HEADER HYDROLASE/TRANSCRIPTION 28-AUG-14 4WA6
TITLE STRUCTURE OF YEAST SAGA DUBM WITH SGF73 N59D MUTANT AT 2.36 ANGSTROMS
TITLE 2 RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 8;
COMPND 3 CHAIN: A, D;
COMPND 4 SYNONYM: DEUBIQUITINATING ENZYME 8,UBIQUITIN THIOESTERASE 8,
COMPND 5 UBIQUITIN-SPECIFIC-PROCESSING PROTEASE 8;
COMPND 6 EC: 3.4.19.12;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: TRANSCRIPTION AND MRNA EXPORT FACTOR SUS1;
COMPND 10 CHAIN: B, F;
COMPND 11 ENGINEERED: YES;
COMPND 12 MOL_ID: 3;
COMPND 13 MOLECULE: SAGA-ASSOCIATED FACTOR 11;
COMPND 14 CHAIN: C, G;
COMPND 15 ENGINEERED: YES;
COMPND 16 MOL_ID: 4;
COMPND 17 MOLECULE: SAGA-ASSOCIATED FACTOR 73;
COMPND 18 CHAIN: E, H;
COMPND 19 SYNONYM: 73 KDA SAGA-ASSOCIATED FACTOR,SAGA HISTONE ACETYLTRANSFERASE
COMPND 20 COMPLEX 73 KDA SUBUNIT;
COMPND 21 ENGINEERED: YES;
COMPND 22 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 559292;
SOURCE 5 STRAIN: ATCC 204508 / S288C;
SOURCE 6 GENE: UBP8, YMR223W, YM9959.05;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 11 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 12 ORGANISM_TAXID: 559292;
SOURCE 13 STRAIN: ATCC 204508 / S288C;
SOURCE 14 GENE: SUS1, YBR111W-A;
SOURCE 15 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 16 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 17 MOL_ID: 3;
SOURCE 18 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 19 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 20 ORGANISM_TAXID: 307796;
SOURCE 21 STRAIN: YJM789;
SOURCE 22 GENE: SGF11, SCY_5678;
SOURCE 23 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 24 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 25 MOL_ID: 4;
SOURCE 26 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 27 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 28 ORGANISM_TAXID: 559292;
SOURCE 29 STRAIN: ATCC 204508 / S288C;
SOURCE 30 GENE: SGF73, YGL066W;
SOURCE 31 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 32 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS MULTI-PROTEIN COMPLEX, HYDROLASE-TRANSCRIPTION COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR C.WOLBERGER,M.YAN
REVDAT 5 27-DEC-23 4WA6 1 REMARK LINK
REVDAT 4 25-DEC-19 4WA6 1 REMARK
REVDAT 3 22-NOV-17 4WA6 1 REMARK
REVDAT 2 13-SEP-17 4WA6 1 SOURCE REMARK ATOM
REVDAT 1 04-MAR-15 4WA6 0
JRNL AUTH C.WOLBERGER,M.YAN
JRNL TITL STRUCTURE OF YEAST SAGA DUBM WITH SGF73 N59D MUTANT AT 2.36
JRNL TITL 2 ANGSTROMS RESOLUTION
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.36 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0029
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.36
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.41
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 56297
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) : 0.186
REMARK 3 R VALUE (WORKING SET) : 0.183
REMARK 3 FREE R VALUE : 0.244
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2993
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.36
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.42
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4070
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.03
REMARK 3 BIN R VALUE (WORKING SET) : 0.2740
REMARK 3 BIN FREE R VALUE SET COUNT : 219
REMARK 3 BIN FREE R VALUE : 0.3650
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 10935
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 15
REMARK 3 SOLVENT ATOMS : 139
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.68
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.10000
REMARK 3 B22 (A**2) : 2.75000
REMARK 3 B33 (A**2) : -2.47000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.89000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.428
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.261
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.204
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 18.851
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.962
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.930
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 11231 ; 0.014 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 10731 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 15108 ; 1.654 ; 1.957
REMARK 3 BOND ANGLES OTHERS (DEGREES): 24724 ; 0.831 ; 3.003
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1357 ; 6.587 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 531 ;40.629 ;25.367
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2100 ;16.522 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 42 ;17.831 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1697 ; 0.091 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 12531 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 2539 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 8
