HEADER COMPLEX (TRANSCRIPTION REGULATION/DNA) 02-MAR-98 1TF6 TITLE CO-CRYSTAL STRUCTURE OF XENOPUS TFIIIA ZINC FINGER DOMAIN TITLE 2 BOUND TO THE 5S RIBOSOMAL RNA GENE INTERNAL CONTROL REGION COMPND MOL_ID: 1; COMPND 2 MOLECULE: TFIIIA; COMPND 3 CHAIN: A, D; COMPND 4 FRAGMENT: NH2-TERMINAL SIX FINGERS, RESIDUE 1 - 190; COMPND 5 ENGINEERED: YES; COMPND 6 BIOLOGICAL_UNIT: MONOMER; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: 5S RIBOSOMAL RNA GENE; COMPND 9 CHAIN: B, C, E, F; COMPND 10 FRAGMENT: INTERNAL PROMOTER REGION; COMPND 11 ENGINEERED: YES; COMPND 12 OTHER_DETAILS: CHAINS B AND E ARE NONCODING STRAND COMPND 13 NUCLEOTIDES +62 - +92, CHAINS C AND F ARE CODING STRAND COMPND 14 NUCLEOTIDES +63' - +93' SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: XENOPUS LAEVIS; SOURCE 3 ORGANISM_COMMON: AFRICAN CLAWED FROG; SOURCE 4 ORGAN: OVARY; SOURCE 5 CELL: OOCYTE; SOURCE 6 ORGANELLE: NUCLEUS; SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3); SOURCE 9 EXPRESSION_SYSTEM_CELLULAR_LOCATION: INCLUSION BODY; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PRSET B; SOURCE 11 OTHER_DETAILS: CDNA; SOURCE 12 MOL_ID: 2; SOURCE 13 SYNTHETIC: YES KEYWDS COMPLEX (TRANSCRIPTION REGULATION/DNA), RNA POLYMERASE III, KEYWDS 2 TRANSCRIPTION INITIATION, ZINC FINGER PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR R.T.NOLTE,R.M.CONLIN,S.C.HARRISON,R.S.BROWN REVDAT 1 08-JUL-98 1TF6 0 JRNL AUTH R.T.NOLTE,R.M.CONLIN,S.C.HARRISON,R.S.BROWN JRNL TITL DIFFERING ROLES FOR ZINC FINGERS IN DNA JRNL TITL 2 RECOGNITION: STRUCTURE OF A SIX-FINGER JRNL TITL 3 TRANSCRIPTION FACTOR IIIA COMPLEX JRNL REF PROC.NAT.ACAD.SCI.USA V. 95 2938 1998 JRNL REFN ASTM PNASA6 US ISSN 0027-8424 0040 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 3.1 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.851 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.1 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 8.0 REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.0 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1000000.0 REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.00001 REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 81.4 REMARK 3 NUMBER OF REFLECTIONS : 17014 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) : 0.308 REMARK 3 FREE R VALUE : 0.363 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.9 REMARK 3 FREE R VALUE TEST SET COUNT : 497 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.016 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 : 2953 REMARK 3 NUCLEIC ACID ATOMS : 2530 REMARK 3 HETEROGEN ATOMS : 12 REMARK 3 SOLVENT ATOMS : 0 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 39.7 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 65.0 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 17.26 REMARK 3 B22 (A**2) : -5.82 REMARK 3 B33 (A**2) : -11.44 REMARK 3 B12 (A**2) : 4.52 REMARK 3 B13 (A**2) : -0.72 REMARK 3 B23 (A**2) : 1.02 REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.55 