HEADER HYDROLASE/TRANSCRIPTION REGULATOR/PROTEI08-APR-10 3MHS
TITLE STRUCTURE OF THE SAGA UBP8/SGF11/SUS1/SGF73 DUB MODULE BOUND TO
TITLE 2 UBIQUITIN ALDEHYDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 8;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: UBIQUITIN THIOESTERASE 8, UBIQUITIN-SPECIFIC-PROCESSING
COMPND 5 PROTEASE 8, DEUBIQUITINATING ENZYME 8;
COMPND 6 EC: 3.1.2.15;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: PROTEIN SUS1;
COMPND 10 CHAIN: B;
COMPND 11 ENGINEERED: YES;
COMPND 12 MOL_ID: 3;
COMPND 13 MOLECULE: SAGA-ASSOCIATED FACTOR 11;
COMPND 14 CHAIN: C;
COMPND 15 SYNONYM: 11 KDA SAGA-ASSOCIATED FACTOR;
COMPND 16 ENGINEERED: YES;
COMPND 17 MOL_ID: 4;
COMPND 18 MOLECULE: UBIQUITIN;
COMPND 19 CHAIN: D;
COMPND 20 ENGINEERED: YES;
COMPND 21 MOL_ID: 5;
COMPND 22 MOLECULE: SAGA-ASSOCIATED FACTOR 73;
COMPND 23 CHAIN: E;
COMPND 24 SYNONYM: 73 KDA SAGA-ASSOCIATED FACTOR, SAGA HISTONE
COMPND 25 ACETYLTRANSFERASE COMPLEX 73 KDA SUBUNIT;
COMPND 26 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BREWER'S YEAST,LAGER BEER YEAST,YEAST;
SOURCE 4 ORGANISM_TAXID: 4932;
SOURCE 5 GENE: UBP8, YMR223W, YM9959.05;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: ROSETTTA2 PLYSS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET32A, PCDF, PRSF;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 13 ORGANISM_COMMON: BREWER'S YEAST,LAGER BEER YEAST,YEAST;
SOURCE 14 ORGANISM_TAXID: 4932;
SOURCE 15 GENE: SUS1, YBR111W-A;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: ROSETTTA2 PLYSS;
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PET32A, PCDF, PRSF;
SOURCE 21 MOL_ID: 3;
SOURCE 22 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 23 ORGANISM_COMMON: BREWER'S YEAST,LAGER BEER YEAST,YEAST;
SOURCE 24 ORGANISM_TAXID: 4932;
SOURCE 25 GENE: SGF11, YPL047W;
SOURCE 26 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 27 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 28 EXPRESSION_SYSTEM_STRAIN: ROSETTTA2 PLYSS;
SOURCE 29 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 30 EXPRESSION_SYSTEM_PLASMID: PET32A, PCDF, PRSF;
SOURCE 31 MOL_ID: 4;
SOURCE 32 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 33 ORGANISM_COMMON: HUMAN;
SOURCE 34 ORGANISM_TAXID: 9606;
SOURCE 35 GENE: RPS27A, UBA52, UBB, UBC;
SOURCE 36 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 37 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 38 EXPRESSION_SYSTEM_STRAIN: ROSETTTA2 PLYSS;
SOURCE 39 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 40 EXPRESSION_SYSTEM_PLASMID: PET32A, PCDF, PRSF;
SOURCE 41 MOL_ID: 5;
SOURCE 42 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 43 ORGANISM_COMMON: BREWER'S YEAST,LAGER BEER YEAST,YEAST;
SOURCE 44 ORGANISM_TAXID: 4932;
SOURCE 45 GENE: SGF73, YGL066W;
SOURCE 46 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 47 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 48 EXPRESSION_SYSTEM_STRAIN: ROSETTTA2 PLYSS;
SOURCE 49 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 50 EXPRESSION_SYSTEM_PLASMID: PET32A, PCDF, PRSF
KEYWDS MULTI-PROTEIN COMPLEX, HYDROLASE-TRANSCRIPTION REGULATOR-PROTEIN
KEYWDS 2 BINDING COMPLEX, ACETYLATION, CYTOPLASM, ISOPEPTIDE BOND, NUCLEUS,
KEYWDS 3 PHOSPHOPROTEIN, UBL CONJUGATION
EXPDTA X-RAY DIFFRACTION
AUTHOR N.L.SAMARA,A.B.DATTA,C.E.BERNDSEN,X.ZHANG,T.YAO,R.E.COHEN,C.WOLBERGER
REVDAT 3 09-JUN-10 3MHS 1 JRNL
REVDAT 2 05-MAY-10 3MHS 1 JRNL
REVDAT 1 21-APR-10 3MHS 0
JRNL AUTH N.L.SAMARA,A.B.DATTA,C.E.BERNDSEN,X.ZHANG,T.YAO,R.E.COHEN,
JRNL AUTH 2 C.WOLBERGER
JRNL TITL STRUCTURAL INSIGHTS INTO THE ASSEMBLY AND FUNCTION OF THE
JRNL TITL 2 SAGA DEUBIQUITINATING MODULE.
