HEADER LYASE/LYASE INHIBITOR 12-AUG-16 5SZ6
TITLE CARBONIC ANHYDRASE IX-MIMIC IN COMPLEX WITH 4-(3-FORMYLPHENYL)-
TITLE 2 BENZENESULFONAMIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CARBONIC ANHYDRASE 2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 4-260;
COMPND 5 SYNONYM: CARBONATE DEHYDRATASE II,CARBONIC ANHYDRASE C,CAC,CARBONIC
COMPND 6 ANHYDRASE II,CA-II;
COMPND 7 EC: 4.2.1.1;
COMPND 8 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 SULFONAMIDE, INHIBITOR, ZINC-BINDING, LYASE-LYASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR A.BHATT,B.P.MAHON,B.CORNELIO,R.MCKENNA
REVDAT 3 04-OCT-23 5SZ6 1 REMARK
REVDAT 2 01-FEB-17 5SZ6 1 JRNL
REVDAT 1 28-DEC-16 5SZ6 0
JRNL AUTH A.BHATT,B.P.MAHON,V.W.CRUZEIRO,B.CORNELIO,M.LARONZE-COCHARD,
JRNL AUTH 2 M.CERUSO,J.SAPI,G.A.RANCE,A.N.KHLOBYSTOV,A.FONTANA,
JRNL AUTH 3 A.ROITBERG,C.T.SUPURAN,R.MCKENNA
JRNL TITL STRUCTURE-ACTIVITY RELATIONSHIPS OF BENZENESULFONAMIDE-BASED
JRNL TITL 2 INHIBITORS TOWARDS CARBONIC ANHYDRASE ISOFORM SPECIFICITY.
JRNL REF CHEMBIOCHEM V. 18 213 2017
JRNL REFN ESSN 1439-7633
JRNL PMID 27860128
JRNL DOI 10.1002/CBIC.201600513
REMARK 2
REMARK 2 RESOLUTION. 1.15 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX DEV_1839
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.15
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.95
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 3 NUMBER OF REFLECTIONS : 84634
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.144
REMARK 3 R VALUE (WORKING SET) : 0.144
REMARK 3 FREE R VALUE : 0.159
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.370
REMARK 3 FREE R VALUE TEST SET COUNT : 2010
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 19.9563 - 2.7688 0.96 5915 145 0.1338 0.1526
REMARK 3 2 2.7688 - 2.1986 1.00 6033 149 0.1322 0.1607
REMARK 3 3 2.1986 - 1.9209 1.00 6047 148 0.1316 0.1376
REMARK 3 4 1.9209 - 1.7454 1.00 5967 144 0.1385 0.1359
REMARK 3 5 1.7454 - 1.6204 1.00 6014 148 0.1403 0.1546
REMARK 3 6 1.6204 - 1.5249 1.00 5976 135 0.1410 0.1630
REMARK 3 7 1.5249 - 1.4485 1.00 5966 148 0.1478 0.1563
REMARK 3 8 1.4485 - 1.3855 0.99 5897 145 0.1495 0.1582
REMARK 3 9 1.3855 - 1.3322 0.98 5876 135 0.1603 0.1623
REMARK 3 10 1.3322 - 1.2862 0.98 5884 138 0.1604 0.1909
REMARK 3 11 1.2862 - 1.2460 0.98 5838 148 0.1728 0.1888
REMARK 3 12 1.2460 - 1.2104 0.97 5788 139 0.1782 0.2165
REMARK 3 13 1.2104 - 1.1785 0.97 5781 136 0.1865 0.1871
REMARK 3 14 1.1785 - 1.1498 0.95 5642 152 0.2163 0.2117
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.090
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 15.300
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 9.40
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.008 2166
REMARK 3 ANGLE : 1.318 2947
REMARK 3 CHIRALITY : 0.077 312
REMARK 3 PLANARITY : 0.007 378
REMARK 3 DIHEDRAL : 13.286 790
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): 12.0547 -1.6117 16.0338
REMARK 3 T TENSOR
REMARK 3 T11: 0.0642 T22: 0.0622
REMARK 3 T33: 0.0637 T12: 0.0012
REMARK 3 T13: 0.0037 T23: 0.0024
REMARK 3 L TENSOR
REMARK 3 L11: 0.6116 L22: 0.5215
REMARK 3 L33: 0.5226 L12: -0.0108
REMARK 3 L13: 0.1646 L23: -0.0596
REMARK 3 S TENSOR
REMARK 3 S11: -0.0113 S12: 0.0083 S13: 0.0323
REMARK 3 S21: -0.0250 S22: 0.0210 S23: -0.0090
REMARK 3 S31: 0.0056 S32: 0.0160 S33: 0.0544
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5SZ6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-AUG-16.
