HEADER LYASE 02-FEB-17 5N0E
TITLE CRYSTAL STRUCTURE OF HUMAN CARBONIC ANHYDRASE II IN COMPLEX WITH (S)-
TITLE 2 4-(6,7-DIHYDROXY-1-PHENYL-3,4-TETRAHYDROISOQUINOLINE-1H-2-CARBONYL)
TITLE 3 BENZENESULFONAMIDE.
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;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HUMAN CARBONIC ANHYDRASE, BENZESULFONAMIDE, PROTEIN-INHIBITOR ADDUCT,
KEYWDS 2 LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.DI FIORE,G.DE SIMONE
REVDAT 3 17-JAN-24 5N0E 1 REMARK
REVDAT 2 07-JUN-17 5N0E 1 JRNL
REVDAT 1 10-MAY-17 5N0E 0
JRNL AUTH E.BRUNO,M.R.BUEMI,A.DI FIORE,L.DE LUCA,S.FERRO,A.ANGELI,
JRNL AUTH 2 R.CIRILLI,D.SADUTTO,V.ALTERIO,S.M.MONTI,C.T.SUPURAN,
JRNL AUTH 3 G.DE SIMONE,R.GITTO
JRNL TITL PROBING MOLECULAR INTERACTIONS BETWEEN HUMAN CARBONIC
JRNL TITL 2 ANHYDRASES (HCAS) AND A NOVEL CLASS OF BENZENESULFONAMIDES.
JRNL REF J. MED. CHEM. V. 60 4316 2017
JRNL REFN ISSN 1520-4804
JRNL PMID 28453941
JRNL DOI 10.1021/ACS.JMEDCHEM.7B00264
REMARK 2
REMARK 2 RESOLUTION. 1.75 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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.60
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 92.9
REMARK 3 NUMBER OF REFLECTIONS : 22852
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : FREE R-VALUE
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.166
REMARK 3 FREE R VALUE : 0.198
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.500
REMARK 3 FREE R VALUE TEST SET COUNT : 1110
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 : 22
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.75
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.78
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2240
REMARK 3 BIN FREE R VALUE : 0.2440
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 44
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 : 2049
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 31
REMARK 3 SOLVENT ATOMS : 234
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 11.60
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) : 0.014
REMARK 3 BOND ANGLES (DEGREES) : 1.700
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 5N0E COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 02-FEB-17.
REMARK 100 THE DEPOSITION ID IS D_1200003351.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-JUL-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
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 MICROMAX-007 HF
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54178
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU SATURN 944
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 23683
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.750
REMARK 200 RESOLUTION RANGE LOW (A) : 24.600
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.7
REMARK 200 DATA REDUNDANCY : 4.300
REMARK 200 R MERGE (I) : 0.09000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.81
REMARK 200 COMPLETENESS FOR SHELL (%) : 86.8
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.36000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.000
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: 1CA2
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.61
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.07
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.3 M SODIUM CITRATE, 0.1 M TRIS-HCL,
REMARK 280 PH 8.5., VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
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 20.70000
