOH CB 8 .   ? 21.800  -10.636 111.806 1.00 12.14  ? 874  HOH D O   1 
HETATM 14180 O  O   . HOH CB 8 .   ? 46.187  -10.119 133.775 1.00 46.44  ? 875  HOH D O   1 
HETATM 14181 O  O   . HOH CB 8 .   ? 56.051  -16.802 100.812 1.00 21.89  ? 876  HOH D O   1 
HETATM 14182 O  O   . HOH CB 8 .   ? 37.497  -0.455  134.904 1.00 21.88  ? 877  HOH D O   1 
HETATM 14183 O  O   . HOH CB 8 .   ? 50.076  -22.134 121.306 1.00 41.33  ? 878  HOH D O   1 
HETATM 14184 O  O   . HOH CB 8 .   ? 16.822  -0.410  107.909 1.00 33.59  ? 879  HOH D O   1 
HETATM 14185 O  O   . HOH CB 8 .   ? 13.776  -28.848 101.906 1.00 29.22  ? 880  HOH D O   1 
HETATM 14186 O  O   . HOH CB 8 .   ? 37.524  8.388   121.109 1.00 21.30  ? 881  HOH D O   1 
HETATM 14187 O  O   . HOH CB 8 .   ? 29.602  5.891   129.629 1.00 32.53  ? 882  HOH D O   1 
HETATM 14188 O  O   . HOH CB 8 .   ? 33.598  12.616  81.632  1.00 16.95  ? 883  HOH D O   1 
HETATM 14189 O  O   . HOH CB 8 .   ? 22.913  -14.692 92.442  1.00 38.10  ? 884  HOH D O   1 
HETATM 14190 O  O   . HOH CB 8 .   ? 20.972  -5.441  132.669 1.00 25.18  ? 885  HOH D O   1 
HETATM 14191 O  O   . HOH CB 8 .   ? 28.057  10.440  107.755 1.00 12.26  ? 886  HOH D O   1 
HETATM 14192 O  O   . HOH CB 8 .   ? 17.554  -30.538 114.118 1.00 25.49  ? 887  HOH D O   1 
HETATM 14193 O  O   . HOH CB 8 .   ? 6.794   -18.622 95.643  1.00 42.54  ? 888  HOH D O   1 
HETATM 14194 O  O   . HOH CB 8 .   ? 23.865  -18.805 91.611  1.00 11.31  ? 889  HOH D O   1 
HETATM 14195 O  O   . HOH CB 8 .   ? 4.613   0.745   109.250 1.00 19.48  ? 890  HOH D O   1 
HETATM 14196 O  O   . HOH CB 8 .   ? 20.334  -23.591 91.158  1.00 40.70  ? 891  HOH D O   1 
HETATM 14197 O  O   . HOH CB 8 .   ? 39.987  2.344   126.231 1.00 24.21  ? 892  HOH D O   1 
HETATM 14198 O  O   . HOH CB 8 .   ? 22.668  6.210   106.438 1.00 13.48  ? 893  HOH D O   1 
HETATM 14199 O  O   . HOH CB 8 .   ? 46.507  -9.373  127.666 1.00 39.24  ? 894  HOH D O   1 
HETATM 14200 O  O   . HOH CB 8 .   ? 9.763   4.994   104.040 1.00 25.83  ? 895  HOH D O   1 
HETATM 14201 O  O   . HOH CB 8 .   ? -0.775  -8.146  109.342 1.00 39.74  ? 896  HOH D O   1 
HETATM 14202 O  O   . HOH CB 8 .   ? 19.840  -31.752 112.442 1.00 38.24  ? 897  HOH D O   1 
HETATM 14203 O  O   . HOH CB 8 .   ? 10.101  -19.333 116.036 1.00 34.20  ? 898  HOH D O   1 
HETATM 14204 O  O   . HOH CB 8 .   ? 36.218  13.546  105.356 1.00 29.49  ? 899  HOH D O   1 
HETATM 14205 O  O   . HOH CB 8 .   ? 23.313  16.364  109.014 1.00 65.97  ? 900  HOH D O   1 
HETATM 14206 O  O   . HOH CB 8 .   ? 15.842  6.320   108.111 1.00 19.62  ? 901  HOH D O   1 
HETATM 14207 O  O   . HOH CB 8 .   ? 57.322  -10.816 107.503 1.00 19.67  ? 902  HOH D O   1 
HETATM 14208 O  O   . HOH CB 8 .   ? 7.509   -12.060 117.674 1.00 32.09  ? 903  HOH D O   1 
HETATM 14209 O  O   . HOH CB 8 .   ? 13.421  -22.522 119.153 1.00 23.70  ? 904  HOH D O   1 
HETATM 14210 O  O   . HOH CB 8 .   ? 10.968  4.144   107.826 1.00 25.83  ? 905  HOH D O   1 
HETATM 14211 O  O   . HOH CB 8 .   ? 24.516  -4.630  132.019 1.00 24.60  ? 906  HOH D O   1 
HETATM 14212 O  O   . HOH CB 8 .   ? 48.509  6.473   106.258 1.00 28.36  ? 907  HOH D O   1 
HETATM 14213 O  O   . HOH CB 8 .   ? 18.065  -12.874 89.430  1.00 29.62  ? 908  HOH D O   1 
HETATM 14214 O  O   . HOH CB 8 .   ? 25.493  16.647  93.486  1.00 12.36  ? 909  HOH D O   1 
HETATM 14215 O  O   . HOH CB 8 .   ? 3.619   -9.974  108.659 1.00 22.44  ? 910  HOH D O   1 
HETATM 14216 O  O   . HOH CB 8 .   ? 11.447  7.319   100.641 1.00 28.69  ? 911  HOH D O   1 
HETATM 14217 O  O   . HOH CB 8 .   ? 38.154  10.293  118.476 1.00 33.05  ? 912  HOH D O   1 
HETATM 14218 O  O   . HOH CB 8 .   ? 12.833  -9.696  96.319  1.00 9.70   ? 913  HOH D O   1 
HETATM 14219 O  O   . HOH CB 8 .   ? 24.372  6.134   124.126 1.00 32.61  ? 914  HOH D O   1 
HETATM 14220 O  O   . HOH CB 8 .   ? 30.289  11.603  123.334 1.00 48.06  ? 915  HOH D O   1 
HETATM 14221 O  O   . HOH CB 8 .   ? -0.691  -0.215  108.406 1.00 36.43  ? 916  HOH D O   1 
HETATM 14222 O  O   . HOH CB 8 .   ? 30.996  -33.569 111.922 1.00 41.28  ? 917  HOH D O   1 
HETATM 14223 O  O   . HOH CB 8 .   ? 38.304  -21.625 115.215 1.00 34.41  ? 918  HOH D O   1 
HETATM 14224 O  O   . HOH CB 8 .   ? 24.946  19.038  110.707 1.00 41.18  ? 919  HOH D O   1 
HETATM 14225 O  O   . HOH CB 8 .   ? 33.133  -1.885  114.514 1.00 10.36  ? 920  HOH D O   1 
HETATM 14226 O  O   . HOH CB 8 .   ? 19.913  -1.708  112.450 1.00 37.81  ? 921  HOH D O   1 
HETATM 14227 O  O   . HOH CB 8 .   ? 27.233  17.790  110.576 1.00 45.47  ? 922  HOH D O   1 
HETATM 14228 O  O   . HOH CB 8 .   ? 24.831  7.669   107.671 1.00 18.65  ? 923  HOH D O   1 
HETATM 14229 O  O   . HOH CB 8 .   ? 18.796  1.754   124.519 1.00 43.18  ? 924  HOH D O   1 
HETATM 14230 O  O   . HOH CB 8 .   ? 40.036  -14.048 96.634  1.00 29.27  ? 925  HOH D O   1 
HETATM 14231 O  O   . HOH CB 8 .   ? 51.606  -11.575 116.086 1.00 37.10  ? 926  HOH D O   1 
HETATM 14232 O  O   . HOH CB 8 .   ? 6.835   2.363   107.183 1.00 15.70  ? 927  HOH D O   1 
HETATM 14233 O  O   . HOH CB 8 .   ? 31.592  -5.971  84.806  1.00 43.10  ? 928  HOH D O   1 
HETATM 14234 O  O   . HOH CB 8 .   ? 18.162  7.487   108.744 1.00 60.57  ? 929  HOH D O   1 
HETATM 14235 O  O   . HOH CB 8 .   ? 37.527  9.457   129.100 1.00 41.97  ? 930  HOH D O   1 
HETATM 14236 O  O   . HOH CB 8 .   ? 7.670   -15.402 116.905 1.00 39.34  ? 931  HOH D O   1 
HETATM 14237 O  O   . HOH CB 8 .   ? 44.458  11.533  105.849 1.00 24.97  ? 932  HOH D O   1 
HETATM 14238 O  O   . HOH CB 8 .   ? 39.761  -25.212 96.816  1.00 42.92  ? 933  HOH D O   1 
HETATM 14239 O  O   . HOH CB 8 .   ? 20.857  -21.278 88.533  1.00 39.72  ? 934  HOH D O   1 
HETATM 14240 O  O   . HOH CB 8 .   ? 38.033  14.168  106.373 1.00 54.47  ? 935  HOH D O   1 
HETATM 14241 O  O   . HOH CB 8 .   ? 27.079  22.267  106.415 1.00 42.06  ? 936  HOH D O   1 
HETATM 14242 O  O   . HOH CB 8 .   ? 35.773  -6.330  83.574  1.00 30.15  ? 937  HOH D O   1 
HETATM 14243 O  O   . HOH CB 8 .   ? 30.250  16.656  87.893  1.00 36.29  ? 938  HOH D O   1 
HETATM 14244 O  O   . HOH CB 8 .   ? 32.689  -13.328 132.683 1.00 24.10  ? 939  HOH D O   1 
HETATM 14245 O  O   . HOH CB 8 .   ? 44.209  3.020   121.658 1.00 46.26  ? 940  HOH D O   1 
HETATM 14246 O  O   . HOH CB 8 .   ? 21.404  3.730   115.586 1.00 28.80  ? 941  HOH D O   1 
HETATM 14247 O  O   . HOH CB 8 .   ? 13.061  -30.093 107.176 1.00 36.52  ? 942  HOH D O   1 
HETATM 14248 O  O   . HOH CB 8 .   ? 46.318  -21.550 92.761  1.00 20.55  ? 943  HOH D O   1 
HETATM 14249 O  O   . HOH CB 8 .   ? 21.426  14.601  108.482 1.00 23.97  ? 944  HOH D O   1 
HETATM 14250 O  O   . HOH CB 8 .   ? 3.174   -8.780  112.981 1.00 44.58  ? 945  HOH D O   1 
HETATM 14251 O  O   . HOH CB 8 .   ? 42.605  12.494  104.566 1.00 28.16  ? 946  HOH D O   1 
HETATM 14252 O  O   . HOH CB 8 .   ? 21.111  1.456   108.915 1.00 39.94  ? 947  HOH D O   1 
HETATM 14253 O  O   . HOH CB 8 .   ? 24.925  6.396   114.246 1.00 29.59  ? 948  HOH D O   1 
HETATM 14254 O  O   . HOH CB 8 .   ? 25.698  20.330  94.416  1.00 41.49  ? 949  HOH D O   1 
HETATM 14255 O  O   . HOH CB 8 .   ? 31.918  -30.909 110.877 1.00 29.48  ? 950  HOH D O   1 
HETATM 14256 O  O   . HOH CB 8 .   ? 58.795  -12.691 101.803 1.00 39.72  ? 951  HOH D O   1 
HETATM 14257 O  O   . HOH CB 8 .   ? 9.799   5.125   101.536 1.00 23.59  ? 952  HOH D O   1 
HETATM 14258 O  O   . HOH CB 8 .   ? 33.094  -19.535 123.788 1.00 35.97  ? 953  HOH D O   1 
HETATM 14259 O  O   . HOH CB 8 .   ? 15.826  -11.664 123.369 1.00 21.45  ? 954  HOH D O   1 
HETATM 14260 O  O   . HOH CB 8 .   ? 40.111  21.206  97.682  1.00 47.20  ? 955  HOH D O   1 
HETATM 14261 O  O   . HOH CB 8 .   ? 23.974  8.643   125.444 1.00 43.43  ? 956  HOH D O   1 
HETATM 14262 O  O   . HOH CB 8 .   ? 33.600  -32.369 99.469  1.00 36.03  ? 957  HOH D O   1 
HETATM 14263 O  O   . HOH CB 8 .   ? 38.364  -13.763 89.931  1.00 34.35  ? 958  HOH D O   1 
HETATM 14264 O  O   . HOH CB 8 .   ? 35.206  -20.936 122.557 1.00 40.47  ? 959  HOH D O   1 
HETATM 14265 O  O   . HOH CB 8 .   ? 27.567  17.574  88.900  1.00 50.20  ? 960  HOH D O   1 
HETATM 14266 O  O   . HOH CB 8 .   ? 36.291  -30.045 110.632 1.00 51.03  ? 961  HOH D O   1 
HETATM 14267 O  O   . HOH CB 8 .   ? 37.443  -25.120 96.306  1.00 39.67  ? 962  HOH D O   1 
HETATM 14268 O  O   . HOH CB 8 .   ? 9.697   2.906   105.676 1.00 19.57  ? 963  HOH D O   1 
HETATM 14269 O  O   . HOH CB 8 .   ? 41.952  0.011   131.887 1.00 46.78  ? 964  HOH D O   1 
HETATM 14270 O  O   . HOH CB 8 .   ? 37.719  -9.642  90.840  1.00 29.37  ? 965  HOH D O   1 
HETATM 14271 O  O   . HOH CB 8 .   ? 45.634  -17.779 128.584 1.00 42.18  ? 966  HOH D O   1 
HETATM 14272 O  O   . HOH CB 8 .   ? 33.716  -29.932 109.312 1.00 29.19  ? 967  HOH D O   1 
HETATM 14273 O  O   . HOH CB 8 .   ? 25.647  -33.638 108.597 1.00 38.33  ? 968  HOH D O   1 
HETATM 14274 O  O   . HOH CB 8 .   ? 29.508  20.752  107.093 1.00 37.55  ? 969  HOH D O   1 
HETATM 14275 O  O   . HOH CB 8 .   ? 49.811  3.027   110.583 1.00 47.67  ? 970  HOH D O   1 
HETATM 14276 O  O   . HOH CB 8 .   ? 20.633  -32.649 98.122  1.00 46.19  ? 971  HOH D O   1 
HETATM 14277 O  O   . HOH CB 8 .   ? 3.274   -8.795  115.465 1.00 40.44  ? 972  HOH D O   1 
HETATM 14278 O  O   . HOH CB 8 .   ? 15.250  -1.222  113.394 1.00 23.30  ? 973  HOH D O   1 
HETATM 14279 O  O   . HOH CB 8 .   ? 12.721  -29.801 104.879 1.00 43.26  ? 974  HOH D O   1 
HETATM 14280 O  O   . HOH CB 8 .   ? -1.533  -1.914  104.272 1.00 36.95  ? 975  HOH D O   1 
HETATM 14281 O  O   . HOH CB 8 .   ? 48.087  -8.376  126.672 1.00 36.75  ? 976  HOH D O   1 
HETATM 14282 O  O   . HOH CB 8 .   ? 19.338  -0.674  114.477 1.00 41.97  ? 977  HOH D O   1 
HETATM 14283 O  O   . HOH CB 8 .   ? 29.499  -4.976  83.014  1.00 34.89  ? 978  HOH D O   1 
HETATM 14284 O  O   . HOH CB 8 .   ? 21.446  -19.671 129.096 1.00 47.03  ? 979  HOH D O   1 
HETATM 14285 O  O   . HOH CB 8 .   ? 5.684   -10.599 118.868 1.00 46.27  ? 980  HOH D O   1 
HETATM 14286 O  O   . HOH CB 8 .   ? 38.352  13.806  103.700 1.00 42.91  ? 981  HOH D O   1 
HETATM 14287 O  O   . HOH CB 8 .   ? 29.153  -25.479 117.433 1.00 21.01  ? 982  HOH D O   1 
HETATM 14288 O  O   . HOH CB 8 .   ? 33.425  -10.247 82.858  1.00 56.34  ? 983  HOH D O   1 
HETATM 14289 O  O   . HOH CB 8 .   ? 44.821  -0.586  125.305 1.00 44.03  ? 984  HOH D O   1 
HETATM 14290 O  O   . HOH CB 8 .   ? 4.345   -15.020 111.380 1.00 43.66  ? 985  HOH D O   1 
HETATM 14291 O  O   . HOH CB 8 .   ? 20.236  6.485   121.191 1.00 49.38  ? 986  HOH D O   1 
HETATM 14292 O  O   . HOH CB 8 .   ? 11.250  -27.865 102.796 1.00 43.02  ? 987  HOH D O   1 
HETATM 14293 O  O   . HOH CB 8 .   ? 22.300  5.045   110.577 1.00 39.66  ? 988  HOH D O   1 
HETATM 14294 O  O   . HOH CB 8 .   ? 4.976   0.963   112.275 1.00 42.18  ? 989  HOH D O   1 
HETATM 14295 O  O   . HOH CB 8 .   ? 16.328  7.187   110.558 1.00 66.13  ? 990  HOH D O   1 
HETATM 14296 O  O   . HOH CB 8 .   ? 21.791  -22.084 125.236 1.00 35.41  ? 991  HOH D O   1 
HETATM 14297 O  O   . HOH CB 8 .   ? 59.015  -13.267 104.474 1.00 40.67  ? 992  HOH D O   1 
HETATM 14298 O  O   . HOH CB 8 .   ? 14.016  21.402  93.197  1.00 34.10  ? 993  HOH D O   1 
HETATM 14299 O  O   . HOH CB 8 .   ? 47.987  -15.308 126.571 1.00 43.86  ? 994  HOH D O   1 
HETATM 14300 O  O   . HOH CB 8 .   ? 30.925  -20.863 123.179 1.00 46.99  ? 995  HOH D O   1 
HETATM 14301 O  O   . HOH CB 8 .   ? 9.908   -6.181  126.298 1.00 35.91  ? 996  HOH D O   1 
HETATM 14302 O  O   . HOH CB 8 .   ? 24.656  18.858  92.501  1.00 27.73  ? 997  HOH D O   1 
HETATM 14303 O  O   . HOH CB 8 .   ? 45.442  -3.416  127.387 1.00 27.41  ? 998  HOH D O   1 
HETATM 14304 O  O   . HOH CB 8 .   ? 24.890  7.804   112.145 1.00 25.83  ? 999  HOH D O   1 
HETATM 14305 O  O   . HOH CB 8 .   ? 48.202  -16.849 104.684 1.00 22.79  ? 1000 HOH D O   1 
HETATM 14306 O  O   . HOH CB 8 .   ? 18.697  -23.840 121.806 1.00 39.82  ? 1001 HOH D O   1 
HETATM 14307 O  O   . HOH CB 8 .   ? 18.354  14.672  104.101 1.00 20.86  ? 1002 HOH D O   1 
HETATM 14308 O  O   . HOH CB 8 .   ? 37.300  9.770   123.314 1.00 46.75  ? 1003 HOH D O   1 
HETATM 14309 O  O   . HOH CB 8 .   ? 13.512  -12.595 124.239 1.00 42.13  ? 1004 HOH D O   1 
HETATM 14310 O  O   . HOH CB 8 .   ? 15.231  1.238   113.212 1.00 37.07  ? 1005 HOH D O   1 
HETATM 14311 O  O   . HOH CB 8 .   ? 22.350  16.086  96.002  1.00 11.13  ? 1006 HOH D O   1 
HETATM 14312 O  O   . HOH CB 8 .   ? 10.557  -25.392 109.766 1.00 38.71  ? 1007 HOH D O   1 
HETATM 14313 O  O   . HOH CB 8 .   ? 47.909  5.213   109.431 1.00 35.96  ? 1008 HOH D O   1 
HETATM 14314 O  O   . HOH CB 8 .   ? 20.498  -13.135 88.648  1.00 42.38  ? 1009 HOH D O   1 
HETATM 14315 O  O   . HOH CB 8 .   ? 15.483  -16.984 126.079 1.00 37.81  ? 1010 HOH D O   1 
HETATM 14316 O  O   . HOH CB 8 .   ? 34.654  -26.906 98.441  1.00 19.14  ? 1011 HOH D O   1 
HETATM 14317 O  O   . HOH CB 8 .   ? 30.747  -23.216 122.017 1.00 37.21  ? 1012 HOH D O   1 
HETATM 14318 O  O   . HOH CB 8 .   ? 35.510  21.043  103.331 1.00 39.23  ? 1013 HOH D O   1 
HETATM 14319 O  O   . HOH CB 8 .   ? 31.411  23.181  105.254 1.00 42.75  ? 1014 HOH D O   1 
HETATM 14320 O  O   . HOH CB 8 .   ? 40.553  -27.459 112.824 1.00 26.94  ? 1015 HOH D O   1 
HETATM 14321 O  O   . HOH CB 8 .   ? 21.001  17.768  94.368  1.00 17.28  ? 1016 HOH D O   1 
HETATM 14322 O  O   . HOH CB 8 .   ? 20.409  -0.095  89.138  1.00 15.58  ? 1017 HOH D O   1 
HETATM 14323 O  O   . HOH CB 8 .   ? 17.005  9.390   108.868 1.00 38.43  ? 1018 HOH D O   1 
HETATM 14324 O  O   . HOH CB 8 .   ? 45.946  -23.035 90.512  1.00 43.95  ? 1019 HOH D O   1 
HETATM 14325 O  O   . HOH CB 8 .   ? 43.727  2.239   125.380 1.00 38.97  ? 1020 HOH D O   1 
HETATM 14326 O  O   . HOH CB 8 .   ? 17.633  -1.931  109.174 1.00 38.10  ? 1021 HOH D O   1 
HETATM 14327 O  O   . HOH CB 8 .   ? 39.590  -13.138 99.124  1.00 26.24  ? 1022 HOH D O   1 
HETATM 14328 O  O   . HOH CB 8 .   ? 23.847  20.220  97.369  1.00 21.78  ? 1023 HOH D O   1 
HETATM 14329 O  O   . HOH CB 8 .   ? 24.210  -31.606 107.451 1.00 21.51  ? 1024 HOH D O   1 
HETATM 14330 O  O   . HOH CB 8 .   ? 31.354  -8.796  83.043  1.00 41.92  ? 1025 HOH D O   1 
HETATM 14331 O  O   . HOH CB 8 .   ? 23.390  7.491   110.110 1.00 30.61  ? 1026 HOH D O   1 
HETATM 14332 O  O   . HOH CB 8 .   ? 41.446  -14.401 100.339 1.00 20.05  ? 1027 HOH D O   1 
HETATM 14333 O  O   . HOH CB 8 .   ? 36.283  -24.799 93.897  1.00 30.35  ? 1028 HOH D O   1 
HETATM 14334 O  O   . HOH CB 8 .   ? 47.883  8.774   101.622 1.00 29.86  ? 1029 HOH D O   1 
HETATM 14335 O  O   . HOH CB 8 .   ? 18.390  3.742   120.773 1.00 41.40  ? 1030 HOH D O   1 
HETATM 14336 O  O   . HOH CB 8 .   ? 23.266  15.570  112.969 1.00 40.65  ? 1031 HOH D O   1 
HETATM 14337 O  O   . HOH CB 8 .   ? 32.693  18.516  106.112 1.00 29.07  ? 1032 HOH D O   1 
HETATM 14338 O  O   . HOH CB 8 .   ? 17.036  20.374  102.128 1.00 42.43  ? 1033 HOH D O   1 
HETATM 14339 O  O   . HOH CB 8 .   ? 7.867   6.858   105.424 1.00 39.11  ? 1034 HOH D O   1 
HETATM 14340 O  O   . HOH CB 8 .   ? 36.448  -28.168 96.457  1.00 41.54  ? 1035 HOH D O   1 
HETATM 14341 O  O   . HOH CB 8 .   ? 33.214  4.121   131.968 1.00 25.75  ? 1036 HOH D O   1 
HETATM 14342 O  O   . HOH CB 8 .   ? 33.957  -25.983 92.342  1.00 38.72  ? 1037 HOH D O   1 
HETATM 14343 O  O   . HOH CB 8 .   ? 51.156  6.487   106.169 1.00 27.39  ? 1038 HOH D O   1 
HETATM 14344 O  O   . HOH CB 8 .   ? 47.023  6.672   112.115 1.00 31.93  ? 1039 HOH D O   1 
HETATM 14345 O  O   . HOH CB 8 .   ? 28.506  8.274   109.401 1.00 12.38  ? 1040 HOH D O   1 
HETATM 14346 O  O   . HOH CB 8 .   ? 16.524  2.862   115.398 1.00 42.72  ? 1041 HOH D O   1 
HETATM 14347 O  O   . HOH CB 8 .   ? 61.614  -12.133 107.012 1.00 37.82  ? 1042 HOH D 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   ARG 1   88  88  ARG ARG A . n 
A 1 2   THR 2   89  89  THR THR A . n 
A 1 3   PHE 3   90  90  PHE PHE A . n 
A 1 4   LEU 4   91  91  LEU LEU A . n 
A 1 5   ASN 5   92  92  ASN ASN A . n 
A 1 6   LEU 6   93  93  LEU LEU A . n 
A 1 7   THR 7   94  94  THR THR A . n 
A 1 8   LYS 8   95  95  LYS LYS A . n 
A 1 9   PRO 9   96  96  PRO PRO A . n 
A 1 10  LEU 10  97  97  LEU LEU A . n 
A 1 11  CYS 11  98  98  CYS CYS A . n 
A 1 12  GLU 12  99  99  GLU GLU A . n 
A 1 13  VAL 13  100 100 VAL VAL A . n 
A 1 14  ASN 14  101 101 ASN ASN A . n 
A 1 15  SER 15  102 102 SER SER A . n 
A 1 16  TRP 16  103 103 TRP TRP A . n 
A 1 17  HIS 17  104 104 HIS HIS A . n 
A 1 18  ILE 18  105 105 ILE ILE A . n 
A 1 19  LEU 19  106 106 LEU LEU A . n 
A 1 20  SER 20  107 107 SER SER A . n 
A 1 21  LYS 21  108 108 LYS LYS A . n 
A 1 22  ASP 22  109 109 ASP ASP A . n 
A 1 23  ASN 23  110 110 ASN ASN A . n 
A 1 24  ALA 24  111 111 ALA ALA A . n 
A 1 25  ILE 25  112 112 ILE ILE A . n 
A 1 26  ARG 26  113 113 ARG ARG A . n 
A 1 27  ILE 27  114 114 ILE ILE A . n 
A 1 28  GLY 28  115 115 GLY GLY A . n 
A 1 29  GLU 29  116 116 GLU GLU A . n 
A 1 30  ASP 30  117 117 ASP ASP A . n 
A 1 31  ALA 31  118 118 ALA ALA A . n 
A 1 32  HIS 32  119 119 HIS HIS A . n 
A 1 33  ILE 33  120 120 ILE ILE A . n 
A 1 34  LEU 34  121 121 LEU LEU A . n 
A 1 35  VAL 35  122 122 VAL VAL A . n 
A 1 36  THR 36  123 123 THR THR A . n 
A 1 37  ARG 37  124 124 ARG ARG A . n 
A 1 38  GLU 38  125 125 GLU GLU A . n 
A 1 39  PRO 39  126 126 PRO PRO A . n 
A 1 40  TYR 40  127 127 TYR TYR A . n 
A 1 41  LEU 41  128 128 LEU LEU A . n 
A 1 42  SER 42  129 129 SER SER A . n 
A 1 43  CYS 43  130 130 CYS CYS A . n 
A 1 44  ASP 44  131 131 ASP ASP A . n 
A 1 45  PRO 45  132 132 PRO PRO A . n 
A 1 46  GLN 46  133 133 GLN GLN A . n 
A 1 47  GLY 47  134 134 GLY GLY A . n 
A 1 48  CYS 48  135 135 CYS CYS A . n 
A 1 49  ARG 49  136 136 ARG ARG A . n 
A 1 50  MET 50  137 137 MET MET A . n 
A 1 51  PHE 51  138 138 PHE PHE A . n 
A 1 52  ALA 52  139 139 ALA ALA A . n 
A 1 53  LEU 53  140 140 LEU LEU A . n 
A 1 54  SER 54  141 141 SER SER A . n 
A 1 55  GLN 55  142 142 GLN GLN A . n 
A 1 56  GLY 56  143 143 GLY GLY A . n 
A 1 57  THR 57  144 144 THR THR A . n 
A 1 58  THR 58  145 145 THR THR A . n 
A 1 59  LEU 59  146 146 LEU LEU A . n 
A 1 60  ARG 60  147 147 ARG ARG A . n 
A 1 61  GLY 61  148 148 GLY GLY A . n 
A 1 62  ARG 62  149 149 ARG ARG A . n 
A 1 63  HIS 63  150 150 HIS HIS A . n 
A 1 64  ALA 64  151 151 ALA ALA A . n 
A 1 65  ASN 65  152 152 ASN ASN A . n 
A 1 66  GLY 66  153 153 GLY GLY A . n 
A 1 67  THR 67  154 154 THR THR A . n 
A 1 68  ILE 68  155 155 ILE ILE A . n 
A 1 69  HIS 69  156 156 HIS HIS A . n 
A 1 70  ASP 70  157 157 ASP ASP A . n 
A 1 71  ARG 71  158 158 ARG ARG A . n 
A 1 72  SER 72  159 159 SER SER A . n 
A 1 73  PRO 73  160 160 PRO PRO A . n 
A 1 74  PHE 74  161 161 PHE PHE A . n 
A 1 75  ARG 75  162 162 ARG ARG A . n 
A 1 76  ALA 76  163 163 ALA ALA A . n 
A 1 77  LEU 77  164 164 LEU LEU A . n 
A 1 78  ILE 78  165 165 ILE ILE A . n 
A 1 79  SER 79  166 166 SER SER A . n 
A 1 80  TRP 80  167 167 TRP TRP A . n 
A 1 81  GLU 81  168 168 GLU GLU A . n 
A 1 82  MET 82  169 169 MET MET A . n 
A 1 83  GLY 83  170 170 GLY GLY A . n 
A 1 84  GLN 84  171 171 GLN GLN A . n 
A 1 85  ALA 85  172 172 ALA ALA A . n 
A 1 86  PRO 86  173 173 PRO PRO A . n 
A 1 87  SER 87  174 174 SER SER A . n 
A 1 88  PRO 88  175 175 PRO PRO A . n 
A 1 89  TYR 89  176 176 TYR TYR A . n 
A 1 90  ASN 90  177 177 ASN ASN A . n 
A 1 91  THR 91  178 178 THR THR A . n 
A 1 92  ARG 92  179 179 ARG ARG A . n 
A 1 93  VAL 93  180 180 VAL VAL A . n 
A 1 94  GLU 94  181 181 GLU GLU A . n 
A 1 95  CYS 95  182 182 CYS CYS A . n 
A 1 96  ILE 96  183 183 ILE ILE A . n 
A 1 97  GLY 97  184 184 GLY GLY A . n 
A 1 98  TRP 98  185 185 TRP TRP A . n 
A 1 99  SER 99  186 186 SER SER A . n 
A 1 100 SER 100 187 187 SER SER A . n 
A 1 101 THR 101 188 188 THR THR A . n 
A 1 102 SER 102 189 189 SER SER A . n 
A 1 103 CYS 103 190 190 CYS CYS A . n 
A 1 104 HIS 104 191 191 HIS HIS A . n 
A 1 105 ASP 105 192 192 ASP ASP A . n 
A 1 106 GLY 106 193 193 GLY GLY A . n 
A 1 107 MET 107 194 194 MET MET A . n 
A 1 108 SER 108 195 195 SER SER A . n 
A 1 109 ARG 109 196 196 ARG ARG A . n 
A 1 110 MET 110 197 197 MET MET A . n 
A 1 111 SER 111 198 198 SER SER A . n 
A 1 112 ILE 112 199 199 ILE ILE A . n 
A 1 113 CYS 113 200 200 CYS CYS A . n 
A 1 114 MET 114 201 201 MET MET A . n 
A 1 115 SER 115 202 202 SER SER A . n 
A 1 116 GLY 116 203 203 GLY GLY A . n 
A 1 117 PRO 117 204 204 PRO PRO A . n 
A 1 118 ASN 118 205 205 ASN ASN A . n 
A 1 119 ASN 119 206 206 ASN ASN A . n 
A 1 120 ASN 120 207 207 ASN ASN A . n 
A 1 121 ALA 121 208 208 ALA ALA A . n 
A 1 122 SER 122 209 209 SER SER A . n 
A 1 123 ALA 123 210 210 ALA ALA A . n 
A 1 124 VAL 124 211 211 VAL VAL A . n 
