HEADER LYASE/LYASE INHIBITOR 07-OCT-14 4RIU
TITLE A CARBONIC ANHYDRASE IX MIMIC IN COMPLEX WITH A SACCHARIN-BASED
TITLE 2 INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CARBONIC ANHYDRASE 2;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CARBONATE DEHYDRATASE II, CARBONIC ANHYDRASE C, CAC,
COMPND 5 CARBONIC ANHYDRASE II, CA-II;
COMPND 6 EC: 4.2.1.1;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: 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: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21DE3
KEYWDS CARBONIC ANHYDRASE FOLD, REVERSIBLE HYDRATION OF CO2, ACTIVE SITE
KEYWDS 2 POINT MUTATIONS, CYTOSOLIC, LYASE-LYASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR B.P.MAHON,R.MCKENNA
REVDAT 3 20-SEP-23 4RIU 1 REMARK SEQADV LINK
REVDAT 2 25-FEB-15 4RIU 1 JRNL
REVDAT 1 04-FEB-15 4RIU 0
JRNL AUTH B.P.MAHON,A.M.HENDON,J.M.DRISCOLL,G.M.RANKIN,S.A.POULSEN,
JRNL AUTH 2 C.T.SUPURAN,R.MCKENNA
JRNL TITL SACCHARIN: A LEAD COMPOUND FOR STRUCTURE-BASED DRUG DESIGN
JRNL TITL 2 OF CARBONIC ANHYDRASE IX INHIBITORS.
JRNL REF BIOORG.MED.CHEM. V. 23 849 2015
JRNL REFN ISSN 0968-0896
JRNL PMID 25614109
JRNL DOI 10.1016/J.BMC.2014.12.030
REMARK 2
REMARK 2 RESOLUTION. 1.65 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.9_1692)
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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.65
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.86
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.9
REMARK 3 NUMBER OF REFLECTIONS : 27169
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.153
REMARK 3 R VALUE (WORKING SET) : 0.151
REMARK 3 FREE R VALUE : 0.176
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 1361
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 19.8602 - 3.5499 0.99 2809 151 0.1417 0.1527
REMARK 3 2 3.5499 - 2.8202 0.98 2702 141 0.1548 0.1774
REMARK 3 3 2.8202 - 2.4645 0.96 2647 142 0.1603 0.1875
REMARK 3 4 2.4645 - 2.2395 0.96 2613 148 0.1517 0.1689
REMARK 3 5 2.2395 - 2.0792 0.94 2594 128 0.1425 0.1925
REMARK 3 6 2.0792 - 1.9567 0.93 2552 131 0.1445 0.1694
REMARK 3 7 1.9567 - 1.8588 0.91 2510 127 0.1423 0.1901
REMARK 3 8 1.8588 - 1.7779 0.91 2474 133 0.1649 0.2104
REMARK 3 9 1.7779 - 1.7095 0.91 2466 127 0.1758 0.1988
REMARK 3 10 1.7095 - 1.6505 0.90 2441 133 0.1951 0.2419
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
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) : 0.160
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.680
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 2205
REMARK 3 ANGLE : 1.118 3003
REMARK 3 CHIRALITY : 0.048 316
REMARK 3 PLANARITY : 0.005 385
REMARK 3 DIHEDRAL : 13.235 800
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): -5.3799 -1.3636 85.6690
REMARK 3 T TENSOR
REMARK 3 T11: 0.1000 T22: 0.0988
REMARK 3 T33: 0.0980 T12: 0.0004
REMARK 3 T13: 0.0026 T23: 0.0004
REMARK 3 L TENSOR
REMARK 3 L11: 0.7208 L22: 0.6603
REMARK 3 L33: 0.4883 L12: -0.0056
REMARK 3 L13: 0.0866 L23: -0.0348
REMARK 3 S TENSOR
REMARK 3 S11: -0.0079 S12: -0.0394 S13: 0.0080
REMARK 3 S21: -0.0431 S22: 0.0199 S23: -0.0034
REMARK 3 S31: -0.0019 S32: 0.0166 S33: 0.0000
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 4RIU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-OCT-14.