JRNL REF SCIENCE V. 328 1025 2010
JRNL REFN ISSN 0036-8075
JRNL PMID 20395473
JRNL DOI 10.1126/SCIENCE.1190049
REMARK 2
REMARK 2 RESOLUTION. 1.89 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0102
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.89
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.10
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 73928
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) : 0.161
REMARK 3 R VALUE (WORKING SET) : 0.159
REMARK 3 FREE R VALUE : 0.208
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3934
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) : 1.89
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.94
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4990
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 92.26
REMARK 3 BIN R VALUE (WORKING SET) : 0.2350
REMARK 3 BIN FREE R VALUE SET COUNT : 240
REMARK 3 BIN FREE R VALUE : 0.2880
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6391
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 18
REMARK 3 SOLVENT ATOMS : 845
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.09
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.48000
REMARK 3 B22 (A**2) : 0.18000
REMARK 3 B33 (A**2) : -0.65000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.126
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.127
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.083
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.921
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.966
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.940
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6776 ; 0.015 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 4631 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9167 ; 1.399 ; 1.960
REMARK 3 BOND ANGLES OTHERS (DEGREES): 11385 ; 0.859 ; 3.003
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 858 ; 5.499 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 334 ;38.263 ;25.539
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1276 ;14.993 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 29 ;16.456 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1024 ; 0.180 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7505 ; 0.008 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1285 ; 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): 4098 ; 1.347 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1655 ; 0.428 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6673 ; 2.293 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2678 ; 3.792 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2465 ; 5.245 ; 4.500
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 : 5
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A -10 A 9999
REMARK 3 ORIGIN FOR THE GROUP (A): 50.9447 23.1207 85.7836
REMARK 3 T TENSOR
REMARK 3 T11: 0.0386 T22: 0.0491
REMARK 3 T33: 0.0437 T12: 0.0163
REMARK 3 T13: 0.0073 T23: 0.0100
REMARK 3 L TENSOR
REMARK 3 L11: 0.5815 L22: 0.9011
REMARK 3 L33: 0.5412 L12: 0.2181
REMARK 3 L13: -0.0042 L23: -0.1203
REMARK 3 S TENSOR
REMARK 3 S11: 0.0104 S12: -0.1215 S13: -0.0003
REMARK 3 S21: 0.1473 S22: -0.0343 S23: -0.0291
REMARK 3 S31: 0.0290 S32: 0.0394 S33: 0.0240
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B -10 B 9999
REMARK 3 ORIGIN FOR THE GROUP (A): 76.2298 25.4928 91.2926
REMARK 3 T TENSOR
REMARK 3 T11: 0.0631 T22: 0.2820
REMARK 3 T33: 0.2661 T12: 0.0921
REMARK 3 T13: -0.0490 T23: 0.0888
REMARK 3 L TENSOR
REMARK 3 L11: 1.4763 L22: 1.5178