A 1 125 VAL 125 212 212 VAL VAL A . n 
A 1 126 TRP 126 213 213 TRP TRP A . n 
A 1 127 TYR 127 214 214 TYR TYR A . n 
A 1 128 GLY 128 215 215 GLY GLY A . n 
A 1 129 GLY 129 216 216 GLY GLY A . n 
A 1 130 ARG 130 217 217 ARG ARG A . n 
A 1 131 PRO 131 218 218 PRO PRO A . n 
A 1 132 ILE 132 219 219 ILE ILE A . n 
A 1 133 THR 133 220 220 THR THR A . n 
A 1 134 GLU 134 221 221 GLU GLU A . n 
A 1 135 ILE 135 222 222 ILE ILE A . n 
A 1 136 PRO 136 223 223 PRO PRO A . n 
A 1 137 SER 137 224 224 SER SER A . n 
A 1 138 TRP 138 225 225 TRP TRP A . n 
A 1 139 ALA 139 226 226 ALA ALA A . n 
A 1 140 GLY 140 227 227 GLY GLY A . n 
A 1 141 ASN 141 228 228 ASN ASN A . n 
A 1 142 ILE 142 229 229 ILE ILE A . n 
A 1 143 LEU 143 230 230 LEU LEU A . n 
A 1 144 ARG 144 231 231 ARG ARG A . n 
A 1 145 THR 145 232 232 THR THR A . n 
A 1 146 GLN 146 233 233 GLN GLN A . n 
A 1 147 GLU 147 234 234 GLU GLU A . n 
A 1 148 SER 148 235 235 SER SER A . n 
A 1 149 GLU 149 236 236 GLU GLU A . n 
A 1 150 CYS 150 237 237 CYS CYS A . n 
A 1 151 VAL 151 238 238 VAL VAL A . n 
A 1 152 CYS 152 239 239 CYS CYS A . n 
A 1 153 HIS 153 240 240 HIS HIS A . n 
A 1 154 LYS 154 241 241 LYS LYS A . n 
A 1 155 GLY 155 242 242 GLY GLY A . n 
A 1 156 VAL 156 243 243 VAL VAL A . n 
A 1 157 CYS 157 244 244 CYS CYS A . n 
A 1 158 PRO 158 245 245 PRO PRO A . n 
A 1 159 VAL 159 246 246 VAL VAL A . n 
A 1 160 VAL 160 247 247 VAL VAL A . n 
A 1 161 MET 161 248 248 MET MET A . n 
A 1 162 THR 162 249 249 THR THR A . n 
A 1 163 ASP 163 250 250 ASP ASP A . n 
A 1 164 GLY 164 251 251 GLY GLY A . n 
A 1 165 PRO 165 252 252 PRO PRO A . n 
A 1 166 ALA 166 253 253 ALA ALA A . n 
A 1 167 ASN 167 254 254 ASN ASN A . n 
A 1 168 ASN 168 255 255 ASN ASN A . n 
A 1 169 ARG 169 256 256 ARG ARG A . n 
A 1 170 ALA 170 257 257 ALA ALA A . n 
A 1 171 ALA 171 258 258 ALA ALA A . n 
A 1 172 THR 172 259 259 THR THR A . n 
A 1 173 LYS 173 260 260 LYS LYS A . n 
A 1 174 ILE 174 261 261 ILE ILE A . n 
A 1 175 ILE 175 262 262 ILE ILE A . n 
A 1 176 TYR 176 263 263 TYR TYR A . n 
A 1 177 PHE 177 264 264 PHE PHE A . n 
A 1 178 LYS 178 265 265 LYS LYS A . n 
A 1 179 GLU 179 266 266 GLU GLU A . n 
A 1 180 GLY 180 267 267 GLY GLY A . n 
A 1 181 LYS 181 268 268 LYS LYS A . n 
A 1 182 ILE 182 269 269 ILE ILE A . n 
A 1 183 GLN 183 270 270 GLN GLN A . n 
A 1 184 LYS 184 271 271 LYS LYS A . n 
A 1 185 ILE 185 272 272 ILE ILE A . n 
A 1 186 GLU 186 273 273 GLU GLU A . n 
A 1 187 GLU 187 274 274 GLU GLU A . n 
A 1 188 LEU 188 275 275 LEU LEU A . n 
A 1 189 ALA 189 276 276 ALA ALA A . n 
A 1 190 GLY 190 277 277 GLY GLY A . n 
A 1 191 ASN 191 278 278 ASN ASN A . n 
A 1 192 ALA 192 279 279 ALA ALA A . n 
A 1 193 GLN 193 280 280 GLN GLN A . n 
A 1 194 HIS 194 281 281 HIS HIS A . n 
A 1 195 ILE 195 282 282 ILE ILE A . n 
A 1 196 GLU 196 283 283 GLU GLU A . n 
A 1 197 GLU 197 284 284 GLU GLU A . n 
A 1 198 CYS 198 285 285 CYS CYS A . n 
A 1 199 SER 199 286 286 SER SER A . n 
A 1 200 CYS 200 287 287 CYS CYS A . n 
A 1 201 TYR 201 288 288 TYR TYR A . n 
A 1 202 GLY 202 289 289 GLY GLY A . n 
A 1 203 ALA 203 290 290 ALA ALA A . n 
A 1 204 GLY 204 291 291 GLY GLY A . n 
A 1 205 GLY 205 292 292 GLY GLY A . n 
A 1 206 VAL 206 293 293 VAL VAL A . n 
A 1 207 ILE 207 294 294 ILE ILE A . n 
A 1 208 LYS 208 295 295 LYS LYS A . n 
A 1 209 CYS 209 296 296 CYS CYS A . n 
A 1 210 ILE 210 297 297 ILE ILE A . n 
A 1 211 CYS 211 298 298 CYS CYS A . n 
A 1 212 ARG 212 299 299 ARG ARG A . n 
A 1 213 ASP 213 300 300 ASP ASP A . n 
A 1 214 ASN 214 301 301 ASN ASN A . n 
A 1 215 TRP 215 302 302 TRP TRP A . n 
A 1 216 LYS 216 303 303 LYS LYS A . n 
A 1 217 GLY 217 304 304 GLY GLY A . n 
A 1 218 ALA 218 305 305 ALA ALA A . n 
A 1 219 ASN 219 306 306 ASN ASN A . n 
A 1 220 ARG 220 307 307 ARG ARG A . n 
A 1 221 PRO 221 308 308 PRO PRO A . n 
A 1 222 VAL 222 309 309 VAL VAL A . n 
A 1 223 ILE 223 310 310 ILE ILE A . n 
A 1 224 THR 224 311 311 THR THR A . n 
A 1 225 ILE 225 312 312 ILE ILE A . n 
A 1 226 ASP 226 313 313 ASP ASP A . n 
A 1 227 PRO 227 314 314 PRO PRO A . n 
A 1 228 GLU 228 315 315 GLU GLU A . n 
A 1 229 MET 229 316 316 MET MET A . n 
A 1 230 MET 230 317 317 MET MET A . n 
A 1 231 THR 231 318 318 THR THR A . n 
A 1 232 HIS 232 319 319 HIS HIS A . n 
A 1 233 THR 233 320 320 THR THR A . n 
A 1 234 SER 234 321 321 SER SER A . n 
A 1 235 LYS 235 322 322 LYS LYS A . n 
A 1 236 TYR 236 323 323 TYR TYR A . n 
A 1 237 LEU 237 324 324 LEU LEU A . n 
A 1 238 CYS 238 325 325 CYS CYS A . n 
A 1 239 SER 239 326 326 SER SER A . n 
A 1 240 LYS 240 327 327 LYS LYS A . n 
A 1 241 VAL 241 328 328 VAL VAL A . n 
A 1 242 LEU 242 329 329 LEU LEU A . n 
A 1 243 THR 243 330 330 THR THR A . n 
A 1 244 ASP 244 331 331 ASP ASP A . n 
A 1 245 THR 245 332 332 THR THR A . n 
A 1 246 SER 246 333 333 SER SER A . n 
A 1 247 ARG 247 334 334 ARG ARG A . n 
A 1 248 PRO 248 335 335 PRO PRO A . n 
A 1 249 ASN 249 336 336 ASN ASN A . n 
A 1 250 ASP 250 337 337 ASP ASP A . n 
A 1 251 PRO 251 338 338 PRO PRO A . n 
A 1 252 THR 252 339 339 THR THR A . n 
A 1 253 ASN 253 340 340 ASN ASN A . n 
A 1 254 GLY 254 341 341 GLY GLY A . n 
A 1 255 ASN 255 342 342 ASN ASN A . n 
A 1 256 CYS 256 343 343 CYS CYS A . n 
A 1 257 ASP 257 344 344 ASP ASP A . n 
A 1 258 ALA 258 345 345 ALA ALA A . n 
A 1 259 PRO 259 346 346 PRO PRO A . n 
A 1 260 ILE 260 347 347 ILE ILE A . n 
A 1 261 THR 261 348 348 THR THR A . n 
A 1 262 GLY 262 349 349 GLY GLY A . n 
A 1 263 GLY 263 350 350 GLY GLY A . n 
A 1 264 SER 264 351 351 SER SER A . n 
A 1 265 PRO 265 352 352 PRO PRO A . n 
A 1 266 ASP 266 353 353 ASP ASP A . n 
A 1 267 PRO 267 354 354 PRO PRO A . n 
A 1 268 GLY 268 355 355 GLY GLY A . n 
A 1 269 VAL 269 356 356 VAL VAL A . n 
A 1 270 LYS 270 357 357 LYS LYS A . n 
A 1 271 GLY 271 358 358 GLY GLY A . n 
A 1 272 PHE 272 359 359 PHE PHE A . n 
A 1 273 ALA 273 360 360 ALA ALA A . n 
A 1 274 PHE 274 361 361 PHE PHE A . n 
A 1 275 LEU 275 362 362 LEU LEU A . n 
A 1 276 ASP 276 363 363 ASP ASP A . n 
A 1 277 GLY 277 364 364 GLY GLY A . n 
A 1 278 GLU 278 365 365 GLU GLU A . n 
A 1 279 ASN 279 366 366 ASN ASN A . n 
A 1 280 SER 280 367 367 SER SER A . n 
A 1 281 TRP 281 368 368 TRP TRP A . n 
A 1 282 LEU 282 369 369 LEU LEU A . n 
A 1 283 GLY 283 370 370 GLY GLY A . n 
A 1 284 ARG 284 371 371 ARG ARG A . n 
A 1 285 THR 285 372 372 THR THR A . n 
A 1 286 ILE 286 373 373 ILE ILE A . n 
A 1 287 SER 287 374 374 SER SER A . n 
A 1 288 LYS 288 375 375 LYS LYS A . n 
A 1 289 ASP 289 376 376 ASP ASP A . n 
A 1 290 SER 290 377 377 SER SER A . n 
A 1 291 ARG 291 378 378 ARG ARG A . n 
A 1 292 SER 292 379 379 SER SER A . n 
A 1 293 GLY 293 380 380 GLY GLY A . n 
A 1 294 TYR 294 381 381 TYR TYR A . n 
A 1 295 GLU 295 382 382 GLU GLU A . n 
A 1 296 MET 296 383 383 MET MET A . n 
A 1 297 LEU 297 384 384 LEU LEU A . n 
A 1 298 LYS 298 385 385 LYS LYS A . n 
A 1 299 VAL 299 386 386 VAL VAL A . n 
A 1 300 PRO 300 387 387 PRO PRO A . n 
A 1 301 ASN 301 388 388 ASN ASN A . n 
A 1 302 ALA 302 389 389 ALA ALA A . n 
A 1 303 GLU 303 390 390 GLU GLU A . n 
A 1 304 THR 304 391 391 THR THR A . n 
A 1 305 ASP 305 392 392 ASP ASP A . n 
A 1 306 ILE 306 393 393 ILE ILE A . n 
A 1 307 GLN 307 394 394 GLN GLN A . n 
A 1 308 SER 308 395 395 SER SER A . n 
A 1 309 GLY 309 396 396 GLY GLY A . n 
A 1 310 PRO 310 397 397 PRO PRO A . n 
A 1 311 ILE 311 398 398 ILE ILE A . n 
A 1 312 SER 312 399 399 SER SER A . n 
A 1 313 ASN 313 400 400 ASN ASN A . n 
A 1 314 GLN 314 401 401 GLN GLN A . n 
A 1 315 VAL 315 402 402 VAL VAL A . n 
A 1 316 ILE 316 403 403 ILE ILE A . n 
A 1 317 VAL 317 404 404 VAL VAL A . n 
A 1 318 ASN 318 405 405 ASN ASN A . n 
A 1 319 ASN 319 406 406 ASN ASN A . n 
A 1 320 GLN 320 407 407 GLN GLN A . n 
A 1 321 ASN 321 408 408 ASN ASN A . n 
A 1 322 TRP 322 409 409 TRP TRP A . n 
A 1 323 SER 323 410 410 SER SER A . n 
A 1 324 GLY 324 411 411 GLY GLY A . n 
A 1 325 TYR 325 412 412 TYR TYR A . n 
A 1 326 SER 326 413 413 SER SER A . n 
A 1 327 GLY 327 414 414 GLY GLY A . n 
A 1 328 ALA 328 415 415 ALA ALA A . n 
A 1 329 PHE 329 416 416 PHE PHE A . n 
A 1 330 ILE 330 417 417 ILE ILE A . n 
A 1 331 ASP 331 418 418 ASP ASP A . n 
A 1 332 TYR 332 419 419 TYR TYR A . n 
A 1 333 TRP 333 420 420 TRP TRP A . n 
A 1 334 ALA 334 421 421 ALA ALA A . n 
A 1 335 ASN 335 422 422 ASN ASN A . n 
A 1 336 LYS 336 423 423 LYS LYS A . n 
A 1 337 GLU 337 424 424 GLU GLU A . n 
A 1 338 CYS 338 425 425 CYS CYS A . n 
A 1 339 PHE 339 426 426 PHE PHE A . n 
A 1 340 ASN 340 427 427 ASN ASN A . n 
A 1 341 PRO 341 428 428 PRO PRO A . n 
A 1 342 CYS 342 429 429 CYS CYS A . n 
A 1 343 PHE 343 430 430 PHE PHE A . n 
A 1 344 TYR 344 431 431 TYR TYR A . n 
A 1 345 VAL 345 432 432 VAL VAL A . n 
A 1 346 GLU 346 433 433 GLU GLU A . n 
A 1 347 LEU 347 434 434 LEU LEU A . n 
A 1 348 ILE 348 435 435 ILE ILE A . n 
A 1 349 ARG 349 436 436 ARG ARG A . n 
A 1 350 GLY 350 437 437 GLY GLY A . n 
A 1 351 ARG 351 438 438 ARG ARG A . n 
A 1 352 PRO 352 439 439 PRO PRO A . n 
A 1 353 LYS 353 440 440 LYS LYS A . n 
A 1 354 GLU 354 441 441 GLU GLU A . n 
A 1 355 SER 355 442 442 SER SER A . n 
A 1 356 SER 356 443 443 SER SER A . n 
A 1 357 VAL 357 444 444 VAL VAL A . n 
A 1 358 LEU 358 445 445 LEU LEU A . n 
A 1 359 TRP 359 446 446 TRP TRP A . n 
A 1 360 THR 360 447 447 THR THR A . n 
A 1 361 SER 361 448 448 SER SER A . n 
A 1 362 ASN 362 449 449 ASN ASN A . n 
A 1 363 SER 363 450 450 SER SER A . n 
A 1 364 ILE 364 451 451 ILE ILE A . n 
A 1 365 VAL 365 452 452 VAL VAL A . n 
A 1 366 ALA 366 453 453 ALA ALA A . n 
A 1 367 LEU 367 454 454 LEU LEU A . n 
A 1 368 CYS 368 455 455 CYS CYS A . n 
A 1 369 GLY 369 456 456 GLY GLY A . n 
A 1 370 SER 370 457 457 SER SER A . n 
A 1 371 LYS 371 458 458 LYS LYS A . n 
A 1 372 LYS 372 459 459 LYS LYS A . n 
A 1 373 ARG 373 460 460 ARG ARG A . n 
A 1 374 LEU 374 461 461 LEU LEU A . n 
A 1 375 GLY 375 462 462 GLY GLY A . n 
A 1 376 SER 376 463 463 SER SER A . n 
A 1 377 TRP 377 464 464 TRP TRP A . n 
A 1 378 SER 378 465 465 SER SER A . n 
A 1 379 TRP 379 466 466 TRP TRP A . n 
A 1 380 HIS 380 467 467 HIS HIS A . n 
A 1 381 ASP 381 468 468 ASP ASP A . n 
A 1 382 GLY 382 469 469 GLY GLY A . n 
A 1 383 ALA 383 470 470 ALA ALA A . n 
A 1 384 GLU 384 471 471 GLU GLU A . n 
A 1 385 ILE 385 472 472 ILE ILE A . n 
A 1 386 ILE 386 473 473 ILE ILE A . n 
A 1 387 TYR 387 474 474 TYR TYR A . n 
A 1 388 PHE 388 475 475 PHE PHE A . n 
A 1 389 GLU 389 476 476 GLU GLU A . n 
B 1 1   ARG 1   88  88  ARG ARG B . n 
B 1 2   THR 2   89  89  THR THR B . n 
B 1 3   PHE 3   90  90  PHE PHE B . n 
B 1 4   LEU 4   91  91  LEU LEU B . n 
B 1 5   ASN 5   92  92  ASN ASN B . n 
B 1 6   LEU 6   93  93  LEU LEU B . n 
B 1 7   THR 7   94  94  THR THR B . n 
B 1 8   LYS 8   95  95  LYS LYS B . n 
B 1 9   PRO 9   96  96  PRO PRO B . n 
B 1 10  LEU 10  97  97  LEU LEU B . n 
B 1 11  CYS 11  98  98  CYS CYS B . n 
B 1 12  GLU 12  99  99  GLU GLU B . n 
B 1 13  VAL 13  100 100 VAL VAL B . n 
B 1 14  ASN 14  101 101 ASN ASN B . n 
B 1 15  SER 15  102 102 SER SER B . n 
B 1 16  TRP 16  103 103 TRP TRP B . n 
B 1 17  HIS 17  104 104 HIS HIS B . n 
B 1 18  ILE 18  105 105 ILE ILE B . n 
B 1 19  LEU 19  106 106 LEU LEU B . n 
B 1 20  SER 20  107 107 SER SER B . n 
B 1 21  LYS 21  108 108 LYS LYS B . n 
B 1 22  ASP 22  109 109 ASP ASP B . n 
B 1 23  ASN 23  110 110 ASN ASN B . n 
B 1 24  ALA 24  111 111 ALA ALA B . n 
B 1 25  ILE 25  112 112 ILE ILE B . n 
B 1 26  ARG 26  113 113 ARG ARG B . n 
B 1 27  ILE 27  114 114 ILE ILE B . n 
B 1 28  GLY 28  115 115 GLY GLY B . n 
B 1 29  GLU 29  116 116 GLU GLU B . n 
B 1 30  ASP 30  117 117 ASP ASP B . n 
B 1 31  ALA 31  118 118 ALA ALA B . n 
B 1 32  HIS 32  119 119 HIS HIS B . n 
B 1 33  ILE 33  120 120 ILE ILE B . n 
B 1 34  LEU 34  121 121 LEU LEU B . n 
B 1 35  VAL 35  122 122 VAL VAL B . n 
B 1 36  THR 36  123 123 THR THR B . n 
B 1 37  ARG 37  124 124 ARG ARG B . n 
B 1 38  GLU 38  125 125 GLU GLU B . n 
B 1 39  PRO 39  126 126 PRO PRO B . n 
B 1 40  TYR 40  127 127 TYR TYR B . n 
B 1 41  LEU 41  128 128 LEU LEU B . n 
B 1 42  SER 42  129 129 SER SER B . n 
B 1 43  CYS 43  130 130 CYS CYS B . n 
B 1 44  ASP 44  131 131 ASP ASP B . n 
B 1 45  PRO 45  132 132 PRO PRO B . n 
B 1 46  GLN 46  133 133 GLN GLN B . n 
B 1 47  GLY 47  134 134 GLY GLY B . n 
B 1 48  CYS 48  135 135 CYS CYS B . n 
B 1 49  ARG 49  136 136 ARG ARG B . n 
B 1 50  MET 50  137 137 MET MET B . n 
B 1 51  PHE 51  138 138 PHE PHE B . n 
B 1 52  ALA 52  139 139 ALA ALA B . n 
B 1 53  LEU 53  140 140 LEU LEU B . n 
B 1 54  SER 54  141 141 SER SER B . n 
B 1 55  GLN 55  142 142 GLN GLN B . n 
B 1 56  GLY 56  143 143 GLY GLY B . n 
B 1 57  THR 57  144 144 THR THR B . n 
B 1 58  THR 58  145 145 THR THR B . n 
B 1 59  LEU 59  146 146 LEU LEU B . n 
B 1 60  ARG 60  147 147 ARG ARG B . n 
B 1 61  GLY 61  148 148 GLY GLY B . n 
B 1 62  ARG 62  149 149 ARG ARG B . n 
B 1 63  HIS 63  150 150 HIS HIS B . n 
B 1 64  ALA 64  151 151 ALA ALA B . n 
B 1 65  ASN 65  152 152 ASN ASN B . n 
B 1 66  GLY 66  153 153 GLY GLY B . n 
B 1 67  THR 67  154 154 THR THR B . n 
B 1 68  ILE 68  155 155 ILE ILE B . n 
B 1 69  HIS 69  156 156 HIS HIS B . n 
B 1 70  ASP 70  157 157 ASP ASP B . n 
B 1 71  ARG 71  158 158 ARG ARG B . n 
B 1 72  SER 72  159 159 SER SER B . n 
B 1 73  PRO 73  160 160 PRO PRO B . n 
B 1 74  PHE 74  161 161 PHE PHE B . n 
B 1 75  ARG 75  162 162 ARG ARG B . n 
B 1 76  ALA 76  163 163 ALA ALA B . n 
B 1 77  LEU 77  164 164 LEU LEU B . n 
B 1 78  ILE 78  165 165 ILE ILE B . n 
B 1 79  SER 79  166 166 SER SER B . n 
B 1 80  TRP 80  167 167 TRP TRP B . n 
B 1 81  GLU 81  168 168 GLU GLU B . n 
B 1 82  MET 82  169 169 MET MET B . n 
B 1 83  GLY 83  170 170 GLY GLY B . n 
B 1 84  GLN 84  171 171 GLN GLN B . n 
B 1 85  ALA 85  172 172 ALA ALA B . n 
B 1 86  PRO 86  173 173 PRO PRO B . n 
B 1 87  SER 87  174 174 SER SER B . n 
B 1 88  PRO 88  175 175 PRO PRO B . n 
B 1 89  TYR 89  176 176 TYR TYR B . n 
B 1 90  ASN 90  177 177 ASN ASN B . n 
B 1 91  THR 91  178 178 THR THR B . n 
B 1 92  ARG 92  179 179 ARG ARG B . n 
B 1 93  VAL 93  180 180 VAL VAL B . n 
B 1 94  GLU 94  181 181 GLU GLU B . n 
B 1 95  CYS 95  182 182 CYS CYS B . n 
B 1 96  ILE 96  183 183 ILE ILE B . n 
B 1 97  GLY 97  184 184 GLY GLY B . n 
B 1 98  TRP 98  185 185 TRP TRP B . n 
B 1 99  SER 99  186 186 SER SER B . n 
B 1 100 SER 100 187 187 SER SER B . n 
B 1 101 THR 101 188 188 THR THR B . n 
B 1 102 SER 102 189 189 SER SER B . n 
B 1 103 CYS 103 190 190 CYS CYS B . n 
B 1 104 HIS 104 191 191 HIS HIS B . n 
B 1 105 ASP 105 192 192 ASP ASP B . n 
B 1 106 GLY 106 193 193 GLY GLY B . n 
B 1 107 MET 107 194 194 MET MET B . n 
B 1 108 SER 108 195 195 SER SER B . n 
B 1 109 ARG 109 196 196 ARG ARG B . n 
B 1 110 MET 110 197 197 MET MET B . n 
B 1 111 SER 111 198 198 SER SER B . n 
B 1 112 ILE 112 199 199 ILE ILE B . n 
B 1 113 CYS 113 200 200 CYS CYS B . n 
B 1 114 MET 114 201 201 MET MET B . n 
B 1 115 SER 115 202 202 SER SER B . n 
B 1 116 GLY 116 203 203 GLY GLY B . n 
B 1 117 PRO 117 204 204 PRO PRO B . n 
B 1 118 ASN 118 205 205 ASN ASN B . n 
B 1 119 ASN 119 206 206 ASN ASN B . n 
B 1 120 ASN 120 207 207 ASN ASN B . n 
B 1 121 ALA 121 208 208 ALA ALA B . n 
B 1 122 SER 122 209 209 SER SER B . n 
B 1 123 ALA 123 210 210 ALA ALA B . n 
B 1 124 VAL 124 211 211 VAL VAL B . n 
B 1 125 VAL 125 212 212 VAL VAL B . n 
B 1 126 TRP 126 213 213 TRP TRP B . n 
B 1 127 TYR 127 214 214 TYR TYR B . n 
B 1 128 GLY 128 215 215 GLY GLY B . n 
B 1 129 GLY 129 216 216 GLY GLY B . n 
B 1 130 ARG 130 217 217 ARG ARG B . n 
B 1 131 PRO 131 218 218 PRO PRO B . n 
B 1 132 ILE 132 219 219 ILE ILE B . n 
B 1 133 THR 133 220 220 THR THR B . n 
B 1 134 GLU 134 221 221 GLU GLU B . n 
B 1 135 ILE 135 222 222 ILE ILE B . n 
B 1 136 PRO 136 223 223 PRO PRO B . n 
B 1 137 SER 137 224 224 SER SER B . n 
B 1 138 TRP 138 225 225 TRP TRP B . n 
B 1 139 ALA 139 226 226 ALA ALA B . n 
B 1 140 GLY 140 227 227 GLY GLY B . n 
B 1 141 ASN 141 228 228 ASN ASN B . n 
B 1 142 ILE 142 229 229 ILE ILE B . n 
B 1 143 LEU 143 230 230 LEU LEU B . n 
B 1 144 ARG 144 231 231 ARG ARG B . n 
B 1 145 THR 145 232 232 THR THR B . n 
B 1 146 GLN 146 233 233 GLN GLN B . n 
B 1 147 GLU 147 234 234 GLU GLU B . n 
B 1 148 SER 148 235 235 SER SER B . n 
B 1 149 GLU 149 236 236 GLU GLU B . n 
B 1 150 CYS 150 237 237 CYS CYS B . n 
B 1 151 VAL 151 238 238 VAL VAL B . n 
B 1 152 CYS 152 239 239 CYS CYS B . n 
B 1 153 HIS 153 240 240 HIS HIS B . n 
B 1 154 LYS 154 241 241 LYS LYS B . n 
B 1 155 GLY 155 242 242 GLY GLY B . n 
B 1 156 VAL 156 243 243 VAL VAL B . n 
B 1 157 CYS 157 244 244 CYS CYS B . n 
B 1 158 PRO 158 245 245 PRO PRO B . n 
B 1 159 VAL 159 246 246 VAL VAL B . n 
B 1 160 VAL 160 247 247 VAL VAL B . n 
B 1 161 MET 161 248 248 MET MET B . n 
B 1 162 THR 162 249 249 THR THR B . n 
B 1 163 ASP 163 250 250 ASP ASP B . n 
B 1 164 GLY 164 251 251 GLY GLY B . n 
B 1 165 PRO 165 252 252 PRO PRO B . n 
B 1 166 ALA 166 253 253 ALA ALA B . n 
B 1 167 ASN 167 254 254 ASN ASN B . n 
B 1 168 ASN 168 255 255 ASN ASN B . n 
B 1 169 ARG 169 256 256 ARG ARG B . n 
B 1 170 ALA 170 257 257 ALA ALA B . n 
B 1 171 ALA 171 258 258 ALA ALA B . n 
B 1 172 THR 172 259 259 THR THR B . n 
B 1 173 LYS 173 260 260 LYS LYS B . n 
B 1 174 ILE 174 261 261 ILE ILE B . n 
B 1 175 ILE 175 262 262 ILE ILE B . n 
B 1 176 TYR 176 263 263 TYR TYR B . n 
B 1 177 PHE 177 264 264 PHE PHE B . n 
B 1 178 LYS 178 265 265 LYS LYS B . n 
B 1 179 GLU 179 266 266 GLU GLU B . n 
B 1 180 GLY 180 267 267 GLY GLY B . n 
B 1 181 LYS 181 268 268 LYS LYS B . n 
B 1 182 ILE 182 269 269 ILE ILE B . n 
B 1 183 GLN 183 270 270 GLN GLN B . n 
B 1 184 LYS 184 271 271 LYS LYS B . n 
B 1 185 ILE 185 272 272 ILE ILE B . n 
B 1 186 GLU 186 273 273 GLU GLU B . n 
B 1 187 GLU 187 274 274 GLU GLU B . n 
B 1 188 LEU 188 275 275 LEU LEU B . n 
B 1 189 ALA 189 276 276 ALA ALA B . n 
B 1 190 GLY 190 277 277 GLY GLY B . n 
B 1 191 ASN 191 278 278 ASN ASN B . n 
B 1 192 ALA 192 279 279 ALA ALA B . n 
B 1 193 GLN 193 280 280 GLN GLN B . n 
B 1 194 HIS 194 281 281 HIS HIS B . n 
B 1 195 ILE 195 282 282 ILE ILE B . n 
B 1 196 GLU 196 283 283 GLU GLU B . n 
B 1 197 GLU 197 284 284 GLU GLU B . n 
B 1 198 CYS 198 285 285 CYS CYS B . n 
B 1 199 SER 199 286 286 SER SER B . n 
B 1 200 CYS 200 287 287 CYS CYS B . n 
B 1 201 TYR 201 288 288 TYR TYR B . n 
B 1 202 GLY 202 289 289 GLY GLY B . n 
B 1 203 ALA 203 290 290 ALA ALA B . n 
B 1 204 GLY 204 291 291 GLY GLY B . n 
B 1 205 GLY 205 292 292 GLY GLY B . n 
B 1 206 VAL 206 293 293 VAL VAL B . n 
B 1 207 ILE 207 294 294 ILE ILE B . n 
B 1 208 LYS 208 295 295 LYS LYS B . n 
B 1 209 CYS 209 296 296 CYS CYS B . n 
B 1 210 ILE 210 297 297 ILE ILE B . n 
B 1 211 CYS 211 298 298 CYS CYS B . n 
B 1 212 ARG 212 299 299 ARG ARG B . n 
B 1 213 ASP 213 300 300 ASP ASP B . n 
B 1 214 ASN 214 301 301 ASN ASN B . n 
B 1 215 TRP 215 302 302 TRP TRP B . n 
B 1 216 LYS 216 303 303 LYS LYS B . n 
B 1 217 GLY 217 304 304 GLY GLY B . n 
B 1 218 ALA 218 305 305 ALA ALA B . n 
B 1 219 ASN 219 306 306 ASN ASN B . n 
B 1 220 ARG 220 307 307 ARG ARG B . n 
B 1 221 PRO 221 308 308 PRO PRO B . n 
B 1 222 VAL 222 309 309 VAL VAL B . n 
B 1 223 ILE 223 310 310 ILE ILE B . n 
B 1 224 THR 224 311 311 THR THR B . n 
B 1 225 ILE 225 312 312 ILE ILE B . n 
B 1 226 ASP 226 313 313 ASP ASP B . n 
B 1 227 PRO 227 314 314 PRO PRO B . n 
B 1 228 GLU 228 315 315 GLU GLU B . n 
B 1 229 MET 229 316 316 MET MET B . n 
B 1 230 MET 230 317 317 MET MET B . n 
B 1 231 THR 231 318 318 THR THR B . n 
B 1 232 HIS 232 319 319 HIS HIS B . n 
B 1 233 THR 233 320 320 THR THR B . n 
B 1 234 SER 234 321 321 SER SER B . n 
B 1 235 LYS 235 322 322 LYS LYS B . n 
B 1 236 TYR 236 323 323 TYR TYR B . n 
B 1 237 LEU 237 324 324 LEU LEU B . n 
B 1 238 CYS 238 325 325 CYS CYS B . n 
B 1 239 SER 239 326 326 SER SER B . n 
B 1 240 LYS 240 327 327 LYS LYS B . n 
B 1 241 VAL 241 328 328 VAL VAL B . n 
B 1 242 LEU 242 329 329 LEU LEU B . n 
B 1 243 THR 243 330 330 THR THR B . n 
B 1 244 ASP 244 331 331 ASP ASP B . n 
B 1 245 THR 245 332 332 THR THR B . n 
B 1 246 SER 246 333 333 SER SER B . n 
B 1 247 ARG 247 334 334 ARG ARG B . n 
B 1 248 PRO 248 335 335 PRO PRO B . n 
B 1 249 ASN 249 336 336 ASN ASN B . n 
B 1 250 ASP 250 337 337 ASP ASP B . n 
B 1 251 PRO 251 338 338 PRO PRO B . n 
B 1 252 THR 252 339 339 THR THR B . n 
B 1 253 ASN 253 340 340 ASN ASN B . n 
B 1 254 GLY 254 341 341 GLY GLY B . n 
B 1 255 ASN 255 342 342 ASN ASN B . n 
B 1 256 CYS 256 343 343 CYS CYS B . n 
B 1 257 ASP 257 344 344 ASP ASP B . n 
B 1 258 ALA 258 345 345 ALA ALA B . n 
B 1 259 PRO 259 346 346 PRO PRO B . n 
B 1 260 ILE 260 347 347 ILE ILE B . n 
B 1 261 THR 261 348 348 THR THR B . n 
B 1 262 GLY 262 349 349 GLY GLY B . n 
