HEADER LYASE 04-APR-13 4K0T
TITLE STRUCTURE OF HCAIX MIMIC (HCAII WITH 5 MUTATIONS IN ACTIVE SITE) IN
TITLE 2 COMPLEX WITH CHLORZOLAMIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CARBONIC ANHYDRASE 2;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CARBONATE DEHYDRATASE II, CARBONIC ANHYDRASE C, CAC,
COMPND 5 CARBONIC ANHYDRASE II, CA-II;
COMPND 6 EC: 4.2.1.1;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: 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: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS ALPHA BETA FOLD, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.BISWAS,R.MCKENNA
REVDAT 2 20-SEP-23 4K0T 1 REMARK SEQADV LINK
REVDAT 1 09-APR-14 4K0T 0
JRNL AUTH S.BISWAS,D.WEST,M.PINARD,R.MCKENNA
JRNL TITL DESIGNING ISOFORM SPECIFIC INHIBITORS AGAINST HCAIX USING
JRNL TITL 2 CAIX MIMIC
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.78 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.8_1069
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) : 1.78
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.40
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.2
REMARK 3 NUMBER OF REFLECTIONS : 21895
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.155
REMARK 3 R VALUE (WORKING SET) : 0.153
REMARK 3 FREE R VALUE : 0.197
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1117
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 35.4021 - 3.5582 0.96 2692 151 0.1357 0.1611
REMARK 3 2 3.5582 - 2.8246 0.96 2646 131 0.1567 0.2025
REMARK 3 3 2.8246 - 2.4676 0.96 2609 146 0.1686 0.2216
REMARK 3 4 2.4676 - 2.2421 0.96 2612 136 0.1572 0.1935
REMARK 3 5 2.2421 - 2.0814 0.95 2604 123 0.1518 0.2073
REMARK 3 6 2.0814 - 1.9587 0.95 2571 133 0.1533 0.2402
REMARK 3 7 1.9587 - 1.8606 0.94 2563 140 0.1557 0.2059
REMARK 3 8 1.8606 - 1.7800 0.93 2481 157 0.1867 0.2406
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) : 0.190
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.670
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 18.49
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 13.77
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 : 0.007 2199
REMARK 3 ANGLE : 1.180 3000
REMARK 3 CHIRALITY : 0.079 314
REMARK 3 PLANARITY : 0.005 388
REMARK 3 DIHEDRAL : 15.075 824
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
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 4K0T COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-APR-13.
REMARK 100 THE DEPOSITION ID IS D_1000078747.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-SEP-11
REMARK 200 TEMPERATURE (KELVIN) : 100
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 RUH3R
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : VARIMAX OPTICS
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV++
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21896
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.780
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.2
REMARK 200 DATA REDUNDANCY : 2.700
REMARK 200 R MERGE (I) : 0.05000
REMARK 200 R SYM (I) : 0.05000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.1200
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.78
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.84
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.1
REMARK 200 DATA REDUNDANCY IN SHELL : 2.70
REMARK 200 R MERGE FOR SHELL (I) : 0.19600
REMARK 200 R SYM FOR SHELL (I) : 0.19600
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.680
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: PDB ENTRY 2ILI
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.75
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.08
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.6 M SODIUM CITRATE, 50 MM TRIS, PH