REMARK 3 L33: 3.5259 L12: 0.8384
REMARK 3 L13: -0.4621 L23: -0.0943
REMARK 3 S TENSOR
REMARK 3 S11: -0.0643 S12: -0.0740 S13: -0.1049
REMARK 3 S21: 0.0333 S22: -0.0359 S23: -0.3790
REMARK 3 S31: 0.3011 S32: 0.8153 S33: 0.1002
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C -10 C 9999
REMARK 3 ORIGIN FOR THE GROUP (A): 50.1470 8.8945 92.2796
REMARK 3 T TENSOR
REMARK 3 T11: 0.1520 T22: 0.1371
REMARK 3 T33: 0.0921 T12: 0.0733
REMARK 3 T13: 0.0191 T23: 0.0891
REMARK 3 L TENSOR
REMARK 3 L11: 1.2640 L22: 1.0433
REMARK 3 L33: 0.5630 L12: 0.4351
REMARK 3 L13: 0.2765 L23: -0.0193
REMARK 3 S TENSOR
REMARK 3 S11: 0.0652 S12: -0.0124 S13: -0.1970
REMARK 3 S21: 0.1783 S22: -0.0228 S23: -0.1220
REMARK 3 S31: 0.1401 S32: 0.0572 S33: -0.0424
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D -10 D 9999
REMARK 3 ORIGIN FOR THE GROUP (A): 36.7994 27.2892 60.2129
REMARK 3 T TENSOR
REMARK 3 T11: 0.0468 T22: 0.0535
REMARK 3 T33: 0.0789 T12: -0.0307
REMARK 3 T13: -0.0162 T23: 0.0051
REMARK 3 L TENSOR
REMARK 3 L11: 1.3345 L22: 1.8965
REMARK 3 L33: 0.6849 L12: -0.3020
REMARK 3 L13: 0.6666 L23: 0.3521
REMARK 3 S TENSOR
REMARK 3 S11: -0.0239 S12: 0.0735 S13: 0.0341
REMARK 3 S21: -0.1870 S22: -0.0465 S23: 0.2337
REMARK 3 S31: 0.0041 S32: -0.0735 S33: 0.0703
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E -10 E 9999
REMARK 3 ORIGIN FOR THE GROUP (A): 59.0590 34.6380 96.5105
REMARK 3 T TENSOR
REMARK 3 T11: 0.1467 T22: 0.1856
REMARK 3 T33: 0.1537 T12: 0.0204
REMARK 3 T13: -0.0443 T23: -0.0596
REMARK 3 L TENSOR
REMARK 3 L11: 0.3300 L22: 1.3448
REMARK 3 L33: 0.7576 L12: 0.3722
REMARK 3 L13: 0.1339 L23: -0.3566
REMARK 3 S TENSOR
REMARK 3 S11: 0.0182 S12: -0.1259 S13: 0.0810
REMARK 3 S21: 0.3002 S22: -0.0676 S23: -0.1452
REMARK 3 S31: -0.1029 S32: 0.0737 S33: 0.0494
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
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 3MHS COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-APR-10.
REMARK 100 THE RCSB ID CODE IS RCSB058562.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-MAR-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 23-ID-B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.94944
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL MONOCHROMATOR
REMARK 200 OPTICS : K-B PAIR OF BIOMORPH MIRRORS
REMARK 200 WITH TWO ADDITIONAL HORIZONTALLY
REMARK 200 DEFLECTING MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 73928
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.890
REMARK 200 RESOLUTION RANGE LOW (A) : 35.100
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 13.700
REMARK 200 R MERGE (I) : 0.09600
REMARK 200 R SYM (I) : 0.09600
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 29.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.89
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.93
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.8
REMARK 200 DATA REDUNDANCY IN SHELL : 8.40
REMARK 200 R MERGE FOR SHELL (I) : 0.88600
REMARK 200 R SYM FOR SHELL (I) : 0.88600
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.250
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SHELXD
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: THE INITIAL STRUCTURE WAS DETERMINED WITH 3 WAVELENGTH SE-
REMARK 200 MAD USING THE FOLLOWING WAVELENGTHS (EV): PEAK: 12658.7 HIGH
REMARK 200 REMOTE: 13058.7 INFLECTION: 12656.9 THE STRUCTURE WAS THEN
REMARK 200 REFINED AGAINST A NATIVE DATA SET COLLECTED AT A WAVELENGTH OF
REMARK 200 13058.7 (EV). THE FINAL COORDINATES REPRESENT THE NATIVE DATA SET.