B 1 263 GLY 263 350 350 GLY GLY B . n 
B 1 264 SER 264 351 351 SER SER B . n 
B 1 265 PRO 265 352 352 PRO PRO B . n 
B 1 266 ASP 266 353 353 ASP ASP B . n 
B 1 267 PRO 267 354 354 PRO PRO B . n 
B 1 268 GLY 268 355 355 GLY GLY B . n 
B 1 269 VAL 269 356 356 VAL VAL B . n 
B 1 270 LYS 270 357 357 LYS LYS B . n 
B 1 271 GLY 271 358 358 GLY GLY B . n 
B 1 272 PHE 272 359 359 PHE PHE B . n 
B 1 273 ALA 273 360 360 ALA ALA B . n 
B 1 274 PHE 274 361 361 PHE PHE B . n 
B 1 275 LEU 275 362 362 LEU LEU B . n 
B 1 276 ASP 276 363 363 ASP ASP B . n 
B 1 277 GLY 277 364 364 GLY GLY B . n 
B 1 278 GLU 278 365 365 GLU GLU B . n 
B 1 279 ASN 279 366 366 ASN ASN B . n 
B 1 280 SER 280 367 367 SER SER B . n 
B 1 281 TRP 281 368 368 TRP TRP B . n 
B 1 282 LEU 282 369 369 LEU LEU B . n 
B 1 283 GLY 283 370 370 GLY GLY B . n 
B 1 284 ARG 284 371 371 ARG ARG B . n 
B 1 285 THR 285 372 372 THR THR B . n 
B 1 286 ILE 286 373 373 ILE ILE B . n 
B 1 287 SER 287 374 374 SER SER B . n 
B 1 288 LYS 288 375 375 LYS LYS B . n 
B 1 289 ASP 289 376 376 ASP ASP B . n 
B 1 290 SER 290 377 377 SER SER B . n 
B 1 291 ARG 291 378 378 ARG ARG B . n 
B 1 292 SER 292 379 379 SER SER B . n 
B 1 293 GLY 293 380 380 GLY GLY B . n 
B 1 294 TYR 294 381 381 TYR TYR B . n 
B 1 295 GLU 295 382 382 GLU GLU B . n 
B 1 296 MET 296 383 383 MET MET B . n 
B 1 297 LEU 297 384 384 LEU LEU B . n 
B 1 298 LYS 298 385 385 LYS LYS B . n 
B 1 299 VAL 299 386 386 VAL VAL B . n 
B 1 300 PRO 300 387 387 PRO PRO B . n 
B 1 301 ASN 301 388 388 ASN ASN B . n 
B 1 302 ALA 302 389 389 ALA ALA B . n 
B 1 303 GLU 303 390 390 GLU GLU B . n 
B 1 304 THR 304 391 391 THR THR B . n 
B 1 305 ASP 305 392 392 ASP ASP B . n 
B 1 306 ILE 306 393 393 ILE ILE B . n 
B 1 307 GLN 307 394 394 GLN GLN B . n 
B 1 308 SER 308 395 395 SER SER B . n 
B 1 309 GLY 309 396 396 GLY GLY B . n 
B 1 310 PRO 310 397 397 PRO PRO B . n 
B 1 311 ILE 311 398 398 ILE ILE B . n 
B 1 312 SER 312 399 399 SER SER B . n 
B 1 313 ASN 313 400 400 ASN ASN B . n 
B 1 314 GLN 314 401 401 GLN GLN B . n 
B 1 315 VAL 315 402 402 VAL VAL B . n 
B 1 316 ILE 316 403 403 ILE ILE B . n 
B 1 317 VAL 317 404 404 VAL VAL B . n 
B 1 318 ASN 318 405 405 ASN ASN B . n 
B 1 319 ASN 319 406 406 ASN ASN B . n 
B 1 320 GLN 320 407 407 GLN GLN B . n 
B 1 321 ASN 321 408 408 ASN ASN B . n 
B 1 322 TRP 322 409 409 TRP TRP B . n 
B 1 323 SER 323 410 410 SER SER B . n 
B 1 324 GLY 324 411 411 GLY GLY B . n 
B 1 325 TYR 325 412 412 TYR TYR B . n 
B 1 326 SER 326 413 413 SER SER B . n 
B 1 327 GLY 327 414 414 GLY GLY B . n 
B 1 328 ALA 328 415 415 ALA ALA B . n 
B 1 329 PHE 329 416 416 PHE PHE B . n 
B 1 330 ILE 330 417 417 ILE ILE B . n 
B 1 331 ASP 331 418 418 ASP ASP B . n 
B 1 332 TYR 332 419 419 TYR TYR B . n 
B 1 333 TRP 333 420 420 TRP TRP B . n 
B 1 334 ALA 334 421 421 ALA ALA B . n 
B 1 335 ASN 335 422 422 ASN ASN B . n 
B 1 336 LYS 336 423 423 LYS LYS B . n 
B 1 337 GLU 337 424 424 GLU GLU B . n 
B 1 338 CYS 338 425 425 CYS CYS B . n 
B 1 339 PHE 339 426 426 PHE PHE B . n 
B 1 340 ASN 340 427 427 ASN ASN B . n 
B 1 341 PRO 341 428 428 PRO PRO B . n 
B 1 342 CYS 342 429 429 CYS CYS B . n 
B 1 343 PHE 343 430 430 PHE PHE B . n 
B 1 344 TYR 344 431 431 TYR TYR B . n 
B 1 345 VAL 345 432 432 VAL VAL B . n 
B 1 346 GLU 346 433 433 GLU GLU B . n 
B 1 347 LEU 347 434 434 LEU LEU B . n 
B 1 348 ILE 348 435 435 ILE ILE B . n 
B 1 349 ARG 349 436 436 ARG ARG B . n 
B 1 350 GLY 350 437 437 GLY GLY B . n 
B 1 351 ARG 351 438 438 ARG ARG B . n 
B 1 352 PRO 352 439 439 PRO PRO B . n 
B 1 353 LYS 353 440 440 LYS LYS B . n 
B 1 354 GLU 354 441 441 GLU GLU B . n 
B 1 355 SER 355 442 442 SER SER B . n 
B 1 356 SER 356 443 443 SER SER B . n 
B 1 357 VAL 357 444 444 VAL VAL B . n 
B 1 358 LEU 358 445 445 LEU LEU B . n 
B 1 359 TRP 359 446 446 TRP TRP B . n 
B 1 360 THR 360 447 447 THR THR B . n 
B 1 361 SER 361 448 448 SER SER B . n 
B 1 362 ASN 362 449 449 ASN ASN B . n 
B 1 363 SER 363 450 450 SER SER B . n 
B 1 364 ILE 364 451 451 ILE ILE B . n 
B 1 365 VAL 365 452 452 VAL VAL B . n 
B 1 366 ALA 366 453 453 ALA ALA B . n 
B 1 367 LEU 367 454 454 LEU LEU B . n 
B 1 368 CYS 368 455 455 CYS CYS B . n 
B 1 369 GLY 369 456 456 GLY GLY B . n 
B 1 370 SER 370 457 457 SER SER B . n 
B 1 371 LYS 371 458 458 LYS LYS B . n 
B 1 372 LYS 372 459 459 LYS LYS B . n 
B 1 373 ARG 373 460 460 ARG ARG B . n 
B 1 374 LEU 374 461 461 LEU LEU B . n 
B 1 375 GLY 375 462 462 GLY GLY B . n 
B 1 376 SER 376 463 463 SER SER B . n 
B 1 377 TRP 377 464 464 TRP TRP B . n 
B 1 378 SER 378 465 465 SER SER B . n 
B 1 379 TRP 379 466 466 TRP TRP B . n 
B 1 380 HIS 380 467 467 HIS HIS B . n 
B 1 381 ASP 381 468 468 ASP ASP B . n 
B 1 382 GLY 382 469 469 GLY GLY B . n 
B 1 383 ALA 383 470 470 ALA ALA B . n 
B 1 384 GLU 384 471 471 GLU GLU B . n 
B 1 385 ILE 385 472 472 ILE ILE B . n 
B 1 386 ILE 386 473 473 ILE ILE B . n 
B 1 387 TYR 387 474 474 TYR TYR B . n 
B 1 388 PHE 388 475 475 PHE PHE B . n 
B 1 389 GLU 389 476 476 GLU GLU B . n 
C 1 1   ARG 1   88  88  ARG ARG C . n 
C 1 2   THR 2   89  89  THR THR C . n 
C 1 3   PHE 3   90  90  PHE PHE C . n 
C 1 4   LEU 4   91  91  LEU LEU C . n 
C 1 5   ASN 5   92  92  ASN ASN C . n 
C 1 6   LEU 6   93  93  LEU LEU C . n 
C 1 7   THR 7   94  94  THR THR C . n 
C 1 8   LYS 8   95  95  LYS LYS C . n 
C 1 9   PRO 9   96  96  PRO PRO C . n 
C 1 10  LEU 10  97  97  LEU LEU C . n 
C 1 11  CYS 11  98  98  CYS CYS C . n 
C 1 12  GLU 12  99  99  GLU GLU C . n 
C 1 13  VAL 13  100 100 VAL VAL C . n 
C 1 14  ASN 14  101 101 ASN ASN C . n 
C 1 15  SER 15  102 102 SER SER C . n 
C 1 16  TRP 16  103 103 TRP TRP C . n 
C 1 17  HIS 17  104 104 HIS HIS C . n 
C 1 18  ILE 18  105 105 ILE ILE C . n 
C 1 19  LEU 19  106 106 LEU LEU C . n 
C 1 20  SER 20  107 107 SER SER C . n 
C 1 21  LYS 21  108 108 LYS LYS C . n 
C 1 22  ASP 22  109 109 ASP ASP C . n 
C 1 23  ASN 23  110 110 ASN ASN C . n 
C 1 24  ALA 24  111 111 ALA ALA C . n 
C 1 25  ILE 25  112 112 ILE ILE C . n 
C 1 26  ARG 26  113 113 ARG ARG C . n 
C 1 27  ILE 27  114 114 ILE ILE C . n 
C 1 28  GLY 28  115 115 GLY GLY C . n 
C 1 29  GLU 29  116 116 GLU GLU C . n 
C 1 30  ASP 30  117 117 ASP ASP C . n 
C 1 31  ALA 31  118 118 ALA ALA C . n 
C 1 32  HIS 32  119 119 HIS HIS C . n 
C 1 33  ILE 33  120 120 ILE ILE C . n 
C 1 34  LEU 34  121 121 LEU LEU C . n 
C 1 35  VAL 35  122 122 VAL VAL C . n 
C 1 36  THR 36  123 123 THR THR C . n 
C 1 37  ARG 37  124 124 ARG ARG C . n 
C 1 38  GLU 38  125 125 GLU GLU C . n 
C 1 39  PRO 39  126 126 PRO PRO C . n 
C 1 40  TYR 40  127 127 TYR TYR C . n 
C 1 41  LEU 41  128 128 LEU LEU C . n 
C 1 42  SER 42  129 129 SER SER C . n 
C 1 43  CYS 43  130 130 CYS CYS C . n 
C 1 44  ASP 44  131 131 ASP ASP C . n 
C 1 45  PRO 45  132 132 PRO PRO C . n 
C 1 46  GLN 46  133 133 GLN GLN C . n 
C 1 47  GLY 47  134 134 GLY GLY C . n 
C 1 48  CYS 48  135 135 CYS CYS C . n 
C 1 49  ARG 49  136 136 ARG ARG C . n 
C 1 50  MET 50  137 137 MET MET C . n 
C 1 51  PHE 51  138 138 PHE PHE C . n 
C 1 52  ALA 52  139 139 ALA ALA C . n 
C 1 53  LEU 53  140 140 LEU LEU C . n 
C 1 54  SER 54  141 141 SER SER C . n 
C 1 55  GLN 55  142 142 GLN GLN C . n 
C 1 56  GLY 56  143 143 GLY GLY C . n 
C 1 57  THR 57  144 144 THR THR C . n 
C 1 58  THR 58  145 145 THR THR C . n 
C 1 59  LEU 59  146 146 LEU LEU C . n 
C 1 60  ARG 60  147 147 ARG ARG C . n 
C 1 61  GLY 61  148 148 GLY GLY C . n 
C 1 62  ARG 62  149 149 ARG ARG C . n 
C 1 63  HIS 63  150 150 HIS HIS C . n 
C 1 64  ALA 64  151 151 ALA ALA C . n 
C 1 65  ASN 65  152 152 ASN ASN C . n 
C 1 66  GLY 66  153 153 GLY GLY C . n 
C 1 67  THR 67  154 154 THR THR C . n 
C 1 68  ILE 68  155 155 ILE ILE C . n 
C 1 69  HIS 69  156 156 HIS HIS C . n 
C 1 70  ASP 70  157 157 ASP ASP C . n 
C 1 71  ARG 71  158 158 ARG ARG C . n 
C 1 72  SER 72  159 159 SER SER C . n 
C 1 73  PRO 73  160 160 PRO PRO C . n 
C 1 74  PHE 74  161 161 PHE PHE C . n 
C 1 75  ARG 75  162 162 ARG ARG C . n 
C 1 76  ALA 76  163 163 ALA ALA C . n 
C 1 77  LEU 77  164 164 LEU LEU C . n 
C 1 78  ILE 78  165 165 ILE ILE C . n 
C 1 79  SER 79  166 166 SER SER C . n 
C 1 80  TRP 80  167 167 TRP TRP C . n 
C 1 81  GLU 81  168 168 GLU GLU C . n 
C 1 82  MET 82  169 169 MET MET C . n 
C 1 83  GLY 83  170 170 GLY GLY C . n 
C 1 84  GLN 84  171 171 GLN GLN C . n 
C 1 85  ALA 85  172 172 ALA ALA C . n 
C 1 86  PRO 86  173 173 PRO PRO C . n 
C 1 87  SER 87  174 174 SER SER C . n 
C 1 88  PRO 88  175 175 PRO PRO C . n 
C 1 89  TYR 89  176 176 TYR TYR C . n 
C 1 90  ASN 90  177 177 ASN ASN C . n 
C 1 91  THR 91  178 178 THR THR C . n 
C 1 92  ARG 92  179 179 ARG ARG C . n 
C 1 93  VAL 93  180 180 VAL VAL C . n 
C 1 94  GLU 94  181 181 GLU GLU C . n 
C 1 95  CYS 95  182 182 CYS CYS C . n 
C 1 96  ILE 96  183 183 ILE ILE C . n 
C 1 97  GLY 97  184 184 GLY GLY C . n 
C 1 98  TRP 98  185 185 TRP TRP C . n 
C 1 99  SER 99  186 186 SER SER C . n 
C 1 100 SER 100 187 187 SER SER C . n 
C 1 101 THR 101 188 188 THR THR C . n 
C 1 102 SER 102 189 189 SER SER C . n 
C 1 103 CYS 103 190 190 CYS CYS C . n 
C 1 104 HIS 104 191 191 HIS HIS C . n 
C 1 105 ASP 105 192 192 ASP ASP C . n 
C 1 106 GLY 106 193 193 GLY GLY C . n 
C 1 107 MET 107 194 194 MET MET C . n 
C 1 108 SER 108 195 195 SER SER C . n 
C 1 109 ARG 109 196 196 ARG ARG C . n 
C 1 110 MET 110 197 197 MET MET C . n 
C 1 111 SER 111 198 198 SER SER C . n 
C 1 112 ILE 112 199 199 ILE ILE C . n 
C 1 113 CYS 113 200 200 CYS CYS C . n 
C 1 114 MET 114 201 201 MET MET C . n 
C 1 115 SER 115 202 202 SER SER C . n 
C 1 116 GLY 116 203 203 GLY GLY C . n 
C 1 117 PRO 117 204 204 PRO PRO C . n 
C 1 118 ASN 118 205 205 ASN ASN C . n 
C 1 119 ASN 119 206 206 ASN ASN C . n 
C 1 120 ASN 120 207 207 ASN ASN C . n 
C 1 121 ALA 121 208 208 ALA ALA C . n 
C 1 122 SER 122 209 209 SER SER C . n 
C 1 123 ALA 123 210 210 ALA ALA C . n 
C 1 124 VAL 124 211 211 VAL VAL C . n 
C 1 125 VAL 125 212 212 VAL VAL C . n 
C 1 126 TRP 126 213 213 TRP TRP C . n 
C 1 127 TYR 127 214 214 TYR TYR C . n 
C 1 128 GLY 128 215 215 GLY GLY C . n 
C 1 129 GLY 129 216 216 GLY GLY C . n 
C 1 130 ARG 130 217 217 ARG ARG C . n 
C 1 131 PRO 131 218 218 PRO PRO C . n 
C 1 132 ILE 132 219 219 ILE ILE C . n 
C 1 133 THR 133 220 220 THR THR C . n 
C 1 134 GLU 134 221 221 GLU GLU C . n 
C 1 135 ILE 135 222 222 ILE ILE C . n 
C 1 136 PRO 136 223 223 PRO PRO C . n 
C 1 137 SER 137 224 224 SER SER C . n 
C 1 138 TRP 138 225 225 TRP TRP C . n 
C 1 139 ALA 139 226 226 ALA ALA C . n 
C 1 140 GLY 140 227 227 GLY GLY C . n 
C 1 141 ASN 141 228 228 ASN ASN C . n 
C 1 142 ILE 142 229 229 ILE ILE C . n 
C 1 143 LEU 143 230 230 LEU LEU C . n 
C 1 144 ARG 144 231 231 ARG ARG C . n 
C 1 145 THR 145 232 232 THR THR C . n 
C 1 146 GLN 146 233 233 GLN GLN C . n 
C 1 147 GLU 147 234 234 GLU GLU C . n 
C 1 148 SER 148 235 235 SER SER C . n 
C 1 149 GLU 149 236 236 GLU GLU C . n 
C 1 150 CYS 150 237 237 CYS CYS C . n 
C 1 151 VAL 151 238 238 VAL VAL C . n 
C 1 152 CYS 152 239 239 CYS CYS C . n 
C 1 153 HIS 153 240 240 HIS HIS C . n 
C 1 154 LYS 154 241 241 LYS LYS C . n 
C 1 155 GLY 155 242 242 GLY GLY C . n 
C 1 156 VAL 156 243 243 VAL VAL C . n 
C 1 157 CYS 157 244 244 CYS CYS C . n 
C 1 158 PRO 158 245 245 PRO PRO C . n 
C 1 159 VAL 159 246 246 VAL VAL C . n 
C 1 160 VAL 160 247 247 VAL VAL C . n 
C 1 161 MET 161 248 248 MET MET C . n 
C 1 162 THR 162 249 249 THR THR C . n 
C 1 163 ASP 163 250 250 ASP ASP C . n 
C 1 164 GLY 164 251 251 GLY GLY C . n 
C 1 165 PRO 165 252 252 PRO PRO C . n 
C 1 166 ALA 166 253 253 ALA ALA C . n 
C 1 167 ASN 167 254 254 ASN ASN C . n 
C 1 168 ASN 168 255 255 ASN ASN C . n 
C 1 169 ARG 169 256 256 ARG ARG C . n 
C 1 170 ALA 170 257 257 ALA ALA C . n 
C 1 171 ALA 171 258 258 ALA ALA C . n 
C 1 172 THR 172 259 259 THR THR C . n 
C 1 173 LYS 173 260 260 LYS LYS C . n 
C 1 174 ILE 174 261 261 ILE ILE C . n 
C 1 175 ILE 175 262 262 ILE ILE C . n 
C 1 176 TYR 176 263 263 TYR TYR C . n 
C 1 177 PHE 177 264 264 PHE PHE C . n 
C 1 178 LYS 178 265 265 LYS LYS C . n 
C 1 179 GLU 179 266 266 GLU GLU C . n 
C 1 180 GLY 180 267 267 GLY GLY C . n 
C 1 181 LYS 181 268 268 LYS LYS C . n 
C 1 182 ILE 182 269 269 ILE ILE C . n 
C 1 183 GLN 183 270 270 GLN GLN C . n 
C 1 184 LYS 184 271 271 LYS LYS C . n 
C 1 185 ILE 185 272 272 ILE ILE C . n 
C 1 186 GLU 186 273 273 GLU GLU C . n 
C 1 187 GLU 187 274 274 GLU GLU C . n 
C 1 188 LEU 188 275 275 LEU LEU C . n 
C 1 189 ALA 189 276 276 ALA ALA C . n 
C 1 190 GLY 190 277 277 GLY GLY C . n 
C 1 191 ASN 191 278 278 ASN ASN C . n 
C 1 192 ALA 192 279 279 ALA ALA C . n 
C 1 193 GLN 193 280 280 GLN GLN C . n 
C 1 194 HIS 194 281 281 HIS HIS C . n 
C 1 195 ILE 195 282 282 ILE ILE C . n 
C 1 196 GLU 196 283 283 GLU GLU C . n 
C 1 197 GLU 197 284 284 GLU GLU C . n 
C 1 198 CYS 198 285 285 CYS CYS C . n 
C 1 199 SER 199 286 286 SER SER C . n 
C 1 200 CYS 200 287 287 CYS CYS C . n 
C 1 201 TYR 201 288 288 TYR TYR C . n 
C 1 202 GLY 202 289 289 GLY GLY C . n 
C 1 203 ALA 203 290 290 ALA ALA C . n 
C 1 204 GLY 204 291 291 GLY GLY C . n 
C 1 205 GLY 205 292 292 GLY GLY C . n 
C 1 206 VAL 206 293 293 VAL VAL C . n 
C 1 207 ILE 207 294 294 ILE ILE C . n 
C 1 208 LYS 208 295 295 LYS LYS C . n 
C 1 209 CYS 209 296 296 CYS CYS C . n 
C 1 210 ILE 210 297 297 ILE ILE C . n 
C 1 211 CYS 211 298 298 CYS CYS C . n 
C 1 212 ARG 212 299 299 ARG ARG C . n 
C 1 213 ASP 213 300 300 ASP ASP C . n 
C 1 214 ASN 214 301 301 ASN ASN C . n 
C 1 215 TRP 215 302 302 TRP TRP C . n 
C 1 216 LYS 216 303 303 LYS LYS C . n 
C 1 217 GLY 217 304 304 GLY GLY C . n 
C 1 218 ALA 218 305 305 ALA ALA C . n 
C 1 219 ASN 219 306 306 ASN ASN C . n 
C 1 220 ARG 220 307 307 ARG ARG C . n 
C 1 221 PRO 221 308 308 PRO PRO C . n 
C 1 222 VAL 222 309 309 VAL VAL C . n 
C 1 223 ILE 223 310 310 ILE ILE C . n 
C 1 224 THR 224 311 311 THR THR C . n 
C 1 225 ILE 225 312 312 ILE ILE C . n 
C 1 226 ASP 226 313 313 ASP ASP C . n 
C 1 227 PRO 227 314 314 PRO PRO C . n 
C 1 228 GLU 228 315 315 GLU GLU C . n 
C 1 229 MET 229 316 316 MET MET C . n 
C 1 230 MET 230 317 317 MET MET C . n 
C 1 231 THR 231 318 318 THR THR C . n 
C 1 232 HIS 232 319 319 HIS HIS C . n 
C 1 233 THR 233 320 320 THR THR C . n 
C 1 234 SER 234 321 321 SER SER C . n 
C 1 235 LYS 235 322 322 LYS LYS C . n 
C 1 236 TYR 236 323 323 TYR TYR C . n 
C 1 237 LEU 237 324 324 LEU LEU C . n 
C 1 238 CYS 238 325 325 CYS CYS C . n 
C 1 239 SER 239 326 326 SER SER C . n 
C 1 240 LYS 240 327 327 LYS LYS C . n 
C 1 241 VAL 241 328 328 VAL VAL C . n 
C 1 242 LEU 242 329 329 LEU LEU C . n 
C 1 243 THR 243 330 330 THR THR C . n 
C 1 244 ASP 244 331 331 ASP ASP C . n 
C 1 245 THR 245 332 332 THR THR C . n 
C 1 246 SER 246 333 333 SER SER C . n 
C 1 247 ARG 247 334 334 ARG ARG C . n 
C 1 248 PRO 248 335 335 PRO PRO C . n 
C 1 249 ASN 249 336 336 ASN ASN C . n 
C 1 250 ASP 250 337 337 ASP ASP C . n 
C 1 251 PRO 251 338 338 PRO PRO C . n 
C 1 252 THR 252 339 339 THR THR C . n 
C 1 253 ASN 253 340 340 ASN ASN C . n 
C 1 254 GLY 254 341 341 GLY GLY C . n 
C 1 255 ASN 255 342 342 ASN ASN C . n 
C 1 256 CYS 256 343 343 CYS CYS C . n 
C 1 257 ASP 257 344 344 ASP ASP C . n 
C 1 258 ALA 258 345 345 ALA ALA C . n 
C 1 259 PRO 259 346 346 PRO PRO C . n 
C 1 260 ILE 260 347 347 ILE ILE C . n 
C 1 261 THR 261 348 348 THR THR C . n 
C 1 262 GLY 262 349 349 GLY GLY C . n 
C 1 263 GLY 263 350 350 GLY GLY C . n 
C 1 264 SER 264 351 351 SER SER C . n 
C 1 265 PRO 265 352 352 PRO PRO C . n 
C 1 266 ASP 266 353 353 ASP ASP C . n 
C 1 267 PRO 267 354 354 PRO PRO C . n 
C 1 268 GLY 268 355 355 GLY GLY C . n 
C 1 269 VAL 269 356 356 VAL VAL C . n 
C 1 270 LYS 270 357 357 LYS LYS C . n 
C 1 271 GLY 271 358 358 GLY GLY C . n 
C 1 272 PHE 272 359 359 PHE PHE C . n 
C 1 273 ALA 273 360 360 ALA ALA C . n 
C 1 274 PHE 274 361 361 PHE PHE C . n 
C 1 275 LEU 275 362 362 LEU LEU C . n 
C 1 276 ASP 276 363 363 ASP ASP C . n 
C 1 277 GLY 277 364 364 GLY GLY C . n 
C 1 278 GLU 278 365 365 GLU GLU C . n 
C 1 279 ASN 279 366 366 ASN ASN C . n 
C 1 280 SER 280 367 367 SER SER C . n 
C 1 281 TRP 281 368 368 TRP TRP C . n 
C 1 282 LEU 282 369 369 LEU LEU C . n 
C 1 283 GLY 283 370 370 GLY GLY C . n 
C 1 284 ARG 284 371 371 ARG ARG C . n 
C 1 285 THR 285 372 372 THR THR C . n 
C 1 286 ILE 286 373 373 ILE ILE C . n 
C 1 287 SER 287 374 374 SER SER C . n 
C 1 288 LYS 288 375 375 LYS LYS C . n 
C 1 289 ASP 289 376 376 ASP ASP C . n 
C 1 290 SER 290 377 377 SER SER C . n 
C 1 291 ARG 291 378 378 ARG ARG C . n 
C 1 292 SER 292 379 379 SER SER C . n 
C 1 293 GLY 293 380 380 GLY GLY C . n 
C 1 294 TYR 294 381 381 TYR TYR C . n 
C 1 295 GLU 295 382 382 GLU GLU C . n 
C 1 296 MET 296 383 383 MET MET C . n 
C 1 297 LEU 297 384 384 LEU LEU C . n 
C 1 298 LYS 298 385 385 LYS LYS C . n 
C 1 299 VAL 299 386 386 VAL VAL C . n 
C 1 300 PRO 300 387 387 PRO PRO C . n 
C 1 301 ASN 301 388 388 ASN ASN C . n 
C 1 302 ALA 302 389 389 ALA ALA C . n 
C 1 303 GLU 303 390 390 GLU GLU C . n 
C 1 304 THR 304 391 391 THR THR C . n 
C 1 305 ASP 305 392 392 ASP ASP C . n 
C 1 306 ILE 306 393 393 ILE ILE C . n 
C 1 307 GLN 307 394 394 GLN GLN C . n 
C 1 308 SER 308 395 395 SER SER C . n 
C 1 309 GLY 309 396 396 GLY GLY C . n 
C 1 310 PRO 310 397 397 PRO PRO C . n 
C 1 311 ILE 311 398 398 ILE ILE C . n 
C 1 312 SER 312 399 399 SER SER C . n 
C 1 313 ASN 313 400 400 ASN ASN C . n 
C 1 314 GLN 314 401 401 GLN GLN C . n 
C 1 315 VAL 315 402 402 VAL VAL C . n 
C 1 316 ILE 316 403 403 ILE ILE C . n 
C 1 317 VAL 317 404 404 VAL VAL C . n 
C 1 318 ASN 318 405 405 ASN ASN C . n 
C 1 319 ASN 319 406 406 ASN ASN C . n 
C 1 320 GLN 320 407 407 GLN GLN C . n 
C 1 321 ASN 321 408 408 ASN ASN C . n 
C 1 322 TRP 322 409 409 TRP TRP C . n 
C 1 323 SER 323 410 410 SER SER C . n 
C 1 324 GLY 324 411 411 GLY GLY C . n 
C 1 325 TYR 325 412 412 TYR TYR C . n 
C 1 326 SER 326 413 413 SER SER C . n 
C 1 327 GLY 327 414 414 GLY GLY C . n 
C 1 328 ALA 328 415 415 ALA ALA C . n 
C 1 329 PHE 329 416 416 PHE PHE C . n 
C 1 330 ILE 330 417 417 ILE ILE C . n 
C 1 331 ASP 331 418 418 ASP ASP C . n 
C 1 332 TYR 332 419 419 TYR TYR C . n 
C 1 333 TRP 333 420 420 TRP TRP C . n 
C 1 334 ALA 334 421 421 ALA ALA C . n 
C 1 335 ASN 335 422 422 ASN ASN C . n 
C 1 336 LYS 336 423 423 LYS LYS C . n 
C 1 337 GLU 337 424 424 GLU GLU C . n 
C 1 338 CYS 338 425 425 CYS CYS C . n 
C 1 339 PHE 339 426 426 PHE PHE C . n 
C 1 340 ASN 340 427 427 ASN ASN C . n 
C 1 341 PRO 341 428 428 PRO PRO C . n 
C 1 342 CYS 342 429 429 CYS CYS C . n 
C 1 343 PHE 343 430 430 PHE PHE C . n 
C 1 344 TYR 344 431 431 TYR TYR C . n 
C 1 345 VAL 345 432 432 VAL VAL C . n 
C 1 346 GLU 346 433 433 GLU GLU C . n 
C 1 347 LEU 347 434 434 LEU LEU C . n 
C 1 348 ILE 348 435 435 ILE ILE C . n 
C 1 349 ARG 349 436 436 ARG ARG C . n 
C 1 350 GLY 350 437 437 GLY GLY C . n 
C 1 351 ARG 351 438 438 ARG ARG C . n 
C 1 352 PRO 352 439 439 PRO PRO C . n 
C 1 353 LYS 353 440 440 LYS LYS C . n 
C 1 354 GLU 354 441 441 GLU GLU C . n 
C 1 355 SER 355 442 442 SER SER C . n 
C 1 356 SER 356 443 443 SER SER C . n 
C 1 357 VAL 357 444 444 VAL VAL C . n 
C 1 358 LEU 358 445 445 LEU LEU C . n 
C 1 359 TRP 359 446 446 TRP TRP C . n 
C 1 360 THR 360 447 447 THR THR C . n 
C 1 361 SER 361 448 448 SER SER C . n 
C 1 362 ASN 362 449 449 ASN ASN C . n 
C 1 363 SER 363 450 450 SER SER C . n 
C 1 364 ILE 364 451 451 ILE ILE C . n 
C 1 365 VAL 365 452 452 VAL VAL C . n 
C 1 366 ALA 366 453 453 ALA ALA C . n 
C 1 367 LEU 367 454 454 LEU LEU C . n 
C 1 368 CYS 368 455 455 CYS CYS C . n 
C 1 369 GLY 369 456 456 GLY GLY C . n 
C 1 370 SER 370 457 457 SER SER C . n 
C 1 371 LYS 371 458 458 LYS LYS C . n 
C 1 372 LYS 372 459 459 LYS LYS C . n 
C 1 373 ARG 373 460 460 ARG ARG C . n 
C 1 374 LEU 374 461 461 LEU LEU C . n 
C 1 375 GLY 375 462 462 GLY GLY C . n 
C 1 376 SER 376 463 463 SER SER C . n 
C 1 377 TRP 377 464 464 TRP TRP C . n 
C 1 378 SER 378 465 465 SER SER C . n 
C 1 379 TRP 379 466 466 TRP TRP C . n 
C 1 380 HIS 380 467 467 HIS HIS C . n 
C 1 381 ASP 381 468 468 ASP ASP C . n 
C 1 382 GLY 382 469 469 GLY GLY C . n 
C 1 383 ALA 383 470 470 ALA ALA C . n 
C 1 384 GLU 384 471 471 GLU GLU C . n 
C 1 385 ILE 385 472 472 ILE ILE C . n 
C 1 386 ILE 386 473 473 ILE ILE C . n 
C 1 387 TYR 387 474 474 TYR TYR C . n 
C 1 388 PHE 388 475 475 PHE PHE C . n 
C 1 389 GLU 389 476 476 GLU GLU C . n 
D 1 1   ARG 1   88  88  ARG ARG D . n 
D 1 2   THR 2   89  89  THR THR D . n 
D 1 3   PHE 3   90  90  PHE PHE D . n 
D 1 4   LEU 4   91  91  LEU LEU D . n 
D 1 5   ASN 5   92  92  ASN ASN D . n 
D 1 6   LEU 6   93  93  LEU LEU D . n 
D 1 7   THR 7   94  94  THR THR D . n 
D 1 8   LYS 8   95  95  LYS LYS D . n 
D 1 9   PRO 9   96  96  PRO PRO D . n 
D 1 10  LEU 10  97  97  LEU LEU D . n 
D 1 11  CYS 11  98  98  CYS CYS D . n 
D 1 12  GLU 12  99  99  GLU GLU D . n 
