HEADER LYASE 23-OCT-06 2NN7
TITLE STRUCTURE OF INHIBITOR BINDING TO CARBONIC ANHYDRASE I
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CARBONIC ANHYDRASE 1;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: CARBONIC ANHYDRASE I, CARBONATE DEHYDRATASE I, CA-I;
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 GENE: CA1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS ZINC METALLOENZYME, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.W.CHRISTIANSON,K.M.JUDE
REVDAT 4 30-AUG-23 2NN7 1 REMARK LINK
REVDAT 3 18-OCT-17 2NN7 1 REMARK
REVDAT 2 24-FEB-09 2NN7 1 VERSN
REVDAT 1 08-MAY-07 2NN7 0
JRNL AUTH D.K.SRIVASTAVA,K.M.JUDE,A.L.BANERJEE,M.HALDAR,S.MANOKARAN,
JRNL AUTH 2 J.KOOREN,S.MALLIK,D.W.CHRISTIANSON
JRNL TITL STRUCTURAL ANALYSIS OF CHARGE DISCRIMINATION IN THE BINDING
JRNL TITL 2 OF INHIBITORS TO HUMAN CARBONIC ANHYDRASES I AND II.
JRNL REF J.AM.CHEM.SOC. V. 129 5528 2007
JRNL REFN ISSN 0002-7863
JRNL PMID 17407288
JRNL DOI 10.1021/JA068359W
REMARK 2
REMARK 2 RESOLUTION. 1.85 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
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) : 1.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.28
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 49703.609
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 92.1
REMARK 3 NUMBER OF REFLECTIONS : 43754
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 SET) : 0.204
REMARK 3 FREE R VALUE : 0.233
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1759
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.006
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.85
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.97
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 80.20
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 6038
REMARK 3 BIN R VALUE (WORKING SET) : 0.2640
REMARK 3 BIN FREE R VALUE : 0.3130
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 3.70
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 235
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.020
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4039
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 40
REMARK 3 SOLVENT ATOMS : 447
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 18.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.60
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -3.83000
REMARK 3 B22 (A**2) : 7.42000
REMARK 3 B33 (A**2) : -3.59000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.22
REMARK 3 ESD FROM SIGMAA (A) : 0.20
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.26
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.22
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.30
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.810
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.090 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.740 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.960 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.920 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.29
REMARK 3 BSOL : 32.12
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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : MH129.PAR
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : ION.PARAM
REMARK 3 PARAMETER FILE 5 : CCN.PAR
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : MH129.TOP
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : ION.TOP
REMARK 3 TOPOLOGY FILE 5 : CCN.TOP
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2NN7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-OCT-06.
REMARK 100 THE DEPOSITION ID IS D_1000040067.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-NOV-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : 1.85
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 46613
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.850
REMARK 200 RESOLUTION RANGE LOW (A) : 60.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 200 DATA REDUNDANCY : 3.900
REMARK 200 R MERGE (I) : 0.11300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.92
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.3
REMARK 200 DATA REDUNDANCY IN SHELL : 2.70
REMARK 200 R MERGE FOR SHELL (I) : 0.39100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.600
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: 2FOY
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.47
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.39
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, NACL, HEPES, TRIS, PH 7.0,
REMARK 280 VAPOR DIFFUSION, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-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 31.21050
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 60.98250
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 35.90900
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 60.98250
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 31.21050
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 35.90900
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 300 REMARK: THERE ARE 2 BIOLOGICAL UNITS IN THE ASYMMETRIC UNIT.