REMARK 3 ESD FROM SIGMAA (A) : 0.43 REMARK 3 LOW RESOLUTION CUTOFF (A) : 8.0 REMARK 3 REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.64 REMARK 3 ESD FROM C-V SIGMAA (A) : NULL REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.005 REMARK 3 BOND ANGLES (DEGREES) : 0.9 REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.9 REMARK 3 IMPROPER ANGLES (DEGREES) : 0.94 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) : 2.47 ; 2.00 REMARK 3 MAIN-CHAIN ANGLE (A**2) : 4.45 ; 4.00 REMARK 3 SIDE-CHAIN BOND (A**2) : 2.49 ; 2.00 REMARK 3 SIDE-CHAIN ANGLE (A**2) : 4.48 ; 4.00 REMARK 3 REMARK 3 NCS MODEL : NONE 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 : PARAM_NDBX.DNA REMARK 3 PARAMETER FILE 3 : PARAM19.ION REMARK 3 TOPOLOGY FILE 1 : TOPHCSDX.PRO REMARK 3 TOPOLOGY FILE 2 : TOP_NBDX.DNA REMARK 3 TOPOLOGY FILE 3 : TOPH19.ION REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: ISOTROPIC B FACTORS WERE REFINED REMARK 3 AGAINST UNSHARPENED NATIVE DATA WHICH HAS AN INHERENT B REMARK 3 FACTOR OF 65.0, AND R-FACTORS WERE CALCULATED USING REMARK 3 ANISOTROPICALLY SHARPENED DATA. REMARK 4 REMARK 4 1TF6 COMPLIES WITH FORMAT V. 2.2, 16-DEC-1996 REMARK 6 REMARK 6 THE ENTRY CONTAINS TWO COPIES OF THE PROTEIN WITH CHAIN REMARK 6 IDENTIFIERS A AND D, AND TWO COPIES OF THE DNA DUPLEX WITH REMARK 6 CHAIN IDENTIFIERS B, C, AND E, F. REMARK 7 REMARK 7 THE FOLLOWING RESIDUES ARE DISORDERED AND ARE NOT INCLUDED REMARK 7 IN THE ENTRY: REMARK 7 MET A 1, GLY A 2, GLU A 3, LYS A 4, ALA A 5, LEU A 6, REMARK 7 PRO A 7, VAL A 8, VAL A 9, GLN A 189, ASP A 190, MET D 1, REMARK 7 GLY D 2, GLU D 3, LYS D 4, ALA D 5, LEU D 6, GLN D 189, AND REMARK 7 ASP D 190. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : OCT-1996 REMARK 200 TEMPERATURE (KELVIN) : 113 REMARK 200 PH : 8.0 REMARK 200 NUMBER OF CRYSTALS USED : 3 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : NSLS REMARK 200 BEAMLINE : X12B REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.283 REMARK 200 MONOCHROMATOR : SI(111) REMARK 200 OPTICS : MIRRORS REMARK 200 REMARK 200 DETECTOR TYPE : IMAGE PLATE REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19034 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.0 REMARK 200 RESOLUTION RANGE LOW (A) : 25.0 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.0 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 77.4 REMARK 200 DATA REDUNDANCY : 6.7 REMARK 200 R MERGE (I) : 0.128 REMARK 200 R SYM (I) : 0.060 REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.6 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL REMARK 200 REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR REMARK 200 SOFTWARE USED: CCP4 RAVE DM REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: DATA WERE FILTERED LOCALLY WITH AN I/SIGMA(I) REMARK 200 CUTOFF OF 1.0 - ELIMINATION OF UNRELIABLE MEASUREMENTS. REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 70. REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.8 