D 1 13  VAL 13  100 100 VAL VAL D . n 
D 1 14  ASN 14  101 101 ASN ASN D . n 
D 1 15  SER 15  102 102 SER SER D . n 
D 1 16  TRP 16  103 103 TRP TRP D . n 
D 1 17  HIS 17  104 104 HIS HIS D . n 
D 1 18  ILE 18  105 105 ILE ILE D . n 
D 1 19  LEU 19  106 106 LEU LEU D . n 
D 1 20  SER 20  107 107 SER SER D . n 
D 1 21  LYS 21  108 108 LYS LYS D . n 
D 1 22  ASP 22  109 109 ASP ASP D . n 
D 1 23  ASN 23  110 110 ASN ASN D . n 
D 1 24  ALA 24  111 111 ALA ALA D . n 
D 1 25  ILE 25  112 112 ILE ILE D . n 
D 1 26  ARG 26  113 113 ARG ARG D . n 
D 1 27  ILE 27  114 114 ILE ILE D . n 
D 1 28  GLY 28  115 115 GLY GLY D . n 
D 1 29  GLU 29  116 116 GLU GLU D . n 
D 1 30  ASP 30  117 117 ASP ASP D . n 
D 1 31  ALA 31  118 118 ALA ALA D . n 
D 1 32  HIS 32  119 119 HIS HIS D . n 
D 1 33  ILE 33  120 120 ILE ILE D . n 
D 1 34  LEU 34  121 121 LEU LEU D . n 
D 1 35  VAL 35  122 122 VAL VAL D . n 
D 1 36  THR 36  123 123 THR THR D . n 
D 1 37  ARG 37  124 124 ARG ARG D . n 
D 1 38  GLU 38  125 125 GLU GLU D . n 
D 1 39  PRO 39  126 126 PRO PRO D . n 
D 1 40  TYR 40  127 127 TYR TYR D . n 
D 1 41  LEU 41  128 128 LEU LEU D . n 
D 1 42  SER 42  129 129 SER SER D . n 
D 1 43  CYS 43  130 130 CYS CYS D . n 
D 1 44  ASP 44  131 131 ASP ASP D . n 
D 1 45  PRO 45  132 132 PRO PRO D . n 
D 1 46  GLN 46  133 133 GLN GLN D . n 
D 1 47  GLY 47  134 134 GLY GLY D . n 
D 1 48  CYS 48  135 135 CYS CYS D . n 
D 1 49  ARG 49  136 136 ARG ARG D . n 
D 1 50  MET 50  137 137 MET MET D . n 
D 1 51  PHE 51  138 138 PHE PHE D . n 
D 1 52  ALA 52  139 139 ALA ALA D . n 
D 1 53  LEU 53  140 140 LEU LEU D . n 
D 1 54  SER 54  141 141 SER SER D . n 
D 1 55  GLN 55  142 142 GLN GLN D . n 
D 1 56  GLY 56  143 143 GLY GLY D . n 
D 1 57  THR 57  144 144 THR THR D . n 
D 1 58  THR 58  145 145 THR THR D . n 
D 1 59  LEU 59  146 146 LEU LEU D . n 
D 1 60  ARG 60  147 147 ARG ARG D . n 
D 1 61  GLY 61  148 148 GLY GLY D . n 
D 1 62  ARG 62  149 149 ARG ARG D . n 
D 1 63  HIS 63  150 150 HIS HIS D . n 
D 1 64  ALA 64  151 151 ALA ALA D . n 
D 1 65  ASN 65  152 152 ASN ASN D . n 
D 1 66  GLY 66  153 153 GLY GLY D . n 
D 1 67  THR 67  154 154 THR THR D . n 
D 1 68  ILE 68  155 155 ILE ILE D . n 
D 1 69  HIS 69  156 156 HIS HIS D . n 
D 1 70  ASP 70  157 157 ASP ASP D . n 
D 1 71  ARG 71  158 158 ARG ARG D . n 
D 1 72  SER 72  159 159 SER SER D . n 
D 1 73  PRO 73  160 160 PRO PRO D . n 
D 1 74  PHE 74  161 161 PHE PHE D . n 
D 1 75  ARG 75  162 162 ARG ARG D . n 
D 1 76  ALA 76  163 163 ALA ALA D . n 
D 1 77  LEU 77  164 164 LEU LEU D . n 
D 1 78  ILE 78  165 165 ILE ILE D . n 
D 1 79  SER 79  166 166 SER SER D . n 
D 1 80  TRP 80  167 167 TRP TRP D . n 
D 1 81  GLU 81  168 168 GLU GLU D . n 
D 1 82  MET 82  169 169 MET MET D . n 
D 1 83  GLY 83  170 170 GLY GLY D . n 
D 1 84  GLN 84  171 171 GLN GLN D . n 
D 1 85  ALA 85  172 172 ALA ALA D . n 
D 1 86  PRO 86  173 173 PRO PRO D . n 
D 1 87  SER 87  174 174 SER SER D . n 
D 1 88  PRO 88  175 175 PRO PRO D . n 
D 1 89  TYR 89  176 176 TYR TYR D . n 
D 1 90  ASN 90  177 177 ASN ASN D . n 
D 1 91  THR 91  178 178 THR THR D . n 
D 1 92  ARG 92  179 179 ARG ARG D . n 
D 1 93  VAL 93  180 180 VAL VAL D . n 
D 1 94  GLU 94  181 181 GLU GLU D . n 
D 1 95  CYS 95  182 182 CYS CYS D . n 
D 1 96  ILE 96  183 183 ILE ILE D . n 
D 1 97  GLY 97  184 184 GLY GLY D . n 
D 1 98  TRP 98  185 185 TRP TRP D . n 
D 1 99  SER 99  186 186 SER SER D . n 
D 1 100 SER 100 187 187 SER SER D . n 
D 1 101 THR 101 188 188 THR THR D . n 
D 1 102 SER 102 189 189 SER SER D . n 
D 1 103 CYS 103 190 190 CYS CYS D . n 
D 1 104 HIS 104 191 191 HIS HIS D . n 
D 1 105 ASP 105 192 192 ASP ASP D . n 
D 1 106 GLY 106 193 193 GLY GLY D . n 
D 1 107 MET 107 194 194 MET MET D . n 
D 1 108 SER 108 195 195 SER SER D . n 
D 1 109 ARG 109 196 196 ARG ARG D . n 
D 1 110 MET 110 197 197 MET MET D . n 
D 1 111 SER 111 198 198 SER SER D . n 
D 1 112 ILE 112 199 199 ILE ILE D . n 
D 1 113 CYS 113 200 200 CYS CYS D . n 
D 1 114 MET 114 201 201 MET MET D . n 
D 1 115 SER 115 202 202 SER SER D . n 
D 1 116 GLY 116 203 203 GLY GLY D . n 
D 1 117 PRO 117 204 204 PRO PRO D . n 
D 1 118 ASN 118 205 205 ASN ASN D . n 
D 1 119 ASN 119 206 206 ASN ASN D . n 
D 1 120 ASN 120 207 207 ASN ASN D . n 
D 1 121 ALA 121 208 208 ALA ALA D . n 
D 1 122 SER 122 209 209 SER SER D . n 
D 1 123 ALA 123 210 210 ALA ALA D . n 
D 1 124 VAL 124 211 211 VAL VAL D . n 
D 1 125 VAL 125 212 212 VAL VAL D . n 
D 1 126 TRP 126 213 213 TRP TRP D . n 
D 1 127 TYR 127 214 214 TYR TYR D . n 
D 1 128 GLY 128 215 215 GLY GLY D . n 
D 1 129 GLY 129 216 216 GLY GLY D . n 
D 1 130 ARG 130 217 217 ARG ARG D . n 
D 1 131 PRO 131 218 218 PRO PRO D . n 
D 1 132 ILE 132 219 219 ILE ILE D . n 
D 1 133 THR 133 220 220 THR THR D . n 
D 1 134 GLU 134 221 221 GLU GLU D . n 
D 1 135 ILE 135 222 222 ILE ILE D . n 
D 1 136 PRO 136 223 223 PRO PRO D . n 
D 1 137 SER 137 224 224 SER SER D . n 
D 1 138 TRP 138 225 225 TRP TRP D . n 
D 1 139 ALA 139 226 226 ALA ALA D . n 
D 1 140 GLY 140 227 227 GLY GLY D . n 
D 1 141 ASN 141 228 228 ASN ASN D . n 
D 1 142 ILE 142 229 229 ILE ILE D . n 
D 1 143 LEU 143 230 230 LEU LEU D . n 
D 1 144 ARG 144 231 231 ARG ARG D . n 
D 1 145 THR 145 232 232 THR THR D . n 
D 1 146 GLN 146 233 233 GLN GLN D . n 
D 1 147 GLU 147 234 234 GLU GLU D . n 
D 1 148 SER 148 235 235 SER SER D . n 
D 1 149 GLU 149 236 236 GLU GLU D . n 
D 1 150 CYS 150 237 237 CYS CYS D . n 
D 1 151 VAL 151 238 238 VAL VAL D . n 
D 1 152 CYS 152 239 239 CYS CYS D . n 
D 1 153 HIS 153 240 240 HIS HIS D . n 
D 1 154 LYS 154 241 241 LYS LYS D . n 
D 1 155 GLY 155 242 242 GLY GLY D . n 
D 1 156 VAL 156 243 243 VAL VAL D . n 
D 1 157 CYS 157 244 244 CYS CYS D . n 
D 1 158 PRO 158 245 245 PRO PRO D . n 
D 1 159 VAL 159 246 246 VAL VAL D . n 
D 1 160 VAL 160 247 247 VAL VAL D . n 
D 1 161 MET 161 248 248 MET MET D . n 
D 1 162 THR 162 249 249 THR THR D . n 
D 1 163 ASP 163 250 250 ASP ASP D . n 
D 1 164 GLY 164 251 251 GLY GLY D . n 
D 1 165 PRO 165 252 252 PRO PRO D . n 
D 1 166 ALA 166 253 253 ALA ALA D . n 
D 1 167 ASN 167 254 254 ASN ASN D . n 
D 1 168 ASN 168 255 255 ASN ASN D . n 
D 1 169 ARG 169 256 256 ARG ARG D . n 
D 1 170 ALA 170 257 257 ALA ALA D . n 
D 1 171 ALA 171 258 258 ALA ALA D . n 
D 1 172 THR 172 259 259 THR THR D . n 
D 1 173 LYS 173 260 260 LYS LYS D . n 
D 1 174 ILE 174 261 261 ILE ILE D . n 
D 1 175 ILE 175 262 262 ILE ILE D . n 
D 1 176 TYR 176 263 263 TYR TYR D . n 
D 1 177 PHE 177 264 264 PHE PHE D . n 
D 1 178 LYS 178 265 265 LYS LYS D . n 
D 1 179 GLU 179 266 266 GLU GLU D . n 
D 1 180 GLY 180 267 267 GLY GLY D . n 
D 1 181 LYS 181 268 268 LYS LYS D . n 
D 1 182 ILE 182 269 269 ILE ILE D . n 
D 1 183 GLN 183 270 270 GLN GLN D . n 
D 1 184 LYS 184 271 271 LYS LYS D . n 
D 1 185 ILE 185 272 272 ILE ILE D . n 
D 1 186 GLU 186 273 273 GLU GLU D . n 
D 1 187 GLU 187 274 274 GLU GLU D . n 
D 1 188 LEU 188 275 275 LEU LEU D . n 
D 1 189 ALA 189 276 276 ALA ALA D . n 
D 1 190 GLY 190 277 277 GLY GLY D . n 
D 1 191 ASN 191 278 278 ASN ASN D . n 
D 1 192 ALA 192 279 279 ALA ALA D . n 
D 1 193 GLN 193 280 280 GLN GLN D . n 
D 1 194 HIS 194 281 281 HIS HIS D . n 
D 1 195 ILE 195 282 282 ILE ILE D . n 
D 1 196 GLU 196 283 283 GLU GLU D . n 
D 1 197 GLU 197 284 284 GLU GLU D . n 
D 1 198 CYS 198 285 285 CYS CYS D . n 
D 1 199 SER 199 286 286 SER SER D . n 
D 1 200 CYS 200 287 287 CYS CYS D . n 
D 1 201 TYR 201 288 288 TYR TYR D . n 
D 1 202 GLY 202 289 289 GLY GLY D . n 
D 1 203 ALA 203 290 290 ALA ALA D . n 
D 1 204 GLY 204 291 291 GLY GLY D . n 
D 1 205 GLY 205 292 292 GLY GLY D . n 
D 1 206 VAL 206 293 293 VAL VAL D . n 
D 1 207 ILE 207 294 294 ILE ILE D . n 
D 1 208 LYS 208 295 295 LYS LYS D . n 
D 1 209 CYS 209 296 296 CYS CYS D . n 
D 1 210 ILE 210 297 297 ILE ILE D . n 
D 1 211 CYS 211 298 298 CYS CYS D . n 
D 1 212 ARG 212 299 299 ARG ARG D . n 
D 1 213 ASP 213 300 300 ASP ASP D . n 
D 1 214 ASN 214 301 301 ASN ASN D . n 
D 1 215 TRP 215 302 302 TRP TRP D . n 
D 1 216 LYS 216 303 303 LYS LYS D . n 
D 1 217 GLY 217 304 304 GLY GLY D . n 
D 1 218 ALA 218 305 305 ALA ALA D . n 
D 1 219 ASN 219 306 306 ASN ASN D . n 
D 1 220 ARG 220 307 307 ARG ARG D . n 
D 1 221 PRO 221 308 308 PRO PRO D . n 
D 1 222 VAL 222 309 309 VAL VAL D . n 
D 1 223 ILE 223 310 310 ILE ILE D . n 
D 1 224 THR 224 311 311 THR THR D . n 
D 1 225 ILE 225 312 312 ILE ILE D . n 
D 1 226 ASP 226 313 313 ASP ASP D . n 
D 1 227 PRO 227 314 314 PRO PRO D . n 
D 1 228 GLU 228 315 315 GLU GLU D . n 
D 1 229 MET 229 316 316 MET MET D . n 
D 1 230 MET 230 317 317 MET MET D . n 
D 1 231 THR 231 318 318 THR THR D . n 
D 1 232 HIS 232 319 319 HIS HIS D . n 
D 1 233 THR 233 320 320 THR THR D . n 
D 1 234 SER 234 321 321 SER SER D . n 
D 1 235 LYS 235 322 322 LYS LYS D . n 
D 1 236 TYR 236 323 323 TYR TYR D . n 
D 1 237 LEU 237 324 324 LEU LEU D . n 
D 1 238 CYS 238 325 325 CYS CYS D . n 
D 1 239 SER 239 326 326 SER SER D . n 
D 1 240 LYS 240 327 327 LYS LYS D . n 
D 1 241 VAL 241 328 328 VAL VAL D . n 
D 1 242 LEU 242 329 329 LEU LEU D . n 
D 1 243 THR 243 330 330 THR THR D . n 
D 1 244 ASP 244 331 331 ASP ASP D . n 
D 1 245 THR 245 332 332 THR THR D . n 
D 1 246 SER 246 333 333 SER SER D . n 
D 1 247 ARG 247 334 334 ARG ARG D . n 
D 1 248 PRO 248 335 335 PRO PRO D . n 
D 1 249 ASN 249 336 336 ASN ASN D . n 
D 1 250 ASP 250 337 337 ASP ASP D . n 
D 1 251 PRO 251 338 338 PRO PRO D . n 
D 1 252 THR 252 339 339 THR THR D . n 
D 1 253 ASN 253 340 340 ASN ASN D . n 
D 1 254 GLY 254 341 341 GLY GLY D . n 
D 1 255 ASN 255 342 342 ASN ASN D . n 
D 1 256 CYS 256 343 343 CYS CYS D . n 
D 1 257 ASP 257 344 344 ASP ASP D . n 
D 1 258 ALA 258 345 345 ALA ALA D . n 
D 1 259 PRO 259 346 346 PRO PRO D . n 
D 1 260 ILE 260 347 347 ILE ILE D . n 
D 1 261 THR 261 348 348 THR THR D . n 
D 1 262 GLY 262 349 349 GLY GLY D . n 
D 1 263 GLY 263 350 350 GLY GLY D . n 
D 1 264 SER 264 351 351 SER SER D . n 
D 1 265 PRO 265 352 352 PRO PRO D . n 
D 1 266 ASP 266 353 353 ASP ASP D . n 
D 1 267 PRO 267 354 354 PRO PRO D . n 
D 1 268 GLY 268 355 355 GLY GLY D . n 
D 1 269 VAL 269 356 356 VAL VAL D . n 
D 1 270 LYS 270 357 357 LYS LYS D . n 
D 1 271 GLY 271 358 358 GLY GLY D . n 
D 1 272 PHE 272 359 359 PHE PHE D . n 
D 1 273 ALA 273 360 360 ALA ALA D . n 
D 1 274 PHE 274 361 361 PHE PHE D . n 
D 1 275 LEU 275 362 362 LEU LEU D . n 
D 1 276 ASP 276 363 363 ASP ASP D . n 
D 1 277 GLY 277 364 364 GLY GLY D . n 
D 1 278 GLU 278 365 365 GLU GLU D . n 
D 1 279 ASN 279 366 366 ASN ASN D . n 
D 1 280 SER 280 367 367 SER SER D . n 
D 1 281 TRP 281 368 368 TRP TRP D . n 
D 1 282 LEU 282 369 369 LEU LEU D . n 
D 1 283 GLY 283 370 370 GLY GLY D . n 
D 1 284 ARG 284 371 371 ARG ARG D . n 
D 1 285 THR 285 372 372 THR THR D . n 
D 1 286 ILE 286 373 373 ILE ILE D . n 
D 1 287 SER 287 374 374 SER SER D . n 
D 1 288 LYS 288 375 375 LYS LYS D . n 
D 1 289 ASP 289 376 376 ASP ASP D . n 
D 1 290 SER 290 377 377 SER SER D . n 
D 1 291 ARG 291 378 378 ARG ARG D . n 
D 1 292 SER 292 379 379 SER SER D . n 
D 1 293 GLY 293 380 380 GLY GLY D . n 
D 1 294 TYR 294 381 381 TYR TYR D . n 
D 1 295 GLU 295 382 382 GLU GLU D . n 
D 1 296 MET 296 383 383 MET MET D . n 
D 1 297 LEU 297 384 384 LEU LEU D . n 
D 1 298 LYS 298 385 385 LYS LYS D . n 
D 1 299 VAL 299 386 386 VAL VAL D . n 
D 1 300 PRO 300 387 387 PRO PRO D . n 
D 1 301 ASN 301 388 388 ASN ASN D . n 
D 1 302 ALA 302 389 389 ALA ALA D . n 
D 1 303 GLU 303 390 390 GLU GLU D . n 
D 1 304 THR 304 391 391 THR THR D . n 
D 1 305 ASP 305 392 392 ASP ASP D . n 
D 1 306 ILE 306 393 393 ILE ILE D . n 
D 1 307 GLN 307 394 394 GLN GLN D . n 
D 1 308 SER 308 395 395 SER SER D . n 
D 1 309 GLY 309 396 396 GLY GLY D . n 
D 1 310 PRO 310 397 397 PRO PRO D . n 
D 1 311 ILE 311 398 398 ILE ILE D . n 
D 1 312 SER 312 399 399 SER SER D . n 
D 1 313 ASN 313 400 400 ASN ASN D . n 
D 1 314 GLN 314 401 401 GLN GLN D . n 
D 1 315 VAL 315 402 402 VAL VAL D . n 
D 1 316 ILE 316 403 403 ILE ILE D . n 
D 1 317 VAL 317 404 404 VAL VAL D . n 
D 1 318 ASN 318 405 405 ASN ASN D . n 
D 1 319 ASN 319 406 406 ASN ASN D . n 
D 1 320 GLN 320 407 407 GLN GLN D . n 
D 1 321 ASN 321 408 408 ASN ASN D . n 
D 1 322 TRP 322 409 409 TRP TRP D . n 
D 1 323 SER 323 410 410 SER SER D . n 
D 1 324 GLY 324 411 411 GLY GLY D . n 
D 1 325 TYR 325 412 412 TYR TYR D . n 
D 1 326 SER 326 413 413 SER SER D . n 
D 1 327 GLY 327 414 414 GLY GLY D . n 
D 1 328 ALA 328 415 415 ALA ALA D . n 
D 1 329 PHE 329 416 416 PHE PHE D . n 
D 1 330 ILE 330 417 417 ILE ILE D . n 
D 1 331 ASP 331 418 418 ASP ASP D . n 
D 1 332 TYR 332 419 419 TYR TYR D . n 
D 1 333 TRP 333 420 420 TRP TRP D . n 
D 1 334 ALA 334 421 421 ALA ALA D . n 
D 1 335 ASN 335 422 422 ASN ASN D . n 
D 1 336 LYS 336 423 423 LYS LYS D . n 
D 1 337 GLU 337 424 424 GLU GLU D . n 
D 1 338 CYS 338 425 425 CYS CYS D . n 
D 1 339 PHE 339 426 426 PHE PHE D . n 
D 1 340 ASN 340 427 427 ASN ASN D . n 
D 1 341 PRO 341 428 428 PRO PRO D . n 
D 1 342 CYS 342 429 429 CYS CYS D . n 
D 1 343 PHE 343 430 430 PHE PHE D . n 
D 1 344 TYR 344 431 431 TYR TYR D . n 
D 1 345 VAL 345 432 432 VAL VAL D . n 
D 1 346 GLU 346 433 433 GLU GLU D . n 
D 1 347 LEU 347 434 434 LEU LEU D . n 
D 1 348 ILE 348 435 435 ILE ILE D . n 
D 1 349 ARG 349 436 436 ARG ARG D . n 
D 1 350 GLY 350 437 437 GLY GLY D . n 
D 1 351 ARG 351 438 438 ARG ARG D . n 
D 1 352 PRO 352 439 439 PRO PRO D . n 
D 1 353 LYS 353 440 440 LYS LYS D . n 
D 1 354 GLU 354 441 441 GLU GLU D . n 
D 1 355 SER 355 442 442 SER SER D . n 
D 1 356 SER 356 443 443 SER SER D . n 
D 1 357 VAL 357 444 444 VAL VAL D . n 
D 1 358 LEU 358 445 445 LEU LEU D . n 
D 1 359 TRP 359 446 446 TRP TRP D . n 
D 1 360 THR 360 447 447 THR THR D . n 
D 1 361 SER 361 448 448 SER SER D . n 
D 1 362 ASN 362 449 449 ASN ASN D . n 
D 1 363 SER 363 450 450 SER SER D . n 
D 1 364 ILE 364 451 451 ILE ILE D . n 
D 1 365 VAL 365 452 452 VAL VAL D . n 
D 1 366 ALA 366 453 453 ALA ALA D . n 
D 1 367 LEU 367 454 454 LEU LEU D . n 
D 1 368 CYS 368 455 455 CYS CYS D . n 
D 1 369 GLY 369 456 456 GLY GLY D . n 
D 1 370 SER 370 457 457 SER SER D . n 
D 1 371 LYS 371 458 458 LYS LYS D . n 
D 1 372 LYS 372 459 459 LYS LYS D . n 
D 1 373 ARG 373 460 460 ARG ARG D . n 
D 1 374 LEU 374 461 461 LEU LEU D . n 
D 1 375 GLY 375 462 462 GLY GLY D . n 
D 1 376 SER 376 463 463 SER SER D . n 
D 1 377 TRP 377 464 464 TRP TRP D . n 
D 1 378 SER 378 465 465 SER SER D . n 
D 1 379 TRP 379 466 466 TRP TRP D . n 
D 1 380 HIS 380 467 467 HIS HIS D . n 
D 1 381 ASP 381 468 468 ASP ASP D . n 
D 1 382 GLY 382 469 469 GLY GLY D . n 
D 1 383 ALA 383 470 470 ALA ALA D . n 
D 1 384 GLU 384 471 471 GLU GLU D . n 
D 1 385 ILE 385 472 472 ILE ILE D . n 
D 1 386 ILE 386 473 473 ILE ILE D . n 
D 1 387 TYR 387 474 474 TYR TYR D . n 
D 1 388 PHE 388 475 475 PHE PHE D . n 
D 1 389 GLU 389 476 476 GLU GLU D . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
E  2 CA  1   501  1477 CA  CA  A . 
F  3 GOL 1   502  1478 GOL GOL A . 
G  4 NAG 1   503  1479 NAG NAG A . 
H  4 NAG 2   504  1480 NAG NAG A . 
I  4 NAG 1   505  1481 NAG NAG A . 
J  4 NAG 1   506  1482 NAG NAG A . 
K  5 MAN 1   507  1483 MAN MAN A . 
L  6 BMA 2   510  1486 BMA BMA A . 
M  5 MAN 3   511  1487 MAN MAN A . 
N  4 NAG 4   512  1495 NAG NAG A . 
O  5 MAN 1   508  1484 MAN MAN A . 
P  5 MAN 1   509  1485 MAN MAN A . 
Q  4 NAG 1   513  1481 NAG NAG A . 
R  5 MAN 1   514  1485 MAN MAN A . 
S  4 NAG 1   515  1488 NAG NAG A . 
T  4 NAG 2   516  1489 NAG NAG A . 
U  6 BMA 3   517  1490 BMA BMA A . 
V  5 MAN 4   518  1491 MAN MAN A . 
W  5 MAN 5   519  1492 MAN MAN A . 
X  5 MAN 6   520  1493 MAN MAN A . 
Y  5 MAN 1   521  1494 MAN MAN A . 
Z  2 CA  1   501  1477 CA  CA  B . 
AA 3 GOL 1   502  1478 GOL GOL B . 
BA 4 NAG 1   503  1479 NAG NAG B . 
CA 4 NAG 1   504  1480 NAG NAG B . 
DA 5 MAN 1   505  1483 MAN MAN B . 
EA 6 BMA 2   507  1486 BMA BMA B . 
FA 4 NAG 3   508  1487 NAG NAG B . 
GA 5 MAN 1   506  1484 MAN MAN B . 
HA 5 MAN 1   509  1485 MAN MAN B . 
IA 4 NAG 1   501  1482 NAG NAG C . 
JA 2 CA  1   502  1477 CA  CA  C . 
KA 7 PEG 1   503  1478 PEG PEG C . 
LA 3 GOL 1   504  1479 GOL GOL C . 
MA 4 NAG 1   505  1480 NAG NAG C . 
NA 4 NAG 1   506  1481 NAG NAG C . 
OA 4 NAG 1   507  1483 NAG NAG C . 
PA 4 NAG 2   508  1484 NAG NAG C . 
QA 4 NAG 1   501  1482 NAG NAG D . 
RA 6 BMA 1   502  1486 BMA BMA D . 
SA 5 MAN 2   503  1487 MAN MAN D . 
TA 2 CA  1   504  1477 CA  CA  D . 
UA 3 GOL 1   505  1478 GOL GOL D . 
VA 4 NAG 1   506  1479 NAG NAG D . 
WA 4 NAG 1   507  1480 NAG NAG D . 
XA 4 NAG 1   508  1481 NAG NAG D . 
YA 5 MAN 1   509  1483 MAN MAN D . 
ZA 8 HOH 1   2301 2301 HOH HOH A . 
ZA 8 HOH 2   2302 2215 HOH HOH A . 
ZA 8 HOH 3   2303 2363 HOH HOH A . 
ZA 8 HOH 4   2304 2231 HOH HOH A . 
ZA 8 HOH 5   2305 2425 HOH HOH A . 
ZA 8 HOH 6   2306 2324 HOH HOH A . 
ZA 8 HOH 7   2307 2292 HOH HOH A . 
ZA 8 HOH 8   2308 2452 HOH HOH A . 
ZA 8 HOH 9   2309 2395 HOH HOH A . 
ZA 8 HOH 10  2310 2437 HOH HOH A . 
ZA 8 HOH 11  2311 2426 HOH HOH A . 
ZA 8 HOH 12  2312 2020 HOH HOH A . 
ZA 8 HOH 13  2313 2005 HOH HOH A . 
ZA 8 HOH 14  2314 2151 HOH HOH A . 
ZA 8 HOH 15  2315 2033 HOH HOH A . 
ZA 8 HOH 16  2316 2314 HOH HOH A . 
ZA 8 HOH 17  2317 2298 HOH HOH A . 
ZA 8 HOH 18  2318 2195 HOH HOH A . 
ZA 8 HOH 19  2319 2060 HOH HOH A . 
ZA 8 HOH 20  2320 2190 HOH HOH A . 
ZA 8 HOH 21  2321 2449 HOH HOH A . 
ZA 8 HOH 22  2322 2152 HOH HOH A . 
ZA 8 HOH 23  2323 2319 HOH HOH A . 
ZA 8 HOH 24  2324 2117 HOH HOH A . 
ZA 8 HOH 25  2325 2047 HOH HOH A . 
ZA 8 HOH 26  2326 2235 HOH HOH A . 
ZA 8 HOH 27  2327 2313 HOH HOH A . 
ZA 8 HOH 28  2328 2284 HOH HOH A . 
ZA 8 HOH 29  2329 2034 HOH HOH A . 
ZA 8 HOH 30  2330 2120 HOH HOH A . 
ZA 8 HOH 31  2331 2309 HOH HOH A . 
ZA 8 HOH 32  2332 2308 HOH HOH A . 
ZA 8 HOH 33  2333 2416 HOH HOH A . 
ZA 8 HOH 34  2334 2287 HOH HOH A . 
ZA 8 HOH 35  2335 2443 HOH HOH A . 
ZA 8 HOH 36  2336 2291 HOH HOH A . 
ZA 8 HOH 37  2337 2043 HOH HOH A . 
ZA 8 HOH 38  2338 2022 HOH HOH A . 
ZA 8 HOH 39  2339 2018 HOH HOH A . 
ZA 8 HOH 40  2340 2425 HOH HOH A . 
ZA 8 HOH 41  2341 2424 HOH HOH A . 
ZA 8 HOH 42  2342 2279 HOH HOH A . 
ZA 8 HOH 43  2343 2338 HOH HOH A . 
ZA 8 HOH 44  2344 2076 HOH HOH A . 
ZA 8 HOH 45  2345 2448 HOH HOH A . 
ZA 8 HOH 46  2346 2102 HOH HOH A . 
ZA 8 HOH 47  2347 2346 HOH HOH A . 
ZA 8 HOH 48  2348 2344 HOH HOH A . 
ZA 8 HOH 49  2349 2124 HOH HOH A . 
ZA 8 HOH 50  2350 2123 HOH HOH A . 
ZA 8 HOH 51  2351 2040 HOH HOH A . 
ZA 8 HOH 52  2352 2162 HOH HOH A . 
ZA 8 HOH 53  2353 2342 HOH HOH A . 
ZA 8 HOH 54  2354 2196 HOH HOH A . 
ZA 8 HOH 55  2355 2039 HOH HOH A . 
ZA 8 HOH 56  2356 2100 HOH HOH A . 
ZA 8 HOH 57  2357 2347 HOH HOH A . 
ZA 8 HOH 58  2358 2294 HOH HOH A . 
ZA 8 HOH 59  2359 2377 HOH HOH A . 
ZA 8 HOH 60  2360 2442 HOH HOH A . 
ZA 8 HOH 61  2361 2138 HOH HOH A . 
ZA 8 HOH 62  2362 2343 HOH HOH A . 
ZA 8 HOH 63  2363 2244 HOH HOH A . 
ZA 8 HOH 64  2364 2267 HOH HOH A . 
ZA 8 HOH 65  2365 2270 HOH HOH A . 
ZA 8 HOH 66  2366 2203 HOH HOH A . 
ZA 8 HOH 67  2367 2194 HOH HOH A . 
ZA 8 HOH 68  2368 2212 HOH HOH A . 
ZA 8 HOH 69  2369 2068 HOH HOH A . 
ZA 8 HOH 70  2370 2013 HOH HOH A . 
ZA 8 HOH 71  2371 2422 HOH HOH A . 
ZA 8 HOH 72  2372 2332 HOH HOH A . 
ZA 8 HOH 73  2373 2224 HOH HOH A . 
ZA 8 HOH 74  2374 2380 HOH HOH A . 
ZA 8 HOH 75  2375 2182 HOH HOH A . 
ZA 8 HOH 76  2376 2336 HOH HOH A . 
ZA 8 HOH 77  2377 2312 HOH HOH A . 
ZA 8 HOH 78  2378 2288 HOH HOH A . 
ZA 8 HOH 79  2379 2101 HOH HOH A . 
ZA 8 HOH 80  2380 2257 HOH HOH A . 
ZA 8 HOH 81  2381 2021 HOH HOH A . 
ZA 8 HOH 82  2382 2368 HOH HOH A . 
ZA 8 HOH 83  2383 2002 HOH HOH A . 
ZA 8 HOH 84  2384 2289 HOH HOH A . 
ZA 8 HOH 85  2385 2079 HOH HOH A . 
ZA 8 HOH 86  2386 2008 HOH HOH A . 
ZA 8 HOH 87  2387 2435 HOH HOH A . 
ZA 8 HOH 88  2388 2219 HOH HOH A . 
ZA 8 HOH 89  2389 2413 HOH HOH A . 
ZA 8 HOH 90  2390 2350 HOH HOH A . 
ZA 8 HOH 91  2391 2401 HOH HOH A . 
ZA 8 HOH 92  2392 2265 HOH HOH A . 
ZA 8 HOH 93  2393 2046 HOH HOH A . 
ZA 8 HOH 94  2394 2382 HOH HOH A . 
ZA 8 HOH 95  2395 2172 HOH HOH A . 
ZA 8 HOH 96  2396 2067 HOH HOH A . 
ZA 8 HOH 97  2397 2361 HOH HOH A . 
ZA 8 HOH 98  2398 2159 HOH HOH A . 
ZA 8 HOH 99  2399 2137 HOH HOH A . 
ZA 8 HOH 100 2400 2264 HOH HOH A . 
ZA 8 HOH 101 2401 2001 HOH HOH A . 
ZA 8 HOH 102 2402 2276 HOH HOH A . 
ZA 8 HOH 103 2403 2373 HOH HOH A . 
ZA 8 HOH 104 2404 2233 HOH HOH A . 
ZA 8 HOH 105 2405 2266 HOH HOH A . 
ZA 8 HOH 106 2406 2026 HOH HOH A . 
ZA 8 HOH 107 2407 2410 HOH HOH A . 
ZA 8 HOH 108 2408 2409 HOH HOH A . 
ZA 8 HOH 109 2409 2432 HOH HOH A . 
ZA 8 HOH 110 2410 2011 HOH HOH A . 
ZA 8 HOH 111 2411 2403 HOH HOH A . 
ZA 8 HOH 112 2412 2337 HOH HOH A . 
ZA 8 HOH 113 2413 2113 HOH HOH A . 
ZA 8 HOH 114 2414 2436 HOH HOH A . 
