HEADER LYASE 11-MAY-17 5NXW
TITLE CARBONIC ANHYDRASE II INHIBITOR RA9
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 CARBONIC ANHYDRASE II, CA INHIBITOR, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.BRYNDA,P.REZACOVA,M.HOREJSI,J.FANFRLIK
REVDAT 4 17-JAN-24 5NXW 1 REMARK
REVDAT 3 18-APR-18 5NXW 1 JRNL
REVDAT 2 24-JAN-18 5NXW 1 REMARK
REVDAT 1 17-JAN-18 5NXW 0
JRNL AUTH A.PECINA,J.BRYNDA,L.VRZAL,R.GNANASEKARAN,M.HOREJSI,
JRNL AUTH 2 S.M.EYRILMEZ,J.REZAC,M.LEPSIK,P.REZACOVA,P.HOBZA,P.MAJER,
JRNL AUTH 3 V.VEVERKA,J.FANFRLIK
JRNL TITL RANKING POWER OF THE SQM/COSMO SCORING FUNCTION ON CARBONIC
JRNL TITL 2 ANHYDRASE II-INHIBITOR COMPLEXES.
JRNL REF CHEMPHYSCHEM V. 19 873 2018
JRNL REFN ISSN 1439-7641
JRNL PMID 29316128
JRNL DOI 10.1002/CPHC.201701104
REMARK 2
REMARK 2 RESOLUTION. 1.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC REFMAC_5.8.0103
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.99
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 84.2
REMARK 3 NUMBER OF REFLECTIONS : 82136
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) : 0.127
REMARK 3 R VALUE (WORKING SET) : 0.127
REMARK 3 FREE R VALUE : 0.155
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 0.600
REMARK 3 FREE R VALUE TEST SET COUNT : 521
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2031
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 43
REMARK 3 SOLVENT ATOMS : 340
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 12.27
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 12.36
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.28000
REMARK 3 B22 (A**2) : -0.05000
REMARK 3 B33 (A**2) : -0.13000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.15000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.031
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.032
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.019
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.879
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : NULL ; NULL
REMARK 3 ANGLE DISTANCE (A) : NULL ; NULL
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : NULL ; NULL
REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : NULL ; NULL
REMARK 3 STAGGERED (DEGREES) : NULL ; NULL
REMARK 3 TRANSVERSE (DEGREES) : NULL ; 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 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 5NXW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-MAY-17.
REMARK 100 THE DEPOSITION ID IS D_1200004912.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-DEC-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) : Y
REMARK 200 RADIATION SOURCE : BESSY
REMARK 200 BEAMLINE : 14.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.91841
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 159770
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.100
REMARK 200 RESOLUTION RANGE LOW (A) : 40.990
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 82.9
REMARK 200 DATA REDUNDANCY : 3.005
REMARK 200 R MERGE (I) : 0.04900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.1200
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.17
REMARK 200 COMPLETENESS FOR SHELL (%) : 33.2
REMARK 200 DATA REDUNDANCY IN SHELL : 1.84
REMARK 200 R MERGE FOR SHELL (I) : 0.25700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.480
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: 3PO6
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.65
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.11
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 50 MM TRIS 1.6 M NATRIUM CITRATE, PH
REMARK 280 7.8, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K
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 20.66350
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: 11710 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 LYS A 9 CG CD CE NZ
REMARK 470 LYS A 45 CE NZ
REMARK 470 ALA A 54 N
REMARK 470 LYS A 80 CE NZ
REMARK 470 LYS A 149 NZ
REMARK 470 LYS A 159 CD CE NZ
REMARK 470 LYS A 261 CG CD CE NZ
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 LYS A 76 CB CG CD CE NZ