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: COMPLEX WAS CRYSTALLIZED FROM REMARK 280 22.5% PEG 4000, 165 MM NACL, 35 MM SODIUM ACETATE, 3.2 MM REMARK 280 DTT, 9.2% (VOL/VOL) GLYCEROL, 1.8 MM NAN3, 1.8 MM REMARK 280 CADAVERINE-2HCL, 5.5 MM TRIS-HCL, PH 8.0 REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,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 REMARK 290 REMARK: NULL REMARK 295 REMARK 295 NON-CRYSTALLOGRAPHIC SYMMETRY REMARK 295 THE TRANSFORMATIONS PRESENTED ON THE MTRIX RECORDS BELOW REMARK 295 DESCRIBE NON-CRYSTALLOGRAPHIC RELATIONSHIPS AMONG ATOMS REMARK 295 IN THIS ENTRY. APPLYING THE APPROPRIATE MTRIX REMARK 295 TRANSFORMATION TO THE RESIDUES LISTED FIRST WILL YIELD REMARK 295 APPROXIMATE COORDINATES FOR THE RESIDUES LISTED SECOND. REMARK 295 CHAIN IDENTIFIERS GIVEN AS "?" REFER TO CHAINS FOR WHICH REMARK 295 ATOMS ARE NOT FOUND IN THIS ENTRY. REMARK 295 REMARK 295 APPLIED TO TRANSFORMED TO REMARK 295 TRANSFORM CHAIN RESIDUES CHAIN RESIDUES RMSD REMARK 295 SSS REMARK 295 M 1 A 10 .. 188 D 10 .. 188 0.664 REMARK 295 M 2 A 201 .. 206 D 201 .. 206 0.466 REMARK 295 M 3 B 1 .. 31 E 1 .. 31 0.103 REMARK 295 M 4 C 33 .. 63 F 33 .. 63 0.119 REMARK 295 REMARK 295 WHERE SSS -> COLUMNS 8-10 OF MTRIX RECORDS REMARK 295 REMARK 295 REMARK: NULL REMARK 650 REMARK 650 HELIX REMARK 650 DETERMINATION METHOD: AUTHOR-DETERMINED REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AN1 REMARK 800 SITE_DESCRIPTION: ZN-BINDING SITE. REMARK 800 REMARK 800 SITE_IDENTIFIER: AN2 REMARK 800 SITE_DESCRIPTION: ZN-BINDING SITE. REMARK 800 REMARK 800 SITE_IDENTIFIER: AN3 REMARK 800 SITE_DESCRIPTION: ZN-BINDING SITE. REMARK 800 REMARK 800 SITE_IDENTIFIER: AN4 REMARK 800 SITE_DESCRIPTION: ZN-BINDING SITE. REMARK 800 REMARK 800 SITE_IDENTIFIER: AN5 REMARK 800 SITE_DESCRIPTION: ZN-BINDING SITE. REMARK 800 REMARK 800 SITE_IDENTIFIER: AN6 REMARK 800 SITE_DESCRIPTION: ZN-BINDING SITE. REMARK 800 REMARK 800 SITE_IDENTIFIER: DN1 REMARK 800 SITE_DESCRIPTION: ZN-BINDING SITE. REMARK 800 REMARK 800 SITE_IDENTIFIER: DN2 REMARK 800 SITE_DESCRIPTION: ZN-BINDING SITE. REMARK 800 REMARK 800 SITE_IDENTIFIER: DN3 REMARK 800 SITE_DESCRIPTION: ZN-BINDING SITE. REMARK 800 REMARK 800 SITE_IDENTIFIER: DN4 REMARK 800 SITE_DESCRIPTION: ZN-BINDING SITE. REMARK 800 REMARK 800 SITE_IDENTIFIER: DN5 REMARK 800 SITE_DESCRIPTION: ZN-BINDING SITE. REMARK 800 REMARK 800 SITE_IDENTIFIER: DN6 REMARK 800 SITE_DESCRIPTION: ZN-BINDING SITE. REMARK 999 REMARK 999 SEQUENCE REMARK 999 1TF6 A SWS P03001 1 - 31 NOT IN ATOMS LIST REMARK 999 1TF6 A SWS P03001 211 - 366 NOT IN ATOMS LIST REMARK 999 1TF6 D SWS P03001 1 - 28 NOT IN ATOMS LIST REMARK 999 1TF6 D SWS P03001 211 - 366 NOT IN ATOMS LIST DBREF 1TF6 A 10 188 SWS P03001 TF3A_XENLA 32 210 DBREF 1TF6 B 1 31 PDB 1TF6 1TF6 1 31 DBREF 1TF6 C 33 63 PDB 1TF6 1TF6 33 63 DBREF 1TF6 D 7 188 SWS P03001 TF3A_XENLA 29 210 DBREF 1TF6 E 1 31 PDB 1TF6 1TF6 1 31 DBREF 1TF6 F 33 63 PDB 1TF6 1TF6 33 