ZA 8 HOH 115 2415 2110 HOH HOH A . 
ZA 8 HOH 116 2416 2407 HOH HOH A . 
ZA 8 HOH 117 2417 2019 HOH HOH A . 
ZA 8 HOH 118 2418 2400 HOH HOH A . 
ZA 8 HOH 119 2419 2303 HOH HOH A . 
ZA 8 HOH 120 2420 2271 HOH HOH A . 
ZA 8 HOH 121 2421 2441 HOH HOH A . 
ZA 8 HOH 122 2422 2149 HOH HOH A . 
ZA 8 HOH 123 2423 2214 HOH HOH A . 
ZA 8 HOH 124 2424 2191 HOH HOH A . 
ZA 8 HOH 125 2425 2112 HOH HOH A . 
ZA 8 HOH 126 2426 2012 HOH HOH A . 
ZA 8 HOH 127 2427 2273 HOH HOH A . 
ZA 8 HOH 128 2428 2316 HOH HOH A . 
ZA 8 HOH 129 2429 2331 HOH HOH A . 
ZA 8 HOH 130 2430 2402 HOH HOH A . 
ZA 8 HOH 131 2431 2307 HOH HOH A . 
ZA 8 HOH 132 2432 2121 HOH HOH A . 
ZA 8 HOH 133 2433 2156 HOH HOH A . 
ZA 8 HOH 134 2434 2349 HOH HOH A . 
ZA 8 HOH 135 2435 2223 HOH HOH A . 
ZA 8 HOH 136 2436 2045 HOH HOH A . 
ZA 8 HOH 137 2437 2283 HOH HOH A . 
ZA 8 HOH 138 2438 2398 HOH HOH A . 
ZA 8 HOH 139 2439 2384 HOH HOH A . 
ZA 8 HOH 140 2440 2210 HOH HOH A . 
ZA 8 HOH 141 2441 2310 HOH HOH A . 
ZA 8 HOH 142 2442 2397 HOH HOH A . 
ZA 8 HOH 143 2443 2199 HOH HOH A . 
ZA 8 HOH 144 2444 2071 HOH HOH A . 
ZA 8 HOH 145 2445 2105 HOH HOH A . 
ZA 8 HOH 146 2446 2352 HOH HOH A . 
ZA 8 HOH 147 2447 2227 HOH HOH A . 
ZA 8 HOH 148 2448 2095 HOH HOH A . 
ZA 8 HOH 149 2449 2188 HOH HOH A . 
ZA 8 HOH 150 2450 2394 HOH HOH A . 
ZA 8 HOH 151 2451 2340 HOH HOH A . 
ZA 8 HOH 152 2452 2234 HOH HOH A . 
ZA 8 HOH 153 2453 2080 HOH HOH A . 
ZA 8 HOH 154 2454 2063 HOH HOH A . 
ZA 8 HOH 155 2455 2354 HOH HOH A . 
ZA 8 HOH 156 2456 2249 HOH HOH A . 
ZA 8 HOH 157 2457 2254 HOH HOH A . 
ZA 8 HOH 158 2458 2069 HOH HOH A . 
ZA 8 HOH 159 2459 2083 HOH HOH A . 
ZA 8 HOH 160 2460 2218 HOH HOH A . 
ZA 8 HOH 161 2461 2417 HOH HOH A . 
ZA 8 HOH 162 2462 2169 HOH HOH A . 
ZA 8 HOH 163 2463 2428 HOH HOH A . 
ZA 8 HOH 164 2464 2278 HOH HOH A . 
ZA 8 HOH 165 2465 2375 HOH HOH A . 
ZA 8 HOH 166 2466 2262 HOH HOH A . 
ZA 8 HOH 167 2467 2037 HOH HOH A . 
ZA 8 HOH 168 2468 2386 HOH HOH A . 
ZA 8 HOH 169 2469 2094 HOH HOH A . 
ZA 8 HOH 170 2470 2334 HOH HOH A . 
ZA 8 HOH 171 2471 2393 HOH HOH A . 
ZA 8 HOH 172 2472 2228 HOH HOH A . 
ZA 8 HOH 173 2473 2142 HOH HOH A . 
ZA 8 HOH 174 2474 2178 HOH HOH A . 
ZA 8 HOH 175 2475 2277 HOH HOH A . 
ZA 8 HOH 176 2476 2438 HOH HOH A . 
ZA 8 HOH 177 2477 2366 HOH HOH A . 
ZA 8 HOH 178 2478 2106 HOH HOH A . 
ZA 8 HOH 179 2479 2445 HOH HOH A . 
ZA 8 HOH 180 2480 2144 HOH HOH A . 
ZA 8 HOH 181 2481 2317 HOH HOH A . 
ZA 8 HOH 182 2482 2240 HOH HOH A . 
ZA 8 HOH 183 2483 2450 HOH HOH A . 
ZA 8 HOH 184 2484 2345 HOH HOH A . 
ZA 8 HOH 185 2485 2081 HOH HOH A . 
ZA 8 HOH 186 2486 2128 HOH HOH A . 
ZA 8 HOH 187 2487 2339 HOH HOH A . 
ZA 8 HOH 188 2488 2131 HOH HOH A . 
ZA 8 HOH 189 2489 2450 HOH HOH A . 
ZA 8 HOH 190 2490 2115 HOH HOH A . 
ZA 8 HOH 191 2491 2282 HOH HOH A . 
ZA 8 HOH 192 2492 2269 HOH HOH A . 
ZA 8 HOH 193 2493 2211 HOH HOH A . 
ZA 8 HOH 194 2494 2302 HOH HOH A . 
ZA 8 HOH 195 2495 2268 HOH HOH A . 
ZA 8 HOH 196 2496 2236 HOH HOH A . 
ZA 8 HOH 197 2497 2245 HOH HOH A . 
ZA 8 HOH 198 2498 2372 HOH HOH A . 
ZA 8 HOH 199 2499 2296 HOH HOH A . 
ZA 8 HOH 200 2500 2290 HOH HOH A . 
ZA 8 HOH 201 2501 2414 HOH HOH A . 
ZA 8 HOH 202 2502 2126 HOH HOH A . 
ZA 8 HOH 203 2503 2184 HOH HOH A . 
ZA 8 HOH 204 2504 2010 HOH HOH A . 
ZA 8 HOH 205 2505 2369 HOH HOH A . 
ZA 8 HOH 206 2506 2238 HOH HOH A . 
ZA 8 HOH 207 2507 2127 HOH HOH A . 
ZA 8 HOH 208 2508 2322 HOH HOH A . 
ZA 8 HOH 209 2509 2434 HOH HOH A . 
ZA 8 HOH 210 2510 2297 HOH HOH A . 
ZA 8 HOH 211 2511 2197 HOH HOH A . 
ZA 8 HOH 212 2512 2139 HOH HOH A . 
ZA 8 HOH 213 2513 2243 HOH HOH A . 
ZA 8 HOH 214 2514 2259 HOH HOH A . 
ZA 8 HOH 215 2515 2330 HOH HOH A . 
ZA 8 HOH 216 2516 2383 HOH HOH A . 
ZA 8 HOH 217 2517 2048 HOH HOH A . 
ZA 8 HOH 218 2518 2109 HOH HOH A . 
ZA 8 HOH 219 2519 2306 HOH HOH A . 
ZA 8 HOH 220 2520 2016 HOH HOH A . 
ZA 8 HOH 221 2521 2241 HOH HOH A . 
ZA 8 HOH 222 2522 2355 HOH HOH A . 
ZA 8 HOH 223 2523 2119 HOH HOH A . 
ZA 8 HOH 224 2524 2096 HOH HOH A . 
ZA 8 HOH 225 2525 2204 HOH HOH A . 
ZA 8 HOH 226 2526 2025 HOH HOH A . 
ZA 8 HOH 227 2527 2399 HOH HOH A . 
ZA 8 HOH 228 2528 2315 HOH HOH A . 
ZA 8 HOH 229 2529 2323 HOH HOH A . 
ZA 8 HOH 230 2530 2251 HOH HOH A . 
ZA 8 HOH 231 2531 2216 HOH HOH A . 
ZA 8 HOH 232 2532 2446 HOH HOH A . 
ZA 8 HOH 233 2533 2444 HOH HOH A . 
ZA 8 HOH 234 2534 2229 HOH HOH A . 
ZA 8 HOH 235 2535 2258 HOH HOH A . 
ZA 8 HOH 236 2536 2325 HOH HOH A . 
ZA 8 HOH 237 2537 2041 HOH HOH A . 
ZA 8 HOH 238 2538 2385 HOH HOH A . 
ZA 8 HOH 239 2539 2423 HOH HOH A . 
ZA 8 HOH 240 2540 2304 HOH HOH A . 
ZA 8 HOH 241 2541 2418 HOH HOH A . 
ZA 8 HOH 242 2542 2378 HOH HOH A . 
ZA 8 HOH 243 2543 2168 HOH HOH A . 
ZA 8 HOH 244 2544 2009 HOH HOH A . 
ZA 8 HOH 245 2545 2017 HOH HOH A . 
ZA 8 HOH 246 2546 2326 HOH HOH A . 
ZA 8 HOH 247 2547 2052 HOH HOH A . 
ZA 8 HOH 248 2548 2077 HOH HOH A . 
ZA 8 HOH 249 2549 2237 HOH HOH A . 
ZA 8 HOH 250 2550 2006 HOH HOH A . 
ZA 8 HOH 251 2551 2024 HOH HOH A . 
ZA 8 HOH 252 2552 2007 HOH HOH A . 
ZA 8 HOH 253 2553 2429 HOH HOH A . 
ZA 8 HOH 254 2554 2051 HOH HOH A . 
ZA 8 HOH 255 2555 2371 HOH HOH A . 
ZA 8 HOH 256 2556 2038 HOH HOH A . 
ZA 8 HOH 257 2557 2274 HOH HOH A . 
ZA 8 HOH 258 2558 2247 HOH HOH A . 
ZA 8 HOH 259 2559 2275 HOH HOH A . 
ZA 8 HOH 260 2560 2220 HOH HOH A . 
ZA 8 HOH 261 2561 2365 HOH HOH A . 
ZA 8 HOH 262 2562 2225 HOH HOH A . 
ZA 8 HOH 263 2563 2353 HOH HOH A . 
ZA 8 HOH 264 2564 2082 HOH HOH A . 
ZA 8 HOH 265 2565 2295 HOH HOH A . 
ZA 8 HOH 266 2566 2252 HOH HOH A . 
ZA 8 HOH 267 2567 2157 HOH HOH A . 
ZA 8 HOH 268 2568 2232 HOH HOH A . 
ZA 8 HOH 269 2569 2222 HOH HOH A . 
ZA 8 HOH 270 2570 2023 HOH HOH A . 
ZA 8 HOH 271 2571 2003 HOH HOH A . 
ZA 8 HOH 272 2572 2420 HOH HOH A . 
ZA 8 HOH 273 2573 2359 HOH HOH A . 
ZA 8 HOH 274 2574 2255 HOH HOH A . 
ZA 8 HOH 275 2575 2440 HOH HOH A . 
ZA 8 HOH 276 2576 2092 HOH HOH A . 
ZA 8 HOH 277 2577 2405 HOH HOH A . 
ZA 8 HOH 278 2578 2392 HOH HOH A . 
ZA 8 HOH 279 2579 2328 HOH HOH A . 
ZA 8 HOH 280 2580 2356 HOH HOH A . 
ZA 8 HOH 281 2581 2318 HOH HOH A . 
ZA 8 HOH 282 2582 2004 HOH HOH A . 
ZA 8 HOH 283 2583 2321 HOH HOH A . 
ZA 8 HOH 284 2584 2280 HOH HOH A . 
ZA 8 HOH 285 2585 2221 HOH HOH A . 
ZA 8 HOH 286 2586 2293 HOH HOH A . 
ZA 8 HOH 287 2587 2208 HOH HOH A . 
ZA 8 HOH 288 2588 2299 HOH HOH A . 
ZA 8 HOH 289 2589 2030 HOH HOH A . 
ZA 8 HOH 290 2590 2014 HOH HOH A . 
ZA 8 HOH 291 2591 2449 HOH HOH A . 
ZA 8 HOH 292 2592 2448 HOH HOH A . 
ZA 8 HOH 293 2593 2032 HOH HOH A . 
ZA 8 HOH 294 2594 2158 HOH HOH A . 
ZA 8 HOH 295 2595 2205 HOH HOH A . 
ZA 8 HOH 296 2596 2272 HOH HOH A . 
ZA 8 HOH 297 2597 2387 HOH HOH A . 
ZA 8 HOH 298 2598 2389 HOH HOH A . 
ZA 8 HOH 299 2599 2451 HOH HOH A . 
ZA 8 HOH 300 2600 2333 HOH HOH A . 
ZA 8 HOH 301 2601 2104 HOH HOH A . 
ZA 8 HOH 302 2602 2329 HOH HOH A . 
ZA 8 HOH 303 2603 2090 HOH HOH A . 
ZA 8 HOH 304 2604 2453 HOH HOH A . 
ZA 8 HOH 305 2605 2256 HOH HOH A . 
ZA 8 HOH 306 2606 2396 HOH HOH A . 
ZA 8 HOH 307 2607 2421 HOH HOH A . 
ZA 8 HOH 308 2608 2411 HOH HOH A . 
ZA 8 HOH 309 2609 2226 HOH HOH A . 
ZA 8 HOH 310 2610 2431 HOH HOH A . 
ZA 8 HOH 311 2611 2167 HOH HOH A . 
ZA 8 HOH 312 2612 2179 HOH HOH A . 
ZA 8 HOH 313 2613 2286 HOH HOH A . 
ZA 8 HOH 314 2614 2150 HOH HOH A . 
ZA 8 HOH 315 2615 2084 HOH HOH A . 
ZA 8 HOH 316 2616 2050 HOH HOH A . 
ZA 8 HOH 317 2617 2427 HOH HOH A . 
ZA 8 HOH 318 2618 2136 HOH HOH A . 
ZA 8 HOH 319 2619 2134 HOH HOH A . 
ZA 8 HOH 320 2620 2348 HOH HOH A . 
ZA 8 HOH 321 2621 2091 HOH HOH A . 
ZA 8 HOH 322 2622 2015 HOH HOH A . 
ZA 8 HOH 323 2623 2074 HOH HOH A . 
ZA 8 HOH 324 2624 2406 HOH HOH A . 
ZA 8 HOH 325 2625 2439 HOH HOH A . 
ZA 8 HOH 326 2626 2351 HOH HOH A . 
ZA 8 HOH 327 2627 2143 HOH HOH A . 
ZA 8 HOH 328 2628 2183 HOH HOH A . 
ZA 8 HOH 329 2629 2412 HOH HOH A . 
ZA 8 HOH 330 2630 2253 HOH HOH A . 
ZA 8 HOH 331 2631 2281 HOH HOH A . 
ZA 8 HOH 332 2632 2367 HOH HOH A . 
ZA 8 HOH 333 2633 2358 HOH HOH A . 
ZA 8 HOH 334 2634 2148 HOH HOH A . 
ZA 8 HOH 335 2635 2370 HOH HOH A . 
ZA 8 HOH 336 2636 2239 HOH HOH A . 
ZA 8 HOH 337 2637 2376 HOH HOH A . 
ZA 8 HOH 338 2638 2160 HOH HOH A . 
ZA 8 HOH 339 2639 2242 HOH HOH A . 
ZA 8 HOH 340 2640 2261 HOH HOH A . 
ZA 8 HOH 341 2641 2070 HOH HOH A . 
ZA 8 HOH 342 2642 2390 HOH HOH A . 
ZA 8 HOH 343 2643 2404 HOH HOH A . 
ZA 8 HOH 344 2644 2433 HOH HOH A . 
ZA 8 HOH 345 2645 2263 HOH HOH A . 
ZA 8 HOH 346 2646 2447 HOH HOH A . 
ZA 8 HOH 347 2647 2285 HOH HOH A . 
ZA 8 HOH 348 2648 2408 HOH HOH A . 
ZA 8 HOH 349 2649 2311 HOH HOH A . 
ZA 8 HOH 350 2650 2180 HOH HOH A . 
ZA 8 HOH 351 2651 2213 HOH HOH A . 
ZA 8 HOH 352 2652 2424 HOH HOH A . 
ZA 8 HOH 353 2653 2250 HOH HOH A . 
ZA 8 HOH 354 2654 2177 HOH HOH A . 
ZA 8 HOH 355 2655 2360 HOH HOH A . 
ZA 8 HOH 356 2656 2388 HOH HOH A . 
ZA 8 HOH 357 2657 2335 HOH HOH A . 
ZA 8 HOH 358 2658 2357 HOH HOH A . 
ZA 8 HOH 359 2659 2430 HOH HOH A . 
ZA 8 HOH 360 2660 2364 HOH HOH A . 
ZA 8 HOH 361 2661 2185 HOH HOH A . 
ZA 8 HOH 362 2662 2327 HOH HOH A . 
ZA 8 HOH 363 2663 2362 HOH HOH A . 
ZA 8 HOH 364 2664 2374 HOH HOH A . 
ZA 8 HOH 365 2665 2391 HOH HOH A . 
ZA 8 HOH 366 2666 2145 HOH HOH A . 
ZA 8 HOH 367 2667 2166 HOH HOH A . 
ZA 8 HOH 368 2668 2381 HOH HOH A . 
ZA 8 HOH 369 2669 2103 HOH HOH A . 
ZA 8 HOH 370 2670 2305 HOH HOH A . 
ZA 8 HOH 371 2671 2118 HOH HOH A . 
ZA 8 HOH 372 2672 2072 HOH HOH A . 
ZA 8 HOH 373 2673 2093 HOH HOH A . 
ZA 8 HOH 374 2674 2379 HOH HOH A . 
ZA 8 HOH 375 2675 2146 HOH HOH A . 
ZA 8 HOH 376 2676 2217 HOH HOH A . 
ZA 8 HOH 377 2677 2320 HOH HOH A . 
ZA 8 HOH 378 2678 2260 HOH HOH A . 
ZA 8 HOH 379 2679 2248 HOH HOH A . 
ZA 8 HOH 380 2680 2300 HOH HOH A . 
ZA 8 HOH 381 2681 2246 HOH HOH A . 
ZA 8 HOH 382 2682 2133 HOH HOH A . 
ZA 8 HOH 383 2683 2341 HOH HOH A . 
ZA 8 HOH 384 2684 2230 HOH HOH A . 
ZA 8 HOH 385 2685 2415 HOH HOH A . 
ZA 8 HOH 386 2686 2130 HOH HOH A . 
ZA 8 HOH 387 2687 2201 HOH HOH A . 
ZA 8 HOH 388 2688 2154 HOH HOH A . 
ZA 8 HOH 389 2689 2065 HOH HOH A . 
ZA 8 HOH 390 2690 2162 HOH HOH A . 
ZA 8 HOH 391 2691 2181 HOH HOH A . 
ZA 8 HOH 392 2692 2114 HOH HOH A . 
ZA 8 HOH 393 2693 2198 HOH HOH A . 
ZA 8 HOH 394 2694 2073 HOH HOH A . 
ZA 8 HOH 395 2695 2176 HOH HOH A . 
ZA 8 HOH 396 2696 2135 HOH HOH A . 
ZA 8 HOH 397 2697 2088 HOH HOH A . 
ZA 8 HOH 398 2698 2075 HOH HOH A . 
ZA 8 HOH 399 2699 2086 HOH HOH A . 
ZA 8 HOH 400 2700 2061 HOH HOH A . 
ZA 8 HOH 401 2701 2419 HOH HOH A . 
ZA 8 HOH 402 2702 2089 HOH HOH A . 
ZA 8 HOH 403 2703 2130 HOH HOH A . 
ZA 8 HOH 404 2704 2171 HOH HOH A . 
ZA 8 HOH 405 2705 2155 HOH HOH A . 
ZA 8 HOH 406 2706 2141 HOH HOH A . 
ZA 8 HOH 407 2707 2087 HOH HOH A . 
ZA 8 HOH 408 2708 2173 HOH HOH A . 
ZA 8 HOH 409 2709 2153 HOH HOH A . 
ZA 8 HOH 410 2710 2140 HOH HOH A . 
ZA 8 HOH 411 2711 2163 HOH HOH A . 
ZA 8 HOH 412 2712 2165 HOH HOH A . 
ZA 8 HOH 413 2713 2170 HOH HOH A . 
ZA 8 HOH 414 2714 2056 HOH HOH A . 
ZA 8 HOH 415 2715 2042 HOH HOH A . 
ZA 8 HOH 416 2716 2122 HOH HOH A . 
ZA 8 HOH 417 2717 2059 HOH HOH A . 
ZA 8 HOH 418 2718 2111 HOH HOH A . 
ZA 8 HOH 419 2719 2055 HOH HOH A . 
ZA 8 HOH 420 2720 2175 HOH HOH A . 
ZA 8 HOH 421 2721 2125 HOH HOH A . 
ZA 8 HOH 422 2722 2060 HOH HOH A . 
ZA 8 HOH 423 2723 2028 HOH HOH A . 
ZA 8 HOH 424 2724 2193 HOH HOH A . 
ZA 8 HOH 425 2725 2088 HOH HOH A . 
ZA 8 HOH 426 2726 2116 HOH HOH A . 
ZA 8 HOH 427 2727 2086 HOH HOH A . 
ZA 8 HOH 428 2728 2186 HOH HOH A . 
ZA 8 HOH 429 2729 2174 HOH HOH A . 
ZA 8 HOH 430 2730 2176 HOH HOH A . 
ZA 8 HOH 431 2731 2027 HOH HOH A . 
ZA 8 HOH 432 2732 2035 HOH HOH A . 
ZA 8 HOH 433 2733 2066 HOH HOH A . 
ZA 8 HOH 434 2734 2057 HOH HOH A . 
ZA 8 HOH 435 2735 2146 HOH HOH A . 
ZA 8 HOH 436 2736 2062 HOH HOH A . 
ZA 8 HOH 437 2737 2061 HOH HOH A . 
ZA 8 HOH 438 2738 2058 HOH HOH A . 
ZA 8 HOH 439 2739 2189 HOH HOH A . 
ZA 8 HOH 440 2740 2132 HOH HOH A . 
ZA 8 HOH 441 2741 2192 HOH HOH A . 
ZA 8 HOH 442 2742 2044 HOH HOH A . 
ZA 8 HOH 443 2743 2200 HOH HOH A . 
ZA 8 HOH 444 2744 2078 HOH HOH A . 
ZA 8 HOH 445 2745 2064 HOH HOH A . 
ZA 8 HOH 446 2746 2031 HOH HOH A . 
ZA 8 HOH 447 2747 2207 HOH HOH A . 
ZA 8 HOH 448 2748 2029 HOH HOH A . 
ZA 8 HOH 449 2749 2202 HOH HOH A . 
ZA 8 HOH 450 2750 2108 HOH HOH A . 
ZA 8 HOH 451 2751 2147 HOH HOH A . 
ZA 8 HOH 452 2752 2085 HOH HOH A . 
ZA 8 HOH 453 2753 2053 HOH HOH A . 
ZA 8 HOH 454 2754 2209 HOH HOH A . 
ZA 8 HOH 455 2755 2098 HOH HOH A . 
ZA 8 HOH 456 2756 2164 HOH HOH A . 
ZA 8 HOH 457 2757 2206 HOH HOH A . 
ZA 8 HOH 458 2758 2187 HOH HOH A . 
ZA 8 HOH 459 2759 2049 HOH HOH A . 
ZA 8 HOH 460 2760 2054 HOH HOH A . 
AB 8 HOH 1   601  2202 HOH HOH B . 
AB 8 HOH 2   602  2402 HOH HOH B . 
AB 8 HOH 3   603  2386 HOH HOH B . 
AB 8 HOH 4   604  2286 HOH HOH B . 
AB 8 HOH 5   605  2223 HOH HOH B . 
AB 8 HOH 6   606  2297 HOH HOH B . 
AB 8 HOH 7   607  2391 HOH HOH B . 
AB 8 HOH 8   608  2370 HOH HOH B . 
AB 8 HOH 9   609  2307 HOH HOH B . 
AB 8 HOH 10  610  2327 HOH HOH B . 
AB 8 HOH 11  611  2280 HOH HOH B . 
AB 8 HOH 12  612  2095 HOH HOH B . 
AB 8 HOH 13  613  2415 HOH HOH B . 
AB 8 HOH 14  614  2016 HOH HOH B . 
AB 8 HOH 15  615  2146 HOH HOH B . 
AB 8 HOH 16  616  2253 HOH HOH B . 
AB 8 HOH 17  617  2273 HOH HOH B . 
AB 8 HOH 18  618  2354 HOH HOH B . 
AB 8 HOH 19  619  2044 HOH HOH B . 
AB 8 HOH 20  620  2065 HOH HOH B . 
AB 8 HOH 21  621  2114 HOH HOH B . 
AB 8 HOH 22  622  2303 HOH HOH B . 
AB 8 HOH 23  623  2413 HOH HOH B . 
AB 8 HOH 24  624  2034 HOH HOH B . 
AB 8 HOH 25  625  2182 HOH HOH B . 
AB 8 HOH 26  626  2427 HOH HOH B . 
AB 8 HOH 27  627  2058 HOH HOH B . 
AB 8 HOH 28  628  2259 HOH HOH B . 
AB 8 HOH 29  629  2376 HOH HOH B . 
AB 8 HOH 30  630  2192 HOH HOH B . 
AB 8 HOH 31  631  2071 HOH HOH B . 
AB 8 HOH 32  632  2040 HOH HOH B . 
AB 8 HOH 33  633  2161 HOH HOH B . 
AB 8 HOH 34  634  2133 HOH HOH B . 
AB 8 HOH 35  635  2319 HOH HOH B . 
AB 8 HOH 36  636  2183 HOH HOH B . 
AB 8 HOH 37  637  2031 HOH HOH B . 
AB 8 HOH 38  638  2096 HOH HOH B . 
AB 8 HOH 39  639  2011 HOH HOH B . 
AB 8 HOH 40  640  2254 HOH HOH B . 
AB 8 HOH 41  641  2181 HOH HOH B . 
AB 8 HOH 42  642  2270 HOH HOH B . 
AB 8 HOH 43  643  2009 HOH HOH B . 
AB 8 HOH 44  644  2115 HOH HOH B . 
AB 8 HOH 45  645  2014 HOH HOH B . 
AB 8 HOH 46  646  2305 HOH HOH B . 
AB 8 HOH 47  647  2320 HOH HOH B . 
AB 8 HOH 48  648  2431 HOH HOH B . 
AB 8 HOH 49  649  2419 HOH HOH B . 
AB 8 HOH 50  650  2239 HOH HOH B . 
AB 8 HOH 51  651  2030 HOH HOH B . 
AB 8 HOH 52  652  2018 HOH HOH B . 
AB 8 HOH 53  653  2257 HOH HOH B . 
AB 8 HOH 54  654  2073 HOH HOH B . 
AB 8 HOH 55  655  2079 HOH HOH B . 
AB 8 HOH 56  656  2429 HOH HOH B . 
AB 8 HOH 57  657  2277 HOH HOH B . 
AB 8 HOH 58  658  2279 HOH HOH B . 
AB 8 HOH 59  659  2410 HOH HOH B . 
AB 8 HOH 60  660  2337 HOH HOH B . 
AB 8 HOH 61  661  2289 HOH HOH B . 
AB 8 HOH 62  662  2324 HOH HOH B . 
AB 8 HOH 63  663  2381 HOH HOH B . 
AB 8 HOH 64  664  2166 HOH HOH B . 
AB 8 HOH 65  665  2362 HOH HOH B . 
AB 8 HOH 66  666  2226 HOH HOH B . 
AB 8 HOH 67  667  2302 HOH HOH B . 
AB 8 HOH 68  668  2269 HOH HOH B . 
AB 8 HOH 69  669  2214 HOH HOH B . 
AB 8 HOH 70  670  2225 HOH HOH B . 
AB 8 HOH 71  671  2017 HOH HOH B . 
AB 8 HOH 72  672  2380 HOH HOH B . 
AB 8 HOH 73  673  2361 HOH HOH B . 
AB 8 HOH 74  674  2304 HOH HOH B . 
AB 8 HOH 75  675  2015 HOH HOH B . 
AB 8 HOH 76  676  2372 HOH HOH B . 
AB 8 HOH 77  677  2154 HOH HOH B . 
AB 8 HOH 78  678  2401 HOH HOH B . 
AB 8 HOH 79  679  2267 HOH HOH B . 
AB 8 HOH 80  680  2374 HOH HOH B . 
AB 8 HOH 81  681  2222 HOH HOH B . 
AB 8 HOH 82  682  2321 HOH HOH B . 
AB 8 HOH 83  683  2098 HOH HOH B . 
AB 8 HOH 84  684  2112 HOH HOH B . 
AB 8 HOH 85  685  2064 HOH HOH B . 
AB 8 HOH 86  686  2158 HOH HOH B . 
AB 8 HOH 87  687  2200 HOH HOH B . 
AB 8 HOH 88  688  2055 HOH HOH B . 
AB 8 HOH 89  689  2229 HOH HOH B . 
AB 8 HOH 90  690  2263 HOH HOH B . 
AB 8 HOH 91  691  2036 HOH HOH B . 
AB 8 HOH 92  692  2201 HOH HOH B . 
AB 8 HOH 93  693  2295 HOH HOH B . 
AB 8 HOH 94  694  2350 HOH HOH B . 
AB 8 HOH 95  695  2390 HOH HOH B . 
AB 8 HOH 96  696  2382 HOH HOH B . 
AB 8 HOH 97  697  2255 HOH HOH B . 
AB 8 HOH 98  698  2311 HOH HOH B . 
AB 8 HOH 99  699  2260 HOH HOH B . 
AB 8 HOH 100 700  2070 HOH HOH B . 
AB 8 HOH 101 701  2336 HOH HOH B . 
AB 8 HOH 102 702  2383 HOH HOH B . 
AB 8 HOH 103 703  2379 HOH HOH B . 
AB 8 HOH 104 704  2377 HOH HOH B . 
AB 8 HOH 105 705  2434 HOH HOH B . 
AB 8 HOH 106 706  2426 HOH HOH B . 
AB 8 HOH 107 707  2124 HOH HOH B . 
AB 8 HOH 108 708  2106 HOH HOH B . 
AB 8 HOH 109 709  2264 HOH HOH B . 
AB 8 HOH 110 710  2256 HOH HOH B . 
AB 8 HOH 111 711  2137 HOH HOH B . 
AB 8 HOH 112 712  2085 HOH HOH B . 
AB 8 HOH 113 713  2323 HOH HOH B . 
AB 8 HOH 114 714  2276 HOH HOH B . 
AB 8 HOH 115 715  2221 HOH HOH B . 
AB 8 HOH 116 716  2409 HOH HOH B . 
AB 8 HOH 117 717  2141 HOH HOH B . 
AB 8 HOH 118 718  2013 HOH HOH B . 
AB 8 HOH 119 719  2089 HOH HOH B . 
AB 8 HOH 120 720  2105 HOH HOH B . 
AB 8 HOH 121 721  2184 HOH HOH B . 
AB 8 HOH 122 722  2140 HOH HOH B . 
AB 8 HOH 123 723  2010 HOH HOH B . 
AB 8 HOH 124 724  2087 HOH HOH B . 
AB 8 HOH 125 725  2268 HOH HOH B . 
AB 8 HOH 126 726  2075 HOH HOH B . 
AB 8 HOH 127 727  2403 HOH HOH B . 
AB 8 HOH 128 728  2180 HOH HOH B . 
AB 8 HOH 129 729  2252 HOH HOH B . 
AB 8 HOH 130 730  2174 HOH HOH B . 
AB 8 HOH 131 731  2334 HOH HOH B . 
AB 8 HOH 132 732  2290 HOH HOH B . 
AB 8 HOH 133 733  2062 HOH HOH B . 
AB 8 HOH 134 734  2217 HOH HOH B . 
AB 8 HOH 135 735  2072 HOH HOH B . 
AB 8 HOH 136 736  2038 HOH HOH B . 
AB 8 HOH 137 737  2023 HOH HOH B . 
AB 8 HOH 138 738  2271 HOH HOH B . 
AB 8 HOH 139 739  2315 HOH HOH B . 
AB 8 HOH 140 740  2039 HOH HOH B . 
AB 8 HOH 141 741  2288 HOH HOH B . 
AB 8 HOH 142 742  2099 HOH HOH B . 
AB 8 HOH 143 743  2414 HOH HOH B . 
AB 8 HOH 144 744  2406 HOH HOH B . 
AB 8 HOH 145 745  2292 HOH HOH B . 
AB 8 HOH 146 746  2421 HOH HOH B . 
AB 8 HOH 147 747  2408 HOH HOH B . 
AB 8 HOH 148 748  2432 HOH HOH B . 
AB 8 HOH 149 749  2322 HOH HOH B . 
AB 8 HOH 150 750  2357 HOH HOH B . 
AB 8 HOH 151 751  2317 HOH HOH B . 
AB 8 HOH 152 752  2032 HOH HOH B . 
AB 8 HOH 153 753  2233 HOH HOH B . 
AB 8 HOH 154 754  2178 HOH HOH B . 
AB 8 HOH 155 755  2247 HOH HOH B . 
AB 8 HOH 156 756  2119 HOH HOH B . 
AB 8 HOH 157 757  2310 HOH HOH B . 
AB 8 HOH 158 758  2101 HOH HOH B . 
AB 8 HOH 159 759  2230 HOH HOH B . 
AB 8 HOH 160 760  2213 HOH HOH B . 
AB 8 HOH 161 761  2171 HOH HOH B . 
AB 8 HOH 162 762  2127 HOH HOH B . 
AB 8 HOH 163 763  2300 HOH HOH B . 
AB 8 HOH 164 764  2274 HOH HOH B . 