REMARK 280 8.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
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 20.54000
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 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 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 HIS A 4 CG
REMARK 480 LYS A 149 CA CB CG CD CE NZ
REMARK 480 GLU A 239 CD
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 OD2 ASP A 175 O HOH A 637 2.07
REMARK 500 O THR A 37 O HOH A 624 2.12
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 O HOH A 592 O HOH A 627 2656 2.17
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 LYS A 111 -3.73 74.12
REMARK 500 ASN A 244 52.50 -93.62
REMARK 500 LYS A 252 -135.12 52.13
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 106.3
REMARK 620 3 HIS A 119 ND1 114.7 98.6
REMARK 620 4 D9Z A 303 N3 109.7 112.9 114.0
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 DMS A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE D9Z 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 GOL A 305
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4K0S RELATED DB: PDB
REMARK 900 RELATED ID: 4K0Z RELATED DB: PDB
REMARK 900 RELATED ID: 4K13 RELATED DB: PDB
REMARK 900 RELATED ID: 4K1Q RELATED DB: PDB
DBREF 4K0T A 4 261 UNP P00918 CAH2_HUMAN 4 260
SEQADV 4K0T SER A 65 UNP P00918 ALA 65 ENGINEERED MUTATION
SEQADV 4K0T GLN A 67 UNP P00918 ASN 67 ENGINEERED MUTATION
SEQADV 4K0T THR A 69 UNP P00918 GLU 69 ENGINEERED MUTATION
SEQADV 4K0T LEU A 131 UNP P00918 PHE 130 ENGINEERED MUTATION
SEQADV 4K0T GLU A 170 UNP P00918 LYS 169 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 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 LEU 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 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 DMS A 302 4
HET D9Z A 303 16
HET DMS A 304 4
HET GOL A 305 6
HETNAM ZN ZINC ION
HETNAM DMS DIMETHYL SULFOXIDE
HETNAM D9Z 5-(2-CHLOROPHENYL)-1,3,4-THIADIAZOLE-2-SULFONAMIDE
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 ZN ZN 2+
FORMUL 3 DMS 2(C2 H6 O S)
FORMUL 4 D9Z C8 H6 CL N3 O2 S2
FORMUL 6 GOL C3 H8 O3
FORMUL 7 HOH *239(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 ASP A 162 1 6
HELIX 7 7 VAL A 163 LYS A 168 5 6
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 B10 LYS A 39 TYR A 40 0
SHEET 2 B10 LYS A 257 ALA A 258 1 O ALA A 258 N LYS A 39
SHEET 3 B10 TYR A 191 GLY A 196 -1 N THR A 193 O LYS A 257
SHEET 4 B10 VAL A 207 LEU 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 ILE A 146
SHEET 7 B10 TYR A 88 TRP A 97 -1 N GLN A 92 O VAL A 121
SHEET 8 B10 PHE A 66 PHE A 70 -1 N PHE A 70 O ILE A 91
SHEET 9 B10 SER A 56 ASN A 61 -1 N LEU A 57 O THR A 69
SHEET 10 B10 SER A 173 ASP A 175 -1 O ALA A 174 N ILE A 59
SHEET 1 C 6 LEU 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 VAL A 121 N GLN A 92
SHEET 5 C 6 LEU A 141 VAL A 150 -1 O ILE A 146 N LEU A 118
SHEET 6 C 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 1.98
LINK NE2 HIS A 96 ZN ZN A 301 1555 1555 1.99
LINK ND1 HIS A 119 ZN ZN A 301 1555 1555 2.02
LINK ZN ZN A 301 N3 D9Z A 303 1555 1555 1.98
CISPEP 1 SER A 29 PRO A 30 0 0.24
CISPEP 2 PRO A 201 PRO A 202 0 10.31
SITE 1 AC1 4 HIS A 94 HIS A 96 HIS A 119 D9Z A 303
SITE 1 AC2 2 ASP A 243 TRP A 245
SITE 1 AC3 9 HIS A 94 HIS A 96 HIS A 119 VAL A 121
SITE 2 AC3 9 LEU A 198 THR A 199 THR A 200 TRP A 209
SITE 3 AC3 9 ZN A 301
SITE 1 AC4 2 LYS A 159 THR A 177
SITE 1 AC5 3 LYS A 149 PRO A 215 HOH A 474
CRYST1 41.886 41.080 71.794 90.00 103.75 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 0.023874 0.000000 0.005844 0.00000
SCALE2 0.000000 0.024343 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014340 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
