HEADER LYASE/INHIBITOR 27-JUL-17 5WLT
TITLE CARBONIC ANHYDRASE IX-MIMIC IN COMPLEX WITH ARYLOXY-2-
TITLE 2 HYDROXYPROPYLAMMINE SULFONAMIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CARBONIC ANHYDRASE 2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 4-260;
COMPND 5 SYNONYM: CARBONATE DEHYDRATASE II,CARBONIC ANHYDRASE C,CAC,CARBONIC
COMPND 6 ANHYDRASE II,CA-II;
COMPND 7 EC: 4.2.1.1;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: CA2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS CARBONIC ANHYDRASE, BETA ADRENERGIC RECEPTOR, SULFONAMIDE, ARYLOXY-2-
KEYWDS 2 HYDROXYPROPYLAMMINE, LYASE, LYASE-INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR C.L.LOMELINO,J.T.ANDRING,R.MCKENNA
REVDAT 3 04-OCT-23 5WLT 1 REMARK
REVDAT 2 05-SEP-18 5WLT 1 JRNL
REVDAT 1 01-AUG-18 5WLT 0
JRNL AUTH A.NOCENTINI,M.CERUSO,S.BUA,C.L.LOMELINO,J.T.ANDRING,
JRNL AUTH 2 R.MCKENNA,C.LANZI,S.SGAMBELLONE,R.PECORI,R.MATUCCI,
JRNL AUTH 3 L.FILIPPI,P.GRATTERI,F.CARTA,E.MASINI,S.SELLERI,C.T.SUPURAN
JRNL TITL DISCOVERY OF BETA-ADRENERGIC RECEPTORS BLOCKER-CARBONIC
JRNL TITL 2 ANHYDRASE INHIBITOR HYBRIDS FOR MULTITARGETED ANTIGLAUCOMA
JRNL TITL 3 THERAPY.
JRNL REF J. MED. CHEM. V. 61 5380 2018
JRNL REFN ISSN 1520-4804
JRNL PMID 29851481
JRNL DOI 10.1021/ACS.JMEDCHEM.8B00625
REMARK 2
REMARK 2 RESOLUTION. 1.57 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.10.1_2155
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.57
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.30
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 78.4
REMARK 3 NUMBER OF REFLECTIONS : 53038
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.147
REMARK 3 R VALUE (WORKING SET) : 0.145
REMARK 3 FREE R VALUE : 0.176
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.950
REMARK 3 FREE R VALUE TEST SET COUNT : 2625
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 40.3238 - 4.1867 0.99 3342 177 0.1303 0.1429
REMARK 3 2 4.1867 - 3.3236 0.99 3371 178 0.1210 0.1565
REMARK 3 3 3.3236 - 2.9036 0.99 3352 171 0.1476 0.1715
REMARK 3 4 2.9036 - 2.6382 0.99 3332 181 0.1537 0.1795
REMARK 3 5 2.6382 - 2.4491 0.97 3286 171 0.1515 0.1775
REMARK 3 6 2.4491 - 2.3048 0.97 3291 161 0.1500 0.1690
REMARK 3 7 2.3048 - 2.1893 0.94 3143 169 0.1413 0.2080
REMARK 3 8 2.1893 - 2.0940 0.91 3075 160 0.1459 0.1964
REMARK 3 9 2.0940 - 2.0134 0.85 2894 154 0.1525 0.1825
REMARK 3 10 2.0134 - 1.9440 0.82 2748 137 0.1534 0.1716
REMARK 3 11 1.9440 - 1.8832 0.77 2606 135 0.1513 0.1809
REMARK 3 12 1.8832 - 1.8293 0.73 2491 129 0.1463 0.1939
REMARK 3 13 1.8293 - 1.7812 0.70 2342 120 0.1549 0.2441
REMARK 3 14 1.7812 - 1.7377 0.64 2184 106 0.1626 0.2108
REMARK 3 15 1.7377 - 1.6982 0.61 2047 119 0.1766 0.1732
REMARK 3 16 1.6982 - 1.6621 0.56 1906 105 0.1831 0.2151
REMARK 3 17 1.6621 - 1.6288 0.50 1738 90 0.1764 0.2219
REMARK 3 18 1.6288 - 1.5981 0.52 1733 84 0.1872 0.2044
REMARK 3 19 1.5981 - 1.5696 0.45 1532 78 0.1892 0.2500
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.130
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.250
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 12.34
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.27
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.006 2243
REMARK 3 ANGLE : 0.918 3054
REMARK 3 CHIRALITY : 0.057 310
REMARK 3 PLANARITY : 0.006 391
REMARK 3 DIHEDRAL : 12.151 1302
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): -9.5670 -1.1411 15.9536
REMARK 3 T TENSOR
REMARK 3 T11: 0.0812 T22: 0.0769
REMARK 3 T33: 0.0830 T12: -0.0010
REMARK 3 T13: 0.0015 T23: -0.0046
REMARK 3 L TENSOR
REMARK 3 L11: 0.4766 L22: 0.3119
REMARK 3 L33: 0.4084 L12: -0.0904
REMARK 3 L13: 0.0139 L23: -0.0420
REMARK 3 S TENSOR
REMARK 3 S11: 0.0093 S12: -0.0278 S13: 0.0221
REMARK 3 S21: -0.0152 S22: 0.0009 S23: 0.0070
REMARK 3 S31: 0.0075 S32: 0.0110 S33: 0.0015
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5WLT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-AUG-17.