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.41
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.53
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES PH 6.5, 10% (W/V) PEG
REMARK 280 8000, 20% (V/V) GLYCEROL, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
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 39.30000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 60.45150
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 51.04200
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 60.45150
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 39.30000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 51.04200
REMARK 290 SMTRY3 4 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: PENTAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 21400 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 34050 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -96.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, E, C, B, D
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 GLY A -4
REMARK 465 ALA A -3
REMARK 465 ALA A -2
REMARK 465 ALA A -1
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 ALA A 260
REMARK 465 LYS A 261
REMARK 465 GLU A 262
REMARK 465 VAL A 263
REMARK 465 SER A 264
REMARK 465 ARG A 265
REMARK 465 ALA A 266
REMARK 465 HIS A 400
REMARK 465 SER A 401
REMARK 465 MET B 1
REMARK 465 THR B 2
REMARK 465 MET B 3
REMARK 465 ASP B 4
REMARK 465 GLN B 96
REMARK 465 MET C 1
REMARK 465 THR C 2
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 ARG E 2
REMARK 465 SER E 3
REMARK 465 GLY E 4
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 ASN E 96
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ASN A 267 CG OD1 ND2
REMARK 470 LYS A 399 CG CD CE NZ
REMARK 470 GLU C 3 CG CD OE1 OE2
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 SG CYS A 146 C GLZ D 76 2.00
REMARK 500 OG SER C 94 O HOH C 491 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 132 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
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 ASN A 91 -3.45 -144.47
REMARK 500 ASN A 268 76.20 -115.29
REMARK 500 ASN A 294 -94.55 -127.20
REMARK 500 ASN A 295 -143.57 58.81
REMARK 500 ASP A 444 -118.21 49.80
REMARK 500 SER C 67 51.22 -93.24
REMARK 500 LEU D 71 -169.88 -109.58
REMARK 500 LYS E 12 124.13 -37.23
REMARK 500 TYR E 19 -69.72 -108.00
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH B 852 DISTANCE = 8.49 ANGSTROMS
REMARK 525 HOH E 575 DISTANCE = 5.84 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 474 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 77 NE2
REMARK 620 2 HIS A 83 ND1 113.1
REMARK 620 3 CYS A 63 SG 101.1 110.1
REMARK 620 4 CYS A 60 SG 111.8 105.4 115.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C 100 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 88 NE2
REMARK 620 2 CYS C 73 SG 112.8
REMARK 620 3 CYS C 76 SG 103.3 109.1
REMARK 620 4 CYS C 92 SG 107.0 113.4 110.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN E 97 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS E 93 NE2