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 471
REMARK 3 RESIDUE RANGE : A 501 A 506
REMARK 3 RESIDUE RANGE : A 601 A 649
REMARK 3 ORIGIN FOR THE GROUP (A): 21.991 43.924 136.272
REMARK 3 T TENSOR
REMARK 3 T11: 0.1864 T22: 0.0715
REMARK 3 T33: 0.1840 T12: 0.0160
REMARK 3 T13: -0.1137 T23: -0.0717
REMARK 3 L TENSOR
REMARK 3 L11: 0.5335 L22: 0.5282
REMARK 3 L33: 1.7073 L12: -0.2031
REMARK 3 L13: -0.4504 L23: -0.0860
REMARK 3 S TENSOR
REMARK 3 S11: -0.0190 S12: -0.0505 S13: -0.0255
REMARK 3 S21: 0.0099 S22: -0.0068 S23: -0.0638
REMARK 3 S31: 0.1482 S32: 0.1677 S33: 0.0259
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 1 B 96
REMARK 3 RESIDUE RANGE : B 101 B 108
REMARK 3 ORIGIN FOR THE GROUP (A): 12.804 56.883 113.490
REMARK 3 T TENSOR
REMARK 3 T11: 0.1360 T22: 0.1201
REMARK 3 T33: 0.1105 T12: 0.0122
REMARK 3 T13: -0.0569 T23: -0.0419
REMARK 3 L TENSOR
REMARK 3 L11: 0.9936 L22: 2.8720
REMARK 3 L33: 1.8880 L12: -0.0056
REMARK 3 L13: -0.6368 L23: -0.5947
REMARK 3 S TENSOR
REMARK 3 S11: 0.1818 S12: 0.0705 S13: 0.0795
REMARK 3 S21: 0.1668 S22: 0.0437 S23: 0.0086
REMARK 3 S31: 0.0734 S32: -0.2527 S33: -0.2255
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 5 C 94
REMARK 3 RESIDUE RANGE : C 101 C 101
REMARK 3 RESIDUE RANGE : C 201 C 203
REMARK 3 ORIGIN FOR THE GROUP (A): 14.418 33.068 128.939
REMARK 3 T TENSOR
REMARK 3 T11: 0.4248 T22: 0.1241
REMARK 3 T33: 0.3031 T12: -0.0706
REMARK 3 T13: -0.0818 T23: -0.1292
REMARK 3 L TENSOR
REMARK 3 L11: 0.5322 L22: 0.7510
REMARK 3 L33: 1.0415 L12: 0.0256
REMARK 3 L13: -0.2705 L23: -0.7550
REMARK 3 S TENSOR
REMARK 3 S11: 0.0558 S12: 0.1299 S13: -0.1138
REMARK 3 S21: -0.1246 S22: -0.0618 S23: 0.1377
REMARK 3 S31: 0.2589 S32: -0.0756 S33: 0.0060
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 2 E 95
REMARK 3 RESIDUE RANGE : E 101 E 101
REMARK 3 RESIDUE RANGE : E 201 E 208
REMARK 3 ORIGIN FOR THE GROUP (A): 29.371 52.106 122.978
REMARK 3 T TENSOR
REMARK 3 T11: 0.2066 T22: 0.2089
REMARK 3 T33: 0.1848 T12: 0.0204
REMARK 3 T13: -0.0857 T23: -0.0782
REMARK 3 L TENSOR
REMARK 3 L11: 0.5354 L22: 1.3541
REMARK 3 L33: 1.1195 L12: -0.0502
REMARK 3 L13: -0.6206 L23: -0.4342
REMARK 3 S TENSOR
REMARK 3 S11: 0.0936 S12: -0.1654 S13: 0.0348
REMARK 3 S21: 0.0880 S22: -0.0366 S23: -0.1544
REMARK 3 S31: -0.0255 S32: 0.3861 S33: -0.0569
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 1 D 471
REMARK 3 RESIDUE RANGE : D 501 D 505
REMARK 3 RESIDUE RANGE : D 601 D 649
REMARK 3 ORIGIN FOR THE GROUP (A): -2.370 47.270 70.316
REMARK 3 T TENSOR
REMARK 3 T11: 0.0743 T22: 0.0478
REMARK 3 T33: 0.1555 T12: -0.0153
REMARK 3 T13: -0.0835 T23: 0.0371
REMARK 3 L TENSOR
REMARK 3 L11: 1.1073 L22: 1.0181
REMARK 3 L33: 0.9057 L12: 0.1155
REMARK 3 L13: -0.1013 L23: 0.0447
REMARK 3 S TENSOR
REMARK 3 S11: -0.0442 S12: 0.1668 S13: 0.1382
REMARK 3 S21: 0.0499 S22: -0.0078 S23: -0.2464
REMARK 3 S31: -0.1567 S32: -0.0602 S33: 0.0520
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : F 3 F 95
REMARK 3 RESIDUE RANGE : F 101 F 106
REMARK 3 ORIGIN FOR THE GROUP (A): 12.951 30.696 57.168
REMARK 3 T TENSOR
REMARK 3 T11: 0.0301 T22: 0.4255
REMARK 3 T33: 0.3831 T12: -0.0600
REMARK 3 T13: 0.0500 T23: -0.1490
REMARK 3 L TENSOR
REMARK 3 L11: 0.4372 L22: 4.4497
REMARK 3 L33: 2.5116 L12: -1.3796
REMARK 3 L13: -0.0300 L23: 0.4492
REMARK 3 S TENSOR
REMARK 3 S11: 0.0413 S12: 0.0202 S13: 0.0773
REMARK 3 S21: -0.0736 S22: -0.1215 S23: -0.1161
REMARK 3 S31: 0.1551 S32: 0.3044 S33: 0.0802
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : G 1 G 94
REMARK 3 RESIDUE RANGE : G 101 G 101
REMARK 3 RESIDUE RANGE : G 201 G 203
REMARK 3 ORIGIN FOR THE GROUP (A): 6.966 50.908 66.288
REMARK 3 T TENSOR
REMARK 3 T11: 0.3076 T22: 0.2944
REMARK 3 T33: 0.6221 T12: -0.1304
REMARK 3 T13: 0.0093 T23: -0.0077
REMARK 3 L TENSOR
REMARK 3 L11: 0.3173 L22: 0.0917
REMARK 3 L33: 1.1619 L12: -0.1360
REMARK 3 L13: 0.2692 L23: -0.1521
REMARK 3 S TENSOR
REMARK 3 S11: -0.0131 S12: 0.2320 S13: 0.2050
REMARK 3 S21: 0.0456 S22: -0.0726 S23: -0.2013
REMARK 3 S31: -0.2378 S32: 0.1533 S33: 0.0857
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : H 4 H 96
REMARK 3 RESIDUE RANGE : H 101 H 101
REMARK 3 RESIDUE RANGE : H 201 H 213
REMARK 3 ORIGIN FOR THE GROUP (A): -5.340 39.689 56.767
REMARK 3 T TENSOR
REMARK 3 T11: 0.1281 T22: 0.2225
REMARK 3 T33: 0.1133 T12: -0.0280
REMARK 3 T13: -0.0809 T23: 0.0063
REMARK 3 L TENSOR
REMARK 3 L11: 1.1330 L22: 0.6374
REMARK 3 L33: 0.5276 L12: -0.5683
REMARK 3 L13: -0.2713 L23: 0.1722
REMARK 3 S TENSOR
REMARK 3 S11: 0.0705 S12: 0.4005 S13: 0.0557
REMARK 3 S21: -0.1294 S22: -0.1616 S23: -0.0185
REMARK 3 S31: -0.0258 S32: -0.2115 S33: 0.0911
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 4WA6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-AUG-14.