REMARK 100 THE DEPOSITION ID IS D_1000229255.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-JUN-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CHESS
REMARK 200 BEAMLINE : F1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.98
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 53038
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.570
REMARK 200 RESOLUTION RANGE LOW (A) : 40.300
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 90.2
REMARK 200 DATA REDUNDANCY : 4.000
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: 3KS3
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.96
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.16
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.6M SODIUM CITRATE 50MM TRIS-HCL, PH
REMARK 280 7.8, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 20.77700
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ARG A 27 57.53 -142.91
REMARK 500 ALA A 65 -168.34 -163.89
REMARK 500 ASN A 244 50.12 -90.99
REMARK 500 LYS A 252 -134.51 57.27
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 301 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 94 NE2
REMARK 620 2 HIS A 96 NE2 103.9
REMARK 620 3 HIS A 119 ND1 113.2 98.4
REMARK 620 4 86B A 302 N10 111.3 110.0 118.4
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 86B A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 86B A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 86B A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 86B A 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 306
DBREF 5WLT A 4 261 UNP P00918 CAH2_HUMAN 4 260
SEQRES 1 A 257 HIS TRP GLY TYR GLY LYS HIS ASN GLY PRO GLU HIS TRP
SEQRES 2 A 257 HIS LYS ASP PHE PRO ILE ALA LYS GLY GLU ARG GLN SER
SEQRES 3 A 257 PRO VAL ASP ILE ASP THR HIS THR ALA LYS TYR ASP PRO
SEQRES 4 A 257 SER LEU LYS PRO LEU SER VAL SER TYR ASP GLN ALA THR
SEQRES 5 A 257 SER LEU ARG ILE LEU ASN ASN GLY HIS ALA PHE ASN VAL
SEQRES 6 A 257 GLU PHE ASP ASP SER GLN ASP LYS ALA VAL LEU LYS GLY
SEQRES 7 A 257 GLY PRO LEU ASP GLY THR TYR ARG LEU ILE GLN PHE HIS
SEQRES 8 A 257 PHE HIS TRP GLY SER LEU ASP GLY GLN GLY SER GLU HIS
SEQRES 9 A 257 THR VAL ASP LYS LYS LYS TYR ALA ALA GLU LEU HIS LEU
SEQRES 10 A 257 VAL HIS TRP ASN THR LYS TYR GLY ASP PHE GLY LYS ALA
SEQRES 11 A 257 VAL GLN GLN PRO ASP GLY LEU ALA VAL LEU GLY ILE PHE
SEQRES 12 A 257 LEU LYS VAL GLY SER ALA LYS PRO GLY LEU GLN LYS VAL
SEQRES 13 A 257 VAL ASP VAL LEU ASP SER ILE LYS THR LYS GLY LYS SER
SEQRES 14 A 257 ALA ASP PHE THR ASN PHE ASP PRO ARG GLY LEU LEU PRO
SEQRES 15 A 257 GLU SER LEU ASP TYR TRP THR TYR PRO GLY SER LEU THR
SEQRES 16 A 257 THR PRO PRO LEU LEU GLU CYS VAL THR TRP ILE VAL LEU
SEQRES 17 A 257 LYS GLU PRO ILE SER VAL SER SER GLU GLN VAL LEU LYS
SEQRES 18 A 257 PHE ARG LYS LEU ASN PHE ASN GLY GLU GLY GLU PRO GLU
SEQRES 19 A 257 GLU LEU MET VAL ASP ASN TRP ARG PRO ALA GLN PRO LEU
SEQRES 20 A 257 LYS ASN ARG GLN ILE LYS ALA SER PHE LYS
HET ZN A 301 1
