HEADER LYASE 01-OCT-15 5E2S
TITLE CRYSTAL STRUCTURE OF HUMAN CARBONIC ANHYDRASE II IN COMPLEX WITH THE
TITLE 2 4-(2-ISO-PROPYLPHENYL)BENZENESULFONAMIDE 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,CARBONIC
COMPND 5 ANHYDRASE II,CA-II;
COMPND 6 EC: 4.2.1.1;
COMPND 7 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 BL21;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693
KEYWDS LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.FERRARONI,C.T.SUPURAN
REVDAT 3 10-JAN-24 5E2S 1 REMARK
REVDAT 2 10-FEB-16 5E2S 1 JRNL
REVDAT 1 20-JAN-16 5E2S 0
JRNL AUTH B.CORNELIO,M.LARONZE-COCHARD,M.CERUSO,M.FERRARONI,G.A.RANCE,
JRNL AUTH 2 F.CARTA,A.N.KHLOBYSTOV,A.FONTANA,C.T.SUPURAN,J.SAPI
JRNL TITL 4-ARYLBENZENESULFONAMIDES AS HUMAN CARBONIC ANHYDRASE
JRNL TITL 2 INHIBITORS (HCAIS): SYNTHESIS BY PD NANOCATALYST-MEDIATED
JRNL TITL 3 SUZUKI-MIYAURA REACTION, ENZYME INHIBITION, AND X-RAY
JRNL TITL 4 CRYSTALLOGRAPHIC STUDIES.
JRNL REF J.MED.CHEM. V. 59 721 2016
JRNL REFN ISSN 0022-2623
JRNL PMID 26741028
JRNL DOI 10.1021/ACS.JMEDCHEM.5B01771
REMARK 2
REMARK 2 RESOLUTION. 1.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0073
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.5
REMARK 3 NUMBER OF REFLECTIONS : 34474
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.172
REMARK 3 R VALUE (WORKING SET) : 0.170
REMARK 3 FREE R VALUE : 0.196
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 1773
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.54
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1733
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 63.86
REMARK 3 BIN R VALUE (WORKING SET) : 0.2980
REMARK 3 BIN FREE R VALUE SET COUNT : 80
REMARK 3 BIN FREE R VALUE : 0.3180
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2043
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 20
REMARK 3 SOLVENT ATOMS : 362
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 18.65
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 14.27
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.08000
REMARK 3 B22 (A**2) : 0.01000
REMARK 3 B33 (A**2) : 0.00000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.17000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.085
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.082
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.059
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.635
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.962
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.950
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2204 ; 0.008 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3015 ; 1.315 ; 1.957
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 282 ; 6.480 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 104 ;35.234 ;24.904
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 363 ;12.155 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 7 ;23.511 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 317 ; 0.090 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1717 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1056 ; 0.809 ; 1.153
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1323 ; 1.392 ; 1.724
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1148 ; 1.116 ; 1.248
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 5E2S COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 02-OCT-15.
REMARK 100 THE DEPOSITION ID IS D_1000214260.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-APR-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : BM30A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.980
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 36248
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
REMARK 200 RESOLUTION RANGE LOW (A) : 32.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.5
REMARK 200 DATA REDUNDANCY : 2.600
REMARK 200 R MERGE (I) : 0.06200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.4100
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 70.3
REMARK 200 DATA REDUNDANCY IN SHELL : 2.04
REMARK 200 R MERGE FOR SHELL (I) : 0.48500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.810