REMARK 100 THE DEPOSITION ID IS D_1000203248.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-JUN-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5-6.5
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 23-ID-D
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.034
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL CRYO-COOLED
REMARK 200 SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 59279
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.360
REMARK 200 RESOLUTION RANGE LOW (A) : 47.410
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 3.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 23.0000
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 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.02
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.09
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM BIS TRIS, 18% PEG3350, 100MM
REMARK 280 AMMONIUM SULFATE, PH 5.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
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 34.00200
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 16940 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 32100 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -168.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, E
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 15610 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 29910 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -130.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, F, G, H
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: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 34940 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 59620 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -313.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, E
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 APPLY THE FOLLOWING TO CHAINS: D, F, G, H
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 41.34584
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 34.00200
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 132.00887
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 GLY A -4
REMARK 465 ALA A -3
REMARK 465 ALA A -2
REMARK 465 ALA A -1
REMARK 465 ALA A 0
REMARK 465 ASN A 199
REMARK 465 THR A 200
REMARK 465 LYS A 201
REMARK 465 GLN A 202
REMARK 465 ALA A 203
REMARK 465 SER A 204
REMARK 465 SER A 205
REMARK 465 SER A 206
REMARK 465 SER A 207
REMARK 465 THR A 208
REMARK 465 SER A 209
REMARK 465 THR A 210
REMARK 465 ASN A 227
REMARK 465 GLN A 228
REMARK 465 ASN A 229
REMARK 465 LEU A 230
REMARK 465 ALA A 231
REMARK 465 GLY A 232
REMARK 465 TYR A 233
REMARK 465 SER A 234
REMARK 465 GLN A 235
REMARK 465 LYS A 395
REMARK 465 GLU A 396
REMARK 465 LYS A 397
REMARK 465 ASP A 398
REMARK 465 LYS A 399
REMARK 465 HIS A 400
REMARK 465 SER A 401
REMARK 465 GLU A 402
REMARK 465 ASN A 403
REMARK 465 GLY A 404
REMARK 465 MET C 1
REMARK 465 THR C 2
REMARK 465 GLU C 3
REMARK 465 GLU C 4
REMARK 465 HIS C 72
REMARK 465 CYS C 73
REMARK 465 GLU C 74
REMARK 465 ASN C 75
REMARK 465 CYS C 76
REMARK 465 GLY C 77
REMARK 465 ARG C 78
REMARK 465 ASP C 79
REMARK 465 ARG C 95
REMARK 465 GLY C 96
REMARK 465 ALA C 97
REMARK 465 ARG C 98
REMARK 465 ARG C 99
REMARK 465 MET E 1
REMARK 465 LEU E 21
REMARK 465 SER E 22
REMARK 465 GLN E 23
REMARK 465 GLY E 24
REMARK 465 SER E 25
REMARK 465 GLY E 26
REMARK 465 PRO E 27
REMARK 465 SER E 28
REMARK 465 ASN E 29
REMARK 465 ASN E 96
REMARK 465 GLY D -4
REMARK 465 ALA D -3
REMARK 465 ALA D -2
REMARK 465 ALA D -1
REMARK 465 ALA D 0
REMARK 465 THR D 200
REMARK 465 LYS D 201
REMARK 465 GLN D 202
REMARK 465 ALA D 203
REMARK 465 SER D 204
REMARK 465 SER D 205
REMARK 465 SER D 206
REMARK 465 SER D 207
REMARK 465 THR D 208
REMARK 465 SER D 209
REMARK 465 ASN D 227
REMARK 465 GLN D 228
REMARK 465 ASN D 229
REMARK 465 LEU D 230
REMARK 465 ALA D 231
REMARK 465 GLY D 232
REMARK 465 TYR D 233
REMARK 465 SER D 234
REMARK 465 GLN D 235
REMARK 465 VAL D 288
REMARK 465 CYS D 289
REMARK 465 PRO D 290
REMARK 465 GLY D 291
REMARK 465 CYS D 292
REMARK 465 GLN D 293
REMARK 465 ASN D 294
REMARK 465 ASN D 295
REMARK 465 GLN D 328
REMARK 465 LEU D 329
REMARK 465 LYS D 330
REMARK 465 ASP D 331
REMARK 465 PHE D 332
REMARK 465 ASN D 333
REMARK 465 TYR D 334
REMARK 465 HIS D 335
REMARK 465 CYS D 336
REMARK 465 GLY D 337
REMARK 465 GLU D 338
REMARK 465 CYS D 339
REMARK 465 ASN D 340
REMARK 465 SER D 341
REMARK 465 THR D 342
REMARK 465 GLN D 343
REMARK 465 ASP D 344
REMARK 465 ALA D 345
REMARK 465 THR D 394
REMARK 465 LYS D 395
REMARK 465 GLU D 396
REMARK 465 LYS D 397
REMARK 465 ASP D 398
REMARK 465 LYS D 399
REMARK 465 HIS D 400
REMARK 465 SER D 401
REMARK 465 GLU D 402
REMARK 465 ASN D 403
REMARK 465 GLY D 404
REMARK 465 MET F 1
REMARK 465 THR F 2
REMARK 465 GLN F 96