AB 8 HOH 165 765  2306 HOH HOH B . 
AB 8 HOH 166 766  2405 HOH HOH B . 
AB 8 HOH 167 767  2005 HOH HOH B . 
AB 8 HOH 168 768  2172 HOH HOH B . 
AB 8 HOH 169 769  2262 HOH HOH B . 
AB 8 HOH 170 770  2203 HOH HOH B . 
AB 8 HOH 171 771  2281 HOH HOH B . 
AB 8 HOH 172 772  2129 HOH HOH B . 
AB 8 HOH 173 773  2416 HOH HOH B . 
AB 8 HOH 174 774  2205 HOH HOH B . 
AB 8 HOH 175 775  2118 HOH HOH B . 
AB 8 HOH 176 776  2218 HOH HOH B . 
AB 8 HOH 177 777  2352 HOH HOH B . 
AB 8 HOH 178 778  2348 HOH HOH B . 
AB 8 HOH 179 779  2358 HOH HOH B . 
AB 8 HOH 180 780  2123 HOH HOH B . 
AB 8 HOH 181 781  2235 HOH HOH B . 
AB 8 HOH 182 782  2353 HOH HOH B . 
AB 8 HOH 183 783  2246 HOH HOH B . 
AB 8 HOH 184 784  2025 HOH HOH B . 
AB 8 HOH 185 785  2422 HOH HOH B . 
AB 8 HOH 186 786  2149 HOH HOH B . 
AB 8 HOH 187 787  2175 HOH HOH B . 
AB 8 HOH 188 788  2163 HOH HOH B . 
AB 8 HOH 189 789  2283 HOH HOH B . 
AB 8 HOH 190 790  2078 HOH HOH B . 
AB 8 HOH 191 791  2231 HOH HOH B . 
AB 8 HOH 192 792  2236 HOH HOH B . 
AB 8 HOH 193 793  2395 HOH HOH B . 
AB 8 HOH 194 794  2359 HOH HOH B . 
AB 8 HOH 195 795  2347 HOH HOH B . 
AB 8 HOH 196 796  2193 HOH HOH B . 
AB 8 HOH 197 797  2388 HOH HOH B . 
AB 8 HOH 198 798  2397 HOH HOH B . 
AB 8 HOH 199 799  2002 HOH HOH B . 
AB 8 HOH 200 800  2007 HOH HOH B . 
AB 8 HOH 201 801  2035 HOH HOH B . 
AB 8 HOH 202 802  2363 HOH HOH B . 
AB 8 HOH 203 803  2160 HOH HOH B . 
AB 8 HOH 204 804  2227 HOH HOH B . 
AB 8 HOH 205 805  2389 HOH HOH B . 
AB 8 HOH 206 806  2173 HOH HOH B . 
AB 8 HOH 207 807  2294 HOH HOH B . 
AB 8 HOH 208 808  2212 HOH HOH B . 
AB 8 HOH 209 809  2155 HOH HOH B . 
AB 8 HOH 210 810  2063 HOH HOH B . 
AB 8 HOH 211 811  2355 HOH HOH B . 
AB 8 HOH 212 812  2411 HOH HOH B . 
AB 8 HOH 213 813  2345 HOH HOH B . 
AB 8 HOH 214 814  2008 HOH HOH B . 
AB 8 HOH 215 815  2313 HOH HOH B . 
AB 8 HOH 216 816  2012 HOH HOH B . 
AB 8 HOH 217 817  2360 HOH HOH B . 
AB 8 HOH 218 818  2428 HOH HOH B . 
AB 8 HOH 219 819  2169 HOH HOH B . 
AB 8 HOH 220 820  2027 HOH HOH B . 
AB 8 HOH 221 821  2111 HOH HOH B . 
AB 8 HOH 222 822  2195 HOH HOH B . 
AB 8 HOH 223 823  2335 HOH HOH B . 
AB 8 HOH 224 824  2351 HOH HOH B . 
AB 8 HOH 225 825  2215 HOH HOH B . 
AB 8 HOH 226 826  2272 HOH HOH B . 
AB 8 HOH 227 827  2251 HOH HOH B . 
AB 8 HOH 228 828  2047 HOH HOH B . 
AB 8 HOH 229 829  2196 HOH HOH B . 
AB 8 HOH 230 830  2242 HOH HOH B . 
AB 8 HOH 231 831  2328 HOH HOH B . 
AB 8 HOH 232 832  2299 HOH HOH B . 
AB 8 HOH 233 833  2278 HOH HOH B . 
AB 8 HOH 234 834  2082 HOH HOH B . 
AB 8 HOH 235 835  2291 HOH HOH B . 
AB 8 HOH 236 836  2157 HOH HOH B . 
AB 8 HOH 237 837  2220 HOH HOH B . 
AB 8 HOH 238 838  2206 HOH HOH B . 
AB 8 HOH 239 839  2228 HOH HOH B . 
AB 8 HOH 240 840  2143 HOH HOH B . 
AB 8 HOH 241 841  2048 HOH HOH B . 
AB 8 HOH 242 842  2164 HOH HOH B . 
AB 8 HOH 243 843  2153 HOH HOH B . 
AB 8 HOH 244 844  2207 HOH HOH B . 
AB 8 HOH 245 845  2326 HOH HOH B . 
AB 8 HOH 246 846  2216 HOH HOH B . 
AB 8 HOH 247 847  2275 HOH HOH B . 
AB 8 HOH 248 848  2176 HOH HOH B . 
AB 8 HOH 249 849  2293 HOH HOH B . 
AB 8 HOH 250 850  2316 HOH HOH B . 
AB 8 HOH 251 851  2006 HOH HOH B . 
AB 8 HOH 252 852  2378 HOH HOH B . 
AB 8 HOH 253 853  2249 HOH HOH B . 
AB 8 HOH 254 854  2028 HOH HOH B . 
AB 8 HOH 255 855  2244 HOH HOH B . 
AB 8 HOH 256 856  2404 HOH HOH B . 
AB 8 HOH 257 857  2162 HOH HOH B . 
AB 8 HOH 258 858  2234 HOH HOH B . 
AB 8 HOH 259 859  2043 HOH HOH B . 
AB 8 HOH 260 860  2407 HOH HOH B . 
AB 8 HOH 261 861  2240 HOH HOH B . 
AB 8 HOH 262 862  2139 HOH HOH B . 
AB 8 HOH 263 863  2029 HOH HOH B . 
AB 8 HOH 264 864  2024 HOH HOH B . 
AB 8 HOH 265 865  2325 HOH HOH B . 
AB 8 HOH 266 866  2198 HOH HOH B . 
AB 8 HOH 267 867  2077 HOH HOH B . 
AB 8 HOH 268 868  2003 HOH HOH B . 
AB 8 HOH 269 869  2019 HOH HOH B . 
AB 8 HOH 270 870  2387 HOH HOH B . 
AB 8 HOH 271 871  2197 HOH HOH B . 
AB 8 HOH 272 872  2318 HOH HOH B . 
AB 8 HOH 273 873  2385 HOH HOH B . 
AB 8 HOH 274 874  2120 HOH HOH B . 
AB 8 HOH 275 875  2412 HOH HOH B . 
AB 8 HOH 276 876  2298 HOH HOH B . 
AB 8 HOH 277 877  2369 HOH HOH B . 
AB 8 HOH 278 878  2364 HOH HOH B . 
AB 8 HOH 279 879  2309 HOH HOH B . 
AB 8 HOH 280 880  2241 HOH HOH B . 
AB 8 HOH 281 881  2339 HOH HOH B . 
AB 8 HOH 282 882  2076 HOH HOH B . 
AB 8 HOH 283 883  2285 HOH HOH B . 
AB 8 HOH 284 884  2284 HOH HOH B . 
AB 8 HOH 285 885  2136 HOH HOH B . 
AB 8 HOH 286 886  2343 HOH HOH B . 
AB 8 HOH 287 887  2258 HOH HOH B . 
AB 8 HOH 288 888  2373 HOH HOH B . 
AB 8 HOH 289 889  2132 HOH HOH B . 
AB 8 HOH 290 890  2237 HOH HOH B . 
AB 8 HOH 291 891  2130 HOH HOH B . 
AB 8 HOH 292 892  2394 HOH HOH B . 
AB 8 HOH 293 893  2420 HOH HOH B . 
AB 8 HOH 294 894  2224 HOH HOH B . 
AB 8 HOH 295 895  2208 HOH HOH B . 
AB 8 HOH 296 896  2314 HOH HOH B . 
AB 8 HOH 297 897  2046 HOH HOH B . 
AB 8 HOH 298 898  2067 HOH HOH B . 
AB 8 HOH 299 899  2338 HOH HOH B . 
AB 8 HOH 300 900  2282 HOH HOH B . 
AB 8 HOH 301 901  2331 HOH HOH B . 
AB 8 HOH 302 902  2312 HOH HOH B . 
AB 8 HOH 303 903  2245 HOH HOH B . 
AB 8 HOH 304 904  2250 HOH HOH B . 
AB 8 HOH 305 905  2100 HOH HOH B . 
AB 8 HOH 306 906  2340 HOH HOH B . 
AB 8 HOH 307 907  2366 HOH HOH B . 
AB 8 HOH 308 908  2392 HOH HOH B . 
AB 8 HOH 309 909  2261 HOH HOH B . 
AB 8 HOH 310 910  2084 HOH HOH B . 
AB 8 HOH 311 911  2142 HOH HOH B . 
AB 8 HOH 312 912  2125 HOH HOH B . 
AB 8 HOH 313 913  2219 HOH HOH B . 
AB 8 HOH 314 914  2368 HOH HOH B . 
AB 8 HOH 315 915  2356 HOH HOH B . 
AB 8 HOH 316 916  2346 HOH HOH B . 
AB 8 HOH 317 917  2371 HOH HOH B . 
AB 8 HOH 318 918  2329 HOH HOH B . 
AB 8 HOH 319 919  2001 HOH HOH B . 
AB 8 HOH 320 920  2287 HOH HOH B . 
AB 8 HOH 321 921  2433 HOH HOH B . 
AB 8 HOH 322 922  2209 HOH HOH B . 
AB 8 HOH 323 923  2375 HOH HOH B . 
AB 8 HOH 324 924  2083 HOH HOH B . 
AB 8 HOH 325 925  2238 HOH HOH B . 
AB 8 HOH 326 926  2367 HOH HOH B . 
AB 8 HOH 327 927  2243 HOH HOH B . 
AB 8 HOH 328 928  2417 HOH HOH B . 
AB 8 HOH 329 929  2107 HOH HOH B . 
AB 8 HOH 330 930  2021 HOH HOH B . 
AB 8 HOH 331 931  2384 HOH HOH B . 
AB 8 HOH 332 932  2170 HOH HOH B . 
AB 8 HOH 333 933  2301 HOH HOH B . 
AB 8 HOH 334 934  2041 HOH HOH B . 
AB 8 HOH 335 935  2393 HOH HOH B . 
AB 8 HOH 336 936  2211 HOH HOH B . 
AB 8 HOH 337 937  2265 HOH HOH B . 
AB 8 HOH 338 938  2398 HOH HOH B . 
AB 8 HOH 339 939  2296 HOH HOH B . 
AB 8 HOH 340 940  2308 HOH HOH B . 
AB 8 HOH 341 941  2066 HOH HOH B . 
AB 8 HOH 342 942  2342 HOH HOH B . 
AB 8 HOH 343 943  2074 HOH HOH B . 
AB 8 HOH 344 944  2248 HOH HOH B . 
AB 8 HOH 345 945  2344 HOH HOH B . 
AB 8 HOH 346 946  2365 HOH HOH B . 
AB 8 HOH 347 947  2396 HOH HOH B . 
AB 8 HOH 348 948  2341 HOH HOH B . 
AB 8 HOH 349 949  2423 HOH HOH B . 
AB 8 HOH 350 950  2210 HOH HOH B . 
AB 8 HOH 351 951  2266 HOH HOH B . 
AB 8 HOH 352 952  2103 HOH HOH B . 
AB 8 HOH 353 953  2418 HOH HOH B . 
AB 8 HOH 354 954  2081 HOH HOH B . 
AB 8 HOH 355 955  2204 HOH HOH B . 
AB 8 HOH 356 956  2135 HOH HOH B . 
AB 8 HOH 357 957  2430 HOH HOH B . 
AB 8 HOH 358 958  2399 HOH HOH B . 
AB 8 HOH 359 959  2400 HOH HOH B . 
AB 8 HOH 360 960  2349 HOH HOH B . 
AB 8 HOH 361 961  2049 HOH HOH B . 
AB 8 HOH 362 962  2330 HOH HOH B . 
AB 8 HOH 363 963  2104 HOH HOH B . 
AB 8 HOH 364 964  2097 HOH HOH B . 
AB 8 HOH 365 965  2108 HOH HOH B . 
AB 8 HOH 366 966  2020 HOH HOH B . 
AB 8 HOH 367 967  2109 HOH HOH B . 
AB 8 HOH 368 968  2165 HOH HOH B . 
AB 8 HOH 369 969  2033 HOH HOH B . 
AB 8 HOH 370 970  2117 HOH HOH B . 
AB 8 HOH 371 971  2102 HOH HOH B . 
AB 8 HOH 372 972  2188 HOH HOH B . 
AB 8 HOH 373 973  2004 HOH HOH B . 
AB 8 HOH 374 974  2053 HOH HOH B . 
AB 8 HOH 375 975  2022 HOH HOH B . 
AB 8 HOH 376 976  2094 HOH HOH B . 
AB 8 HOH 377 977  2151 HOH HOH B . 
AB 8 HOH 378 978  2053 HOH HOH B . 
AB 8 HOH 379 979  2147 HOH HOH B . 
AB 8 HOH 380 980  2093 HOH HOH B . 
AB 8 HOH 381 981  2116 HOH HOH B . 
AB 8 HOH 382 982  2232 HOH HOH B . 
AB 8 HOH 383 983  2091 HOH HOH B . 
AB 8 HOH 384 984  2068 HOH HOH B . 
AB 8 HOH 385 985  2104 HOH HOH B . 
AB 8 HOH 386 986  2168 HOH HOH B . 
AB 8 HOH 387 987  2167 HOH HOH B . 
AB 8 HOH 388 988  2061 HOH HOH B . 
AB 8 HOH 389 989  2042 HOH HOH B . 
AB 8 HOH 390 990  2121 HOH HOH B . 
AB 8 HOH 391 991  2126 HOH HOH B . 
AB 8 HOH 392 992  2134 HOH HOH B . 
AB 8 HOH 393 993  2332 HOH HOH B . 
AB 8 HOH 394 994  2138 HOH HOH B . 
AB 8 HOH 395 995  2161 HOH HOH B . 
AB 8 HOH 396 996  2152 HOH HOH B . 
AB 8 HOH 397 997  2148 HOH HOH B . 
AB 8 HOH 398 998  2051 HOH HOH B . 
AB 8 HOH 399 999  2092 HOH HOH B . 
AB 8 HOH 400 1000 2333 HOH HOH B . 
AB 8 HOH 401 1001 2037 HOH HOH B . 
AB 8 HOH 402 1002 2026 HOH HOH B . 
AB 8 HOH 403 1003 2102 HOH HOH B . 
AB 8 HOH 404 1004 2150 HOH HOH B . 
AB 8 HOH 405 1005 2177 HOH HOH B . 
AB 8 HOH 406 1006 2110 HOH HOH B . 
AB 8 HOH 407 1007 2054 HOH HOH B . 
AB 8 HOH 408 1008 2077 HOH HOH B . 
AB 8 HOH 409 1009 2036 HOH HOH B . 
AB 8 HOH 410 1010 2083 HOH HOH B . 
AB 8 HOH 411 1011 2064 HOH HOH B . 
AB 8 HOH 412 1012 2050 HOH HOH B . 
AB 8 HOH 413 1013 2182 HOH HOH B . 
AB 8 HOH 414 1014 2156 HOH HOH B . 
AB 8 HOH 415 1015 2113 HOH HOH B . 
AB 8 HOH 416 1016 2128 HOH HOH B . 
AB 8 HOH 417 1017 2052 HOH HOH B . 
AB 8 HOH 418 1018 2190 HOH HOH B . 
AB 8 HOH 419 1019 2191 HOH HOH B . 
AB 8 HOH 420 1020 2066 HOH HOH B . 
AB 8 HOH 421 1021 2152 HOH HOH B . 
AB 8 HOH 422 1022 2199 HOH HOH B . 
AB 8 HOH 423 1023 2179 HOH HOH B . 
AB 8 HOH 424 1024 2189 HOH HOH B . 
AB 8 HOH 425 1025 2103 HOH HOH B . 
AB 8 HOH 426 1026 2056 HOH HOH B . 
AB 8 HOH 427 1027 2194 HOH HOH B . 
AB 8 HOH 428 1028 2090 HOH HOH B . 
AB 8 HOH 429 1029 2185 HOH HOH B . 
AB 8 HOH 430 1030 2114 HOH HOH B . 
AB 8 HOH 431 1031 2187 HOH HOH B . 
AB 8 HOH 432 1032 2144 HOH HOH B . 
AB 8 HOH 433 1033 2145 HOH HOH B . 
AB 8 HOH 434 1034 2131 HOH HOH B . 
AB 8 HOH 435 1035 2051 HOH HOH B . 
AB 8 HOH 436 1036 2080 HOH HOH B . 
AB 8 HOH 437 1037 2059 HOH HOH B . 
AB 8 HOH 438 1038 2159 HOH HOH B . 
AB 8 HOH 439 1039 2057 HOH HOH B . 
AB 8 HOH 440 1040 2186 HOH HOH B . 
AB 8 HOH 441 1041 2045 HOH HOH B . 
AB 8 HOH 442 1042 2069 HOH HOH B . 
BB 8 HOH 1   601  2383 HOH HOH C . 
BB 8 HOH 2   602  2428 HOH HOH C . 
BB 8 HOH 3   603  2412 HOH HOH C . 
BB 8 HOH 4   604  2045 HOH HOH C . 
BB 8 HOH 5   605  2305 HOH HOH C . 
BB 8 HOH 6   606  2210 HOH HOH C . 
BB 8 HOH 7   607  2304 HOH HOH C . 
BB 8 HOH 8   608  2292 HOH HOH C . 
BB 8 HOH 9   609  2348 HOH HOH C . 
BB 8 HOH 10  610  2132 HOH HOH C . 
BB 8 HOH 11  611  2274 HOH HOH C . 
BB 8 HOH 12  612  2172 HOH HOH C . 
BB 8 HOH 13  613  2089 HOH HOH C . 
BB 8 HOH 14  614  2335 HOH HOH C . 
BB 8 HOH 15  615  2341 HOH HOH C . 
BB 8 HOH 16  616  2227 HOH HOH C . 
BB 8 HOH 17  617  2325 HOH HOH C . 
BB 8 HOH 18  618  2064 HOH HOH C . 
BB 8 HOH 19  619  2275 HOH HOH C . 
BB 8 HOH 20  620  2184 HOH HOH C . 
BB 8 HOH 21  621  2384 HOH HOH C . 
BB 8 HOH 22  622  2069 HOH HOH C . 
BB 8 HOH 23  623  2316 HOH HOH C . 
BB 8 HOH 24  624  2183 HOH HOH C . 
BB 8 HOH 25  625  2012 HOH HOH C . 
BB 8 HOH 26  626  2230 HOH HOH C . 
BB 8 HOH 27  627  2288 HOH HOH C . 
BB 8 HOH 28  628  2399 HOH HOH C . 
BB 8 HOH 29  629  2382 HOH HOH C . 
BB 8 HOH 30  630  2154 HOH HOH C . 
BB 8 HOH 31  631  2037 HOH HOH C . 
BB 8 HOH 32  632  2182 HOH HOH C . 
BB 8 HOH 33  633  2067 HOH HOH C . 
BB 8 HOH 34  634  2091 HOH HOH C . 
BB 8 HOH 35  635  2231 HOH HOH C . 
BB 8 HOH 36  636  2436 HOH HOH C . 
BB 8 HOH 37  637  2377 HOH HOH C . 
BB 8 HOH 38  638  2115 HOH HOH C . 
BB 8 HOH 39  639  2300 HOH HOH C . 
BB 8 HOH 40  640  2401 HOH HOH C . 
BB 8 HOH 41  641  2208 HOH HOH C . 
BB 8 HOH 42  642  2113 HOH HOH C . 
BB 8 HOH 43  643  2137 HOH HOH C . 
BB 8 HOH 44  644  2017 HOH HOH C . 
BB 8 HOH 45  645  2255 HOH HOH C . 
BB 8 HOH 46  646  2053 HOH HOH C . 
BB 8 HOH 47  647  2209 HOH HOH C . 
BB 8 HOH 48  648  2033 HOH HOH C . 
BB 8 HOH 49  649  2323 HOH HOH C . 
BB 8 HOH 50  650  2019 HOH HOH C . 
BB 8 HOH 51  651  2350 HOH HOH C . 
BB 8 HOH 52  652  2235 HOH HOH C . 
BB 8 HOH 53  653  2424 HOH HOH C . 
BB 8 HOH 54  654  2216 HOH HOH C . 
BB 8 HOH 55  655  2395 HOH HOH C . 
BB 8 HOH 56  656  2415 HOH HOH C . 
BB 8 HOH 57  657  2249 HOH HOH C . 
BB 8 HOH 58  658  2281 HOH HOH C . 
BB 8 HOH 59  659  2407 HOH HOH C . 
BB 8 HOH 60  660  2159 HOH HOH C . 
BB 8 HOH 61  661  2262 HOH HOH C . 
BB 8 HOH 62  662  2233 HOH HOH C . 
BB 8 HOH 63  663  2403 HOH HOH C . 
BB 8 HOH 64  664  2234 HOH HOH C . 
BB 8 HOH 65  665  2022 HOH HOH C . 
BB 8 HOH 66  666  2313 HOH HOH C . 
BB 8 HOH 67  667  2163 HOH HOH C . 
BB 8 HOH 68  668  2179 HOH HOH C . 
BB 8 HOH 69  669  2238 HOH HOH C . 
BB 8 HOH 70  670  2180 HOH HOH C . 
BB 8 HOH 71  671  2333 HOH HOH C . 
BB 8 HOH 72  672  2021 HOH HOH C . 
BB 8 HOH 73  673  2217 HOH HOH C . 
BB 8 HOH 74  674  2353 HOH HOH C . 
BB 8 HOH 75  675  2032 HOH HOH C . 
BB 8 HOH 76  676  2005 HOH HOH C . 
BB 8 HOH 77  677  2347 HOH HOH C . 
BB 8 HOH 78  678  2018 HOH HOH C . 
BB 8 HOH 79  679  2386 HOH HOH C . 
BB 8 HOH 80  680  2354 HOH HOH C . 
BB 8 HOH 81  681  2400 HOH HOH C . 
BB 8 HOH 82  682  2087 HOH HOH C . 
BB 8 HOH 83  683  2110 HOH HOH C . 
BB 8 HOH 84  684  2283 HOH HOH C . 
BB 8 HOH 85  685  2405 HOH HOH C . 
BB 8 HOH 86  686  2122 HOH HOH C . 
BB 8 HOH 87  687  2439 HOH HOH C . 
BB 8 HOH 88  688  2101 HOH HOH C . 
BB 8 HOH 89  689  2196 HOH HOH C . 
BB 8 HOH 90  690  2404 HOH HOH C . 
BB 8 HOH 91  691  2093 HOH HOH C . 
BB 8 HOH 92  692  2141 HOH HOH C . 
BB 8 HOH 93  693  2406 HOH HOH C . 
BB 8 HOH 94  694  2185 HOH HOH C . 
BB 8 HOH 95  695  2039 HOH HOH C . 
BB 8 HOH 96  696  2267 HOH HOH C . 
BB 8 HOH 97  697  2285 HOH HOH C . 
BB 8 HOH 98  698  2310 HOH HOH C . 
BB 8 HOH 99  699  2237 HOH HOH C . 
BB 8 HOH 100 700  2156 HOH HOH C . 
BB 8 HOH 101 701  2109 HOH HOH C . 
BB 8 HOH 102 702  2119 HOH HOH C . 
BB 8 HOH 103 703  2013 HOH HOH C . 
BB 8 HOH 104 704  2224 HOH HOH C . 
BB 8 HOH 105 705  2276 HOH HOH C . 
BB 8 HOH 106 706  2260 HOH HOH C . 
BB 8 HOH 107 707  2270 HOH HOH C . 
BB 8 HOH 108 708  2302 HOH HOH C . 
BB 8 HOH 109 709  2433 HOH HOH C . 
BB 8 HOH 110 710  2265 HOH HOH C . 
BB 8 HOH 111 711  2441 HOH HOH C . 
BB 8 HOH 112 712  2004 HOH HOH C . 
BB 8 HOH 113 713  2038 HOH HOH C . 
BB 8 HOH 114 714  2437 HOH HOH C . 
BB 8 HOH 115 715  2396 HOH HOH C . 
BB 8 HOH 116 716  2036 HOH HOH C . 
BB 8 HOH 117 717  2160 HOH HOH C . 
BB 8 HOH 118 718  2435 HOH HOH C . 
BB 8 HOH 119 719  2280 HOH HOH C . 
BB 8 HOH 120 720  2293 HOH HOH C . 
BB 8 HOH 121 721  2062 HOH HOH C . 
BB 8 HOH 122 722  2269 HOH HOH C . 
BB 8 HOH 123 723  2355 HOH HOH C . 
BB 8 HOH 124 724  2169 HOH HOH C . 
BB 8 HOH 125 725  2263 HOH HOH C . 
BB 8 HOH 126 726  2322 HOH HOH C . 
BB 8 HOH 127 727  2321 HOH HOH C . 
BB 8 HOH 128 728  2218 HOH HOH C . 
BB 8 HOH 129 729  2081 HOH HOH C . 
BB 8 HOH 130 730  2360 HOH HOH C . 
BB 8 HOH 131 731  2279 HOH HOH C . 
BB 8 HOH 132 732  2030 HOH HOH C . 
BB 8 HOH 133 733  2252 HOH HOH C . 
BB 8 HOH 134 734  2029 HOH HOH C . 
BB 8 HOH 135 735  2432 HOH HOH C . 
BB 8 HOH 136 736  2268 HOH HOH C . 
BB 8 HOH 137 737  2189 HOH HOH C . 
BB 8 HOH 138 738  2286 HOH HOH C . 
BB 8 HOH 139 739  2106 HOH HOH C . 
BB 8 HOH 140 740  2376 HOH HOH C . 
BB 8 HOH 141 741  2291 HOH HOH C . 
BB 8 HOH 142 742  2385 HOH HOH C . 
BB 8 HOH 143 743  2417 HOH HOH C . 
BB 8 HOH 144 744  2068 HOH HOH C . 
BB 8 HOH 145 745  2311 HOH HOH C . 
BB 8 HOH 146 746  2170 HOH HOH C . 
BB 8 HOH 147 747  2058 HOH HOH C . 
BB 8 HOH 148 748  2337 HOH HOH C . 
BB 8 HOH 149 749  2150 HOH HOH C . 
BB 8 HOH 150 750  2001 HOH HOH C . 
BB 8 HOH 151 751  2425 HOH HOH C . 
BB 8 HOH 152 752  2416 HOH HOH C . 
BB 8 HOH 153 753  2211 HOH HOH C . 
BB 8 HOH 154 754  2331 HOH HOH C . 
BB 8 HOH 155 755  2356 HOH HOH C . 
BB 8 HOH 156 756  2241 HOH HOH C . 
BB 8 HOH 157 757  2120 HOH HOH C . 
BB 8 HOH 158 758  2066 HOH HOH C . 
BB 8 HOH 159 759  2271 HOH HOH C . 
BB 8 HOH 160 760  2124 HOH HOH C . 
BB 8 HOH 161 761  2213 HOH HOH C . 
BB 8 HOH 162 762  2057 HOH HOH C . 
BB 8 HOH 163 763  2212 HOH HOH C . 
BB 8 HOH 164 764  2147 HOH HOH C . 
BB 8 HOH 165 765  2343 HOH HOH C . 
BB 8 HOH 166 766  2314 HOH HOH C . 
BB 8 HOH 167 767  2023 HOH HOH C . 
BB 8 HOH 168 768  2243 HOH HOH C . 
BB 8 HOH 169 769  2006 HOH HOH C . 
BB 8 HOH 170 770  2336 HOH HOH C . 
BB 8 HOH 171 771  2369 HOH HOH C . 
BB 8 HOH 172 772  2278 HOH HOH C . 
BB 8 HOH 173 773  2312 HOH HOH C . 
BB 8 HOH 174 774  2076 HOH HOH C . 
BB 8 HOH 175 775  2370 HOH HOH C . 
BB 8 HOH 176 776  2127 HOH HOH C . 
BB 8 HOH 177 777  2444 HOH HOH C . 
BB 8 HOH 178 778  2011 HOH HOH C . 
BB 8 HOH 179 779  2402 HOH HOH C . 
BB 8 HOH 180 780  2393 HOH HOH C . 
BB 8 HOH 181 781  2358 HOH HOH C . 
BB 8 HOH 182 782  2247 HOH HOH C . 
BB 8 HOH 183 783  2364 HOH HOH C . 
BB 8 HOH 184 784  2372 HOH HOH C . 
BB 8 HOH 185 785  2108 HOH HOH C . 
BB 8 HOH 186 786  2342 HOH HOH C . 
BB 8 HOH 187 787  2282 HOH HOH C . 
BB 8 HOH 188 788  2346 HOH HOH C . 
BB 8 HOH 189 789  2239 HOH HOH C . 
BB 8 HOH 190 790  2178 HOH HOH C . 
BB 8 HOH 191 791  2020 HOH HOH C . 
BB 8 HOH 192 792  2434 HOH HOH C . 
BB 8 HOH 193 793  2339 HOH HOH C . 
BB 8 HOH 194 794  2245 HOH HOH C . 
BB 8 HOH 195 795  2419 HOH HOH C . 
BB 8 HOH 196 796  2099 HOH HOH C . 
BB 8 HOH 197 797  2394 HOH HOH C . 
BB 8 HOH 198 798  2166 HOH HOH C . 
BB 8 HOH 199 799  2136 HOH HOH C . 
BB 8 HOH 200 800  2111 HOH HOH C . 
BB 8 HOH 201 801  2140 HOH HOH C . 
BB 8 HOH 202 802  2388 HOH HOH C . 
BB 8 HOH 203 803  2266 HOH HOH C . 
BB 8 HOH 204 804  2197 HOH HOH C . 
BB 8 HOH 205 805  2102 HOH HOH C . 
BB 8 HOH 206 806  2082 HOH HOH C . 
BB 8 HOH 207 807  2221 HOH HOH C . 
BB 8 HOH 208 808  2016 HOH HOH C . 
BB 8 HOH 209 809  2003 HOH HOH C . 
BB 8 HOH 210 810  2165 HOH HOH C . 
BB 8 HOH 211 811  2357 HOH HOH C . 
BB 8 HOH 212 812  2002 HOH HOH C . 
BB 8 HOH 213 813  2361 HOH HOH C . 
BB 8 HOH 214 814  2104 HOH HOH C . 
BB 8 HOH 215 815  2171 HOH HOH C . 
BB 8 HOH 216 816  2365 HOH HOH C . 
BB 8 HOH 217 817  2205 HOH HOH C . 
BB 8 HOH 218 818  2257 HOH HOH C . 
BB 8 HOH 219 819  2290 HOH HOH C . 
BB 8 HOH 220 820  2222 HOH HOH C . 
BB 8 HOH 221 821  2408 HOH HOH C . 
BB 8 HOH 222 822  2040 HOH HOH C . 
BB 8 HOH 223 823  2387 HOH HOH C . 
BB 8 HOH 224 824  2065 HOH HOH C . 
BB 8 HOH 225 825  2340 HOH HOH C . 
BB 8 HOH 226 826  2049 HOH HOH C . 
BB 8 HOH 227 827  2420 HOH HOH C . 
BB 8 HOH 228 828  2095 HOH HOH C . 
BB 8 HOH 229 829  2025 HOH HOH C . 
BB 8 HOH 230 830  2338 HOH HOH C . 
BB 8 HOH 231 831  2430 HOH HOH C . 
BB 8 HOH 232 832  2251 HOH HOH C . 
BB 8 HOH 233 833  2158 HOH HOH C . 
BB 8 HOH 234 834  2083 HOH HOH C . 
BB 8 HOH 235 835  2149 HOH HOH C . 
BB 8 HOH 236 836  2152 HOH HOH C . 
BB 8 HOH 237 837  2229 HOH HOH C . 
BB 8 HOH 238 838  2226 HOH HOH C . 
BB 8 HOH 239 839  2374 HOH HOH C . 
BB 8 HOH 240 840  2301 HOH HOH C . 
BB 8 HOH 241 841  2173 HOH HOH C . 
BB 8 HOH 242 842  2204 HOH HOH C . 
BB 8 HOH 243 843  2359 HOH HOH C . 
BB 8 HOH 244 844  2070 HOH HOH C . 
BB 8 HOH 245 845  2378 HOH HOH C . 
BB 8 HOH 246 846  2194 HOH HOH C . 
BB 8 HOH 247 847  2299 HOH HOH C . 
BB 8 HOH 248 848  2008 HOH HOH C . 
BB 8 HOH 249 849  2236 HOH HOH C . 
BB 8 HOH 250 850  2201 HOH HOH C . 
BB 8 HOH 251 851  2248 HOH HOH C . 
BB 8 HOH 252 852  2031 HOH HOH C . 
BB 8 HOH 253 853  2131 HOH HOH C . 
BB 8 HOH 254 854  2046 HOH HOH C . 
BB 8 HOH 255 855  2429 HOH HOH C . 
BB 8 HOH 256 856  2015 HOH HOH C . 
BB 8 HOH 257 857  2413 HOH HOH C . 
BB 8 HOH 258 858  2261 HOH HOH C . 