REMARK 620 2 GLU E 95 OE2 97.2
REMARK 620 3 CYS E 81A SG 113.1 126.4
REMARK 620 4 CYS E 78 SG 105.1 102.3 110.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 475 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 170 NE2
REMARK 620 2 CYS A 185 SG 120.3
REMARK 620 3 CYS A 182 SG 104.6 113.7
REMARK 620 4 CYS A 174 SG 98.2 106.4 112.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 476 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 276 ND1
REMARK 620 2 HIS A 250 ND1 98.9
REMARK 620 3 CYS A 273 SG 108.8 118.1
REMARK 620 4 CYS A 271 SG 114.2 104.0 112.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 472 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 6 ND1
REMARK 620 2 CYS A 4 SG 105.8
REMARK 620 3 CYS A 99 SG 103.6 115.1
REMARK 620 4 CYS A 96 SG 104.9 108.0 118.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 473 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 73 ND1
REMARK 620 2 CYS A 46 SG 103.0
REMARK 620 3 CYS A 68 SG 109.4 114.4
REMARK 620 4 CYS A 49 SG 107.0 99.4 121.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 477 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 336 SG
REMARK 620 2 CYS A 339 SG 104.8
REMARK 620 3 CYS A 289 SG 107.4 112.7
REMARK 620 4 CYS A 292 SG 110.9 107.3 113.4
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 EDO A 1295
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1487
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 472
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 473
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 474
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 475
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 100
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN E 97
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 477
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3MHH RELATED DB: PDB
REMARK 900 SAGA APO- DUB MODULE
DBREF 3MHS A 1 471 UNP P50102 UBP8_YEAST 1 471
DBREF 3MHS B 1 96 UNP Q6WNK7 SUS1_YEAST 1 96
DBREF 3MHS C 1 99 UNP Q03067 SGF11_YEAST 1 99
DBREF 3MHS D 1 76 UNP P62988 UBIQ_HUMAN 1 76
DBREF 3MHS E 1 96 UNP P53165 SGF73_YEAST 1 96
SEQADV 3MHS GLY A -4 UNP P50102 EXPRESSION TAG
SEQADV 3MHS ALA A -3 UNP P50102 EXPRESSION TAG
SEQADV 3MHS ALA A -2 UNP P50102 EXPRESSION TAG
SEQADV 3MHS ALA A -1 UNP P50102 EXPRESSION TAG
SEQADV 3MHS ALA A 0 UNP P50102 EXPRESSION TAG
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 D 76 MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE
SEQRES 2 D 76 THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU ASN VAL
SEQRES 3 D 76 LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP
SEQRES 4 D 76 GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP
SEQRES 5 D 76 GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER
SEQRES 6 D 76 THR LEU HIS LEU VAL LEU ARG LEU ARG GLY GLZ
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 ASN 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