REMARK 100 THE DEPOSITION ID IS D_1000223364.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-MAY-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.2-8.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CHESS
REMARK 200 BEAMLINE : F1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.98
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 270
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 84634
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.150
REMARK 200 RESOLUTION RANGE LOW (A) : 19.953
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 200 DATA REDUNDANCY : 6.600
REMARK 200 R MERGE (I) : 0.11200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 3.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.15
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.18
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.5
REMARK 200 DATA REDUNDANCY IN SHELL : 6.00
REMARK 200 R MERGE FOR SHELL (I) : 0.61800
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 3KS3
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.96
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.12
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.6M SODIUM CITRATE, 50MM TRIS PH 7.8,
REMARK 280 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 20.73700
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 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 HE2 HIS A 107 HH TYR A 194 1.06
REMARK 500 O HOH A 479 O HOH A 557 1.67
REMARK 500 O HOH A 402 O HOH A 615 2.00
REMARK 500 O HOH A 549 O HOH A 622 2.03
REMARK 500 O HOH A 468 O HOH A 628 2.08
REMARK 500 O HOH A 459 O HOH A 664 2.15
REMARK 500 OE2 GLU A 214 O HOH A 401 2.18
REMARK 500 O GLU A 238 O HOH A 402 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 OE1 GLN A 103 HZ1 LYS A 133 1545 1.57
REMARK 500 O HOH A 557 O HOH A 595 2645 1.95
REMARK 500 O HOH A 717 O HOH A 753 2545 2.12
REMARK 500 OD1 ASP A 52 O HOH A 538 1455 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 ARG A 27 56.26 -144.81
REMARK 500 GLU A 106 -60.59 -93.39
REMARK 500 LYS A 111 -3.48 72.68
REMARK 500 ASN A 244 50.06 -93.54
REMARK 500 LYS A 252 -137.48 52.56
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 = 5.90 ANGSTROMS
REMARK 525 HOH A 762 DISTANCE = 5.97 ANGSTROMS
REMARK 525 HOH A 763 DISTANCE = 6.16 ANGSTROMS
REMARK 525 HOH A 764 DISTANCE = 8.94 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 102.6
REMARK 620 3 HIS A 119 ND1 113.1 99.9
REMARK 620 4 72G A 302 NAP 106.3 115.2 118.7
REMARK 620 5 72G A 302 SAM 99.4 143.3 97.9 29.2
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 72G A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 305
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5SZ0 RELATED DB: PDB
REMARK 900 RELATED ID: 5SZ1 RELATED DB: PDB
REMARK 900 RELATED ID: 5SZ2 RELATED DB: PDB
REMARK 900 RELATED ID: 5SZ3 RELATED DB: PDB
REMARK 900 RELATED ID: 5SZ4 RELATED DB: PDB
REMARK 900 RELATED ID: 5SZ5 RELATED DB: PDB
REMARK 900 RELATED ID: 5SZ7 RELATED DB: PDB
DBREF 5SZ6 A 4 261 UNP P00918 CAH2_HUMAN 4 260
SEQADV 5SZ6 SER A 65 UNP P00918 ALA 65 ENGINEERED MUTATION
SEQADV 5SZ6 GLN A 67 UNP P00918 ASN 67 ENGINEERED MUTATION
SEQADV 5SZ6 THR A 69 UNP P00918 GLU 69 ENGINEERED MUTATION
SEQADV 5SZ6 LEU A 91 UNP P00918 ILE 91 ENGINEERED MUTATION
SEQADV 5SZ6 VAL A 131 UNP P00918 PHE 130 ENGINEERED MUTATION
SEQADV 5SZ6 GLU A 170 UNP P00918 LYS 169 ENGINEERED MUTATION
SEQADV 5SZ6 ALA A 204 UNP P00918 LEU 203 ENGINEERED MUTATION
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 SER PHE GLN VAL
SEQRES 6 A 257 THR 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 LEU 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 VAL 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 GLU 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 ALA 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 72G A 302 29
HET GOL A 303 14
HET DMS A 304 10
HET DMS A 305 4
HETNAM ZN ZINC ION
HETNAM 72G 4-(3-FORMYLPHENYL)-BENZENESULFONAMIDE
HETNAM GOL GLYCEROL
HETNAM DMS DIMETHYL SULFOXIDE
HETSYN 72G 3'-FORMYL[1,1'-BIPHENYL]-4-SULFONAMIDE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 ZN ZN 2+
FORMUL 3 72G C13 H11 N O3 S
FORMUL 4 GOL C3 H8 O3
FORMUL 5 DMS 2(C2 H6 O S)
FORMUL 7 HOH *364(H2 O)
HELIX 1 AA1 HIS A 15 ASP A 19 5 5
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 ASP A 162 1 6
HELIX 7 AA7 VAL A 163 LYS A 168 5 6
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 LEU A 212
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 GLN A 92 O VAL A 121
SHEET 8 AA210 PHE A 66 PHE A 70 -1 N PHE A 70 O LEU A 91
SHEET 9 AA210 SER A 56 ASN A 61 -1 N LEU A 57 O THR 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 VAL A 121 N GLN A 92
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 2.04
LINK NE2 HIS A 96 ZN ZN A 301 1555 1555 2.05
LINK ND1 HIS A 119 ZN ZN A 301 1555 1555 2.04
LINK ZN ZN A 301 NAP 72G A 302 1555 1555 1.92
LINK ZN ZN A 301 SAM 72G A 302 1555 1555 3.00
CISPEP 1 SER A 29 PRO A 30 0 -0.74
CISPEP 2 PRO A 201 PRO A 202 0 13.86
SITE 1 AC1 4 HIS A 94 HIS A 96 HIS A 119 72G A 302
SITE 1 AC2 9 HIS A 94 HIS A 96 HIS A 119 LEU A 198
SITE 2 AC2 9 THR A 199 THR A 200 TRP A 209 ZN A 301
SITE 3 AC2 9 HOH A 567
SITE 1 AC3 6 SER A 99 LEU A 100 LEU A 240 VAL A 242
SITE 2 AC3 6 HOH A 404 HOH A 468
SITE 1 AC4 5 THR A 177 ASN A 178 PHE A 179 HOH A 407
SITE 2 AC4 5 HOH A 411
SITE 1 AC5 9 PRO A 13 GLU A 14 HIS A 17 ALA A 23
SITE 2 AC5 9 LYS A 24 HOH A 450 HOH A 512 HOH A 518
SITE 3 AC5 9 HOH A 574
CRYST1 42.020 41.474 72.229 90.00 103.77 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 0.023798 0.000000 0.005830 0.00000
SCALE2 0.000000 0.024111 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014254 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