BB 8 HOH 259 859  2327 HOH HOH C . 
BB 8 HOH 260 860  2273 HOH HOH C . 
BB 8 HOH 261 861  2228 HOH HOH C . 
BB 8 HOH 262 862  2060 HOH HOH C . 
BB 8 HOH 263 863  2391 HOH HOH C . 
BB 8 HOH 264 864  2151 HOH HOH C . 
BB 8 HOH 265 865  2414 HOH HOH C . 
BB 8 HOH 266 866  2315 HOH HOH C . 
BB 8 HOH 267 867  2298 HOH HOH C . 
BB 8 HOH 268 868  2426 HOH HOH C . 
BB 8 HOH 269 869  2368 HOH HOH C . 
BB 8 HOH 270 870  2352 HOH HOH C . 
BB 8 HOH 271 871  2206 HOH HOH C . 
BB 8 HOH 272 872  2077 HOH HOH C . 
BB 8 HOH 273 873  2079 HOH HOH C . 
BB 8 HOH 274 874  2380 HOH HOH C . 
BB 8 HOH 275 875  2303 HOH HOH C . 
BB 8 HOH 276 876  2232 HOH HOH C . 
BB 8 HOH 277 877  2329 HOH HOH C . 
BB 8 HOH 278 878  2324 HOH HOH C . 
BB 8 HOH 279 879  2409 HOH HOH C . 
BB 8 HOH 280 880  2330 HOH HOH C . 
BB 8 HOH 281 881  2397 HOH HOH C . 
BB 8 HOH 282 882  2320 HOH HOH C . 
BB 8 HOH 283 883  2167 HOH HOH C . 
BB 8 HOH 284 884  2219 HOH HOH C . 
BB 8 HOH 285 885  2287 HOH HOH C . 
BB 8 HOH 286 886  2027 HOH HOH C . 
BB 8 HOH 287 887  2142 HOH HOH C . 
BB 8 HOH 288 888  2442 HOH HOH C . 
BB 8 HOH 289 889  2071 HOH HOH C . 
BB 8 HOH 290 890  2349 HOH HOH C . 
BB 8 HOH 291 891  2010 HOH HOH C . 
BB 8 HOH 292 892  2009 HOH HOH C . 
BB 8 HOH 293 893  2126 HOH HOH C . 
BB 8 HOH 294 894  2145 HOH HOH C . 
BB 8 HOH 295 895  2080 HOH HOH C . 
BB 8 HOH 296 896  2307 HOH HOH C . 
BB 8 HOH 297 897  2246 HOH HOH C . 
BB 8 HOH 298 898  2410 HOH HOH C . 
BB 8 HOH 299 899  2014 HOH HOH C . 
BB 8 HOH 300 900  2253 HOH HOH C . 
BB 8 HOH 301 901  2389 HOH HOH C . 
BB 8 HOH 302 902  2250 HOH HOH C . 
BB 8 HOH 303 903  2438 HOH HOH C . 
BB 8 HOH 304 904  2445 HOH HOH C . 
BB 8 HOH 305 905  2317 HOH HOH C . 
BB 8 HOH 306 906  2431 HOH HOH C . 
BB 8 HOH 307 907  2048 HOH HOH C . 
BB 8 HOH 308 908  2242 HOH HOH C . 
BB 8 HOH 309 909  2215 HOH HOH C . 
BB 8 HOH 310 910  2332 HOH HOH C . 
BB 8 HOH 311 911  2256 HOH HOH C . 
BB 8 HOH 312 912  2259 HOH HOH C . 
BB 8 HOH 313 913  2418 HOH HOH C . 
BB 8 HOH 314 914  2272 HOH HOH C . 
BB 8 HOH 315 915  2284 HOH HOH C . 
BB 8 HOH 316 916  2427 HOH HOH C . 
BB 8 HOH 317 917  2326 HOH HOH C . 
BB 8 HOH 318 918  2007 HOH HOH C . 
BB 8 HOH 319 919  2059 HOH HOH C . 
BB 8 HOH 320 920  2398 HOH HOH C . 
BB 8 HOH 321 921  2306 HOH HOH C . 
BB 8 HOH 322 922  2135 HOH HOH C . 
BB 8 HOH 323 923  2105 HOH HOH C . 
BB 8 HOH 324 924  2092 HOH HOH C . 
BB 8 HOH 325 925  2277 HOH HOH C . 
BB 8 HOH 326 926  2042 HOH HOH C . 
BB 8 HOH 327 927  2168 HOH HOH C . 
BB 8 HOH 328 928  2363 HOH HOH C . 
BB 8 HOH 329 929  2367 HOH HOH C . 
BB 8 HOH 330 930  2223 HOH HOH C . 
BB 8 HOH 331 931  2125 HOH HOH C . 
BB 8 HOH 332 932  2318 HOH HOH C . 
BB 8 HOH 333 933  2440 HOH HOH C . 
BB 8 HOH 334 934  2297 HOH HOH C . 
BB 8 HOH 335 935  2123 HOH HOH C . 
BB 8 HOH 336 936  2379 HOH HOH C . 
BB 8 HOH 337 937  2157 HOH HOH C . 
BB 8 HOH 338 938  2116 HOH HOH C . 
BB 8 HOH 339 939  2392 HOH HOH C . 
BB 8 HOH 340 940  2334 HOH HOH C . 
BB 8 HOH 341 941  2295 HOH HOH C . 
BB 8 HOH 342 942  2345 HOH HOH C . 
BB 8 HOH 343 943  2258 HOH HOH C . 
BB 8 HOH 344 944  2308 HOH HOH C . 
BB 8 HOH 345 945  2411 HOH HOH C . 
BB 8 HOH 346 946  2296 HOH HOH C . 
BB 8 HOH 347 947  2328 HOH HOH C . 
BB 8 HOH 348 948  2294 HOH HOH C . 
BB 8 HOH 349 949  2138 HOH HOH C . 
BB 8 HOH 350 950  2422 HOH HOH C . 
BB 8 HOH 351 951  2309 HOH HOH C . 
BB 8 HOH 352 952  2100 HOH HOH C . 
BB 8 HOH 353 953  2373 HOH HOH C . 
BB 8 HOH 354 954  2423 HOH HOH C . 
BB 8 HOH 355 955  2207 HOH HOH C . 
BB 8 HOH 356 956  2225 HOH HOH C . 
BB 8 HOH 357 957  2254 HOH HOH C . 
BB 8 HOH 358 958  2214 HOH HOH C . 
BB 8 HOH 359 959  2240 HOH HOH C . 
BB 8 HOH 360 960  2289 HOH HOH C . 
BB 8 HOH 361 961  2088 HOH HOH C . 
BB 8 HOH 362 962  2381 HOH HOH C . 
BB 8 HOH 363 963  2375 HOH HOH C . 
BB 8 HOH 364 964  2351 HOH HOH C . 
BB 8 HOH 365 965  2078 HOH HOH C . 
BB 8 HOH 366 966  2390 HOH HOH C . 
BB 8 HOH 367 967  2264 HOH HOH C . 
BB 8 HOH 368 968  2024 HOH HOH C . 
BB 8 HOH 369 969  2344 HOH HOH C . 
BB 8 HOH 370 970  2371 HOH HOH C . 
BB 8 HOH 371 971  2366 HOH HOH C . 
BB 8 HOH 372 972  2193 HOH HOH C . 
BB 8 HOH 373 973  2244 HOH HOH C . 
BB 8 HOH 374 974  2319 HOH HOH C . 
BB 8 HOH 375 975  2421 HOH HOH C . 
BB 8 HOH 376 976  2098 HOH HOH C . 
BB 8 HOH 377 977  2443 HOH HOH C . 
BB 8 HOH 378 978  2188 HOH HOH C . 
BB 8 HOH 379 979  2362 HOH HOH C . 
BB 8 HOH 380 980  2220 HOH HOH C . 
BB 8 HOH 381 981  2074 HOH HOH C . 
BB 8 HOH 382 982  2044 HOH HOH C . 
BB 8 HOH 383 983  2118 HOH HOH C . 
BB 8 HOH 384 984  2028 HOH HOH C . 
BB 8 HOH 385 985  2097 HOH HOH C . 
BB 8 HOH 386 986  2075 HOH HOH C . 
BB 8 HOH 387 987  2231 HOH HOH C . 
BB 8 HOH 388 988  2096 HOH HOH C . 
BB 8 HOH 389 989  2177 HOH HOH C . 
BB 8 HOH 390 990  2148 HOH HOH C . 
BB 8 HOH 391 991  2084 HOH HOH C . 
BB 8 HOH 392 992  2035 HOH HOH C . 
BB 8 HOH 393 993  2187 HOH HOH C . 
BB 8 HOH 394 994  2212 HOH HOH C . 
BB 8 HOH 395 995  2144 HOH HOH C . 
BB 8 HOH 396 996  2086 HOH HOH C . 
BB 8 HOH 397 997  2045 HOH HOH C . 
BB 8 HOH 398 998  2162 HOH HOH C . 
BB 8 HOH 399 999  2051 HOH HOH C . 
BB 8 HOH 400 1000 2034 HOH HOH C . 
BB 8 HOH 401 1001 2117 HOH HOH C . 
BB 8 HOH 402 1002 2103 HOH HOH C . 
BB 8 HOH 403 1003 2146 HOH HOH C . 
BB 8 HOH 404 1004 2191 HOH HOH C . 
BB 8 HOH 405 1005 2161 HOH HOH C . 
BB 8 HOH 406 1006 2129 HOH HOH C . 
BB 8 HOH 407 1007 2041 HOH HOH C . 
BB 8 HOH 408 1008 2122 HOH HOH C . 
BB 8 HOH 409 1009 2107 HOH HOH C . 
BB 8 HOH 410 1010 2050 HOH HOH C . 
BB 8 HOH 411 1011 2026 HOH HOH C . 
BB 8 HOH 412 1012 2107 HOH HOH C . 
BB 8 HOH 413 1013 2164 HOH HOH C . 
BB 8 HOH 414 1014 2186 HOH HOH C . 
BB 8 HOH 415 1015 2228 HOH HOH C . 
BB 8 HOH 416 1016 2129 HOH HOH C . 
BB 8 HOH 417 1017 2174 HOH HOH C . 
BB 8 HOH 418 1018 2202 HOH HOH C . 
BB 8 HOH 419 1019 2056 HOH HOH C . 
BB 8 HOH 420 1020 2192 HOH HOH C . 
BB 8 HOH 421 1021 2052 HOH HOH C . 
BB 8 HOH 422 1022 2133 HOH HOH C . 
BB 8 HOH 423 1023 2071 HOH HOH C . 
BB 8 HOH 424 1024 2090 HOH HOH C . 
BB 8 HOH 425 1025 2075 HOH HOH C . 
BB 8 HOH 426 1026 2134 HOH HOH C . 
BB 8 HOH 427 1027 2099 HOH HOH C . 
BB 8 HOH 428 1028 2072 HOH HOH C . 
BB 8 HOH 429 1029 2195 HOH HOH C . 
BB 8 HOH 430 1030 2112 HOH HOH C . 
BB 8 HOH 431 1031 2198 HOH HOH C . 
BB 8 HOH 432 1032 2181 HOH HOH C . 
BB 8 HOH 433 1033 2054 HOH HOH C . 
BB 8 HOH 434 1034 2139 HOH HOH C . 
BB 8 HOH 435 1035 2143 HOH HOH C . 
BB 8 HOH 436 1036 2097 HOH HOH C . 
BB 8 HOH 437 1037 2154 HOH HOH C . 
BB 8 HOH 438 1038 2121 HOH HOH C . 
BB 8 HOH 439 1039 2153 HOH HOH C . 
BB 8 HOH 440 1040 2128 HOH HOH C . 
BB 8 HOH 441 1041 2199 HOH HOH C . 
BB 8 HOH 442 1042 2190 HOH HOH C . 
BB 8 HOH 443 1043 2200 HOH HOH C . 
BB 8 HOH 444 1044 2055 HOH HOH C . 
BB 8 HOH 445 1045 2043 HOH HOH C . 
BB 8 HOH 446 1046 2073 HOH HOH C . 
BB 8 HOH 447 1047 2155 HOH HOH C . 
BB 8 HOH 448 1048 2175 HOH HOH C . 
BB 8 HOH 449 1049 2203 HOH HOH C . 
BB 8 HOH 450 1050 2047 HOH HOH C . 
BB 8 HOH 451 1051 2063 HOH HOH C . 
BB 8 HOH 452 1052 2120 HOH HOH C . 
BB 8 HOH 453 1053 2226 HOH HOH C . 
BB 8 HOH 454 1054 2094 HOH HOH C . 
CB 8 HOH 1   601  2460 HOH HOH D . 
CB 8 HOH 2   602  2029 HOH HOH D . 
CB 8 HOH 3   603  2110 HOH HOH D . 
CB 8 HOH 4   604  2047 HOH HOH D . 
CB 8 HOH 5   605  2363 HOH HOH D . 
CB 8 HOH 6   606  2297 HOH HOH D . 
CB 8 HOH 7   607  2027 HOH HOH D . 
CB 8 HOH 8   608  2356 HOH HOH D . 
CB 8 HOH 9   609  2454 HOH HOH D . 
CB 8 HOH 10  610  2272 HOH HOH D . 
CB 8 HOH 11  611  2172 HOH HOH D . 
CB 8 HOH 12  612  2417 HOH HOH D . 
CB 8 HOH 13  613  2024 HOH HOH D . 
CB 8 HOH 14  614  2210 HOH HOH D . 
CB 8 HOH 15  615  2338 HOH HOH D . 
CB 8 HOH 16  616  2371 HOH HOH D . 
CB 8 HOH 17  617  2123 HOH HOH D . 
CB 8 HOH 18  618  2369 HOH HOH D . 
CB 8 HOH 19  619  2279 HOH HOH D . 
CB 8 HOH 20  620  2035 HOH HOH D . 
CB 8 HOH 21  621  2306 HOH HOH D . 
CB 8 HOH 22  622  2214 HOH HOH D . 
CB 8 HOH 23  623  2367 HOH HOH D . 
CB 8 HOH 24  624  2256 HOH HOH D . 
CB 8 HOH 25  625  2299 HOH HOH D . 
CB 8 HOH 26  626  2036 HOH HOH D . 
CB 8 HOH 27  627  2396 HOH HOH D . 
CB 8 HOH 28  628  2130 HOH HOH D . 
CB 8 HOH 29  629  2447 HOH HOH D . 
CB 8 HOH 30  630  2398 HOH HOH D . 
CB 8 HOH 31  631  2040 HOH HOH D . 
CB 8 HOH 32  632  2394 HOH HOH D . 
CB 8 HOH 33  633  2303 HOH HOH D . 
CB 8 HOH 34  634  2302 HOH HOH D . 
CB 8 HOH 35  635  2364 HOH HOH D . 
CB 8 HOH 36  636  2344 HOH HOH D . 
CB 8 HOH 37  637  2114 HOH HOH D . 
CB 8 HOH 38  638  2176 HOH HOH D . 
CB 8 HOH 39  639  2057 HOH HOH D . 
CB 8 HOH 40  640  2068 HOH HOH D . 
CB 8 HOH 41  641  2397 HOH HOH D . 
CB 8 HOH 42  642  2158 HOH HOH D . 
CB 8 HOH 43  643  2258 HOH HOH D . 
CB 8 HOH 44  644  2355 HOH HOH D . 
CB 8 HOH 45  645  2287 HOH HOH D . 
CB 8 HOH 46  646  2426 HOH HOH D . 
CB 8 HOH 47  647  2326 HOH HOH D . 
CB 8 HOH 48  648  2361 HOH HOH D . 
CB 8 HOH 49  649  2260 HOH HOH D . 
CB 8 HOH 50  650  2127 HOH HOH D . 
CB 8 HOH 51  651  2246 HOH HOH D . 
CB 8 HOH 52  652  2078 HOH HOH D . 
CB 8 HOH 53  653  2116 HOH HOH D . 
CB 8 HOH 54  654  2309 HOH HOH D . 
CB 8 HOH 55  655  2317 HOH HOH D . 
CB 8 HOH 56  656  2263 HOH HOH D . 
CB 8 HOH 57  657  2222 HOH HOH D . 
CB 8 HOH 58  658  2391 HOH HOH D . 
CB 8 HOH 59  659  2084 HOH HOH D . 
CB 8 HOH 60  660  2407 HOH HOH D . 
CB 8 HOH 61  661  2405 HOH HOH D . 
CB 8 HOH 62  662  2213 HOH HOH D . 
CB 8 HOH 63  663  2178 HOH HOH D . 
CB 8 HOH 64  664  2138 HOH HOH D . 
CB 8 HOH 65  665  2109 HOH HOH D . 
CB 8 HOH 66  666  2436 HOH HOH D . 
CB 8 HOH 67  667  2254 HOH HOH D . 
CB 8 HOH 68  668  2433 HOH HOH D . 
CB 8 HOH 69  669  2444 HOH HOH D . 
CB 8 HOH 70  670  2305 HOH HOH D . 
CB 8 HOH 71  671  2022 HOH HOH D . 
CB 8 HOH 72  672  2275 HOH HOH D . 
CB 8 HOH 73  673  2337 HOH HOH D . 
CB 8 HOH 74  674  2248 HOH HOH D . 
CB 8 HOH 75  675  2451 HOH HOH D . 
CB 8 HOH 76  676  2018 HOH HOH D . 
CB 8 HOH 77  677  2318 HOH HOH D . 
CB 8 HOH 78  678  2422 HOH HOH D . 
CB 8 HOH 79  679  2240 HOH HOH D . 
CB 8 HOH 80  680  2235 HOH HOH D . 
CB 8 HOH 81  681  2429 HOH HOH D . 
CB 8 HOH 82  682  2403 HOH HOH D . 
CB 8 HOH 83  683  2314 HOH HOH D . 
CB 8 HOH 84  684  2137 HOH HOH D . 
CB 8 HOH 85  685  2339 HOH HOH D . 
CB 8 HOH 86  686  2443 HOH HOH D . 
CB 8 HOH 87  687  2010 HOH HOH D . 
CB 8 HOH 88  688  2449 HOH HOH D . 
CB 8 HOH 89  689  2012 HOH HOH D . 
CB 8 HOH 90  690  2285 HOH HOH D . 
CB 8 HOH 91  691  2322 HOH HOH D . 
CB 8 HOH 92  692  2148 HOH HOH D . 
CB 8 HOH 93  693  2079 HOH HOH D . 
CB 8 HOH 94  694  2424 HOH HOH D . 
CB 8 HOH 95  695  2376 HOH HOH D . 
CB 8 HOH 96  696  2169 HOH HOH D . 
CB 8 HOH 97  697  2375 HOH HOH D . 
CB 8 HOH 98  698  2273 HOH HOH D . 
CB 8 HOH 99  699  2061 HOH HOH D . 
CB 8 HOH 100 700  2039 HOH HOH D . 
CB 8 HOH 101 701  2160 HOH HOH D . 
CB 8 HOH 102 702  2323 HOH HOH D . 
CB 8 HOH 103 703  2329 HOH HOH D . 
CB 8 HOH 104 704  2353 HOH HOH D . 
CB 8 HOH 105 705  2016 HOH HOH D . 
CB 8 HOH 106 706  2308 HOH HOH D . 
CB 8 HOH 107 707  2442 HOH HOH D . 
CB 8 HOH 108 708  2298 HOH HOH D . 
CB 8 HOH 109 709  2313 HOH HOH D . 
CB 8 HOH 110 710  2452 HOH HOH D . 
CB 8 HOH 111 711  2271 HOH HOH D . 
CB 8 HOH 112 712  2381 HOH HOH D . 
CB 8 HOH 113 713  2259 HOH HOH D . 
CB 8 HOH 114 714  2173 HOH HOH D . 
CB 8 HOH 115 715  2185 HOH HOH D . 
CB 8 HOH 116 716  2245 HOH HOH D . 
CB 8 HOH 117 717  2215 HOH HOH D . 
CB 8 HOH 118 718  2147 HOH HOH D . 
CB 8 HOH 119 719  2253 HOH HOH D . 
CB 8 HOH 120 720  2342 HOH HOH D . 
CB 8 HOH 121 721  2135 HOH HOH D . 
CB 8 HOH 122 722  2416 HOH HOH D . 
CB 8 HOH 123 723  2294 HOH HOH D . 
CB 8 HOH 124 724  2345 HOH HOH D . 
CB 8 HOH 125 725  2437 HOH HOH D . 
CB 8 HOH 126 726  2425 HOH HOH D . 
CB 8 HOH 127 727  2200 HOH HOH D . 
CB 8 HOH 128 728  2239 HOH HOH D . 
CB 8 HOH 129 729  2362 HOH HOH D . 
CB 8 HOH 130 730  2209 HOH HOH D . 
CB 8 HOH 131 731  2126 HOH HOH D . 
CB 8 HOH 132 732  2352 HOH HOH D . 
CB 8 HOH 133 733  2292 HOH HOH D . 
CB 8 HOH 134 734  2330 HOH HOH D . 
CB 8 HOH 135 735  2216 HOH HOH D . 
CB 8 HOH 136 736  2390 HOH HOH D . 
CB 8 HOH 137 737  2067 HOH HOH D . 
CB 8 HOH 138 738  2267 HOH HOH D . 
CB 8 HOH 139 739  2278 HOH HOH D . 
CB 8 HOH 140 740  2307 HOH HOH D . 
CB 8 HOH 141 741  2282 HOH HOH D . 
CB 8 HOH 142 742  2021 HOH HOH D . 
CB 8 HOH 143 743  2237 HOH HOH D . 
CB 8 HOH 144 744  2295 HOH HOH D . 
CB 8 HOH 145 745  2349 HOH HOH D . 
CB 8 HOH 146 746  2374 HOH HOH D . 
CB 8 HOH 147 747  2001 HOH HOH D . 
CB 8 HOH 148 748  2270 HOH HOH D . 
CB 8 HOH 149 749  2368 HOH HOH D . 
CB 8 HOH 150 750  2190 HOH HOH D . 
CB 8 HOH 151 751  2133 HOH HOH D . 
CB 8 HOH 152 752  2350 HOH HOH D . 
CB 8 HOH 153 753  2450 HOH HOH D . 
CB 8 HOH 154 754  2165 HOH HOH D . 
CB 8 HOH 155 755  2082 HOH HOH D . 
CB 8 HOH 156 756  2357 HOH HOH D . 
CB 8 HOH 157 757  2291 HOH HOH D . 
CB 8 HOH 158 758  2392 HOH HOH D . 
CB 8 HOH 159 759  2315 HOH HOH D . 
CB 8 HOH 160 760  2380 HOH HOH D . 
CB 8 HOH 161 761  2373 HOH HOH D . 
CB 8 HOH 162 762  2206 HOH HOH D . 
CB 8 HOH 163 763  2439 HOH HOH D . 
CB 8 HOH 164 764  2118 HOH HOH D . 
CB 8 HOH 165 765  2009 HOH HOH D . 
CB 8 HOH 166 766  2341 HOH HOH D . 
CB 8 HOH 167 767  2088 HOH HOH D . 
CB 8 HOH 168 768  2023 HOH HOH D . 
CB 8 HOH 169 769  2269 HOH HOH D . 
CB 8 HOH 170 770  2435 HOH HOH D . 
CB 8 HOH 171 771  2288 HOH HOH D . 
CB 8 HOH 172 772  2333 HOH HOH D . 
CB 8 HOH 173 773  2143 HOH HOH D . 
CB 8 HOH 174 774  2193 HOH HOH D . 
CB 8 HOH 175 775  2025 HOH HOH D . 
CB 8 HOH 176 776  2427 HOH HOH D . 
CB 8 HOH 177 777  2266 HOH HOH D . 
CB 8 HOH 178 778  2301 HOH HOH D . 
CB 8 HOH 179 779  2312 HOH HOH D . 
CB 8 HOH 180 780  2393 HOH HOH D . 
CB 8 HOH 181 781  2234 HOH HOH D . 
CB 8 HOH 182 782  2091 HOH HOH D . 
CB 8 HOH 183 783  2384 HOH HOH D . 
CB 8 HOH 184 784  2414 HOH HOH D . 
CB 8 HOH 185 785  2327 HOH HOH D . 
CB 8 HOH 186 786  2003 HOH HOH D . 
CB 8 HOH 187 787  2274 HOH HOH D . 
CB 8 HOH 188 788  2098 HOH HOH D . 
CB 8 HOH 189 789  2099 HOH HOH D . 
CB 8 HOH 190 790  2296 HOH HOH D . 
CB 8 HOH 191 791  2382 HOH HOH D . 
CB 8 HOH 192 792  2020 HOH HOH D . 
CB 8 HOH 193 793  2331 HOH HOH D . 
CB 8 HOH 194 794  2159 HOH HOH D . 
CB 8 HOH 195 795  2041 HOH HOH D . 
CB 8 HOH 196 796  2004 HOH HOH D . 
CB 8 HOH 197 797  2404 HOH HOH D . 
CB 8 HOH 198 798  2243 HOH HOH D . 
CB 8 HOH 199 799  2170 HOH HOH D . 
CB 8 HOH 200 800  2189 HOH HOH D . 
CB 8 HOH 201 801  2167 HOH HOH D . 
CB 8 HOH 202 802  2280 HOH HOH D . 
CB 8 HOH 203 803  2456 HOH HOH D . 
CB 8 HOH 204 804  2037 HOH HOH D . 
CB 8 HOH 205 805  2142 HOH HOH D . 
CB 8 HOH 206 806  2046 HOH HOH D . 
CB 8 HOH 207 807  2014 HOH HOH D . 
CB 8 HOH 208 808  2286 HOH HOH D . 
CB 8 HOH 209 809  2457 HOH HOH D . 
CB 8 HOH 210 810  2043 HOH HOH D . 
CB 8 HOH 211 811  2150 HOH HOH D . 
CB 8 HOH 212 812  2188 HOH HOH D . 
CB 8 HOH 213 813  2238 HOH HOH D . 
CB 8 HOH 214 814  2262 HOH HOH D . 
CB 8 HOH 215 815  2232 HOH HOH D . 
CB 8 HOH 216 816  2446 HOH HOH D . 
CB 8 HOH 217 817  2201 HOH HOH D . 
CB 8 HOH 218 818  2031 HOH HOH D . 
CB 8 HOH 219 819  2360 HOH HOH D . 
CB 8 HOH 220 820  2094 HOH HOH D . 
CB 8 HOH 221 821  2348 HOH HOH D . 
CB 8 HOH 222 822  2265 HOH HOH D . 
CB 8 HOH 223 823  2401 HOH HOH D . 
CB 8 HOH 224 824  2343 HOH HOH D . 
CB 8 HOH 225 825  2141 HOH HOH D . 
CB 8 HOH 226 826  2121 HOH HOH D . 
CB 8 HOH 227 827  2048 HOH HOH D . 
CB 8 HOH 228 828  2366 HOH HOH D . 
CB 8 HOH 229 829  2423 HOH HOH D . 
CB 8 HOH 230 830  2445 HOH HOH D . 
CB 8 HOH 231 831  2441 HOH HOH D . 
CB 8 HOH 232 832  2406 HOH HOH D . 
CB 8 HOH 233 833  2180 HOH HOH D . 
CB 8 HOH 234 834  2255 HOH HOH D . 
CB 8 HOH 235 835  2276 HOH HOH D . 
CB 8 HOH 236 836  2247 HOH HOH D . 
CB 8 HOH 237 837  2038 HOH HOH D . 
CB 8 HOH 238 838  2008 HOH HOH D . 
CB 8 HOH 239 839  2249 HOH HOH D . 
CB 8 HOH 240 840  2430 HOH HOH D . 
CB 8 HOH 241 841  2261 HOH HOH D . 
CB 8 HOH 242 842  2223 HOH HOH D . 
CB 8 HOH 243 843  2197 HOH HOH D . 
CB 8 HOH 244 844  2300 HOH HOH D . 
CB 8 HOH 245 845  2049 HOH HOH D . 
CB 8 HOH 246 846  2320 HOH HOH D . 
CB 8 HOH 247 847  2440 HOH HOH D . 
CB 8 HOH 248 848  2310 HOH HOH D . 
CB 8 HOH 249 849  2324 HOH HOH D . 
CB 8 HOH 250 850  2304 HOH HOH D . 
CB 8 HOH 251 851  2415 HOH HOH D . 
CB 8 HOH 252 852  2359 HOH HOH D . 
CB 8 HOH 253 853  2073 HOH HOH D . 
CB 8 HOH 254 854  2388 HOH HOH D . 
CB 8 HOH 255 855  2125 HOH HOH D . 
CB 8 HOH 256 856  2101 HOH HOH D . 
CB 8 HOH 257 857  2385 HOH HOH D . 
CB 8 HOH 258 858  2111 HOH HOH D . 
CB 8 HOH 259 859  2428 HOH HOH D . 
CB 8 HOH 260 860  2002 HOH HOH D . 
CB 8 HOH 261 861  2227 HOH HOH D . 
CB 8 HOH 262 862  2379 HOH HOH D . 
CB 8 HOH 263 863  2015 HOH HOH D . 
CB 8 HOH 264 864  2351 HOH HOH D . 
CB 8 HOH 265 865  2011 HOH HOH D . 
CB 8 HOH 266 866  2408 HOH HOH D . 
CB 8 HOH 267 867  2086 HOH HOH D . 
CB 8 HOH 268 868  2199 HOH HOH D . 
CB 8 HOH 269 869  2013 HOH HOH D . 
CB 8 HOH 270 870  2019 HOH HOH D . 
CB 8 HOH 271 871  2446 HOH HOH D . 
CB 8 HOH 272 872  2358 HOH HOH D . 
CB 8 HOH 273 873  2455 HOH HOH D . 
CB 8 HOH 274 874  2224 HOH HOH D . 
CB 8 HOH 275 875  2377 HOH HOH D . 
CB 8 HOH 276 876  2431 HOH HOH D . 
CB 8 HOH 277 877  2321 HOH HOH D . 
CB 8 HOH 278 878  2347 HOH HOH D . 
CB 8 HOH 279 879  2095 HOH HOH D . 
CB 8 HOH 280 880  2251 HOH HOH D . 
CB 8 HOH 281 881  2354 HOH HOH D . 
CB 8 HOH 282 882  2334 HOH HOH D . 
CB 8 HOH 283 883  2028 HOH HOH D . 
CB 8 HOH 284 884  2134 HOH HOH D . 
CB 8 HOH 285 885  2283 HOH HOH D . 
CB 8 HOH 286 886  2409 HOH HOH D . 
CB 8 HOH 287 887  2252 HOH HOH D . 
CB 8 HOH 288 888  2191 HOH HOH D . 
CB 8 HOH 289 889  2151 HOH HOH D . 
CB 8 HOH 290 890  2171 HOH HOH D . 
CB 8 HOH 291 891  2149 HOH HOH D . 
CB 8 HOH 292 892  2316 HOH HOH D . 
CB 8 HOH 293 893  2034 HOH HOH D . 
CB 8 HOH 294 894  2378 HOH HOH D . 
CB 8 HOH 295 895  2087 HOH HOH D . 
CB 8 HOH 296 896  2458 HOH HOH D . 
CB 8 HOH 297 897  2293 HOH HOH D . 
CB 8 HOH 298 898  2241 HOH HOH D . 
CB 8 HOH 299 899  2418 HOH HOH D . 
CB 8 HOH 300 900  2410 HOH HOH D . 
CB 8 HOH 301 901  2089 HOH HOH D . 
CB 8 HOH 302 902  2434 HOH HOH D . 
CB 8 HOH 303 903  2195 HOH HOH D . 
CB 8 HOH 304 904  2257 HOH HOH D . 
CB 8 HOH 305 905  2093 HOH HOH D . 
CB 8 HOH 306 906  2328 HOH HOH D . 
CB 8 HOH 307 907  2438 HOH HOH D . 
CB 8 HOH 308 908  2179 HOH HOH D . 
CB 8 HOH 309 909  2074 HOH HOH D . 
CB 8 HOH 310 910  2194 HOH HOH D . 
CB 8 HOH 311 911  2453 HOH HOH D . 
CB 8 HOH 312 912  2386 HOH HOH D . 
CB 8 HOH 313 913  2175 HOH HOH D . 
CB 8 HOH 314 914  2332 HOH HOH D . 
CB 8 HOH 315 915  2335 HOH HOH D . 
CB 8 HOH 316 916  2459 HOH HOH D . 
CB 8 HOH 317 917  2289 HOH HOH D . 
CB 8 HOH 318 918  2346 HOH HOH D . 
CB 8 HOH 319 919  2421 HOH HOH D . 
CB 8 HOH 320 920  2284 HOH HOH D . 
CB 8 HOH 321 921  2268 HOH HOH D . 
CB 8 HOH 322 922  2413 HOH HOH D . 
CB 8 HOH 323 923  2412 HOH HOH D . 
CB 8 HOH 324 924  2281 HOH HOH D . 
CB 8 HOH 325 925  2395 HOH HOH D . 
CB 8 HOH 326 926  2017 HOH HOH D . 
CB 8 HOH 327 927  2166 HOH HOH D . 
CB 8 HOH 328 928  2117 HOH HOH D . 
CB 8 HOH 329 929  2085 HOH HOH D . 
CB 8 HOH 330 930  2311 HOH HOH D . 
CB 8 HOH 331 931  2242 HOH HOH D . 
CB 8 HOH 332 932  2383 HOH HOH D . 
CB 8 HOH 333 933  2400 HOH HOH D . 
CB 8 HOH 334 934  2177 HOH HOH D . 
CB 8 HOH 335 935  2387 HOH HOH D . 
CB 8 HOH 336 936  2420 HOH HOH D . 
CB 8 HOH 337 937  2115 HOH HOH D . 
CB 8 HOH 338 938  2026 HOH HOH D . 