MODRES 3MHS GLZ D 76 GLY AMINO-ACETALDEHYDE
HET GLZ D 76 4
HET EDO A1295 4
HET GOL A1487 6
HET ZN A 472 1
HET ZN A 473 1
HET ZN A 474 1
HET ZN A 475 1
HET ZN A 476 1
HET ZN A 477 1
HET ZN C 100 1
HET ZN E 97 1
HETNAM GLZ AMINO-ACETALDEHYDE
HETNAM EDO 1,2-ETHANEDIOL
HETNAM GOL GLYCEROL
HETNAM ZN ZINC ION
HETSYN EDO ETHYLENE GLYCOL
FORMUL 4 GLZ C2 H5 N O
FORMUL 6 EDO C2 H6 O2
FORMUL 7 GOL C3 H8 O3
FORMUL 8 ZN 8(ZN 2+)
FORMUL 16 HOH *845(H2 O)
HELIX 1 1 CYS A 4 PHE A 11 1 8
HELIX 2 2 ASN A 13 HIS A 33 1 21
HELIX 3 3 VAL A 35 MET A 44 1 10
HELIX 4 4 SER A 72 GLY A 82 1 11
HELIX 5 5 ILE A 106 ASP A 111 1 6
HELIX 6 6 ALA A 112 LYS A 116 5 5
HELIX 7 7 TYR A 117 LYS A 124 1 8
HELIX 8 8 SER A 129 ARG A 133 5 5
HELIX 9 9 THR A 145 HIS A 157 1 13
HELIX 10 10 ASN A 158 SER A 167 1 10
HELIX 11 11 GLN A 168 CYS A 174 1 7
HELIX 12 12 CYS A 182 GLY A 196 1 15
HELIX 13 13 GLN A 213 ASN A 227 1 15
HELIX 14 14 GLN A 228 ALA A 231 5 4
HELIX 15 15 ALA A 238 LEU A 257 1 20
HELIX 16 16 CYS A 273 PHE A 279 1 7
HELIX 17 17 LYS A 315 LYS A 325 1 11
HELIX 18 18 LYS A 389 CYS A 392 5 4
HELIX 19 19 SER A 451 LEU A 456 1 6
HELIX 20 20 ALA B 6 SER B 19 1 14
HELIX 21 21 GLY B 20 GLU B 36 1 17
HELIX 22 22 GLY B 37 GLU B 54 1 18
HELIX 23 23 ASN B 57 MET B 72 1 16
HELIX 24 24 SER B 74 ILE B 92 1 19
HELIX 25 25 THR C 7 TYR C 42 1 36
HELIX 26 26 ARG C 84 LEU C 93 1 10
HELIX 27 27 THR D 22 GLY D 35 1 14
HELIX 28 28 PRO D 37 GLN D 41 5 5
HELIX 29 29 LEU D 56 ASN D 60 5 5
HELIX 30 30 LYS E 12 TYR E 19 1 8
HELIX 31 31 SER E 31 SER E 34 5 4
HELIX 32 32 LEU E 35 THR E 42 1 8
HELIX 33 33 ASN E 50 PHE E 58 1 9
HELIX 34 34 ALA E 86 ILE E 90 5 5
SHEET 1 A 5 CYS A 66 CYS A 68 0
SHEET 2 A 5 THR A 57 CYS A 60 -1 N PHE A 58 O GLY A 67
SHEET 3 A 5 PHE A 85 ASN A 88 -1 O ILE A 87 N MET A 59
SHEET 4 A 5 LEU A 94 CYS A 96 -1 O PHE A 95 N GLY A 86
SHEET 5 A 5 ASP A 101 ILE A 103 -1 O ILE A 103 N LEU A 94
SHEET 1 B 3 THR A 125 MET A 126 0
SHEET 2 B 3 ARG E 76 CYS E 78 -1 O VAL E 77 N MET A 126
SHEET 3 B 3 PRO E 84 LEU E 85 -1 O LEU E 85 N ARG E 76
SHEET 1 C 2 GLN A 236 ASP A 237 0
SHEET 2 C 2 ARG D 74 GLY D 75 -1 O GLY D 75 N GLN A 236
SHEET 1 D 4 LYS A 297 PHE A 303 0
SHEET 2 D 4 GLY A 281 VAL A 288 -1 N LEU A 283 O ASP A 301
SHEET 3 D 4 ILE A 346 LYS A 353 -1 O GLY A 350 N GLU A 284
SHEET 4 D 4 GLU A 327 GLN A 328 -1 N GLU A 327 O LYS A 347
SHEET 1 E 5 LEU A 306 LEU A 308 0
SHEET 2 E 5 VAL A 357 LEU A 362 1 O GLN A 361 N LEU A 306
SHEET 3 E 5 ALA A 460 VAL A 470 -1 O TYR A 465 N LEU A 358
SHEET 4 E 5 ILE A 409 THR A 422 -1 N ILE A 410 O GLN A 469
SHEET 5 E 5 TYR A 385 ASN A 387 -1 N LEU A 386 O TYR A 411
SHEET 1 F 7 LEU A 306 LEU A 308 0
SHEET 2 F 7 VAL A 357 LEU A 362 1 O GLN A 361 N LEU A 306
SHEET 3 F 7 ALA A 460 VAL A 470 -1 O TYR A 465 N LEU A 358
SHEET 4 F 7 ILE A 409 THR A 422 -1 N ILE A 410 O GLN A 469
SHEET 5 F 7 GLU A 425 LYS A 433 -1 O GLU A 425 N THR A 422
SHEET 6 F 7 TRP A 439 ASN A 443 -1 O PHE A 442 N ALA A 430
SHEET 7 F 7 MET A 446 ILE A 450 -1 O MET A 446 N ASN A 443