REMARK 100 THE DEPOSITION ID IS D_1000087399.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-JUN-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RUH3R
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : VARIMAX OPTICS
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV++
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 27169
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 19.870
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.66
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.4
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 (%): 40.50
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.07
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.6 M SODIUM CITRATE, 50MM TRIS, PH
REMARK 280 7.8, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298.0K
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 20.60750
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 SER A 2
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 58.66 -143.33
REMARK 500 SER A 65 -169.93 -160.30
REMARK 500 LYS A 111 -3.36 72.87
REMARK 500 ASN A 244 50.84 -93.96
REMARK 500 LYS A 252 -136.85 52.84
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 105.2
REMARK 620 3 HIS A 119 ND1 112.7 102.3
REMARK 620 4 3QR A 305 NAZ 99.5 120.9 116.1
REMARK 620 5 3QR A 305 OBD 70.4 83.1 172.4 56.3
REMARK 620 N 1 2 3 4
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 GOL A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 3QR A 305
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4RIV RELATED DB: PDB
DBREF 4RIU A 1 261 UNP P00918 CAH2_HUMAN 1 260
SEQADV 4RIU SER A 65 UNP P00918 ALA 65 ENGINEERED MUTATION
SEQADV 4RIU GLN A 67 UNP P00918 ASN 67 ENGINEERED MUTATION
SEQADV 4RIU THR A 69 UNP P00918 GLU 69 ENGINEERED MUTATION
SEQADV 4RIU LEU A 91 UNP P00918 ILE 91 ENGINEERED MUTATION
SEQADV 4RIU VAL A 131 UNP P00918 PHE 130 ENGINEERED MUTATION
SEQADV 4RIU GLU A 170 UNP P00918 LYS 169 ENGINEERED MUTATION
SEQADV 4RIU ALA A 204 UNP P00918 LEU 203 ENGINEERED MUTATION
SEQRES 1 A 260 MET SER HIS HIS TRP GLY TYR GLY LYS HIS ASN GLY PRO
SEQRES 2 A 260 GLU HIS TRP HIS LYS ASP PHE PRO ILE ALA LYS GLY GLU
SEQRES 3 A 260 ARG GLN SER PRO VAL ASP ILE ASP THR HIS THR ALA LYS
SEQRES 4 A 260 TYR ASP PRO SER LEU LYS PRO LEU SER VAL SER TYR ASP
SEQRES 5 A 260 GLN ALA THR SER LEU ARG ILE LEU ASN ASN GLY HIS SER
SEQRES 6 A 260 PHE GLN VAL THR PHE ASP ASP SER GLN ASP LYS ALA VAL
SEQRES 7 A 260 LEU LYS GLY GLY PRO LEU ASP GLY THR TYR ARG LEU LEU
SEQRES 8 A 260 GLN PHE HIS PHE HIS TRP GLY SER LEU ASP GLY GLN GLY
SEQRES 9 A 260 SER GLU HIS THR VAL ASP LYS LYS LYS TYR ALA ALA GLU
SEQRES 10 A 260 LEU HIS LEU VAL HIS TRP ASN THR LYS TYR GLY ASP VAL
SEQRES 11 A 260 GLY LYS ALA VAL GLN GLN PRO ASP GLY LEU ALA VAL LEU
SEQRES 12 A 260 GLY ILE PHE LEU LYS VAL GLY SER ALA LYS PRO GLY LEU
SEQRES 13 A 260 GLN LYS VAL VAL ASP VAL LEU ASP SER ILE LYS THR GLU
SEQRES 14 A 260 GLY LYS SER ALA ASP PHE THR ASN PHE ASP PRO ARG GLY
