HEADER LYASE 16-MAR-01 1I91
TITLE CARBONIC ANHYDRASE II COMPLEXED WITH AL-6619 2H-THIENO[3,2-E]-1,2-
TITLE 2 THIAZINE-6-SULFONAMIDE, 2-(3-HYDROXYPHENYL)-3-(4-MORPHOLINYL)-, 1,1-
TITLE 3 DIOXIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CARBONIC ANHYDRASE II;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CARBONATE DEHYDRATASE II;
COMPND 5 EC: 4.2.1.1;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS CARBONIC ANHYDRASE II, AL-6619, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.-Y.KIM,J.S.CHANG,J.LIAO,J.A.MAY,D.W.CHRISTIANSON
REVDAT 6 07-FEB-24 1I91 1 REMARK HETSYN LINK
REVDAT 5 04-APR-18 1I91 1 REMARK
REVDAT 4 24-FEB-09 1I91 1 VERSN
REVDAT 3 01-APR-03 1I91 1 JRNL
REVDAT 2 13-MAR-02 1I91 1 JRNL REMARK
REVDAT 1 28-MAR-01 1I91 0
JRNL AUTH C.Y.KIM,D.A.WHITTINGTON,J.S.CHANG,J.LIAO,J.A.MAY,
JRNL AUTH 2 D.W.CHRISTIANSON
JRNL TITL STRUCTURAL ASPECTS OF ISOZYME SELECTIVITY IN THE BINDING OF
JRNL TITL 2 INHIBITORS TO CARBONIC ANHYDRASES II AND IV.
JRNL REF J.MED.CHEM. V. 45 888 2002
JRNL REFN ISSN 0022-2623
JRNL PMID 11831900
JRNL DOI 10.1021/JM010163D
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 15740
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.151
REMARK 3 FREE R VALUE : 0.205
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 767
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) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
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 : 2058
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 31
REMARK 3 SOLVENT ATOMS : 107
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 20.49
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) : 0.009
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 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 1I91 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-MAR-01.
REMARK 100 THE DEPOSITION ID IS D_1000013056.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-SEP-98
REMARK 200 TEMPERATURE (KELVIN) : 298
REMARK 200 PH : 8.0
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 RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IIC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 16912
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
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 (%) : 99.1
REMARK 200 DATA REDUNDANCY : 3.200
REMARK 200 R MERGE (I) : 0.10500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.39700
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: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.83
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.08
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: METHYL MERCURIC ACETATE, TRIS-SULFATE,
REMARK 280 AMMONIUM SULFATE, PH 8.0, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 277K
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 20.50000
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 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 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 THR A 35 O HOH A 369 1.02
REMARK 500 C THR A 35 O HOH A 369 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 NH1 ARG A 27 O HIS A 36 2556 1.38
REMARK 500 O VAL A 150 O HOH A 265 1545 1.59
REMARK 500 N GLY A 102 OD2 ASP A 130 1545 1.62
REMARK 500 OD2 ASP A 110 O HOH A 350 2546 1.98
REMARK 500 CA GLY A 102 OD2 ASP A 130 1545 2.01
REMARK 500 NH1 ARG A 27 C HIS A 36 2556 2.09
REMARK 500 O LYS A 113 O HOH A 306 1545 2.10
REMARK 500 OE1 GLN A 103 NZ LYS A 133 1545 2.10
REMARK 500 CA GLY A 129 O HOH A 352 1565 2.17
REMARK 500 CG LYS A 39 OE1 GLN A 137 2546 2.18
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 HIS A 4 149.85 -179.79
REMARK 500 ASN A 11 21.80 -145.61
REMARK 500 ALA A 65 -176.67 -176.25
REMARK 500 ASP A 75 60.83 -65.35
REMARK 500 ASN A 244 55.27 -94.01
REMARK 500 LYS A 252 -135.15 56.90
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 262 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 94 NE2
REMARK 620 2 HIS A 96 NE2 117.4
REMARK 620 3 HIS A 119 ND1 111.1 97.9
REMARK 620 4 INQ A 555 N03 101.0 116.3 113.7
REMARK 620 5 INQ A 555 S01 92.8 138.7 96.3 24.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HG A 263 HG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 VAL A 135 O
REMARK 620 2 GLN A 137 O 96.0
REMARK 620 3 GLU A 205 O 154.5 89.0
REMARK 620 4 CYS A 206 SG 61.0 83.8 94.9
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 262
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG A 263
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE INQ A 555
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1I8Z RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II COMPLEXED WITH AL-6629
REMARK 900 RELATED ID: 1I90 RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II COMPLEXED WITH AL-8520
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE RESIDUE NUMBERING IS NOT SEQUENTIAL.