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
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 ALA A 1
REMARK 465 SER A 2
REMARK 465 ALA B 1
REMARK 465 SER B 2
REMARK 465 PRO B 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 LYS A 57 -56.67 -125.95
REMARK 500 SER A 65 -170.03 -170.89
REMARK 500 ASN A 75 40.70 -96.55
REMARK 500 PHE A 91 -16.46 -146.96
REMARK 500 ASN A 124 94.75 -69.72
REMARK 500 ASN A 244 32.55 -156.98
REMARK 500 LYS B 57 -60.54 -126.28
REMARK 500 SER B 65 -168.74 -167.73
REMARK 500 ASN B 75 34.38 -96.55
REMARK 500 ASN B 124 88.15 -68.71
REMARK 500 ASN B 244 35.71 -156.11
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 106.9
REMARK 620 3 HIS A 119 ND1 112.2 102.5
REMARK 620 4 M29 A 311 N 116.6 101.9 114.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 302 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 94 NE2
REMARK 620 2 HIS B 96 NE2 107.9
REMARK 620 3 HIS B 119 ND1 111.8 102.0
REMARK 620 4 M29 B 312 N 117.4 103.4 112.6
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 ZN B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE M29 A 311
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE M29 B 312
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 341
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2NMX RELATED DB: PDB
REMARK 900 STRUCTURE OF INHIBITOR BINDING TO CARBONIC ANHYDRASE I
REMARK 900 RELATED ID: 2NN1 RELATED DB: PDB
REMARK 900 STRUCTURE OF INHIBITOR BINDING TO CARBONIC ANHYDRASE I
REMARK 900 RELATED ID: 2NNG RELATED DB: PDB
REMARK 900 STRUCTURE OF INHIBITOR BINDING TO CARBONIC ANHYDRASE II
REMARK 900 RELATED ID: 2NNO RELATED DB: PDB
REMARK 900 STRUCTURE OF INHIBITOR BINDING TO CARBONIC ANHYDRASE II
REMARK 900 RELATED ID: 2NNS RELATED DB: PDB
REMARK 900 STRUCTURE OF INHIBITOR BINDING TO CARBONIC ANHYDRASE II
REMARK 900 RELATED ID: 2NNV RELATED DB: PDB
REMARK 900 STRUCTURE OF INHIBITOR BINDING TO CARBONIC ANHYDRASE II
DBREF 2NN7 A 1 260 UNP P00915 CAH1_HUMAN 1 260
DBREF 2NN7 B 1 260 UNP P00915 CAH1_HUMAN 1 260
SEQRES 1 A 260 ALA SER PRO ASP TRP GLY TYR ASP ASP LYS ASN GLY PRO
SEQRES 2 A 260 GLU GLN TRP SER LYS LEU TYR PRO ILE ALA ASN GLY ASN
SEQRES 3 A 260 ASN GLN SER PRO VAL ASP ILE LYS THR SER GLU THR LYS
SEQRES 4 A 260 HIS ASP THR SER LEU LYS PRO ILE SER VAL SER TYR ASN
SEQRES 5 A 260 PRO ALA THR ALA LYS GLU ILE ILE ASN VAL GLY HIS SER
SEQRES 6 A 260 PHE HIS VAL ASN PHE GLU ASP ASN ASP ASN ARG SER VAL
SEQRES 7 A 260 LEU LYS GLY GLY PRO PHE SER ASP SER TYR ARG LEU PHE
SEQRES 8 A 260 GLN PHE HIS PHE HIS TRP GLY SER THR ASN GLU HIS GLY
SEQRES 9 A 260 SER GLU HIS THR VAL ASP GLY VAL LYS TYR SER ALA GLU
SEQRES 10 A 260 LEU HIS VAL ALA HIS TRP ASN SER ALA LYS TYR SER SER
SEQRES 11 A 260 LEU ALA GLU ALA ALA SER LYS ALA ASP GLY LEU ALA VAL
SEQRES 12 A 260 ILE GLY VAL LEU MET LYS VAL GLY GLU ALA ASN PRO LYS