SEQRES 15 A 260 LEU LEU PRO GLU SER LEU ASP TYR TRP THR TYR PRO GLY
SEQRES 16 A 260 SER LEU THR THR PRO PRO LEU ALA GLU CYS VAL THR TRP
SEQRES 17 A 260 ILE VAL LEU LYS GLU PRO ILE SER VAL SER SER GLU GLN
SEQRES 18 A 260 VAL LEU LYS PHE ARG LYS LEU ASN PHE ASN GLY GLU GLY
SEQRES 19 A 260 GLU PRO GLU GLU LEU MET VAL ASP ASN TRP ARG PRO ALA
SEQRES 20 A 260 GLN PRO LEU LYS ASN ARG GLN ILE LYS ALA SER PHE LYS
HET ZN A 301 1
HET GOL A 302 6
HET GOL A 303 6
HET GOL A 304 6
HET 3QR A 305 30
HETNAM ZN ZINC ION
HETNAM GOL GLYCEROL
HETNAM 3QR [1-(1,1-DIOXIDO-3-OXO-2,3-DIHYDRO-1,2-BENZOTHIAZOL-6-
HETNAM 2 3QR YL)-1H-1,2,3-TRIAZOL-4-YL]METHYL ALPHA-L-IDOPYRANOSIDE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 ZN ZN 2+
FORMUL 3 GOL 3(C3 H8 O3)
FORMUL 6 3QR C16 H18 N4 O9 S
FORMUL 7 HOH *187(H2 O)
HELIX 1 1 HIS A 15 ASP A 19 5 5
HELIX 2 2 PHE A 20 GLY A 25 5 6
HELIX 3 3 LYS A 127 GLY A 129 5 3
HELIX 4 4 ASP A 130 VAL A 135 1 6
HELIX 5 5 LYS A 154 GLY A 156 5 3
HELIX 6 6 LEU A 157 LEU A 164 1 8
HELIX 7 7 ASP A 165 LYS A 168 5 4
HELIX 8 8 ASP A 180 LEU A 185 5 6
HELIX 9 9 SER A 219 ARG A 227 1 9
SHEET 1 A 2 ASP A 32 ILE A 33 0
SHEET 2 A 2 THR A 108 VAL A 109 1 O THR A 108 N ILE A 33
SHEET 1 B10 LYS A 39 TYR A 40 0
SHEET 2 B10 LYS A 257 ALA A 258 1 O ALA A 258 N LYS A 39
SHEET 3 B10 TYR A 191 GLY A 196 -1 N THR A 193 O LYS A 257
SHEET 4 B10 VAL A 207 LEU A 212 -1 O VAL A 207 N GLY A 196
SHEET 5 B10 LEU A 141 VAL A 150 1 N GLY A 145 O LEU A 212
SHEET 6 B10 ALA A 116 ASN A 124 -1 N LEU A 118 O ILE A 146
SHEET 7 B10 TYR A 88 TRP A 97 -1 N LEU A 91 O VAL A 121
SHEET 8 B10 PHE A 66 PHE A 70 -1 N PHE A 70 O LEU A 91
SHEET 9 B10 SER A 56 ASN A 61 -1 N LEU A 57 O THR A 69
SHEET 10 B10 SER A 173 ASP A 175 -1 O ALA A 174 N ILE A 59
SHEET 1 C 6 LEU A 47 SER A 50 0
SHEET 2 C 6 VAL A 78 GLY A 81 -1 O LYS A 80 N SER A 48
SHEET 3 C 6 TYR A 88 TRP A 97 -1 O TYR A 88 N LEU A 79
SHEET 4 C 6 ALA A 116 ASN A 124 -1 O VAL A 121 N LEU A 91
SHEET 5 C 6 LEU A 141 VAL A 150 -1 O ILE A 146 N LEU A 118
SHEET 6 C 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 1.97
LINK NE2 HIS A 96 ZN ZN A 301 1555 1555 2.03
LINK ND1 HIS A 119 ZN ZN A 301 1555 1555 2.05
LINK ZN ZN A 301 NAZ 3QR A 305 1555 1555 1.88
LINK ZN ZN A 301 OBD 3QR A 305 1555 1555 2.67
CISPEP 1 SER A 29 PRO A 30 0 -2.50
CISPEP 2 PRO A 201 PRO A 202 0 11.79
SITE 1 AC1 4 HIS A 94 HIS A 96 HIS A 119 3QR A 305
SITE 1 AC2 5 TYR A 7 ASP A 243 TRP A 245 PRO A 247
SITE 2 AC2 5 HOH A 494
SITE 1 AC3 3 TYR A 114 LYS A 213 PRO A 215
SITE 1 AC4 3 ASN A 253 ARG A 254 GLN A 255
SITE 1 AC5 15 GLN A 67 LEU A 91 GLN A 92 HIS A 94
SITE 2 AC5 15 HIS A 96 HIS A 119 VAL A 121 VAL A 131
SITE 3 AC5 15 LEU A 141 VAL A 143 LEU A 198 THR A 199
SITE 4 AC5 15 THR A 200 ZN A 301 HOH A 453
CRYST1 41.996 41.215 71.834 90.00 103.83 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 0.023812 0.000000 0.005862 0.00000
SCALE2 0.000000 0.024263 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014337 0.00000
(ATOM LINES ARE NOT SHOWN.)
END