REMARK 465 TYR G 48
REMARK 465 TYR G 49
REMARK 465 PHE G 50
REMARK 465 ASP G 51
REMARK 465 PRO G 52
REMARK 465 ASN G 53
REMARK 465 GLY G 54
REMARK 465 SER G 55
REMARK 465 LEU G 56
REMARK 465 ASP G 57
REMARK 465 ILE G 58
REMARK 465 ASN G 59
REMARK 465 GLY G 60
REMARK 465 LEU G 61
REMARK 465 GLN G 62
REMARK 465 LYS G 63
REMARK 465 GLN G 64
REMARK 465 GLN G 65
REMARK 465 GLU G 66
REMARK 465 SER G 67
REMARK 465 SER G 68
REMARK 465 GLN G 69
REMARK 465 ALA G 82
REMARK 465 ARG G 95
REMARK 465 GLY G 96
REMARK 465 ALA G 97
REMARK 465 ARG G 98
REMARK 465 ARG G 99
REMARK 465 MET H 1
REMARK 465 ARG H 2
REMARK 465 SER H 3
REMARK 465 TYR H 19
REMARK 465 SER H 20
REMARK 465 LEU H 21
REMARK 465 SER H 22
REMARK 465 GLN H 23
REMARK 465 GLY H 24
REMARK 465 SER H 25
REMARK 465 GLY H 26
REMARK 465 PRO H 27
REMARK 465 SER H 28
REMARK 465 ASN H 29
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 OG1 THR A 422 O GLU A 425 2.09
REMARK 500 O ILE C 8 OG SER C 12 2.17
REMARK 500 O CYS G 73 O CYS G 76 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 ASP A 111 41.42 -107.84
REMARK 500 SER A 137 138.81 172.80
REMARK 500 LYS A 269 -69.33 -107.38
REMARK 500 GLN A 293 -9.84 72.06
REMARK 500 ASN A 294 129.95 -35.97
REMARK 500 ASP A 444 -140.57 57.82
REMARK 500 GLU B 54 55.89 38.00
REMARK 500 ASN C 53 -7.81 -59.23
REMARK 500 ASP C 57 -166.64 -68.31
REMARK 500 ASN C 83 -9.34 -57.36
REMARK 500 PRO E 43 -176.33 -69.17
REMARK 500 HIS E 48 44.18 -143.07
REMARK 500 LYS D 181 -48.55 -132.62
REMARK 500 LYS D 225 0.72 -67.02
REMARK 500 ASN D 424 -70.25 -82.98
REMARK 500 ASN D 443 79.60 -117.49
REMARK 500 ASP D 444 -123.77 57.70
REMARK 500 LEU H 44 129.72 -35.90
REMARK 500 HIS H 48 44.53 -148.19
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 501 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 4 SG
REMARK 620 2 HIS A 6 ND1 103.5
REMARK 620 3 CYS A 96 SG 114.7 102.0
REMARK 620 4 CYS A 99 SG 114.7 103.6 115.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 502 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 46 SG
REMARK 620 2 CYS A 49 SG 105.1
REMARK 620 3 CYS A 68 SG 109.1 116.1
REMARK 620 4 HIS A 73 ND1 110.3 111.4 104.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 503 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 60 SG
REMARK 620 2 CYS A 63 SG 114.8
REMARK 620 3 HIS A 77 NE2 113.3 102.9
REMARK 620 4 HIS A 83 ND1 104.7 119.0 101.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 504 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 170 NE2
REMARK 620 2 CYS A 174 SG 88.8
REMARK 620 3 CYS A 182 SG 106.9 120.0
REMARK 620 4 CYS A 185 SG 117.9 104.6 116.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 505 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 250 ND1
REMARK 620 2 CYS A 271 SG 100.6
REMARK 620 3 CYS A 273 SG 119.1 109.6
REMARK 620 4 HIS A 276 ND1 104.9 108.7 113.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 506 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 289 SG
REMARK 620 2 CYS A 292 SG 111.5
REMARK 620 3 CYS A 336 SG 116.8 102.7
REMARK 620 4 CYS A 339 SG 109.3 110.8 105.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C 101 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 88 NE2
REMARK 620 2 CYS C 92 SG 108.1
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN E 101 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS E 78 SG
REMARK 620 2 CYS E 81 SG 113.0
REMARK 620 3 HIS E 93 NE2 100.4 116.4
REMARK 620 4 HOH E 203 O 109.7 112.2 104.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D 501 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 4 SG
REMARK 620 2 HIS D 6 ND1 110.7
REMARK 620 3 CYS D 96 SG 119.9 103.9
REMARK 620 4 CYS D 99 SG 108.5 109.8 103.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D 502 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 46 SG
REMARK 620 2 CYS D 49 SG 96.1
REMARK 620 3 CYS D 68 SG 108.7 118.0
REMARK 620 4 HIS D 73 ND1 107.8 114.3 110.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D 503 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 60 SG
REMARK 620 2 CYS D 63 SG 120.6
REMARK 620 3 HIS D 77 NE2 115.4 104.2
REMARK 620 4 HIS D 83 ND1 102.0 112.7 100.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D 504 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS D 170 NE2
REMARK 620 2 CYS D 174 SG 100.8
REMARK 620 3 CYS D 182 SG 104.9 109.8
REMARK 620 4 CYS D 185 SG 121.2 101.7 116.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D 505 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS D 250 ND1
REMARK 620 2 CYS D 271 SG 105.3
REMARK 620 3 CYS D 273 SG 124.1 106.9
REMARK 620 4 HIS D 276 ND1 98.6 113.4 108.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN G 101 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS G 73 SG
REMARK 620 2 CYS G 76 SG 107.2