SEQRES 13 A 260 LEU GLN LYS VAL LEU ASP ALA LEU GLN ALA ILE LYS THR
SEQRES 14 A 260 LYS GLY LYS ARG ALA PRO PHE THR ASN PHE ASP PRO SER
SEQRES 15 A 260 THR LEU LEU PRO SER SER LEU ASP PHE TRP THR TYR PRO
SEQRES 16 A 260 GLY SER LEU THR HIS PRO PRO LEU TYR GLU SER VAL THR
SEQRES 17 A 260 TRP ILE ILE CYS LYS GLU SER ILE SER VAL SER SER GLU
SEQRES 18 A 260 GLN LEU ALA GLN PHE ARG SER LEU LEU SER ASN VAL GLU
SEQRES 19 A 260 GLY ASP ASN ALA VAL PRO MET GLN HIS ASN ASN ARG PRO
SEQRES 20 A 260 THR GLN PRO LEU LYS GLY ARG THR VAL ARG ALA SER PHE
SEQRES 1 B 260 ALA SER PRO ASP TRP GLY TYR ASP ASP LYS ASN GLY PRO
SEQRES 2 B 260 GLU GLN TRP SER LYS LEU TYR PRO ILE ALA ASN GLY ASN
SEQRES 3 B 260 ASN GLN SER PRO VAL ASP ILE LYS THR SER GLU THR LYS
SEQRES 4 B 260 HIS ASP THR SER LEU LYS PRO ILE SER VAL SER TYR ASN
SEQRES 5 B 260 PRO ALA THR ALA LYS GLU ILE ILE ASN VAL GLY HIS SER
SEQRES 6 B 260 PHE HIS VAL ASN PHE GLU ASP ASN ASP ASN ARG SER VAL
SEQRES 7 B 260 LEU LYS GLY GLY PRO PHE SER ASP SER TYR ARG LEU PHE
SEQRES 8 B 260 GLN PHE HIS PHE HIS TRP GLY SER THR ASN GLU HIS GLY
SEQRES 9 B 260 SER GLU HIS THR VAL ASP GLY VAL LYS TYR SER ALA GLU
SEQRES 10 B 260 LEU HIS VAL ALA HIS TRP ASN SER ALA LYS TYR SER SER
SEQRES 11 B 260 LEU ALA GLU ALA ALA SER LYS ALA ASP GLY LEU ALA VAL
SEQRES 12 B 260 ILE GLY VAL LEU MET LYS VAL GLY GLU ALA ASN PRO LYS
SEQRES 13 B 260 LEU GLN LYS VAL LEU ASP ALA LEU GLN ALA ILE LYS THR
SEQRES 14 B 260 LYS GLY LYS ARG ALA PRO PHE THR ASN PHE ASP PRO SER
SEQRES 15 B 260 THR LEU LEU PRO SER SER LEU ASP PHE TRP THR TYR PRO
SEQRES 16 B 260 GLY SER LEU THR HIS PRO PRO LEU TYR GLU SER VAL THR
SEQRES 17 B 260 TRP ILE ILE CYS LYS GLU SER ILE SER VAL SER SER GLU
SEQRES 18 B 260 GLN LEU ALA GLN PHE ARG SER LEU LEU SER ASN VAL GLU
SEQRES 19 B 260 GLY ASP ASN ALA VAL PRO MET GLN HIS ASN ASN ARG PRO
SEQRES 20 B 260 THR GLN PRO LEU LYS GLY ARG THR VAL ARG ALA SER PHE
HET ZN A 301 1
HET M29 A 311 17
HET DMS A 341 4
HET ZN B 302 1
HET M29 B 312 17
HETNAM ZN ZINC ION
HETNAM M29 ETHYL 3-[4-(AMINOSULFONYL)PHENYL]PROPANOATE
HETNAM DMS DIMETHYL SULFOXIDE
HETSYN M29 4-PROPYL BENZENESULFONAMIDE ETHYL ESTER
FORMUL 3 ZN 2(ZN 2+)
FORMUL 4 M29 2(C11 H15 N O4 S)
FORMUL 5 DMS C2 H6 O S
FORMUL 8 HOH *447(H2 O)
HELIX 1 1 GLY A 12 LEU A 19 5 8
HELIX 2 2 TYR A 20 GLY A 25 5 6
HELIX 3 3 LYS A 34 THR A 38 5 5
HELIX 4 4 ASN A 52 ALA A 54 5 3
HELIX 5 5 SER A 130 ALA A 135 1 6
HELIX 6 6 ASN A 154 LYS A 156 5 3
HELIX 7 7 LEU A 157 LEU A 164 1 8
HELIX 8 8 GLN A 165 ILE A 167 5 3
HELIX 9 9 ASP A 180 LEU A 185 5 6
HELIX 10 10 SER A 219 SER A 228 1 10
HELIX 11 11 GLY B 12 LEU B 19 5 8
HELIX 12 12 TYR B 20 GLY B 25 5 6
HELIX 13 13 LYS B 34 THR B 38 5 5
HELIX 14 14 ASN B 52 ALA B 54 5 3
HELIX 15 15 SER B 130 ALA B 135 1 6
HELIX 16 16 ASN B 154 LYS B 156 5 3
HELIX 17 17 LEU B 157 LEU B 164 1 8
HELIX 18 18 GLN B 165 ILE B 167 5 3
HELIX 19 19 ASP B 180 LEU B 185 5 6
