HEADER HYDROLASE 12-JUN-12 4FK5
TITLE STRUCTURE OF THE SAGA UBP8(S144N)/SGF11/SUS1/SGF73 DUB MODULE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 8;
COMPND 3 CHAIN: A;
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 MUTATION: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: PROTEIN SUS1;
COMPND 11 CHAIN: B;
COMPND 12 ENGINEERED: YES;
COMPND 13 MOL_ID: 3;
COMPND 14 MOLECULE: SAGA-ASSOCIATED FACTOR 11;
COMPND 15 CHAIN: C;
COMPND 16 SYNONYM: 11 KDA SAGA-ASSOCIATED FACTOR;
COMPND 17 ENGINEERED: YES;
COMPND 18 MOL_ID: 4;
COMPND 19 MOLECULE: SAGA-ASSOCIATED FACTOR 73;
COMPND 20 CHAIN: E;
COMPND 21 FRAGMENT: UNP RESIDUES 1-96;
COMPND 22 SYNONYM: 73 KDA SAGA-ASSOCIATED FACTOR, SAGA HISTONE
COMPND 23 ACETYLTRANSFERASE COMPLEX 73 KDA SUBUNIT;
COMPND 24 ENGINEERED: 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, YM9959.05, YMR223W;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: ROSETTA2(DE3) PLYSS;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PET-32A;
SOURCE 12 MOL_ID: 2;
SOURCE 13 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 14 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 15 ORGANISM_TAXID: 559292;
SOURCE 16 STRAIN: ATCC 204508 / S288C;
SOURCE 17 GENE: SUS1, YBR111W-A;
SOURCE 18 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 19 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 20 EXPRESSION_SYSTEM_STRAIN: ROSETTA2(DE3) PLYSS;
SOURCE 21 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 22 EXPRESSION_SYSTEM_PLASMID: PRSF;
SOURCE 23 MOL_ID: 3;
SOURCE 24 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 25 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 26 ORGANISM_TAXID: 559292;
SOURCE 27 STRAIN: ATCC 204508 / S288C;
SOURCE 28 GENE: SGF11, YPL047W;
SOURCE 29 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 30 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 31 EXPRESSION_SYSTEM_STRAIN: ROSETTA2(DE3) PLYSS;
SOURCE 32 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 33 EXPRESSION_SYSTEM_PLASMID: PCDFDUET-1;
SOURCE 34 MOL_ID: 4;
SOURCE 35 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 36 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 37 ORGANISM_TAXID: 559292;
SOURCE 38 STRAIN: ATCC 204508 / S288C;
SOURCE 39 GENE: SGF73, YGL066W;
SOURCE 40 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 41 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 42 EXPRESSION_SYSTEM_STRAIN: ROSETTA2(DE3) PLYSS;
SOURCE 43 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 44 EXPRESSION_SYSTEM_PLASMID: PCDFDUET-1
KEYWDS MULTI-PROTEIN COMPLEX, DEUBIQUITINATION, TRANSCRIPTION, NUCLEOSOME,
KEYWDS 2 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR N.L.SAMARA,A.E.RINGEL,C.WOLBERGER
REVDAT 3 28-FEB-24 4FK5 1 REMARK SEQADV LINK
REVDAT 2 29-AUG-12 4FK5 1 JRNL
REVDAT 1 25-JUL-12 4FK5 0
JRNL AUTH N.L.SAMARA,A.E.RINGEL,C.WOLBERGER
JRNL TITL A ROLE FOR INTERSUBUNIT INTERACTIONS IN MAINTAINING SAGA
JRNL TITL 2 DEUBIQUITINATING MODULE STRUCTURE AND ACTIVITY.
JRNL REF STRUCTURE V. 20 1414 2012
JRNL REFN ISSN 0969-2126
JRNL PMID 22771212
JRNL DOI 10.1016/J.STR.2012.05.015
REMARK 2
REMARK 2 RESOLUTION. 2.03 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
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) : 2.03
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 74.87
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 57655
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) : 0.177
REMARK 3 R VALUE (WORKING SET) : 0.175
REMARK 3 FREE R VALUE : 0.212
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3085
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) : 2.03
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.09
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3842
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.27
REMARK 3 BIN R VALUE (WORKING SET) : 0.2060
REMARK 3 BIN FREE R VALUE SET COUNT : 210
REMARK 3 BIN FREE R VALUE : 0.2530
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5681
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 24
REMARK 3 SOLVENT ATOMS : 396
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.27
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.09000
REMARK 3 B22 (A**2) : -1.30000
REMARK 3 B33 (A**2) : 1.21000
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): 0.156
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.143
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.095
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.636
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.962
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5839 ; 0.020 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 3975 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7876 ; 1.277 ; 1.954
REMARK 3 BOND ANGLES OTHERS (DEGREES): 9761 ; 0.852 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 715 ; 7.951 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 282 ;39.719 ;25.390
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1086 ;15.726 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 24 ;15.490 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 881 ; 0.110 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6412 ; 0.010 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1108 ; 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 : 4
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 508