CB 8 HOH 339 939  2325 HOH HOH D . 
CB 8 HOH 340 940  2461 HOH HOH D . 
CB 8 HOH 341 941  2277 HOH HOH D . 
CB 8 HOH 342 942  2250 HOH HOH D . 
CB 8 HOH 343 943  2402 HOH HOH D . 
CB 8 HOH 344 944  2411 HOH HOH D . 
CB 8 HOH 345 945  2198 HOH HOH D . 
CB 8 HOH 346 946  2389 HOH HOH D . 
CB 8 HOH 347 947  2090 HOH HOH D . 
CB 8 HOH 348 948  2340 HOH HOH D . 
CB 8 HOH 349 949  2448 HOH HOH D . 
CB 8 HOH 350 950  2290 HOH HOH D . 
CB 8 HOH 351 951  2432 HOH HOH D . 
CB 8 HOH 352 952  2096 HOH HOH D . 
CB 8 HOH 353 953  2372 HOH HOH D . 
CB 8 HOH 354 954  2236 HOH HOH D . 
CB 8 HOH 355 955  2447 HOH HOH D . 
CB 8 HOH 356 956  2336 HOH HOH D . 
CB 8 HOH 357 957  2005 HOH HOH D . 
CB 8 HOH 358 958  2042 HOH HOH D . 
CB 8 HOH 359 959  2370 HOH HOH D . 
CB 8 HOH 360 960  2072 HOH HOH D . 
CB 8 HOH 361 961  2007 HOH HOH D . 
CB 8 HOH 362 962  2399 HOH HOH D . 
CB 8 HOH 363 963  2168 HOH HOH D . 
CB 8 HOH 364 964  2319 HOH HOH D . 
CB 8 HOH 365 965  2112 HOH HOH D . 
CB 8 HOH 366 966  2365 HOH HOH D . 
CB 8 HOH 367 967  2006 HOH HOH D . 
CB 8 HOH 368 968  2220 HOH HOH D . 
CB 8 HOH 369 969  2419 HOH HOH D . 
CB 8 HOH 370 970  2202 HOH HOH D . 
CB 8 HOH 371 971  2244 HOH HOH D . 
CB 8 HOH 372 972  2107 HOH HOH D . 
CB 8 HOH 373 973  2108 HOH HOH D . 
CB 8 HOH 374 974  2129 HOH HOH D . 
CB 8 HOH 375 975  2097 HOH HOH D . 
CB 8 HOH 376 976  2196 HOH HOH D . 
CB 8 HOH 377 977  2139 HOH HOH D . 
CB 8 HOH 378 978  2076 HOH HOH D . 
CB 8 HOH 379 979  2264 HOH HOH D . 
CB 8 HOH 380 980  2106 HOH HOH D . 
CB 8 HOH 381 981  2205 HOH HOH D . 
CB 8 HOH 382 982  2140 HOH HOH D . 
CB 8 HOH 383 983  2069 HOH HOH D . 
CB 8 HOH 384 984  2163 HOH HOH D . 
CB 8 HOH 385 985  2105 HOH HOH D . 
CB 8 HOH 386 986  2080 HOH HOH D . 
CB 8 HOH 387 987  2128 HOH HOH D . 
CB 8 HOH 388 988  2060 HOH HOH D . 
CB 8 HOH 389 989  2092 HOH HOH D . 
CB 8 HOH 390 990  2058 HOH HOH D . 
CB 8 HOH 391 991  2153 HOH HOH D . 
CB 8 HOH 392 992  2225 HOH HOH D . 
CB 8 HOH 393 993  2183 HOH HOH D . 
CB 8 HOH 394 994  2192 HOH HOH D . 
CB 8 HOH 395 995  2156 HOH HOH D . 
CB 8 HOH 396 996  2122 HOH HOH D . 
CB 8 HOH 397 997  2054 HOH HOH D . 
CB 8 HOH 398 998  2157 HOH HOH D . 
CB 8 HOH 399 999  2174 HOH HOH D . 
CB 8 HOH 400 1000 2032 HOH HOH D . 
CB 8 HOH 401 1001 2132 HOH HOH D . 
CB 8 HOH 402 1002 2056 HOH HOH D . 
CB 8 HOH 403 1003 2181 HOH HOH D . 
CB 8 HOH 404 1004 2124 HOH HOH D . 
CB 8 HOH 405 1005 2063 HOH HOH D . 
CB 8 HOH 406 1006 2052 HOH HOH D . 
CB 8 HOH 407 1007 2131 HOH HOH D . 
CB 8 HOH 408 1008 2203 HOH HOH D . 
CB 8 HOH 409 1009 2100 HOH HOH D . 
CB 8 HOH 410 1010 2136 HOH HOH D . 
CB 8 HOH 411 1011 2030 HOH HOH D . 
CB 8 HOH 412 1012 2155 HOH HOH D . 
CB 8 HOH 413 1013 2233 HOH HOH D . 
CB 8 HOH 414 1014 2219 HOH HOH D . 
CB 8 HOH 415 1015 2085 HOH HOH D . 
CB 8 HOH 416 1016 2055 HOH HOH D . 
CB 8 HOH 417 1017 2050 HOH HOH D . 
CB 8 HOH 418 1018 2059 HOH HOH D . 
CB 8 HOH 419 1019 2211 HOH HOH D . 
CB 8 HOH 420 1020 2164 HOH HOH D . 
CB 8 HOH 421 1021 2065 HOH HOH D . 
CB 8 HOH 422 1022 2207 HOH HOH D . 
CB 8 HOH 423 1023 2221 HOH HOH D . 
CB 8 HOH 424 1024 2113 HOH HOH D . 
CB 8 HOH 425 1025 2070 HOH HOH D . 
CB 8 HOH 426 1026 2186 HOH HOH D . 
CB 8 HOH 427 1027 2033 HOH HOH D . 
CB 8 HOH 428 1028 2044 HOH HOH D . 
CB 8 HOH 429 1029 2229 HOH HOH D . 
CB 8 HOH 430 1030 2144 HOH HOH D . 
CB 8 HOH 431 1031 2217 HOH HOH D . 
CB 8 HOH 432 1032 2218 HOH HOH D . 
CB 8 HOH 433 1033 2184 HOH HOH D . 
CB 8 HOH 434 1034 2062 HOH HOH D . 
CB 8 HOH 435 1035 2208 HOH HOH D . 
CB 8 HOH 436 1036 2161 HOH HOH D . 
CB 8 HOH 437 1037 2081 HOH HOH D . 
CB 8 HOH 438 1038 2230 HOH HOH D . 
CB 8 HOH 439 1039 2204 HOH HOH D . 
CB 8 HOH 440 1040 2187 HOH HOH D . 
CB 8 HOH 441 1041 2145 HOH HOH D . 
CB 8 HOH 442 1042 2119 HOH HOH D . 
# 
loop_
_pdbx_struct_mod_residue.id 
_pdbx_struct_mod_residue.label_asym_id 
_pdbx_struct_mod_residue.label_comp_id 
_pdbx_struct_mod_residue.label_seq_id 
_pdbx_struct_mod_residue.auth_asym_id 
_pdbx_struct_mod_residue.auth_comp_id 
_pdbx_struct_mod_residue.auth_seq_id 
_pdbx_struct_mod_residue.PDB_ins_code 
_pdbx_struct_mod_residue.parent_comp_id 
_pdbx_struct_mod_residue.details 
1 A ASN 5   A ASN 92  ? ASN 'GLYCOSYLATION SITE' 
2 A ASN 65  A ASN 152 ? ASN 'GLYCOSYLATION SITE' 
3 A ASN 120 A ASN 207 ? ASN 'GLYCOSYLATION SITE' 
4 B ASN 65  B ASN 152 ? ASN 'GLYCOSYLATION SITE' 
5 C ASN 65  C ASN 152 ? ASN 'GLYCOSYLATION SITE' 
6 C ASN 120 C ASN 207 ? ASN 'GLYCOSYLATION SITE' 
7 D ASN 65  D ASN 152 ? ASN 'GLYCOSYLATION SITE' 
8 D ASN 120 D ASN 207 ? ASN 'GLYCOSYLATION SITE' 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PQS 
_pdbx_struct_assembly.oligomeric_details   tetrameric 
_pdbx_struct_assembly.oligomeric_count     4 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      
;A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S,T,U,V,W,X,Y,Z,AA,BA,CA,DA,EA,FA,GA,HA,IA,JA,KA,LA,MA,NA,OA,PA,QA,RA,SA,TA,UA,VA,WA,XA,YA,ZA,AB,BB,CB
;
# 
_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  O   ? A  ASP 213 ? A ASP 300  ? 1_555 CA ? E  CA . ? A CA 501 ? 1_555 O   ? A  GLY 217 ? A GLY 304  ? 1_555 84.8  ? 
2  O   ? A  ASP 213 ? A ASP 300  ? 1_555 CA ? E  CA . ? A CA 501 ? 1_555 OD2 ? A  ASP 244 ? A ASP 331  ? 1_555 97.3  ? 
3  O   ? A  GLY 217 ? A GLY 304  ? 1_555 CA ? E  CA . ? A CA 501 ? 1_555 OD2 ? A  ASP 244 ? A ASP 331  ? 1_555 96.8  ? 
4  O   ? A  ASP 213 ? A ASP 300  ? 1_555 CA ? E  CA . ? A CA 501 ? 1_555 O   ? A  PRO 267 ? A PRO 354  ? 1_555 96.1  ? 
5  O   ? A  GLY 217 ? A GLY 304  ? 1_555 CA ? E  CA . ? A CA 501 ? 1_555 O   ? A  PRO 267 ? A PRO 354  ? 1_555 157.4 ? 
6  OD2 ? A  ASP 244 ? A ASP 331  ? 1_555 CA ? E  CA . ? A CA 501 ? 1_555 O   ? A  PRO 267 ? A PRO 354  ? 1_555 105.5 ? 
7  O   ? A  ASP 213 ? A ASP 300  ? 1_555 CA ? E  CA . ? A CA 501 ? 1_555 O   ? ZA HOH .   ? A HOH 2420 ? 1_555 164.6 ? 
8  O   ? A  GLY 217 ? A GLY 304  ? 1_555 CA ? E  CA . ? A CA 501 ? 1_555 O   ? ZA HOH .   ? A HOH 2420 ? 1_555 89.3  ? 
9  OD2 ? A  ASP 244 ? A ASP 331  ? 1_555 CA ? E  CA . ? A CA 501 ? 1_555 O   ? ZA HOH .   ? A HOH 2420 ? 1_555 97.6  ? 
10 O   ? A  PRO 267 ? A PRO 354  ? 1_555 CA ? E  CA . ? A CA 501 ? 1_555 O   ? ZA HOH .   ? A HOH 2420 ? 1_555 84.0  ? 
11 O   ? A  ASP 213 ? A ASP 300  ? 1_555 CA ? E  CA . ? A CA 501 ? 1_555 O   ? ZA HOH .   ? A HOH 2519 ? 1_555 84.9  ? 
12 O   ? A  GLY 217 ? A GLY 304  ? 1_555 CA ? E  CA . ? A CA 501 ? 1_555 O   ? ZA HOH .   ? A HOH 2519 ? 1_555 95.8  ? 
13 OD2 ? A  ASP 244 ? A ASP 331  ? 1_555 CA ? E  CA . ? A CA 501 ? 1_555 O   ? ZA HOH .   ? A HOH 2519 ? 1_555 167.4 ? 
14 O   ? A  PRO 267 ? A PRO 354  ? 1_555 CA ? E  CA . ? A CA 501 ? 1_555 O   ? ZA HOH .   ? A HOH 2519 ? 1_555 61.9  ? 
15 O   ? ZA HOH .   ? A HOH 2420 ? 1_555 CA ? E  CA . ? A CA 501 ? 1_555 O   ? ZA HOH .   ? A HOH 2519 ? 1_555 81.6  ? 
16 O   ? B  ASP 213 ? B ASP 300  ? 1_555 CA ? Z  CA . ? B CA 501 ? 1_555 O   ? B  GLY 217 ? B GLY 304  ? 1_555 86.0  ? 
17 O   ? B  ASP 213 ? B ASP 300  ? 1_555 CA ? Z  CA . ? B CA 501 ? 1_555 OD2 ? B  ASP 244 ? B ASP 331  ? 1_555 95.5  ? 
18 O   ? B  GLY 217 ? B GLY 304  ? 1_555 CA ? Z  CA . ? B CA 501 ? 1_555 OD2 ? B  ASP 244 ? B ASP 331  ? 1_555 94.9  ? 
19 O   ? B  ASP 213 ? B ASP 300  ? 1_555 CA ? Z  CA . ? B CA 501 ? 1_555 O   ? B  PRO 267 ? B PRO 354  ? 1_555 94.9  ? 
20 O   ? B  GLY 217 ? B GLY 304  ? 1_555 CA ? Z  CA . ? B CA 501 ? 1_555 O   ? B  PRO 267 ? B PRO 354  ? 1_555 160.4 ? 
21 OD2 ? B  ASP 244 ? B ASP 331  ? 1_555 CA ? Z  CA . ? B CA 501 ? 1_555 O   ? B  PRO 267 ? B PRO 354  ? 1_555 104.6 ? 
22 O   ? B  ASP 213 ? B ASP 300  ? 1_555 CA ? Z  CA . ? B CA 501 ? 1_555 O   ? AB HOH .   ? B HOH 763  ? 1_555 79.2  ? 
23 O   ? B  GLY 217 ? B GLY 304  ? 1_555 CA ? Z  CA . ? B CA 501 ? 1_555 O   ? AB HOH .   ? B HOH 763  ? 1_555 95.2  ? 
24 OD2 ? B  ASP 244 ? B ASP 331  ? 1_555 CA ? Z  CA . ? B CA 501 ? 1_555 O   ? AB HOH .   ? B HOH 763  ? 1_555 168.3 ? 
25 O   ? B  PRO 267 ? B PRO 354  ? 1_555 CA ? Z  CA . ? B CA 501 ? 1_555 O   ? AB HOH .   ? B HOH 763  ? 1_555 65.8  ? 
26 O   ? B  ASP 213 ? B ASP 300  ? 1_555 CA ? Z  CA . ? B CA 501 ? 1_555 O   ? AB HOH .   ? B HOH 738  ? 1_555 165.5 ? 
27 O   ? B  GLY 217 ? B GLY 304  ? 1_555 CA ? Z  CA . ? B CA 501 ? 1_555 O   ? AB HOH .   ? B HOH 738  ? 1_555 88.4  ? 
28 OD2 ? B  ASP 244 ? B ASP 331  ? 1_555 CA ? Z  CA . ? B CA 501 ? 1_555 O   ? AB HOH .   ? B HOH 738  ? 1_555 98.2  ? 
29 O   ? B  PRO 267 ? B PRO 354  ? 1_555 CA ? Z  CA . ? B CA 501 ? 1_555 O   ? AB HOH .   ? B HOH 738  ? 1_555 86.0  ? 
30 O   ? AB HOH .   ? B HOH 763  ? 1_555 CA ? Z  CA . ? B CA 501 ? 1_555 O   ? AB HOH .   ? B HOH 738  ? 1_555 88.1  ? 
31 O   ? C  ASP 213 ? C ASP 300  ? 1_555 CA ? JA CA . ? C CA 502 ? 1_555 O   ? C  GLY 217 ? C GLY 304  ? 1_555 87.8  ? 
32 O   ? C  ASP 213 ? C ASP 300  ? 1_555 CA ? JA CA . ? C CA 502 ? 1_555 OD2 ? C  ASP 244 ? C ASP 331  ? 1_555 94.8  ? 
33 O   ? C  GLY 217 ? C GLY 304  ? 1_555 CA ? JA CA . ? C CA 502 ? 1_555 OD2 ? C  ASP 244 ? C ASP 331  ? 1_555 99.2  ? 
34 O   ? C  ASP 213 ? C ASP 300  ? 1_555 CA ? JA CA . ? C CA 502 ? 1_555 O   ? C  PRO 267 ? C PRO 354  ? 1_555 96.6  ? 
35 O   ? C  GLY 217 ? C GLY 304  ? 1_555 CA ? JA CA . ? C CA 502 ? 1_555 O   ? C  PRO 267 ? C PRO 354  ? 1_555 159.1 ? 
36 OD2 ? C  ASP 244 ? C ASP 331  ? 1_555 CA ? JA CA . ? C CA 502 ? 1_555 O   ? C  PRO 267 ? C PRO 354  ? 1_555 100.8 ? 
37 O   ? C  ASP 213 ? C ASP 300  ? 1_555 CA ? JA CA . ? C CA 502 ? 1_555 O   ? BB HOH .   ? C HOH 684  ? 1_555 168.6 ? 
38 O   ? C  GLY 217 ? C GLY 304  ? 1_555 CA ? JA CA . ? C CA 502 ? 1_555 O   ? BB HOH .   ? C HOH 684  ? 1_555 92.2  ? 
39 OD2 ? C  ASP 244 ? C ASP 331  ? 1_555 CA ? JA CA . ? C CA 502 ? 1_555 O   ? BB HOH .   ? C HOH 684  ? 1_555 96.4  ? 
40 O   ? C  PRO 267 ? C PRO 354  ? 1_555 CA ? JA CA . ? C CA 502 ? 1_555 O   ? BB HOH .   ? C HOH 684  ? 1_555 79.5  ? 
41 O   ? C  ASP 213 ? C ASP 300  ? 1_555 CA ? JA CA . ? C CA 502 ? 1_555 O   ? BB HOH .   ? C HOH 745  ? 1_555 89.3  ? 
42 O   ? C  GLY 217 ? C GLY 304  ? 1_555 CA ? JA CA . ? C CA 502 ? 1_555 O   ? BB HOH .   ? C HOH 745  ? 1_555 100.8 ? 
43 OD2 ? C  ASP 244 ? C ASP 331  ? 1_555 CA ? JA CA . ? C CA 502 ? 1_555 O   ? BB HOH .   ? C HOH 745  ? 1_555 159.7 ? 
44 O   ? C  PRO 267 ? C PRO 354  ? 1_555 CA ? JA CA . ? C CA 502 ? 1_555 O   ? BB HOH .   ? C HOH 745  ? 1_555 59.0  ? 
45 O   ? BB HOH .   ? C HOH 684  ? 1_555 CA ? JA CA . ? C CA 502 ? 1_555 O   ? BB HOH .   ? C HOH 745  ? 1_555 79.6  ? 
46 O   ? D  ASP 213 ? D ASP 300  ? 1_555 CA ? TA CA . ? D CA 504 ? 1_555 O   ? D  GLY 217 ? D GLY 304  ? 1_555 85.3  ? 
47 O   ? D  ASP 213 ? D ASP 300  ? 1_555 CA ? TA CA . ? D CA 504 ? 1_555 OD2 ? D  ASP 244 ? D ASP 331  ? 1_555 97.5  ? 
48 O   ? D  GLY 217 ? D GLY 304  ? 1_555 CA ? TA CA . ? D CA 504 ? 1_555 OD2 ? D  ASP 244 ? D ASP 331  ? 1_555 96.3  ? 
49 O   ? D  ASP 213 ? D ASP 300  ? 1_555 CA ? TA CA . ? D CA 504 ? 1_555 O   ? D  PRO 267 ? D PRO 354  ? 1_555 96.6  ? 
50 O   ? D  GLY 217 ? D GLY 304  ? 1_555 CA ? TA CA . ? D CA 504 ? 1_555 O   ? D  PRO 267 ? D PRO 354  ? 1_555 158.7 ? 
51 OD2 ? D  ASP 244 ? D ASP 331  ? 1_555 CA ? TA CA . ? D CA 504 ? 1_555 O   ? D  PRO 267 ? D PRO 354  ? 1_555 104.5 ? 
52 O   ? D  ASP 213 ? D ASP 300  ? 1_555 CA ? TA CA . ? D CA 504 ? 1_555 O   ? CB HOH .   ? D HOH 720  ? 1_555 82.9  ? 
53 O   ? D  GLY 217 ? D GLY 304  ? 1_555 CA ? TA CA . ? D CA 504 ? 1_555 O   ? CB HOH .   ? D HOH 720  ? 1_555 95.4  ? 
54 OD2 ? D  ASP 244 ? D ASP 331  ? 1_555 CA ? TA CA . ? D CA 504 ? 1_555 O   ? CB HOH .   ? D HOH 720  ? 1_555 168.3 ? 
55 O   ? D  PRO 267 ? D PRO 354  ? 1_555 CA ? TA CA . ? D CA 504 ? 1_555 O   ? CB HOH .   ? D HOH 720  ? 1_555 63.9  ? 
56 O   ? D  ASP 213 ? D ASP 300  ? 1_555 CA ? TA CA . ? D CA 504 ? 1_555 O   ? CB HOH .   ? D HOH 654  ? 1_555 165.8 ? 
57 O   ? D  GLY 217 ? D GLY 304  ? 1_555 CA ? TA CA . ? D CA 504 ? 1_555 O   ? CB HOH .   ? D HOH 654  ? 1_555 89.8  ? 
58 OD2 ? D  ASP 244 ? D ASP 331  ? 1_555 CA ? TA CA . ? D CA 504 ? 1_555 O   ? CB HOH .   ? D HOH 654  ? 1_555 96.3  ? 
59 O   ? D  PRO 267 ? D PRO 354  ? 1_555 CA ? TA CA . ? D CA 504 ? 1_555 O   ? CB HOH .   ? D HOH 654  ? 1_555 83.3  ? 
60 O   ? CB HOH .   ? D HOH 720  ? 1_555 CA ? TA CA . ? D CA 504 ? 1_555 O   ? CB HOH .   ? D HOH 654  ? 1_555 84.3  ? 
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2006-01-25 
2 'Structure model' 1 1 2011-05-08 
3 'Structure model' 1 2 2011-07-13 
4 'Structure model' 2 0 2017-07-12 
# 
_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_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Version format compliance' 
2 3 'Structure model' 'Version format compliance' 
3 4 'Structure model' Advisory                    
4 4 'Structure model' 'Atomic model'              
5 4 'Structure model' 'Data collection'           
6 4 'Structure model' 'Derived calculations'      
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 4 'Structure model' atom_site                    
2 4 'Structure model' diffrn_radiation             
3 4 'Structure model' pdbx_struct_conn_angle       
4 4 'Structure model' pdbx_unobs_or_zero_occ_atoms 
5 4 'Structure model' pdbx_validate_close_contact  
6 4 'Structure model' struct_conn                  
7 4 'Structure model' struct_site_gen              
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1  4 'Structure model' '_atom_site.B_iso_or_equiv'                   
2  4 'Structure model' '_atom_site.Cartn_x'                          
3  4 'Structure model' '_atom_site.Cartn_y'                          
4  4 'Structure model' '_atom_site.Cartn_z'                          
5  4 'Structure model' '_atom_site.auth_atom_id'                     
6  4 'Structure model' '_atom_site.auth_comp_id'                     
7  4 'Structure model' '_atom_site.auth_seq_id'                      
8  4 'Structure model' '_atom_site.label_asym_id'                    
9  4 'Structure model' '_atom_site.label_atom_id'                    
10 4 'Structure model' '_atom_site.label_comp_id'                    
11 4 'Structure model' '_atom_site.label_entity_id'                  
12 4 'Structure model' '_atom_site.type_symbol'                      
13 4 'Structure model' '_diffrn_radiation.pdbx_diffrn_protocol'      
14 4 'Structure model' '_pdbx_struct_conn_angle.ptnr1_auth_comp_id'  
15 4 'Structure model' '_pdbx_struct_conn_angle.ptnr1_auth_seq_id'   
16 4 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_asym_id' 
17 4 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_atom_id' 
18 4 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_comp_id' 
19 4 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_seq_id'  
20 4 'Structure model' '_pdbx_struct_conn_angle.ptnr3_auth_comp_id'  
21 4 'Structure model' '_pdbx_struct_conn_angle.ptnr3_auth_seq_id'   
22 4 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_asym_id' 
23 4 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_atom_id' 
24 4 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_comp_id' 
25 4 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_seq_id'  
26 4 'Structure model' '_pdbx_struct_conn_angle.value'               
27 4 'Structure model' '_struct_site_gen.label_asym_id'              
# 
loop_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
_software.date 
_software.type 
_software.location 
_software.language 
REFMAC    refinement       5.0 ? 1 ? ? ? ? 
DENZO     'data reduction' .   ? 2 ? ? ? ? 
SCALEPACK 'data scaling'   .   ? 3 ? ? ? ? 
AMoRE     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 NH2 B ARG 460  ? ? O  B HOH 603  ? ? 0.17 
2  1 O6  A MAN 519  ? ? O  A HOH 2646 ? ? 0.18 
3  1 NH1 C ARG 256  ? ? O  C HOH 606  ? ? 0.29 
4  1 NH1 A ARG 256  ? ? O  A HOH 2302 ? ? 0.31 
5  1 NH2 C ARG 256  ? ? O  C HOH 641  ? ? 0.40 
6  1 OD2 A ASP 353  ? ? O  A HOH 2301 ? ? 0.53 
7  1 OE2 C GLU 424  ? ? O  C HOH 601  ? ? 0.59 
8  1 NH2 B ARG 256  ? ? O  B HOH 601  ? ? 0.87 
9  1 OE1 C GLU 471  ? ? O  C HOH 602  ? ? 0.87 
10 1 O4  D MAN 509  ? ? O  D HOH 601  ? ? 0.93 
11 1 CZ  B ARG 460  ? ? O  B HOH 603  ? ? 1.25 
12 1 CD  C GLU 424  ? ? O  C HOH 601  ? ? 1.30 
13 1 OD1 D ASP 117  ? ? O  D HOH 602  ? ? 1.31 
14 1 CZ  A ARG 256  ? ? O  A HOH 2302 ? ? 1.45 
15 1 CZ  C ARG 256  ? ? O  C HOH 606  ? ? 1.55 
16 1 C6  A MAN 519  ? ? O  A HOH 2646 ? ? 1.57 
17 1 NH1 C ARG 460  ? ? O  C HOH 603  ? ? 1.60 
18 1 CZ  C ARG 256  ? ? O  C HOH 641  ? ? 1.72 
19 1 ND2 C ASN 207  ? ? C1 C NAG 507  ? ? 1.75 
20 1 ND2 C ASN 152  ? ? C1 C NAG 506  ? ? 1.75 
21 1 O3  A MAN 520  ? ? C1 A MAN 521  ? ? 1.81 
22 1 ND2 B ASN 152  ? ? C1 B NAG 504  ? ? 1.82 
23 1 CG  A ASP 353  ? ? O  A HOH 2301 ? ? 1.83 
24 1 O6  A MAN 507  ? ? C1 A MAN 508  ? ? 1.85 
25 1 ND2 D ASN 152  ? ? C1 D NAG 507  ? ? 1.85 
26 1 O   C HOH 767  ? ? O  C HOH 1000 ? ? 1.87 
27 1 ND2 D ASN 207  ? ? C1 D NAG 508  ? ? 1.89 
28 1 O6  B MAN 505  ? ? C1 B MAN 506  ? ? 1.90 
29 1 O   B HOH 639  ? ? O  B HOH 794  ? ? 1.90 
30 1 O3  A MAN 507  ? ? C1 A MAN 509  ? ? 1.92 
31 1 C1  A MAN 514  ? ? O6 A MAN 520  ? ? 1.92 
32 1 OE1 C GLU 424  ? ? O  C HOH 601  ? ? 1.94 
33 1 O4  A NAG 506  ? ? C1 A NAG 512  ? ? 1.94 
34 1 O   B ASP 468  ? ? O  B HOH 602  ? ? 1.97 
35 1 CZ  B ARG 256  ? ? O  B HOH 601  ? ? 2.03 
36 1 O   B HOH 942  ? ? O  B HOH 948  ? ? 2.07 
37 1 O   C HOH 715  ? ? O  C HOH 1004 ? ? 2.08 
38 1 O   C HOH 962  ? ? O  C HOH 1032 ? ? 2.11 
39 1 O   D HOH 894  ? ? O  D HOH 976  ? ? 2.12 
40 1 CD  C GLU 471  ? ? O  C HOH 602  ? ? 2.12 
41 1 O   D HOH 879  ? ? O  D HOH 1021 ? ? 2.14 
42 1 C1  B NAG 508  ? ? O4 D NAG 508  ? ? 2.15 
43 1 O   C HOH 638  ? ? O  C HOH 938  ? ? 2.15 
44 1 O   D HOH 899  ? ? O  D HOH 935  ? ? 2.17 
45 1 C4  D MAN 509  ? ? O  D HOH 601  ? ? 2.17 
46 1 NH1 B ARG 460  ? ? O  B HOH 603  ? ? 2.18 
47 1 O   A HOH 2605 ? ? O  A HOH 2740 ? ? 2.19 
48 1 O   D HOH 858  ? ? O  D HOH 928  ? ? 2.19 
49 1 O   C HOH 676  ? ? O  C HOH 848  ? ? 2.19 
# 
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 CA A LEU 128 ? ? CB A LEU 128 ? ? CG A LEU 128 ? ? 129.39 115.30 14.09 2.30 N 
2 1 CA B LEU 128 ? ? CB B LEU 128 ? ? CG B LEU 128 ? ? 129.99 115.30 14.69 2.30 N 
3 1 CA C LEU 128 ? ? CB C LEU 128 ? ? CG C LEU 128 ? ? 131.57 115.30 16.27 2.30 N 
4 1 CA D LEU 128 ? ? CB D LEU 128 ? ? CG D LEU 128 ? ? 130.71 115.30 15.41 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 A 207 ? ? -159.26 40.51   
2  1 ASN A 228 ? ? -150.83 77.03   
3  1 THR A 232 ? ? -145.58 -156.30 
4  1 LYS A 271 ? ? -170.25 146.29  
5  1 CYS A 298 ? ? -120.33 -166.36 
6  1 LYS A 322 ? ? -158.56 -156.29 
7  1 ASP A 363 ? ? -155.29 60.93   
8  1 SER A 410 ? ? -112.79 -133.43 
9  1 TRP A 466 ? ? -105.50 52.31   
10 1 LEU B 93  ? ? -85.63  44.49   
11 1 ASN B 207 ? ? -161.35 43.97   
12 1 THR B 232 ? ? -148.03 -157.52 
13 1 LYS B 303 ? ? -127.56 -58.31  
14 1 LYS B 322 ? ? -165.74 -159.05 
15 1 ASP B 363 ? ? -153.59 60.84   
16 1 SER B 410 ? ? -115.65 -131.72 
17 1 TRP B 466 ? ? -112.05 52.10   
18 1 ASN C 207 ? ? -159.55 41.48   
19 1 THR C 232 ? ? -142.09 -153.08 
20 1 LYS C 271 ? ? -170.85 147.22  
21 1 CYS C 298 ? ? -121.53 -168.75 
22 1 LYS C 322 ? ? -165.92 -158.36 
23 1 SER C 410 ? ? -114.04 -135.20 
24 1 TRP C 466 ? ? -103.82 52.62   
25 1 ASN D 207 ? ? -157.82 38.99   
26 1 ASN D 228 ? ? -150.38 79.55   
27 1 THR D 232 ? ? -143.57 -156.51 
28 1 LYS D 271 ? ? -175.43 146.31  
29 1 CYS D 298 ? ? -121.88 -167.72 
30 1 LYS D 303 ? ? -129.94 -56.44  
31 1 LYS D 322 ? ? -160.42 -154.94 
32 1 ASP D 363 ? ? -156.22 61.01   
33 1 SER D 410 ? ? -111.44 -131.70 
34 1 TRP D 466 ? ? -107.22 52.14   
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? C HOH 1053 ? 5.83 . 
2 1 O ? C HOH 1054 ? 6.39 . 
3 1 O ? D HOH 1042 ? 7.55 . 
# 
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 N 1 A NAG 506 ? O1 ? J  NAG 1 O1 
2  1 N 1 A NAG 512 ? O1 ? K  NAG 4 O1 
3  1 N 1 A MAN 508 ? O1 ? O  MAN 1 O1 
4  1 N 1 A MAN 509 ? O1 ? P  MAN 1 O1 
5  1 N 1 A NAG 513 ? O1 ? Q  NAG 1 O1 
6  1 N 1 A MAN 514 ? O1 ? R  MAN 1 O1 
7  1 N 1 A MAN 521 ? O1 ? Y  MAN 1 O1 
8  1 N 1 B NAG 503 ? O1 ? BA NAG 1 O1 
9  1 N 1 B NAG 504 ? O1 ? CA NAG 1 O1 
10 1 N 1 B NAG 508 ? O1 ? DA NAG 3 O1 
11 1 N 1 B MAN 506 ? O1 ? GA MAN 1 O1 
12 1 N 1 B MAN 509 ? O1 ? HA MAN 1 O1 
13 1 N 1 C NAG 501 ? O1 ? IA NAG 1 O1 
14 1 N 1 C NAG 505 ? O1 ? MA NAG 1 O1 
15 1 N 1 C NAG 506 ? O1 ? NA NAG 1 O1 
16 1 N 1 C NAG 507 ? O1 ? OA NAG 1 O1 
17 1 N 1 D NAG 501 ? O1 ? QA NAG 1 O1 
18 1 N 1 D BMA 502 ? O1 ? RA BMA 1 O1 
19 1 N 1 D NAG 506 ? O1 ? VA NAG 1 O1 
20 1 N 1 D NAG 507 ? O1 ? WA NAG 1 O1 
21 1 N 1 D NAG 508 ? O1 ? XA NAG 1 O1 
22 1 N 1 D MAN 509 ? O1 ? YA MAN 1 O1 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'CALCIUM ION'           CA  
3 GLYCEROL                GOL 
4 N-ACETYL-D-GLUCOSAMINE  NAG 
5 ALPHA-D-MANNOSE         MAN 
6 BETA-D-MANNOSE          BMA 
7 'DI(HYDROXYETHYL)ETHER' PEG 
8 water                   HOH 
# 