SHEET 1 G 2 HIS A 335 CYS A 336 0
SHEET 2 G 2 SER A 341 THR A 342 -1 O SER A 341 N CYS A 336
SHEET 1 H 2 PHE A 365 HIS A 367 0
SHEET 2 H 2 ASN A 373 LYS A 375 -1 O ARG A 374 N GLU A 366
SHEET 1 I 2 VAL B 93 ASP B 94 0
SHEET 2 I 2 GLY E 10 ILE E 11 -1 N GLY E 10 O ASP B 94
SHEET 1 J 2 TYR C 70 HIS C 72 0
SHEET 2 J 2 ASP C 79 SER C 81 -1 O VAL C 80 N ILE C 71
SHEET 1 K 5 THR D 12 GLU D 16 0
SHEET 2 K 5 GLN D 2 LYS D 6 -1 N ILE D 3 O LEU D 15
SHEET 3 K 5 THR D 66 VAL D 70 1 O LEU D 67 N LYS D 6
SHEET 4 K 5 ARG D 42 PHE D 45 -1 N ARG D 42 O VAL D 70
SHEET 5 K 5 LYS D 48 GLN D 49 -1 O LYS D 48 N PHE D 45
LINK C GLY D 75 N GLZ D 76 1555 1555 1.29
LINK NE2 HIS A 77 ZN ZN A 474 1555 1555 1.87
LINK NE2 HIS C 88 ZN ZN C 100 1555 1555 2.01
LINK NE2 HIS E 93 ZN ZN E 97 1555 1555 2.03
LINK SG CYS C 73 ZN ZN C 100 1555 1555 2.06
LINK NE2 HIS A 170 ZN ZN A 475 1555 1555 2.07
LINK ND1 HIS A 276 ZN ZN A 476 1555 1555 2.08
LINK ND1 HIS A 250 ZN ZN A 476 1555 1555 2.08
LINK ND1 HIS A 83 ZN ZN A 474 1555 1555 2.10
LINK ND1 HIS A 6 ZN ZN A 472 1555 1555 2.13
LINK ND1 HIS A 73 ZN ZN A 473 1555 1555 2.14
LINK SG CYS A 185 ZN ZN A 475 1555 1555 2.22
LINK OE2 GLU E 95 ZN ZN E 97 1555 1555 2.23
LINK SG CYS E 81A ZN ZN E 97 1555 1555 2.27
LINK SG CYS A 336 ZN ZN A 477 1555 1555 2.27
LINK SG CYS A 46 ZN ZN A 473 1555 1555 2.28
LINK SG CYS A 4 ZN ZN A 472 1555 1555 2.28
LINK SG CYS A 273 ZN ZN A 476 1555 1555 2.29
LINK SG CYS A 63 ZN ZN A 474 1555 1555 2.30
LINK SG CYS A 271 ZN ZN A 476 1555 1555 2.30
LINK SG CYS E 78 ZN ZN E 97 1555 1555 2.31
LINK SG CYS A 68 ZN ZN A 473 1555 1555 2.31
LINK SG CYS A 99 ZN ZN A 472 1555 1555 2.31
LINK SG CYS A 96 ZN ZN A 472 1555 1555 2.31
LINK SG CYS C 76 ZN ZN C 100 1555 1555 2.32
LINK SG CYS A 49 ZN ZN A 473 1555 1555 2.32
LINK SG CYS A 60 ZN ZN A 474 1555 1555 2.32
LINK SG CYS A 182 ZN ZN A 475 1555 1555 2.33
LINK SG CYS A 339 ZN ZN A 477 1555 1555 2.34
LINK SG CYS A 289 ZN ZN A 477 1555 1555 2.35
LINK SG CYS C 92 ZN ZN C 100 1555 1555 2.35
LINK SG CYS A 174 ZN ZN A 475 1555 1555 2.37
LINK SG CYS A 292 ZN ZN A 477 1555 1555 2.38
CISPEP 1 ASN A 199 THR A 200 0 2.77
CISPEP 2 ASN A 295 SER A 296 0 3.32
CISPEP 3 GLU C 66 SER C 67 0 16.14
SITE 1 AC1 3 GLN A 236 GLU A 240 ARG D 74
SITE 1 AC2 5 HIS A 367 LEU A 369 GLY A 371 HOH A 562
SITE 2 AC2 5 GLY D 35
SITE 1 AC3 4 CYS A 4 HIS A 6 CYS A 96 CYS A 99
SITE 1 AC4 4 CYS A 46 CYS A 49 CYS A 68 HIS A 73
SITE 1 AC5 4 CYS A 60 CYS A 63 HIS A 77 HIS A 83
SITE 1 AC6 4 HIS A 170 CYS A 174 CYS A 182 CYS A 185
SITE 1 AC7 4 HIS A 250 CYS A 271 CYS A 273 HIS A 276
SITE 1 AC8 4 CYS C 73 CYS C 76 HIS C 88 CYS C 92
SITE 1 AC9 4 CYS E 78 CYS E 81A HIS E 93 GLU E 95
SITE 1 BC1 4 CYS A 289 CYS A 292 CYS A 336 CYS A 339
CRYST1 78.600 102.084 120.903 90.00 90.00 90.00 P 21 21 21 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 0.012723 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009796 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008271 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