REMARK 620 3 HIS G 88 NE2 103.2 116.3
REMARK 620 4 CYS G 92 SG 115.4 99.2 115.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN H 101 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS H 78 SG
REMARK 620 2 CYS H 81 SG 103.0
REMARK 620 3 HIS H 93 NE2 112.0 114.3
REMARK 620 4 HOH H 201 O 109.8 113.7 104.2
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 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN C 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN E 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN D 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN D 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN D 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN D 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN D 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN G 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN H 101
DBREF 4WA6 A 1 471 UNP P50102 UBP8_YEAST 1 471
DBREF 4WA6 B 1 96 UNP Q6WNK7 SUS1_YEAST 1 96
DBREF 4WA6 C 1 99 UNP A6ZWK1 SGF11_YEAS7 1 99
DBREF 4WA6 E 1 96 UNP P53165 SGF73_YEAST 1 96
DBREF 4WA6 D 1 471 UNP P50102 UBP8_YEAST 1 471
DBREF 4WA6 F 1 96 UNP Q6WNK7 SUS1_YEAST 1 96
DBREF 4WA6 G 1 99 UNP A6ZWK1 SGF11_YEAS7 1 99
DBREF 4WA6 H 1 96 UNP P53165 SGF73_YEAST 1 96
SEQADV 4WA6 GLY A -4 UNP P50102 EXPRESSION TAG
SEQADV 4WA6 ALA A -3 UNP P50102 EXPRESSION TAG
SEQADV 4WA6 ALA A -2 UNP P50102 EXPRESSION TAG
SEQADV 4WA6 ALA A -1 UNP P50102 EXPRESSION TAG
SEQADV 4WA6 ALA A 0 UNP P50102 EXPRESSION TAG
SEQADV 4WA6 ASP E 59 UNP P53165 ASN 59 ENGINEERED MUTATION
SEQADV 4WA6 GLY D -4 UNP P50102 EXPRESSION TAG
SEQADV 4WA6 ALA D -3 UNP P50102 EXPRESSION TAG
SEQADV 4WA6 ALA D -2 UNP P50102 EXPRESSION TAG
SEQADV 4WA6 ALA D -1 UNP P50102 EXPRESSION TAG
SEQADV 4WA6 ALA D 0 UNP P50102 EXPRESSION TAG
SEQADV 4WA6 ASP H 59 UNP P53165 ASN 59 ENGINEERED MUTATION
SEQRES 1 A 476 GLY ALA ALA ALA ALA MET SER ILE CYS PRO HIS ILE GLN
SEQRES 2 A 476 GLN VAL PHE GLN ASN GLU LYS SER LYS ASP GLY VAL LEU
SEQRES 3 A 476 LYS THR CYS ASN ALA ALA ARG TYR ILE LEU ASN HIS SER
SEQRES 4 A 476 VAL PRO LYS GLU LYS PHE LEU ASN THR MET LYS CYS GLY
SEQRES 5 A 476 THR CYS HIS GLU ILE ASN SER GLY ALA THR PHE MET CYS
SEQRES 6 A 476 LEU GLN CYS GLY PHE CYS GLY CYS TRP ASN HIS SER HIS
SEQRES 7 A 476 PHE LEU SER HIS SER LYS GLN ILE GLY HIS ILE PHE GLY
SEQRES 8 A 476 ILE ASN SER ASN ASN GLY LEU LEU PHE CYS PHE LYS CYS
SEQRES 9 A 476 GLU ASP TYR ILE GLY ASN ILE ASP LEU ILE ASN ASP ALA
SEQRES 10 A 476 ILE LEU ALA LYS TYR TRP ASP ASP VAL CYS THR LYS THR
SEQRES 11 A 476 MET VAL PRO SER MET GLU ARG ARG ASP GLY LEU SER GLY
SEQRES 12 A 476 LEU ILE ASN MET GLY SER THR CYS PHE MET SER SER ILE
SEQRES 13 A 476 LEU GLN CYS LEU ILE HIS ASN PRO TYR PHE ILE ARG HIS
SEQRES 14 A 476 SER MET SER GLN ILE HIS SER ASN ASN CYS LYS VAL ARG
SEQRES 15 A 476 SER PRO ASP LYS CYS PHE SER CYS ALA LEU ASP LYS ILE
SEQRES 16 A 476 VAL HIS GLU LEU TYR GLY ALA LEU ASN THR LYS GLN ALA
SEQRES 17 A 476 SER SER SER SER THR SER THR ASN ARG GLN THR GLY PHE
SEQRES 18 A 476 ILE TYR LEU LEU THR CYS ALA TRP LYS ILE ASN GLN ASN
SEQRES 19 A 476 LEU ALA GLY TYR SER GLN GLN ASP ALA HIS GLU PHE TRP
SEQRES 20 A 476 GLN PHE ILE ILE ASN GLN ILE HIS GLN SER TYR VAL LEU
SEQRES 21 A 476 ASP LEU PRO ASN ALA LYS GLU VAL SER ARG ALA ASN ASN
SEQRES 22 A 476 LYS GLN CYS GLU CYS ILE VAL HIS THR VAL PHE GLU GLY
SEQRES 23 A 476 SER LEU GLU SER SER ILE VAL CYS PRO GLY CYS GLN ASN
SEQRES 24 A 476 ASN SER LYS THR THR ILE ASP PRO PHE LEU ASP LEU SER
SEQRES 25 A 476 LEU ASP ILE LYS ASP LYS LYS LYS LEU TYR GLU CYS LEU
SEQRES 26 A 476 ASP SER PHE HIS LYS LYS GLU GLN LEU LYS ASP PHE ASN
SEQRES 27 A 476 TYR HIS CYS GLY GLU CYS ASN SER THR GLN ASP ALA ILE
SEQRES 28 A 476 LYS GLN LEU GLY ILE HIS LYS LEU PRO SER VAL LEU VAL
SEQRES 29 A 476 LEU GLN LEU LYS ARG PHE GLU HIS LEU LEU ASN GLY SER
SEQRES 30 A 476 ASN ARG LYS LEU ASP ASP PHE ILE GLU PHE PRO THR TYR
SEQRES 31 A 476 LEU ASN MET LYS ASN TYR CYS SER THR LYS GLU LYS ASP
SEQRES 32 A 476 LYS HIS SER GLU ASN GLY LYS VAL PRO ASP ILE ILE TYR
SEQRES 33 A 476 GLU LEU ILE GLY ILE VAL SER HIS LYS GLY THR VAL ASN
SEQRES 34 A 476 GLU GLY HIS TYR ILE ALA PHE CYS LYS ILE SER GLY GLY
SEQRES 35 A 476 GLN TRP PHE LYS PHE ASN ASP SER MET VAL SER SER ILE
SEQRES 36 A 476 SER GLN GLU GLU VAL LEU LYS GLU GLN ALA TYR LEU LEU
SEQRES 37 A 476 PHE TYR THR ILE ARG GLN VAL ASN
SEQRES 1 B 96 MET THR MET ASP THR ALA GLN LEU LYS SER GLN ILE GLN
SEQRES 2 B 96 GLN TYR LEU VAL GLU SER GLY ASN TYR GLU LEU ILE SER
SEQRES 3 B 96 ASN GLU LEU LYS ALA ARG LEU LEU GLN GLU GLY TRP VAL
SEQRES 4 B 96 ASP LYS VAL LYS ASP LEU THR LYS SER GLU MET ASN ILE
SEQRES 5 B 96 ASN GLU SER THR ASN PHE THR GLN ILE LEU SER THR VAL
SEQRES 6 B 96 GLU PRO LYS ALA LEU GLU MET VAL SER ASP SER THR ARG
SEQRES 7 B 96 GLU THR VAL LEU LYS GLN ILE ARG GLU PHE LEU GLU GLU