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 OE2 GLU A 14 O HOH A 730 1655 1.50
REMARK 500 OE1 GLU A 14 O HOH A 577 1655 1.52
REMARK 500 CD GLU A 14 O HOH A 730 1655 1.88
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 LYS A 76 CA LYS A 76 CB -0.902
REMARK 500 THR A 125 C LYS A 127 N 0.162
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 54.30 -140.47
REMARK 500 ALA A 65 -169.01 -161.07
REMARK 500 ALA A 77 84.96 52.74
REMARK 500 ALA A 77 87.13 -161.03
REMARK 500 GLU A 106 -60.05 -92.89
REMARK 500 LYS A 111 -2.90 72.77
REMARK 500 PHE A 176 75.42 -153.31
REMARK 500 PHE A 176 75.42 -154.75
REMARK 500 ASN A 244 45.65 -93.63
REMARK 500 LYS A 252 -139.17 53.11
REMARK 500 ASN A 253 9.03 58.74
REMARK 500 ARG A 254 153.34 -48.77
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLY A 235 GLU A 236 -146.18
REMARK 500 ASN A 253 ARG A 254 148.34
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 738 DISTANCE = 6.09 ANGSTROMS
REMARK 525 HOH A 739 DISTANCE = 6.15 ANGSTROMS
REMARK 525 HOH A 740 DISTANCE = 6.62 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 104.1
REMARK 620 3 HIS A 119 ND1 112.1 98.4
REMARK 620 4 RA9 A 302 N4 109.9 113.5 117.7
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 RA9 A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue RA9 A 303
DBREF 5NXW A 4 261 UNP P00918 CAH2_HUMAN 4 260
SEQRES 1 A 257 HIS TRP GLY TYR GLY LYS HIS ASN GLY PRO GLU HIS TRP
SEQRES 2 A 257 HIS LYS ASP PHE PRO ILE ALA LYS GLY GLU ARG GLN SER
SEQRES 3 A 257 PRO VAL ASP ILE ASP THR HIS THR ALA LYS TYR ASP PRO
SEQRES 4 A 257 SER LEU LYS PRO LEU SER VAL SER TYR ASP GLN ALA THR
SEQRES 5 A 257 SER LEU ARG ILE LEU ASN ASN GLY HIS ALA PHE ASN VAL
SEQRES 6 A 257 GLU PHE ASP ASP SER GLN ASP LYS ALA VAL LEU LYS GLY
SEQRES 7 A 257 GLY PRO LEU ASP GLY THR TYR ARG LEU ILE GLN PHE HIS
SEQRES 8 A 257 PHE HIS TRP GLY SER LEU ASP GLY GLN GLY SER GLU HIS
SEQRES 9 A 257 THR VAL ASP LYS LYS LYS TYR ALA ALA GLU LEU HIS LEU
SEQRES 10 A 257 VAL HIS TRP ASN THR LYS TYR GLY ASP PHE GLY LYS ALA
SEQRES 11 A 257 VAL GLN GLN PRO ASP GLY LEU ALA VAL LEU GLY ILE PHE
SEQRES 12 A 257 LEU LYS VAL GLY SER ALA LYS PRO GLY LEU GLN LYS VAL
SEQRES 13 A 257 VAL ASP VAL LEU ASP SER ILE LYS THR LYS GLY LYS SER
SEQRES 14 A 257 ALA ASP PHE THR ASN PHE ASP PRO ARG GLY LEU LEU PRO
SEQRES 15 A 257 GLU SER LEU ASP TYR TRP THR TYR PRO GLY SER LEU THR
SEQRES 16 A 257 THR PRO PRO LEU LEU GLU CYS VAL THR TRP ILE VAL LEU
SEQRES 17 A 257 LYS GLU PRO ILE SER VAL SER SER GLU GLN VAL LEU LYS
SEQRES 18 A 257 PHE ARG LYS LEU ASN PHE ASN GLY GLU GLY GLU PRO GLU
SEQRES 19 A 257 GLU LEU MET VAL ASP ASN TRP ARG PRO ALA GLN PRO LEU
SEQRES 20 A 257 LYS ASN ARG GLN ILE LYS ALA SER PHE LYS
HET ZN A 301 1
HET RA9 A 302 42
HET RA9 A 303 21
HETNAM ZN ZINC ION
HETNAM RA9 2-[(5-AZANYL-1,3,4-THIADIAZOL-2-YL)SULFANYL]-~{N}-(4-
HETNAM 2 RA9 SULFAMOYLPHENYL)ETHANAMIDE
FORMUL 2 ZN ZN 2+
FORMUL 3 RA9 2(C10 H11 N5 O3 S3)
FORMUL 5 HOH *340(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 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 2.03
LINK NE2 HIS A 96 ZN ZN A 301 1555 1555 2.08
LINK ND1 HIS A 119 ZN ZN A 301 1555 1555 2.05
LINK ZN ZN A 301 N4 RA9 A 302 1555 1555 1.94
CISPEP 1 SER A 29 PRO A 30 0 -2.92
CISPEP 2 PRO A 201 PRO A 202 0 17.43
SITE 1 AC1 4 HIS A 94 HIS A 96 HIS A 119 RA9 A 302
SITE 1 AC2 21 HIS A 64 ASN A 67 GLN A 92 HIS A 94
SITE 2 AC2 21 HIS A 96 HIS A 119 PHE A 131 GLY A 132
SITE 3 AC2 21 LEU A 198 THR A 199 THR A 200 TRP A 209
SITE 4 AC2 21 ZN A 301 HOH A 401 HOH A 402 HOH A 409
SITE 5 AC2 21 HOH A 412 HOH A 419 HOH A 456 HOH A 603
SITE 6 AC2 21 HOH A 637
SITE 1 AC3 13 HIS A 4 TRP A 5 HIS A 10 ASN A 11
SITE 2 AC3 13 HIS A 15 TRP A 16 ASP A 19 ASP A 180
SITE 3 AC3 13 ARG A 182 GLY A 183 HOH A 433 HOH A 600
SITE 4 AC3 13 HOH A 619
CRYST1 42.328 41.327 71.999 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 0.023625 0.000000 0.006078 0.00000
SCALE2 0.000000 0.024197 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014341 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