HET 86B A 302 19
HET 86B A 303 19
HET 86B A 304 19
HET 86B A 305 19
HET GOL A 306 6
HETNAM ZN ZINC ION
HETNAM 86B 4-{(2S)-2-HYDROXY-3-[(PROPAN-2-YL)
HETNAM 2 86B AMINO]PROPOXY}BENZENE-1-SULFONAMIDE
HETNAM GOL GLYCEROL
HETSYN 86B ARYLOXY-2-HYDROXYPROPYLAMMINE SULFONAMIDE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 ZN ZN 2+
FORMUL 3 86B 4(C12 H20 N2 O4 S)
FORMUL 7 GOL C3 H8 O3
FORMUL 8 HOH *213(H2 O)
HELIX 1 AA1 HIS A 15 ASP A 19 5 5
HELIX 2 AA2 PHE A 20 GLY A 25 5 6
HELIX 3 AA3 LYS A 127 GLY A 129 5 3
HELIX 4 AA4 ASP A 130 VAL A 135 1 6
HELIX 5 AA5 LYS A 154 GLY A 156 5 3
HELIX 6 AA6 LEU A 157 LEU A 164 1 8
HELIX 7 AA7 ASP A 165 LYS A 168 5 4
HELIX 8 AA8 ASP A 180 LEU A 185 5 6
HELIX 9 AA9 SER A 219 ARG A 227 1 9
SHEET 1 AA1 2 ASP A 32 ILE A 33 0
SHEET 2 AA1 2 THR A 108 VAL A 109 1 O THR A 108 N ILE A 33
SHEET 1 AA210 LYS A 39 TYR A 40 0
SHEET 2 AA210 LYS A 257 ALA A 258 1 O ALA A 258 N LYS A 39
SHEET 3 AA210 TYR A 191 GLY A 196 -1 N THR A 193 O LYS A 257
SHEET 4 AA210 VAL A 207 LEU A 212 -1 O VAL A 207 N GLY A 196
SHEET 5 AA210 LEU A 141 VAL A 150 1 N GLY A 145 O LEU A 212
SHEET 6 AA210 ALA A 116 ASN A 124 -1 N LEU A 118 O ILE A 146
SHEET 7 AA210 TYR A 88 TRP A 97 -1 N HIS A 94 O HIS A 119
SHEET 8 AA210 PHE A 66 PHE A 70 -1 N VAL A 68 O PHE A 93
SHEET 9 AA210 SER A 56 ASN A 61 -1 N LEU A 57 O GLU A 69
SHEET 10 AA210 SER A 173 ASP A 175 -1 O ALA A 174 N ILE A 59
SHEET 1 AA3 6 LEU A 47 SER A 50 0
SHEET 2 AA3 6 VAL A 78 GLY A 81 -1 O LYS A 80 N SER A 48
SHEET 3 AA3 6 TYR A 88 TRP A 97 -1 O TYR A 88 N LEU A 79
SHEET 4 AA3 6 ALA A 116 ASN A 124 -1 O HIS A 119 N HIS A 94
SHEET 5 AA3 6 LEU A 141 VAL A 150 -1 O ILE A 146 N LEU A 118
SHEET 6 AA3 6 ILE A 216 VAL A 218 1 O ILE A 216 N PHE A 147
LINK NE2 HIS A 94 ZN ZN A 301 1555 1555 2.02
LINK NE2 HIS A 96 ZN ZN A 301 1555 1555 2.06
LINK ND1 HIS A 119 ZN ZN A 301 1555 1555 2.04
LINK ZN ZN A 301 N10 86B A 302 1555 1555 2.07
CISPEP 1 SER A 29 PRO A 30 0 -1.03
CISPEP 2 PRO A 201 PRO A 202 0 9.44
SITE 1 AC1 4 HIS A 94 HIS A 96 HIS A 119 86B A 302
SITE 1 AC2 10 HIS A 94 HIS A 96 HIS A 119 LEU A 198
SITE 2 AC2 10 THR A 199 THR A 200 TRP A 209 ZN A 301
SITE 3 AC2 10 86B A 305 HOH A 405
SITE 1 AC3 9 ASN A 67 GLU A 69 ASP A 71 ASP A 72
SITE 2 AC3 9 SER A 73 ILE A 91 GLN A 92 86B A 305
SITE 3 AC3 9 HOH A 533
SITE 1 AC4 10 HIS A 4 TRP A 5 HIS A 10 ASN A 11
SITE 2 AC4 10 HIS A 15 TRP A 16 ASP A 19 ASP A 180
SITE 3 AC4 10 GLY A 183 HOH A 512
SITE 1 AC5 11 ASP A 72 ILE A 91 ASP A 101 TRP A 123
SITE 2 AC5 11 GLY A 129 ASP A 130 PHE A 131 GLY A 132
SITE 3 AC5 11 86B A 302 86B A 303 HOH A 429
SITE 1 AC6 7 ASN A 62 ASN A 67 GLN A 92 HIS A 94
SITE 2 AC6 7 HOH A 405 HOH A 482 HOH A 505
CRYST1 42.684 41.554 72.660 90.00 104.50 90.00 P 1 21 1 2
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.023428 0.000000 0.006058 0.00000
SCALE2 0.000000 0.024065 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014215 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