SEQRES 8 B 96 ILE VAL ASP THR GLN
SEQRES 1 C 99 MET THR GLU GLU THR ILE THR ILE ASP SER ILE SER ASN
SEQRES 2 C 99 GLY ILE LEU ASN ASN LEU LEU THR THR LEU ILE GLN ASP
SEQRES 3 C 99 ILE VAL ALA ARG GLU THR THR GLN GLN GLN LEU LEU LYS
SEQRES 4 C 99 THR ARG TYR PRO ASP LEU ARG SER TYR TYR PHE ASP PRO
SEQRES 5 C 99 ASN GLY SER LEU ASP ILE ASN GLY LEU GLN LYS GLN GLN
SEQRES 6 C 99 GLU SER SER GLN TYR ILE HIS CYS GLU ASN CYS GLY ARG
SEQRES 7 C 99 ASP VAL SER ALA ASN ARG LEU ALA ALA HIS LEU GLN ARG
SEQRES 8 C 99 CYS LEU SER ARG GLY ALA ARG ARG
SEQRES 1 E 96 MET ARG SER GLY ASP ALA GLU ILE LYS GLY ILE LYS PRO
SEQRES 2 E 96 LYS VAL ILE GLU GLU TYR SER LEU SER GLN GLY SER GLY
SEQRES 3 E 96 PRO SER ASN ASP SER TRP LYS SER LEU MET SER SER ALA
SEQRES 4 E 96 LYS ASP THR PRO LEU GLN TYR ASP HIS MET ASN ARG GLU
SEQRES 5 E 96 SER LEU LYS LYS TYR PHE ASP PRO ASN ALA GLN LEU ILE
SEQRES 6 E 96 GLU ASP PRO LEU ASP LYS PRO ILE GLN TYR ARG VAL CYS
SEQRES 7 E 96 GLU LYS CYS GLY LYS PRO LEU ALA LEU THR ALA ILE VAL
SEQRES 8 E 96 ASP HIS LEU GLU ASN
SEQRES 1 D 476 GLY ALA ALA ALA ALA MET SER ILE CYS PRO HIS ILE GLN
SEQRES 2 D 476 GLN VAL PHE GLN ASN GLU LYS SER LYS ASP GLY VAL LEU
SEQRES 3 D 476 LYS THR CYS ASN ALA ALA ARG TYR ILE LEU ASN HIS SER
SEQRES 4 D 476 VAL PRO LYS GLU LYS PHE LEU ASN THR MET LYS CYS GLY
SEQRES 5 D 476 THR CYS HIS GLU ILE ASN SER GLY ALA THR PHE MET CYS
SEQRES 6 D 476 LEU GLN CYS GLY PHE CYS GLY CYS TRP ASN HIS SER HIS
SEQRES 7 D 476 PHE LEU SER HIS SER LYS GLN ILE GLY HIS ILE PHE GLY
SEQRES 8 D 476 ILE ASN SER ASN ASN GLY LEU LEU PHE CYS PHE LYS CYS
SEQRES 9 D 476 GLU ASP TYR ILE GLY ASN ILE ASP LEU ILE ASN ASP ALA
SEQRES 10 D 476 ILE LEU ALA LYS TYR TRP ASP ASP VAL CYS THR LYS THR
SEQRES 11 D 476 MET VAL PRO SER MET GLU ARG ARG ASP GLY LEU SER GLY
SEQRES 12 D 476 LEU ILE ASN MET GLY SER THR CYS PHE MET SER SER ILE
SEQRES 13 D 476 LEU GLN CYS LEU ILE HIS ASN PRO TYR PHE ILE ARG HIS
SEQRES 14 D 476 SER MET SER GLN ILE HIS SER ASN ASN CYS LYS VAL ARG
SEQRES 15 D 476 SER PRO ASP LYS CYS PHE SER CYS ALA LEU ASP LYS ILE
SEQRES 16 D 476 VAL HIS GLU LEU TYR GLY ALA LEU ASN THR LYS GLN ALA
SEQRES 17 D 476 SER SER SER SER THR SER THR ASN ARG GLN THR GLY PHE
SEQRES 18 D 476 ILE TYR LEU LEU THR CYS ALA TRP LYS ILE ASN GLN ASN
SEQRES 19 D 476 LEU ALA GLY TYR SER GLN GLN ASP ALA HIS GLU PHE TRP
SEQRES 20 D 476 GLN PHE ILE ILE ASN GLN ILE HIS GLN SER TYR VAL LEU
SEQRES 21 D 476 ASP LEU PRO ASN ALA LYS GLU VAL SER ARG ALA ASN ASN
SEQRES 22 D 476 LYS GLN CYS GLU CYS ILE VAL HIS THR VAL PHE GLU GLY
SEQRES 23 D 476 SER LEU GLU SER SER ILE VAL CYS PRO GLY CYS GLN ASN
SEQRES 24 D 476 ASN SER LYS THR THR ILE ASP PRO PHE LEU ASP LEU SER
SEQRES 25 D 476 LEU ASP ILE LYS ASP LYS LYS LYS LEU TYR GLU CYS LEU
SEQRES 26 D 476 ASP SER PHE HIS LYS LYS GLU GLN LEU LYS ASP PHE ASN
SEQRES 27 D 476 TYR HIS CYS GLY GLU CYS ASN SER THR GLN ASP ALA ILE
SEQRES 28 D 476 LYS GLN LEU GLY ILE HIS LYS LEU PRO SER VAL LEU VAL
SEQRES 29 D 476 LEU GLN LEU LYS ARG PHE GLU HIS LEU LEU ASN GLY SER
SEQRES 30 D 476 ASN ARG LYS LEU ASP ASP PHE ILE GLU PHE PRO THR TYR
SEQRES 31 D 476 LEU ASN MET LYS ASN TYR CYS SER THR LYS GLU LYS ASP
SEQRES 32 D 476 LYS HIS SER GLU ASN GLY LYS VAL PRO ASP ILE ILE TYR
SEQRES 33 D 476 GLU LEU ILE GLY ILE VAL SER HIS LYS GLY THR VAL ASN
SEQRES 34 D 476 GLU GLY HIS TYR ILE ALA PHE CYS LYS ILE SER GLY GLY
SEQRES 35 D 476 GLN TRP PHE LYS PHE ASN ASP SER MET VAL SER SER ILE
SEQRES 36 D 476 SER GLN GLU GLU VAL LEU LYS GLU GLN ALA TYR LEU LEU
SEQRES 37 D 476 PHE TYR THR ILE ARG GLN VAL ASN
SEQRES 1 F 96 MET THR MET ASP THR ALA GLN LEU LYS SER GLN ILE GLN
SEQRES 2 F 96 GLN TYR LEU VAL GLU SER GLY ASN TYR GLU LEU ILE SER
SEQRES 3 F 96 ASN GLU LEU LYS ALA ARG LEU LEU GLN GLU GLY TRP VAL
SEQRES 4 F 96 ASP LYS VAL LYS ASP LEU THR LYS SER GLU MET ASN ILE
SEQRES 5 F 96 ASN GLU SER THR ASN PHE THR GLN ILE LEU SER THR VAL
SEQRES 6 F 96 GLU PRO LYS ALA LEU GLU MET VAL SER ASP SER THR ARG
SEQRES 7 F 96 GLU THR VAL LEU LYS GLN ILE ARG GLU PHE LEU GLU GLU
SEQRES 8 F 96 ILE VAL ASP THR GLN
SEQRES 1 G 99 MET THR GLU GLU THR ILE THR ILE ASP SER ILE SER ASN
SEQRES 2 G 99 GLY ILE LEU ASN ASN LEU LEU THR THR LEU ILE GLN ASP
SEQRES 3 G 99 ILE VAL ALA ARG GLU THR THR GLN GLN GLN LEU LEU LYS
SEQRES 4 G 99 THR ARG TYR PRO ASP LEU ARG SER TYR TYR PHE ASP PRO
SEQRES 5 G 99 ASN GLY SER LEU ASP ILE ASN GLY LEU GLN LYS GLN GLN
SEQRES 6 G 99 GLU SER SER GLN TYR ILE HIS CYS GLU ASN CYS GLY ARG
SEQRES 7 G 99 ASP VAL SER ALA ASN ARG LEU ALA ALA HIS LEU GLN ARG
SEQRES 8 G 99 CYS LEU SER ARG GLY ALA ARG ARG
SEQRES 1 H 96 MET ARG SER GLY ASP ALA GLU ILE LYS GLY ILE LYS PRO
SEQRES 2 H 96 LYS VAL ILE GLU GLU TYR SER LEU SER GLN GLY SER GLY
SEQRES 3 H 96 PRO SER ASN ASP SER TRP LYS SER LEU MET SER SER ALA