HELIX 20 20 SER B 219 SER B 228 1 10
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 HIS A 40 0
SHEET 2 B10 ARG A 257 ALA A 258 1 O ALA A 258 N LYS A 39
SHEET 3 B10 PHE A 191 GLY A 196 -1 N THR A 193 O ARG A 257
SHEET 4 B10 VAL A 207 CYS 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 VAL 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 PHE A 70 O PHE A 91
SHEET 9 B10 ALA A 56 ASN A 61 -1 N ILE A 60 O HIS A 67
SHEET 10 B10 ARG A 173 PRO A 175 -1 O ALA A 174 N ILE A 59
SHEET 1 C 6 ILE 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 VAL A 146 N LEU A 118
SHEET 6 C 6 ILE A 216 VAL A 218 1 O ILE A 216 N LYS A 149
SHEET 1 D 2 ASP B 32 ILE B 33 0
SHEET 2 D 2 THR B 108 VAL B 109 1 O THR B 108 N ILE B 33
SHEET 1 E10 LYS B 39 HIS B 40 0
SHEET 2 E10 ARG B 257 ALA B 258 1 O ALA B 258 N LYS B 39
SHEET 3 E10 PHE B 191 GLY B 196 -1 N THR B 193 O ARG B 257
SHEET 4 E10 VAL B 207 CYS B 212 -1 O VAL B 207 N GLY B 196
SHEET 5 E10 LEU B 141 VAL B 150 1 N GLY B 145 O ILE B 210
SHEET 6 E10 ALA B 116 TRP B 123 -1 N LEU B 118 O VAL B 146
SHEET 7 E10 TYR B 88 TRP B 97 -1 N ARG B 89 O TRP B 123
SHEET 8 E10 PHE B 66 PHE B 70 -1 N VAL B 68 O PHE B 93
SHEET 9 E10 ALA B 56 ASN B 61 -1 N GLU B 58 O ASN B 69
SHEET 10 E10 ARG B 173 PRO B 175 -1 O ALA B 174 N ILE B 59
SHEET 1 F 6 ILE B 47 SER B 50 0
SHEET 2 F 6 VAL B 78 GLY B 81 -1 O LYS B 80 N SER B 48
SHEET 3 F 6 TYR B 88 TRP B 97 -1 O TYR B 88 N LEU B 79
SHEET 4 F 6 ALA B 116 TRP B 123 -1 O TRP B 123 N ARG B 89
SHEET 5 F 6 LEU B 141 VAL B 150 -1 O VAL B 146 N LEU B 118
SHEET 6 F 6 ILE B 216 VAL B 218 1 O ILE B 216 N LYS B 149
LINK NE2 HIS A 94 ZN ZN A 301 1555 1555 2.13
LINK NE2 HIS A 96 ZN ZN A 301 1555 1555 2.23
LINK ND1 HIS A 119 ZN ZN A 301 1555 1555 2.12
LINK ZN ZN A 301 N M29 A 311 1555 1555 2.10
LINK NE2 HIS B 94 ZN ZN B 302 1555 1555 2.09
LINK NE2 HIS B 96 ZN ZN B 302 1555 1555 2.13
LINK ND1 HIS B 119 ZN ZN B 302 1555 1555 2.13
LINK ZN ZN B 302 N M29 B 312 1555 1555 2.07
CISPEP 1 SER A 29 PRO A 30 0 0.14
CISPEP 2 PRO A 201 PRO A 202 0 0.05
CISPEP 3 SER B 29 PRO B 30 0 -0.66
CISPEP 4 PRO B 201 PRO B 202 0 1.74
SITE 1 AC1 4 HIS A 94 HIS A 96 HIS A 119 M29 A 311
SITE 1 AC2 4 HIS B 94 HIS B 96 HIS B 119 M29 B 312
SITE 1 AC3 12 ASN A 69 GLN A 92 HIS A 94 HIS A 96
SITE 2 AC3 12 HIS A 119 VAL A 143 LEU A 198 THR A 199
SITE 3 AC3 12 HIS A 200 TRP A 209 ZN A 301 ALA B 132
SITE 1 AC4 12 HOH A 549 ASN B 69 PHE B 91 GLN B 92
SITE 2 AC4 12 HIS B 94 HIS B 96 HIS B 119 LEU B 198
SITE 3 AC4 12 THR B 199 HIS B 200 TRP B 209 ZN B 302
SITE 1 AC5 4 THR A 35 THR A 38 TRP A 192 PHE A 260
CRYST1 62.421 71.818 121.965 90.00 90.00 90.00 P 21 21 21 8
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 0.016020 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013924 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008199 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
