HEADER LYASE 20-JUL-07 2QOA
TITLE CRYSTAL STRUCTURE OF THE COMPLEX OF HCAII WITH AN INDANE-SULFONAMIDE
TITLE 2 INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CARBONIC ANHYDRASE 2;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CARBONIC ANHYDRASE II, CARBONATE DEHYDRATASE II, CA-II,
COMPND 5 CARBONIC ANHYDRASE C;
COMPND 6 EC: 4.2.1.1
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 OTHER_DETAILS: ERYTHROCYTES
KEYWDS CARBONIC ANHYDRASE II, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.D'AMBROSIO,G.DE SIMONE
REVDAT 5 30-AUG-23 2QOA 1 REMARK
REVDAT 4 13-JUL-11 2QOA 1 VERSN
REVDAT 3 24-FEB-09 2QOA 1 VERSN
REVDAT 2 18-MAR-08 2QOA 1 JRNL
REVDAT 1 22-JAN-08 2QOA 0
JRNL AUTH K.D'AMBROSIO,B.MASEREEL,A.THIRY,A.SCOZZAFAVA,C.T.SUPURAN,
JRNL AUTH 2 G.DE SIMONE
JRNL TITL CARBONIC ANHYDRASE INHIBITORS: BINDING OF INDANESULFONAMIDES
JRNL TITL 2 TO THE HUMAN ISOFORM II.
JRNL REF CHEMMEDCHEM V. 3 473 2007
JRNL REFN ISSN 1860-7179
JRNL PMID 18161740
JRNL DOI 10.1002/CMDC.200700274
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 95.0
REMARK 3 NUMBER OF REFLECTIONS : 30482
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.177
REMARK 3 FREE R VALUE : 0.196
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 1514
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.62
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.3430
REMARK 3 BIN FREE R VALUE : 0.4080
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 30
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2048
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 44
REMARK 3 SOLVENT ATOMS : 347
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 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.800
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2QOA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-SEP-07.
REMARK 100 THE DEPOSITION ID IS D_1000043848.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-APR-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ELETTRA
REMARK 200 BEAMLINE : 5.2R
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.2000
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 31132
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06300
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.0000
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 (%) : 92.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.27100
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1CA2
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.28
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.09
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULPHATE, SODIUM CHLORIDE,
REMARK 280 TRIS-HCL, PH 8.2, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 277K, TEMPERATURE 277.0K
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 20.70400
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 SER A 2
REMARK 465 HIS A 3
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 ASN A 11 13.54 -141.62
REMARK 500 ARG A 27 57.89 -143.74
REMARK 500 ALA A 65 -169.56 -175.37
REMARK 500 ALA A 65 -169.56 -172.77
REMARK 500 LYS A 76 -88.90 -108.93
REMARK 500 PHE A 176 70.96 -151.17
REMARK 500 ASN A 244 48.26 -95.99
REMARK 500 LYS A 252 -135.26 53.80
REMARK 500 LYS A 252 -136.23 54.32
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 MBO A 264 HG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 206 SG
REMARK 620 2 MBO A 264 CE1 171.6
REMARK 620 N 1
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 262
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 263
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MBO A 264