SEQRES 4 H 96 LYS ASP THR PRO LEU GLN TYR ASP HIS MET ASN ARG GLU
SEQRES 5 H 96 SER LEU LYS LYS TYR PHE ASP PRO ASN ALA GLN LEU ILE
SEQRES 6 H 96 GLU ASP PRO LEU ASP LYS PRO ILE GLN TYR ARG VAL CYS
SEQRES 7 H 96 GLU LYS CYS GLY LYS PRO LEU ALA LEU THR ALA ILE VAL
SEQRES 8 H 96 ASP HIS LEU GLU ASN
HET ZN A 501 1
HET ZN A 502 1
HET ZN A 503 1
HET ZN A 504 1
HET ZN A 505 1
HET ZN A 506 1
HET ZN C 101 1
HET ZN E 101 1
HET ZN D 501 1
HET ZN D 502 1
HET ZN D 503 1
HET ZN D 504 1
HET ZN D 505 1
HET ZN G 101 1
HET ZN H 101 1
HETNAM ZN ZINC ION
FORMUL 9 ZN 15(ZN 2+)
FORMUL 24 HOH *139(H2 O)
HELIX 1 AA1 CYS A 4 PHE A 11 1 8
HELIX 2 AA2 ASN A 13 HIS A 33 1 21
HELIX 3 AA3 VAL A 35 MET A 44 1 10
HELIX 4 AA4 SER A 72 GLY A 82 1 11
HELIX 5 AA5 ILE A 106 ASP A 111 1 6
HELIX 6 AA6 ALA A 112 LYS A 116 5 5
HELIX 7 AA7 TYR A 117 LYS A 124 1 8
HELIX 8 AA8 THR A 145 HIS A 157 1 13
HELIX 9 AA9 ASN A 158 SER A 167 1 10
HELIX 10 AB1 GLN A 168 CYS A 174 1 7
HELIX 11 AB2 CYS A 182 GLY A 196 1 15
HELIX 12 AB3 GLN A 213 LYS A 225 1 13
HELIX 13 AB4 ASP A 237 ASP A 256 1 20
HELIX 14 AB5 ASN A 259 LYS A 269 1 11
HELIX 15 AB6 CYS A 273 PHE A 279 1 7
HELIX 16 AB7 LYS A 315 LYS A 325 1 11
HELIX 17 AB8 LYS A 389 CYS A 392 5 4
HELIX 18 AB9 SER A 435 GLY A 437 5 3
HELIX 19 AC1 SER A 451 LEU A 456 1 6
HELIX 20 AC2 ASP B 4 GLY B 20 1 17
HELIX 21 AC3 GLY B 20 GLU B 36 1 17
HELIX 22 AC4 GLY B 37 GLU B 54 1 18
HELIX 23 AC5 ASN B 57 VAL B 73 1 17
HELIX 24 AC6 SER B 74 ILE B 92 1 19
HELIX 25 AC7 ILE C 8 TYR C 42 1 35
HELIX 26 AC8 SER C 81 ASN C 83 5 3
HELIX 27 AC9 ARG C 84 LEU C 93 1 10
HELIX 28 AD1 LYS E 12 GLU E 17 1 6
HELIX 29 AD2 SER E 31 SER E 34 5 4
HELIX 30 AD3 LEU E 35 ASP E 41 1 7
HELIX 31 AD4 ASN E 50 PHE E 58 1 9
HELIX 32 AD5 ASP E 67 LYS E 71 5 5
HELIX 33 AD6 ALA E 89 GLU E 95 1 7
HELIX 34 AD7 CYS D 4 PHE D 11 1 8
HELIX 35 AD8 ASN D 13 HIS D 33 1 21
HELIX 36 AD9 VAL D 35 MET D 44 1 10
HELIX 37 AE1 SER D 72 GLY D 82 1 11
HELIX 38 AE2 ILE D 106 ASP D 111 1 6
HELIX 39 AE3 ALA D 112 LYS D 116 5 5
HELIX 40 AE4 TYR D 117 LYS D 124 1 8
HELIX 41 AE5 THR D 145 HIS D 157 1 13
HELIX 42 AE6 ASN D 158 SER D 167 1 10
HELIX 43 AE7 GLN D 168 CYS D 174 1 7
HELIX 44 AE8 CYS D 182 GLY D 196 1 15
HELIX 45 AE9 GLN D 213 LYS D 225 1 13
HELIX 46 AF1 ASP D 237 ASP D 256 1 20
HELIX 47 AF2 ASN D 259 ASN D 268 1 10
HELIX 48 AF3 CYS D 273 PHE D 279 1 7
HELIX 49 AF4 LYS D 315 LYS D 325 1 11
HELIX 50 AF5 LYS D 389 CYS D 392 5 4
HELIX 51 AF6 SER D 451 LYS D 457 1 7
HELIX 52 AF7 ASP F 4 SER F 19 1 16
HELIX 53 AF8 GLY F 20 GLU F 36 1 17
HELIX 54 AF9 GLY F 37 ASN F 53 1 17
HELIX 55 AG1 ASN F 57 MET F 72 1 16
HELIX 56 AG2 SER F 74 ILE F 92 1 19
HELIX 57 AG3 THR G 7 TYR G 42 1 36
HELIX 58 AG4 ARG G 84 LEU G 93 1 10
HELIX 59 AG5 LYS H 12 GLU H 17 1 6
HELIX 60 AG6 SER H 31 LYS H 33 5 3
HELIX 61 AG7 SER H 34 ASP H 41 1 8
HELIX 62 AG8 ASN H 50 PHE H 58 1 9
HELIX 63 AG9 ALA H 89 ASN H 96 1 8
SHEET 1 AA1 5 CYS A 66 CYS A 68 0
SHEET 2 AA1 5 THR A 57 CYS A 60 -1 N PHE A 58 O GLY A 67
SHEET 3 AA1 5 PHE A 85 ASN A 88 -1 O ILE A 87 N MET A 59
SHEET 4 AA1 5 LEU A 94 CYS A 96 -1 O PHE A 95 N GLY A 86
SHEET 5 AA1 5 ASP A 101 TYR A 102 -1 O ASP A 101 N CYS A 96
SHEET 1 AA2 3 THR A 125 MET A 126 0
SHEET 2 AA2 3 TYR E 75 CYS E 78 -1 O VAL E 77 N MET A 126
SHEET 3 AA2 3 PRO E 84 ALA E 86 -1 O LEU E 85 N ARG E 76
SHEET 1 AA3 4 THR A 299 PHE A 303 0
SHEET 2 AA3 4 GLY A 281 VAL A 288 -1 N SER A 285 O THR A 299
SHEET 3 AA3 4 ILE A 346 LYS A 353 -1 O ILE A 346 N VAL A 288
SHEET 4 AA3 4 GLU A 327 GLN A 328 -1 N GLU A 327 O LYS A 347
SHEET 1 AA4 5 LEU A 306 LEU A 308 0
SHEET 2 AA4 5 VAL A 357 LEU A 362 1 O GLN A 361 N LEU A 308
SHEET 3 AA4 5 ALA A 460 VAL A 470 -1 O TYR A 465 N LEU A 358
SHEET 4 AA4 5 ILE A 409 GLY A 421 -1 N ILE A 414 O PHE A 464
SHEET 5 AA4 5 TYR A 385 ASN A 387 -1 N LEU A 386 O TYR A 411
SHEET 1 AA5 7 LEU A 306 LEU A 308 0
SHEET 2 AA5 7 VAL A 357 LEU A 362 1 O GLN A 361 N LEU A 308
SHEET 3 AA5 7 ALA A 460 VAL A 470 -1 O TYR A 465 N LEU A 358
SHEET 4 AA5 7 ILE A 409 GLY A 421 -1 N ILE A 414 O PHE A 464
SHEET 5 AA5 7 GLY A 426 LYS A 433 -1 O HIS A 427 N LYS A 420
SHEET 6 AA5 7 TRP A 439 ASN A 443 -1 O PHE A 442 N ALA A 430
SHEET 7 AA5 7 MET A 446 ILE A 450 -1 O MET A 446 N ASN A 443
SHEET 1 AA6 2 PHE A 365 HIS A 367 0
SHEET 2 AA6 2 ASN A 373 LYS A 375 -1 O ARG A 374 N GLU A 366
SHEET 1 AA7 3 VAL B 93 GLN B 96 0
SHEET 2 AA7 3 GLU E 7 ILE E 11 -1 O GLY E 10 N ASP B 94
SHEET 3 AA7 3 ILE C 6 THR C 7 -1 N ILE C 6 O ILE E 8
SHEET 1 AA8 5 CYS D 66 CYS D 68 0
SHEET 2 AA8 5 THR D 57 CYS D 60 -1 N PHE D 58 O GLY D 67
SHEET 3 AA8 5 PHE D 85 ASN D 88 -1 O ILE D 87 N MET D 59
SHEET 4 AA8 5 LEU D 94 CYS D 96 -1 O PHE D 95 N GLY D 86
SHEET 5 AA8 5 ASP D 101 TYR D 102 -1 O ASP D 101 N CYS D 96
SHEET 1 AA9 3 THR D 125 MET D 126 0
SHEET 2 AA9 3 TYR H 75 CYS H 78 -1 O VAL H 77 N MET D 126