63 SEQRES 1 A 190 MET GLY GLU LYS ALA LEU PRO VAL VAL TYR LYS ARG TYR SEQRES 2 A 190 ILE CYS SER PHE ALA ASP CYS GLY ALA ALA TYR ASN LYS SEQRES 3 A 190 ASN TRP LYS LEU GLN ALA HIS LEU CYS LYS HIS THR GLY SEQRES 4 A 190 GLU LYS PRO PHE PRO CYS LYS GLU GLU GLY CYS GLU LYS SEQRES 5 A 190 GLY PHE THR SER LEU HIS HIS LEU THR ARG HIS SER LEU SEQRES 6 A 190 THR HIS THR GLY GLU LYS ASN PHE THR CYS ASP SER ASP SEQRES 7 A 190 GLY CYS ASP LEU ARG PHE THR THR LYS ALA ASN MET LYS SEQRES 8 A 190 LYS HIS PHE ASN ARG PHE HIS ASN ILE LYS ILE CYS VAL SEQRES 9 A 190 TYR VAL CYS HIS PHE GLU ASN CYS GLY LYS ALA PHE LYS SEQRES 10 A 190 LYS HIS ASN GLN LEU LYS VAL HIS GLN PHE SER HIS THR SEQRES 11 A 190 GLN GLN LEU PRO TYR GLU CYS PRO HIS GLU GLY CYS ASP SEQRES 12 A 190 LYS ARG PHE SER LEU PRO SER ARG LEU LYS ARG HIS GLU SEQRES 13 A 190 LYS VAL HIS ALA GLY TYR PRO CYS LYS LYS ASP ASP SER SEQRES 14 A 190 CYS SER PHE VAL GLY LYS THR TRP THR LEU TYR LEU LYS SEQRES 15 A 190 HIS VAL ALA GLU CYS HIS GLN ASP SEQRES 1 B 31 A C G G G C C T G G T T A SEQRES 2 B 31 G T A C C T G G A T G G G SEQRES 3 B 31 A G A C C SEQRES 1 C 31 T G G T C T C C C A T C C SEQRES 2 C 31 A G G T A C T A A C C A G SEQRES 3 C 31 G C C C G SEQRES 1 D 190 MET GLY GLU LYS ALA LEU PRO VAL VAL TYR LYS ARG TYR SEQRES 2 D 190 ILE CYS SER PHE ALA ASP CYS GLY ALA ALA TYR ASN LYS SEQRES 3 D 190 ASN TRP LYS LEU GLN ALA HIS LEU CYS LYS HIS THR GLY SEQRES 4 D 190 GLU LYS PRO PHE PRO CYS LYS GLU GLU GLY CYS GLU LYS SEQRES 5 D 190 GLY PHE THR SER LEU HIS HIS LEU THR ARG HIS SER LEU SEQRES 6 D 190 THR HIS THR GLY GLU LYS ASN PHE THR CYS ASP SER ASP SEQRES 7 D 190 GLY CYS ASP LEU ARG PHE THR THR LYS ALA ASN MET LYS SEQRES 8 D 190 LYS HIS PHE ASN ARG PHE HIS ASN ILE LYS ILE CYS VAL SEQRES 9 D 190 TYR VAL CYS HIS PHE GLU ASN CYS GLY LYS ALA PHE LYS SEQRES 10 D 190 LYS HIS ASN GLN LEU LYS VAL HIS GLN PHE SER HIS THR SEQRES 11 D 190 GLN GLN LEU PRO TYR GLU CYS PRO HIS GLU GLY CYS ASP SEQRES 12 D 190 LYS ARG PHE SER LEU PRO SER ARG LEU LYS ARG HIS GLU SEQRES 13 D 190 LYS VAL HIS ALA GLY TYR PRO CYS LYS LYS ASP ASP SER SEQRES 14 D 190 CYS SER PHE VAL GLY LYS THR TRP THR LEU TYR LEU LYS SEQRES 15 D 190 HIS VAL ALA GLU CYS HIS GLN ASP SEQRES 1 E 31 A C G G G C C T G G T T A SEQRES 2 E 31 G T A C C T G G A T G G G SEQRES 3 E 31 A G A C C SEQRES 1 F 31 T G G T C T C C C A T C C SEQRES 2 F 31 A G G T A C T A A C C A G SEQRES 3 F 31 G C C C G HET ZN A 201 1 HET ZN A 202 1 HET ZN A 203 1 HET ZN A 204 1 HET ZN A 205 1 HET ZN A 206 1 HET ZN D 201 1 HET ZN D 202 1 HET ZN D 203 1 HET ZN D 204 1 HET ZN D 205 1 HET ZN D 206 1 HETNAM ZN ZINC ION FORMUL 7 ZN 12(ZN1 2+) HELIX 1 AH1 ASN A 27 THR A 38 1 12 HELIX 2 AH2 LEU A 57 THR A 68 1 12 HELIX 3 AH3 LYS A 87 HIS A 98 1 12 HELIX 4 AH4 HIS A 119 THR A 130 1 12 HELIX 5 AH5 PRO A 149 ALA A 160 1 12 HELIX 6 AH6 TRP A 177 HIS A 188 1 12 HELIX 7 DH1 ASN D 27 THR D 38 1 12 HELIX 8 DH2 LEU D 57 THR D 68 1 12 HELIX 9 DH3 LYS D 87 HIS D 98 1 12 HELIX 10 DH4 HIS D 119 THR D 