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAJ A 800
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAJ A 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 802
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1CA2 RELATED DB: PDB
REMARK 900 HUMAN CARBONIC ANHYDRASE II
REMARK 900 RELATED ID: 2QO8 RELATED DB: PDB
REMARK 900 RELATED ID: 2QP6 RELATED DB: PDB
DBREF 2QOA A 2 261 UNP P00918 CAH2_HUMAN 2 260
SEQRES 1 A 259 SER HIS HIS TRP GLY TYR GLY LYS HIS ASN GLY PRO GLU
SEQRES 2 A 259 HIS TRP HIS LYS ASP PHE PRO ILE ALA LYS GLY GLU ARG
SEQRES 3 A 259 GLN SER PRO VAL ASP ILE ASP THR HIS THR ALA LYS TYR
SEQRES 4 A 259 ASP PRO SER LEU LYS PRO LEU SER VAL SER TYR ASP GLN
SEQRES 5 A 259 ALA THR SER LEU ARG ILE LEU ASN ASN GLY HIS ALA PHE
SEQRES 6 A 259 ASN VAL GLU PHE ASP ASP SER GLN ASP LYS ALA VAL LEU
SEQRES 7 A 259 LYS GLY GLY PRO LEU ASP GLY THR TYR ARG LEU ILE GLN
SEQRES 8 A 259 PHE HIS PHE HIS TRP GLY SER LEU ASP GLY GLN GLY SER
SEQRES 9 A 259 GLU HIS THR VAL ASP LYS LYS LYS TYR ALA ALA GLU LEU
SEQRES 10 A 259 HIS LEU VAL HIS TRP ASN THR LYS TYR GLY ASP PHE GLY
SEQRES 11 A 259 LYS ALA VAL GLN GLN PRO ASP GLY LEU ALA VAL LEU GLY
SEQRES 12 A 259 ILE PHE LEU LYS VAL GLY SER ALA LYS PRO GLY LEU GLN
SEQRES 13 A 259 LYS VAL VAL ASP VAL LEU ASP SER ILE LYS THR LYS GLY
SEQRES 14 A 259 LYS SER ALA ASP PHE THR ASN PHE ASP PRO ARG GLY LEU
SEQRES 15 A 259 LEU PRO GLU SER LEU ASP TYR TRP THR TYR PRO GLY SER
SEQRES 16 A 259 LEU THR THR PRO PRO LEU LEU GLU CYS VAL THR TRP ILE
SEQRES 17 A 259 VAL LEU LYS GLU PRO ILE SER VAL SER SER GLU GLN VAL
SEQRES 18 A 259 LEU LYS PHE ARG LYS LEU ASN PHE ASN GLY GLU GLY GLU
SEQRES 19 A 259 PRO GLU GLU LEU MET VAL ASP ASN TRP ARG PRO ALA GLN
SEQRES 20 A 259 PRO LEU LYS ASN ARG GLN ILE LYS ALA SER PHE LYS
HET ZN A 262 1
HET CL A 263 1
HET MBO A 264 10
HET MAJ A 800 13
HET MAJ A 801 13
HET GOL A 802 6
HETNAM ZN ZINC ION
HETNAM CL CHLORIDE ION
HETNAM MBO MERCURIBENZOIC ACID
HETNAM MAJ INDANE-5-SULFONAMIDE
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 ZN ZN 2+
FORMUL 3 CL CL 1-
FORMUL 4 MBO C7 H5 HG O2
FORMUL 5 MAJ 2(C9 H11 N O2 S)
FORMUL 7 GOL C3 H8 O3
FORMUL 8 HOH *347(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 ASP A 162 1 6
HELIX 7 7 VAL A 163 LYS A 168 5 6
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 ILE A 210
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 HIS A 94 O HIS A 119
SHEET 8 B10 PHE A 66 PHE A 70 -1 N VAL A 68 O PHE A 93
SHEET 9 B10 SER A 56 ASN A 61 -1 N ARG A 58 O GLU 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 HIS A 119 N HIS A 94
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 SG CYS A 206 HG MBO A 264 1555 1555 1.90
CISPEP 1 SER A 29 PRO A 30 0 -0.25
CISPEP 2 PRO A 201 PRO A 202 0 -0.49
SITE 1 AC1 4 HIS A 94 HIS A 96 HIS A 119 MAJ A 800
SITE 1 AC2 3 GLU A 239 HOH A 609 HOH A 635
SITE 1 AC3 6 GLN A 136 GLN A 137 PRO A 138 GLU A 205
SITE 2 AC3 6 CYS A 206 HOH A 454
SITE 1 AC4 10 GLN A 92 HIS A 94 HIS A 96 HIS A 119
SITE 2 AC4 10 PHE A 131 LEU A 198 THR A 199 THR A 200
SITE 3 AC4 10 TRP A 209 ZN A 262
SITE 1 AC5 9 TRP A 5 HIS A 10 ASN A 11 HIS A 15
SITE 2 AC5 9 TRP A 16 ASP A 19 PHE A 20 ARG A 182
SITE 3 AC5 9 GLY A 183
SITE 1 AC6 9 ASN A 62 HIS A 64 ALA A 65 ASN A 67
SITE 2 AC6 9 GLN A 92 HIS A 94 HOH A 317 HOH A 328
SITE 3 AC6 9 HOH A 351
CRYST1 42.323 41.408 71.968 90.00 104.43 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 0.023628 0.000000 0.006080 0.00000
SCALE2 0.000000 0.024150 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014348 0.00000
(ATOM LINES ARE NOT SHOWN.)
END