SHEET 3 AA9 3 PRO H 84 ALA H 86 -1 O LEU H 85 N ARG H 76
SHEET 1 AB1 3 THR D 298 PHE D 303 0
SHEET 2 AB1 3 GLY D 281 SER D 286 -1 N SER D 285 O THR D 299
SHEET 3 AB1 3 GLN D 348 LYS D 353 -1 O GLY D 350 N GLU D 284
SHEET 1 AB2 5 LEU D 306 LEU D 308 0
SHEET 2 AB2 5 VAL D 357 LEU D 362 1 O VAL D 359 N LEU D 306
SHEET 3 AB2 5 LEU D 462 VAL D 470 -1 O TYR D 465 N LEU D 358
SHEET 4 AB2 5 ILE D 409 GLY D 421 -1 N GLU D 412 O THR D 466
SHEET 5 AB2 5 TYR D 385 ASN D 387 -1 N LEU D 386 O TYR D 411
SHEET 1 AB3 7 LEU D 306 LEU D 308 0
SHEET 2 AB3 7 VAL D 357 LEU D 362 1 O VAL D 359 N LEU D 306
SHEET 3 AB3 7 LEU D 462 VAL D 470 -1 O TYR D 465 N LEU D 358
SHEET 4 AB3 7 ILE D 409 GLY D 421 -1 N GLU D 412 O THR D 466
SHEET 5 AB3 7 GLY D 426 LYS D 433 -1 O HIS D 427 N LYS D 420
SHEET 6 AB3 7 TRP D 439 ASN D 443 -1 O PHE D 442 N ALA D 430
SHEET 7 AB3 7 MET D 446 ILE D 450 -1 O MET D 446 N ASN D 443
SHEET 1 AB4 2 PHE D 365 HIS D 367 0
SHEET 2 AB4 2 ASN D 373 LYS D 375 -1 O ARG D 374 N GLU D 366
SHEET 1 AB5 2 VAL F 93 ASP F 94 0
SHEET 2 AB5 2 GLY H 10 ILE H 11 -1 O GLY H 10 N ASP F 94
SHEET 1 AB6 2 ILE G 71 CYS G 73 0
SHEET 2 AB6 2 ARG G 78 VAL G 80 -1 O VAL G 80 N ILE G 71
LINK SG CYS A 4 ZN ZN A 501 1555 1555 2.33
LINK ND1 HIS A 6 ZN ZN A 501 1555 1555 2.12
LINK SG CYS A 46 ZN ZN A 502 1555 1555 2.29
LINK SG CYS A 49 ZN ZN A 502 1555 1555 2.29
LINK SG CYS A 60 ZN ZN A 503 1555 1555 2.27
LINK SG CYS A 63 ZN ZN A 503 1555 1555 2.34
LINK SG CYS A 68 ZN ZN A 502 1555 1555 2.34
LINK ND1 HIS A 73 ZN ZN A 502 1555 1555 2.14
LINK NE2 HIS A 77 ZN ZN A 503 1555 1555 2.12
LINK ND1 HIS A 83 ZN ZN A 503 1555 1555 2.16
LINK SG CYS A 96 ZN ZN A 501 1555 1555 2.33
LINK SG CYS A 99 ZN ZN A 501 1555 1555 2.28
LINK NE2 HIS A 170 ZN ZN A 504 1555 1555 2.15
LINK SG CYS A 174 ZN ZN A 504 1555 1555 2.31
LINK SG CYS A 182 ZN ZN A 504 1555 1555 2.28
LINK SG CYS A 185 ZN ZN A 504 1555 1555 2.29
LINK ND1 HIS A 250 ZN ZN A 505 1555 1555 2.12
LINK SG CYS A 271 ZN ZN A 505 1555 1555 2.30
LINK SG CYS A 273 ZN ZN A 505 1555 1555 2.29
LINK ND1 HIS A 276 ZN ZN A 505 1555 1555 2.09
LINK SG CYS A 289 ZN ZN A 506 1555 1555 2.37
LINK SG CYS A 292 ZN ZN A 506 1555 1555 2.31
LINK SG CYS A 336 ZN ZN A 506 1555 1555 2.33
LINK SG CYS A 339 ZN ZN A 506 1555 1555 2.31
LINK NE2 HIS C 88 ZN ZN C 101 1555 1555 2.15
LINK SG CYS C 92 ZN ZN C 101 1555 1555 2.33
LINK SG CYS E 78 ZN ZN E 101 1555 1555 2.32
LINK SG CYS E 81 ZN ZN E 101 1555 1555 2.30
LINK NE2 HIS E 93 ZN ZN E 101 1555 1555 2.11
LINK ZN ZN E 101 O HOH E 203 1555 1555 2.20
LINK SG CYS D 4 ZN ZN D 501 1555 1555 2.31
LINK ND1 HIS D 6 ZN ZN D 501 1555 1555 2.13
LINK SG CYS D 46 ZN ZN D 502 1555 1555 2.31
LINK SG CYS D 49 ZN ZN D 502 1555 1555 2.32
LINK SG CYS D 60 ZN ZN D 503 1555 1555 2.32
LINK SG CYS D 63 ZN ZN D 503 1555 1555 2.34
LINK SG CYS D 68 ZN ZN D 502 1555 1555 2.36
LINK ND1 HIS D 73 ZN ZN D 502 1555 1555 2.12
LINK NE2 HIS D 77 ZN ZN D 503 1555 1555 2.11
LINK ND1 HIS D 83 ZN ZN D 503 1555 1555 2.15
LINK SG CYS D 96 ZN ZN D 501 1555 1555 2.35
LINK SG CYS D 99 ZN ZN D 501 1555 1555 2.33
LINK NE2 HIS D 170 ZN ZN D 504 1555 1555 2.12
LINK SG CYS D 174 ZN ZN D 504 1555 1555 2.36
LINK SG CYS D 182 ZN ZN D 504 1555 1555 2.32
LINK SG CYS D 185 ZN ZN D 504 1555 1555 2.28
LINK ND1 HIS D 250 ZN ZN D 505 1555 1555 2.14
LINK SG CYS D 271 ZN ZN D 505 1555 1555 2.32
LINK SG CYS D 273 ZN ZN D 505 1555 1555 2.22
LINK ND1 HIS D 276 ZN ZN D 505 1555 1555 2.13
LINK SG CYS G 73 ZN ZN G 101 1555 1555 2.35
LINK SG CYS G 76 ZN ZN G 101 1555 1555 2.35
LINK NE2 HIS G 88 ZN ZN G 101 1555 1555 2.16
LINK SG CYS G 92 ZN ZN G 101 1555 1555 2.34
LINK SG CYS H 78 ZN ZN H 101 1555 1555 2.30
LINK SG CYS H 81 ZN ZN H 101 1555 1555 2.33
LINK NE2 HIS H 93 ZN ZN H 101 1555 1555 2.13
LINK ZN ZN H 101 O HOH H 201 1555 1555 2.16
SITE 1 AC1 4 CYS A 4 HIS A 6 CYS A 96 CYS A 99
SITE 1 AC2 4 CYS A 46 CYS A 49 CYS A 68 HIS A 73
SITE 1 AC3 4 CYS A 60 CYS A 63 HIS A 77 HIS A 83
SITE 1 AC4 4 HIS A 170 CYS A 174 CYS A 182 CYS A 185
SITE 1 AC5 4 HIS A 250 CYS A 271 CYS A 273 HIS A 276
SITE 1 AC6 4 CYS A 289 CYS A 292 CYS A 336 CYS A 339
SITE 1 AC7 2 HIS C 88 CYS C 92
SITE 1 AC8 4 CYS E 78 CYS E 81 HIS E 93 HOH E 203
SITE 1 AC9 4 CYS D 4 HIS D 6 CYS D 96 CYS D 99
SITE 1 AD1 4 CYS D 46 CYS D 49 CYS D 68 HIS D 73
SITE 1 AD2 4 CYS D 60 CYS D 63 HIS D 77 HIS D 83
SITE 1 AD3 4 HIS D 170 CYS D 174 CYS D 182 CYS D 185
SITE 1 AD4 4 HIS D 250 CYS D 271 CYS D 273 HIS D 276
SITE 1 AD5 4 CYS G 73 CYS G 76 HIS G 88 CYS G 92
SITE 1 AD6 4 CYS H 78 CYS H 81 HIS H 93 HOH H 201
CRYST1 81.076 68.004 137.858 90.00 106.75 90.00 P 1 21 1 4
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 0.012334 0.000000 0.003713 0.00000
SCALE2 0.000000 0.014705 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007575 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