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 TOTAL BURIED SURFACE AREA: 0 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11600 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 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 GLY A 0
REMARK 465 MET A 1
REMARK 465 SER A 2
REMARK 465 HIS A 3
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 O HOH A 525 O HOH A 614 2.09
REMARK 500 O HOH A 605 O HOH A 608 2.12
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 ARG A 27 57.08 -143.69
REMARK 500 ALA A 65 -174.55 -177.44
REMARK 500 LYS A 76 -83.46 -117.32
REMARK 500 LYS A 111 -2.47 72.60
REMARK 500 ASN A 244 49.09 -95.38
REMARK 500 LYS A 252 -139.28 55.49
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 104.1
REMARK 620 3 HIS A 119 ND1 115.5 98.4
REMARK 620 4 8F3 A 302 N2 109.9 114.0 114.2
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 8F3 A 302
DBREF 5N0E A 1 261 UNP P00918 CAH2_HUMAN 1 260
SEQADV 5N0E MET A -1 UNP P00918 INITIATING METHIONINE
SEQADV 5N0E GLY A 0 UNP P00918 EXPRESSION TAG
SEQRES 1 A 262 MET GLY MET SER HIS HIS TRP GLY TYR GLY LYS HIS ASN
SEQRES 2 A 262 GLY PRO GLU HIS TRP HIS LYS ASP PHE PRO ILE ALA LYS
SEQRES 3 A 262 GLY GLU ARG GLN SER PRO VAL ASP ILE ASP THR HIS THR
SEQRES 4 A 262 ALA LYS TYR ASP PRO SER LEU LYS PRO LEU SER VAL SER
SEQRES 5 A 262 TYR ASP GLN ALA THR SER LEU ARG ILE LEU ASN ASN GLY
SEQRES 6 A 262 HIS ALA PHE ASN VAL GLU PHE ASP ASP SER GLN ASP LYS
SEQRES 7 A 262 ALA VAL LEU LYS GLY GLY PRO LEU ASP GLY THR TYR ARG
SEQRES 8 A 262 LEU ILE GLN PHE HIS PHE HIS TRP GLY SER LEU ASP GLY
SEQRES 9 A 262 GLN GLY SER GLU HIS THR VAL ASP LYS LYS LYS TYR ALA
SEQRES 10 A 262 ALA GLU LEU HIS LEU VAL HIS TRP ASN THR LYS TYR GLY
SEQRES 11 A 262 ASP PHE GLY LYS ALA VAL GLN GLN PRO ASP GLY LEU ALA
SEQRES 12 A 262 VAL LEU GLY ILE PHE LEU LYS VAL GLY SER ALA LYS PRO
SEQRES 13 A 262 GLY LEU GLN LYS VAL VAL ASP VAL LEU ASP SER ILE LYS
SEQRES 14 A 262 THR LYS GLY LYS SER ALA ASP PHE THR ASN PHE ASP PRO
SEQRES 15 A 262 ARG GLY LEU LEU PRO GLU SER LEU ASP TYR TRP THR TYR
SEQRES 16 A 262 PRO GLY SER LEU THR THR PRO PRO LEU LEU GLU CYS VAL
SEQRES 17 A 262 THR TRP ILE VAL LEU LYS GLU PRO ILE SER VAL SER SER
SEQRES 18 A 262 GLU GLN VAL LEU LYS PHE ARG LYS LEU ASN PHE ASN GLY
SEQRES 19 A 262 GLU GLY GLU PRO GLU GLU LEU MET VAL ASP ASN TRP ARG
SEQRES 20 A 262 PRO ALA GLN PRO LEU LYS ASN ARG GLN ILE LYS ALA SER
SEQRES 21 A 262 PHE LYS
HET ZN A 301 1
HET 8F3 A 302 30
HETNAM ZN ZINC ION
HETNAM 8F3 4-[[(1~{S})-6,7-BIS(OXIDANYL)-1-PHENYL-3,4-DIHYDRO-
HETNAM 2 8F3 1~{H}-ISOQUINOLIN-2-YL]CARBONYL]BENZENESULFONAMIDE
FORMUL 2 ZN ZN 2+
FORMUL 3 8F3 C22 H20 N2 O5 S
FORMUL 4 HOH *234(H2 O)
HELIX 1 AA1 HIS A 15 PHE A 20 1 6
HELIX 2 AA2 PRO A 21 GLY A 25 5 5
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 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 2.07
LINK ND1 HIS A 119 ZN ZN A 301 1555 1555 2.06
LINK ZN ZN A 301 N2 8F3 A 302 1555 1555 1.97
CISPEP 1 SER A 29 PRO A 30 0 -0.16
CISPEP 2 PRO A 201 PRO A 202 0 0.62
SITE 1 AC1 4 HIS A 94 HIS A 96 HIS A 119 8F3 A 302
SITE 1 AC2 14 HIS A 64 HIS A 94 HIS A 96 HIS A 119
SITE 2 AC2 14 PHE A 131 VAL A 143 LEU A 198 THR A 199
SITE 3 AC2 14 THR A 200 PRO A 201 PRO A 202 TRP A 209
SITE 4 AC2 14 ZN A 301 HOH A 527
CRYST1 42.310 41.400 71.960 90.00 104.38 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 0.023635 0.000000 0.006060 0.00000
SCALE2 0.000000 0.024155 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014346 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