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: REFMAC
REMARK 200 STARTING MODEL: 4FIK
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.18
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.09
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.5 M SODIUM CITRATE, TRIS 50 MM, PH
REMARK 280 8.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 296K
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 20.64800
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 0 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11590 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL
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 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 HIS A 4 CG ND1 CD2 CE1 NE2
REMARK 470 LYS A 9 CG CD CE NZ
REMARK 470 LYS A 80 NZ
REMARK 470 LYS A 228 NZ
REMARK 470 LYS A 257 CE NZ
REMARK 470 LYS A 261 CD CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 NZ LYS A 213 O HOH A 404 2.15
REMARK 500
REMARK 500 REMARK: NULL
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 LYS A 111 -2.46 72.76
REMARK 500 PHE A 176 70.36 -151.29
REMARK 500 ASN A 244 50.70 -93.37
REMARK 500 LYS A 252 -138.68 55.05
REMARK 500 LYS A 252 -137.40 53.08
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 761 DISTANCE = 6.30 ANGSTROMS
REMARK 525 HOH A 762 DISTANCE = 6.74 ANGSTROMS
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 106.5
REMARK 620 3 HIS A 119 ND1 112.9 96.9
REMARK 620 4 5CX A 302 N1 112.6 110.8 115.6
REMARK 620 5 HOH A 424 O 113.3 106.1 118.7 5.0
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 5CX A 302
DBREF 5E2S A 3 261 UNP P00918 CAH2_HUMAN 3 260
SEQRES 1 A 258 HIS HIS TRP GLY TYR GLY LYS HIS ASN GLY PRO GLU HIS
SEQRES 2 A 258 TRP HIS LYS ASP PHE PRO ILE ALA LYS GLY GLU ARG GLN
SEQRES 3 A 258 SER PRO VAL ASP ILE ASP THR HIS THR ALA LYS TYR ASP
SEQRES 4 A 258 PRO SER LEU LYS PRO LEU SER VAL SER TYR ASP GLN ALA
SEQRES 5 A 258 THR SER LEU ARG ILE LEU ASN ASN GLY HIS ALA PHE ASN
SEQRES 6 A 258 VAL GLU PHE ASP ASP SER GLN ASP LYS ALA VAL LEU LYS
SEQRES 7 A 258 GLY GLY PRO LEU ASP GLY THR TYR ARG LEU ILE GLN PHE
SEQRES 8 A 258 HIS PHE HIS TRP GLY SER LEU ASP GLY GLN GLY SER GLU
SEQRES 9 A 258 HIS THR VAL ASP LYS LYS LYS TYR ALA ALA GLU LEU HIS
SEQRES 10 A 258 LEU VAL HIS TRP ASN THR LYS TYR GLY ASP PHE GLY LYS
SEQRES 11 A 258 ALA VAL GLN GLN PRO ASP GLY LEU ALA VAL LEU GLY ILE
SEQRES 12 A 258 PHE LEU LYS VAL GLY SER ALA LYS PRO GLY LEU GLN LYS
SEQRES 13 A 258 VAL VAL ASP VAL LEU ASP SER ILE LYS THR LYS GLY LYS
SEQRES 14 A 258 SER ALA ASP PHE THR ASN PHE ASP PRO ARG GLY LEU LEU
SEQRES 15 A 258 PRO GLU SER LEU ASP TYR TRP THR TYR PRO GLY SER LEU
SEQRES 16 A 258 THR THR PRO PRO LEU LEU GLU CYS VAL THR TRP ILE VAL
SEQRES 17 A 258 LEU LYS GLU PRO ILE SER VAL SER SER GLU GLN VAL LEU
SEQRES 18 A 258 LYS PHE ARG LYS LEU ASN PHE ASN GLY GLU GLY GLU PRO
SEQRES 19 A 258 GLU GLU LEU MET VAL ASP ASN TRP ARG PRO ALA GLN PRO
SEQRES 20 A 258 LEU LYS ASN ARG GLN ILE LYS ALA SER PHE LYS
HET ZN A 301 1
HET 5CX A 302 19
HETNAM ZN ZINC ION
HETNAM 5CX 2'-(PROPAN-2-YL)BIPHENYL-4-SULFONAMIDE
FORMUL 2 ZN ZN 2+
FORMUL 3 5CX C15 H17 N O2 S
FORMUL 4 HOH *362(H2 O)
HELIX 1 AA1 GLY A 12 ASP A 19 5 8
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 ILE A 210
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 VAL A 78 N SER A 50
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 2.01
LINK NE2 HIS A 96 ZN ZN A 301 1555 1555 2.05
LINK ND1 HIS A 119 ZN ZN A 301 1555 1555 2.06
LINK ZN ZN A 301 N1 5CX A 302 1555 1555 2.12
LINK ZN ZN A 301 O HOH A 424 1555 1555 1.95
CISPEP 1 SER A 29 PRO A 30 0 -1.19
CISPEP 2 PRO A 201 PRO A 202 0 12.54
SITE 1 AC1 5 HIS A 94 HIS A 96 HIS A 119 5CX A 302
SITE 2 AC1 5 HOH A 424
SITE 1 AC2 16 GLN A 92 HIS A 94 HIS A 96 HIS A 119
SITE 2 AC2 16 VAL A 121 PHE A 131 LEU A 198 THR A 199
SITE 3 AC2 16 THR A 200 TRP A 209 ZN A 301 HOH A 410
SITE 4 AC2 16 HOH A 424 HOH A 491 HOH A 664 HOH A 752
CRYST1 42.251 41.296 71.923 90.00 104.34 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 0.023668 0.000000 0.006049 0.00000
SCALE2 0.000000 0.024215 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014351 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