130 1 12 HELIX 11 DH5 PRO D 149 ALA D 160 1 12 HELIX 12 DH6 TRP D 177 HIS D 188 1 12 LINK ZN ZN A 201 SG CYS A 15 LINK ZN ZN A 201 SG CYS A 20 LINK ZN ZN A 201 NE2 HIS A 33 LINK ZN ZN A 201 NE2 HIS A 37 LINK ZN ZN A 202 SG CYS A 45 LINK ZN ZN A 202 SG CYS A 50 LINK ZN ZN A 202 NE2 HIS A 63 LINK ZN ZN A 202 NE2 HIS A 67 LINK ZN ZN A 203 SG CYS A 75 LINK ZN ZN A 203 SG CYS A 80 LINK ZN ZN A 203 NE2 HIS A 93 LINK ZN ZN A 203 NE2 HIS A 98 LINK ZN ZN A 204 SG CYS A 107 LINK ZN ZN A 204 SG CYS A 112 LINK ZN ZN A 204 NE2 HIS A 125 LINK ZN ZN A 204 NE2 HIS A 129 LINK ZN ZN A 205 SG CYS A 137 LINK ZN ZN A 205 SG CYS A 142 LINK ZN ZN A 205 NE2 HIS A 155 LINK ZN ZN A 205 NE2 HIS A 159 LINK ZN ZN A 206 SG CYS A 164 LINK ZN ZN A 206 SG CYS A 170 LINK ZN ZN A 206 NE2 HIS A 183 LINK ZN ZN A 206 NE2 HIS A 188 LINK ZN ZN D 201 SG CYS D 15 LINK ZN ZN D 201 SG CYS D 20 LINK ZN ZN D 201 NE2 HIS D 33 LINK ZN ZN D 201 NE2 HIS D 37 LINK ZN ZN D 202 SG CYS D 45 LINK ZN ZN D 202 SG CYS D 50 LINK ZN ZN D 202 NE2 HIS D 63 LINK ZN ZN D 202 NE2 HIS D 67 LINK ZN ZN D 203 SG CYS D 75 LINK ZN ZN D 203 SG CYS D 80 LINK ZN ZN D 203 NE2 HIS D 93 LINK ZN ZN D 203 NE2 HIS D 98 LINK ZN ZN D 204 SG CYS D 107 LINK ZN ZN D 204 SG CYS D 112 LINK ZN ZN D 204 NE2 HIS D 125 LINK ZN ZN D 204 NE2 HIS D 129 LINK ZN ZN D 205 SG CYS D 137 LINK ZN ZN D 205 SG CYS D 142 LINK ZN ZN D 205 NE2 HIS D 155 LINK ZN ZN D 205 NE2 HIS D 159 LINK ZN ZN D 206 SG CYS D 164 LINK ZN ZN D 206 SG CYS D 170 LINK ZN ZN D 206 NE2 HIS D 183 LINK ZN ZN D 206 NE2 HIS D 188 SITE 1 AN1 4 CYS A 15 CYS A 20 HIS A 33 HIS A 37 SITE 1 AN2 4 CYS A 45 CYS A 50 HIS A 63 HIS A 67 SITE 1 AN3 4 CYS A 75 CYS A 80 HIS A 93 HIS A 98 SITE 1 AN4 4 CYS A 107 CYS A 112 HIS A 125 HIS A 129 SITE 1 AN5 4 CYS A 137 CYS A 142 HIS A 155 HIS A 159 SITE 1 AN6 4 CYS A 164 CYS A 170 HIS A 183 HIS A 188 SITE 1 DN1 4 CYS D 15 CYS D 20 HIS D 33 HIS D 37 SITE 1 DN2 4 CYS D 45 CYS D 50 HIS D 63 HIS D 67 SITE 1 DN3 4 CYS D 75 CYS D 80 HIS D 93 HIS D 98 SITE 1 DN4 4 CYS D 107 CYS D 112 HIS D 125 HIS D 129 SITE 1 DN5 4 CYS D 137 CYS D 142 HIS D 155 HIS D 159 SITE 1 DN6 4 CYS D 164 CYS D 170 HIS D 183 HIS D 188 CRYST1 64.180 64.712 78.035 90.07 92.98 102.95 P 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 0.015581 0.003583 0.000859 0.00000 SCALE2 0.000000 0.015856 0.000210 0.00000 SCALE3 0.000000 0.000000 0.012833 0.00000 MTRIX1 1 -0.900690 -0.434470 0.002040 78.54161 1 MTRIX2 1 -0.434440 0.900670 0.007820 18.46218 1 MTRIX3 1 -0.005240 0.006160 -0.999970 82.12378 1 MTRIX1 2 -0.896830 -0.442290 -0.008730 78.89021 1 MTRIX2 2 -0.442350 0.896810 0.007720 18.84468 1 MTRIX3 2 0.004420 0.010790 -0.999930 81.35723 1 MTRIX1 3 -0.892870 -0.450310 -0.000280 78.95392 1 MTRIX2 3 -0.450310 0.892860 0.005100 19.75191 1 MTRIX3 3 -0.002050 0.004670 -0.999990 82.60930 1 MTRIX1 4 -0.892420 -0.451200 -0.002400 79.06322 1 MTRIX2 4 -0.451210 0.892410 0.004520 19.84412 1 MTRIX3 4 0.000100 0.005110 -0.999990 82.49853 1 (ATOM LINES ARE NOT SHOWN.) END