REMARK 999 RESIDUE 125 IS COVALENTLY BOUND TO RESIDUE 127.
DBREF 1I91 A 2 261 UNP P00918 CAH2_HUMAN 1 259
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 HG A 263 1
HET INQ A 555 29
HETNAM ZN ZINC ION
HETNAM HG MERCURY (II) ION
HETNAM INQ 6-[N-(3-HYDROXY-PHENYL)-3-(MORPHOLIN-4-YLMETHYL)-2H-
HETNAM 2 INQ THIENO[3,2-E]-1,2-THIAZINE-1,1,-DIOXIDE]-SULFONAMIDE
HETSYN INQ AL-6619; [2H-THIENO[3,2-E]-1,2-THIAZINE-6-SULFONAMIDE;
HETSYN 2 INQ 2-(3-HYDROXYPHENYL)-3-(4-MORPHOLINYL)-; 1,1-DIOXIDE]
FORMUL 2 ZN ZN 2+
FORMUL 3 HG HG 2+
FORMUL 4 INQ C17 H19 N3 O6 S3
FORMUL 5 HOH *107(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 B16 LYS A 39 TYR A 40 0
SHEET 2 B16 LYS A 257 ALA A 258 1 N ALA A 258 O LYS A 39
SHEET 3 B16 TYR A 191 GLY A 196 -1 N THR A 193 O LYS A 257
SHEET 4 B16 VAL A 207 LEU A 212 -1 O VAL A 207 N GLY A 196
SHEET 5 B16 LEU A 141 VAL A 150 1 O LEU A 141 N THR A 208
SHEET 6 B16 ILE A 216 VAL A 218 1 O ILE A 216 N LYS A 149
SHEET 7 B16 LEU A 141 VAL A 150 1 O PHE A 147 N ILE A 216
SHEET 8 B16 ALA A 116 ASN A 124 -1 O ALA A 116 N LEU A 148
SHEET 9 B16 TYR A 88 TRP A 97 -1 N ARG A 89 O TRP A 123
SHEET 10 B16 VAL A 78 GLY A 81 -1 N LEU A 79 O TYR A 88
SHEET 11 B16 LEU A 47 SER A 50 -1 N SER A 48 O LYS A 80
SHEET 12 B16 VAL A 78 GLY A 81 -1 N VAL A 78 O SER A 50
SHEET 13 B16 TYR A 88 TRP A 97 -1 O TYR A 88 N LEU A 79
SHEET 14 B16 PHE A 66 PHE A 70 -1 O PHE A 66 N PHE A 95
SHEET 15 B16 SER A 56 ASN A 61 -1 N LEU A 57 O GLU A 69
SHEET 16 B16 SER A 173 ASP A 175 -1 O ALA A 174 N ILE A 59
LINK NE2 HIS A 94 ZN ZN A 262 1555 1555 1.73
LINK NE2 HIS A 96 ZN ZN A 262 1555 1555 1.79
LINK ND1 HIS A 119 ZN ZN A 262 1555 1555 1.95
LINK O VAL A 135 HG HG A 263 1555 1555 3.35
LINK O GLN A 137 HG HG A 263 1555 1555 3.10
LINK O GLU A 205 HG HG A 263 1555 1555 3.26
LINK SG CYS A 206 HG HG A 263 1555 1555 1.60
LINK ZN ZN A 262 N03 INQ A 555 1555 1555 1.81
LINK ZN ZN A 262 S01 INQ A 555 1555 1555 2.92
CISPEP 1 SER A 29 PRO A 30 0 0.18
CISPEP 2 PRO A 201 PRO A 202 0 0.36
SITE 1 AC1 4 HIS A 94 HIS A 96 HIS A 119 INQ A 555
SITE 1 AC2 4 VAL A 135 GLN A 137 GLU A 205 CYS A 206
SITE 1 AC3 11 ASN A 67 GLN A 92 HIS A 94 HIS A 96
SITE 2 AC3 11 HIS A 119 PHE A 131 LEU A 198 THR A 199
SITE 3 AC3 11 THR A 200 ZN A 262 HOH A 303
CRYST1 42.400 41.000 72.200 90.00 104.90 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 0.023585 0.000000 0.006275 0.00000
SCALE2 0.000000 0.024390 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014332 0.00000
(ATOM LINES ARE NOT SHOWN.)
END