REMARK 3 RESIDUE RANGE : A 601 A 842
REMARK 3 ORIGIN FOR THE GROUP (A): 10.5486 24.1123 22.1598
REMARK 3 T TENSOR
REMARK 3 T11: 0.0614 T22: 0.0886
REMARK 3 T33: 0.0644 T12: -0.0089
REMARK 3 T13: 0.0065 T23: 0.0164
REMARK 3 L TENSOR
REMARK 3 L11: 0.2805 L22: 0.7359
REMARK 3 L33: 0.1095 L12: 0.2023
REMARK 3 L13: 0.1652 L23: 0.1662
REMARK 3 S TENSOR
REMARK 3 S11: 0.0113 S12: 0.0386 S13: 0.0085
REMARK 3 S21: 0.0842 S22: -0.0388 S23: 0.0835
REMARK 3 S31: 0.0238 S32: 0.0323 S33: 0.0275
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 5 B 96
REMARK 3 RESIDUE RANGE : B 101 B 143
REMARK 3 ORIGIN FOR THE GROUP (A): 36.8446 27.5216 22.4844
REMARK 3 T TENSOR
REMARK 3 T11: 0.0453 T22: 0.0754
REMARK 3 T33: 0.1681 T12: 0.0276
REMARK 3 T13: 0.0035 T23: -0.0285
REMARK 3 L TENSOR
REMARK 3 L11: 0.8419 L22: 1.1400
REMARK 3 L33: 0.9887 L12: 0.7696
REMARK 3 L13: -0.7534 L23: -0.5280
REMARK 3 S TENSOR
REMARK 3 S11: -0.0799 S12: 0.0358 S13: -0.1075
REMARK 3 S21: -0.0519 S22: 0.1008 S23: -0.2510
REMARK 3 S31: 0.1193 S32: 0.1100 S33: -0.0209
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 4 C 95
REMARK 3 RESIDUE RANGE : C 101 C 102
REMARK 3 RESIDUE RANGE : C 201 C 254
REMARK 3 ORIGIN FOR THE GROUP (A): 11.5949 10.0802 27.3361
REMARK 3 T TENSOR
REMARK 3 T11: 0.0730 T22: 0.0630
REMARK 3 T33: 0.1092 T12: -0.0076
REMARK 3 T13: -0.0133 T23: 0.0190
REMARK 3 L TENSOR
REMARK 3 L11: 0.4771 L22: 1.1873
REMARK 3 L33: 0.0159 L12: 0.4211
REMARK 3 L13: -0.0674 L23: -0.0015
REMARK 3 S TENSOR
REMARK 3 S11: 0.0095 S12: 0.0689 S13: -0.1605
REMARK 3 S21: 0.2059 S22: -0.0190 S23: -0.1174
REMARK 3 S31: 0.0187 S32: -0.0154 S33: 0.0095
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 5 E 95
REMARK 3 RESIDUE RANGE : E 101 E 101
REMARK 3 RESIDUE RANGE : E 201 E 257
REMARK 3 ORIGIN FOR THE GROUP (A): 21.3971 36.5942 29.9770
REMARK 3 T TENSOR
REMARK 3 T11: 0.0913 T22: 0.0875
REMARK 3 T33: 0.1154 T12: -0.0042
REMARK 3 T13: -0.0407 T23: -0.0226
REMARK 3 L TENSOR
REMARK 3 L11: 0.2489 L22: 0.5780
REMARK 3 L33: 0.1005 L12: 0.2228
REMARK 3 L13: 0.0043 L23: 0.1753
REMARK 3 S TENSOR
REMARK 3 S11: -0.0353 S12: -0.0222 S13: 0.0364
REMARK 3 S21: 0.0745 S22: 0.0207 S23: -0.0300
REMARK 3 S31: 0.0392 S32: -0.0138 S33: 0.0146
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 4FK5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-JUN-12.
REMARK 100 THE DEPOSITION ID IS D_1000072999.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-AUG-10
REMARK 200 TEMPERATURE (KELVIN) : 108
REMARK 200 PH : 5.2
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) : 0.9794
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 : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 60890
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.032
REMARK 200 RESOLUTION RANGE LOW (A) : 74.868
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.03
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 14.80
REMARK 200 R MERGE FOR SHELL (I) : 0.86500
REMARK 200 R SYM FOR SHELL (I) : 0.86500
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.640
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.15
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.68
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM CITRATE PH 5.2, 16% PEG3350,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K
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 41.76400
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 53.50900
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 52.38750
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 53.50900
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 41.76400
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 52.38750
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 17590 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 32210 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -96.0 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 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 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 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 LEU A 329
REMARK 465 LYS A 330
REMARK 465 ASP A 331
REMARK 465 PHE A 332
REMARK 465 ASN A 333
REMARK 465 TYR A 334
REMARK 465 HIS A 335
REMARK 465 THR A 342
REMARK 465 GLN A 343
REMARK 465 ASP A 344
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 B 1
REMARK 465 THR B 2
REMARK 465 MET B 3
REMARK 465 ASP B 4
REMARK 465 MET C 1
REMARK 465 THR C 2
REMARK 465 GLU C 3
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 ASN E 96
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 HIS A 6 CG HIS A 6 CD2 0.059
REMARK 500 HIS A 50 CG HIS A 50 CD2 0.054
REMARK 500 HIS A 73 CG HIS A 73 CD2 0.088
REMARK 500 HIS A 250 CG HIS A 250 CD2 0.068
REMARK 500 HIS A 352 CG HIS A 352 CD2 0.055
REMARK 500 HIS A 367 CG HIS A 367 CD2 0.064
REMARK 500 ARG B 86 N ARG B 86 CA 0.121
REMARK 500 GLU B 87 CD GLU B 87 OE2 0.101
REMARK 500 HIS E 93 CG HIS E 93 CD2 0.060
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 LEU A 386 CB - CG - CD2 ANGL. DEV. = 11.4 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 -0.26 -145.53
REMARK 500 ILE A 226 -83.25 -75.21
REMARK 500 ASN A 227 147.30 -176.79
REMARK 500 ASN A 259 45.62 -142.74
REMARK 500 ASN A 294 109.94 -51.54
REMARK 500 LYS A 297 112.05 -162.16
REMARK 500 CYS A 339 -49.08 62.04
REMARK 500 GLU A 425 34.91 -99.73
REMARK 500 ASP A 444 -122.24 47.99
REMARK 500 HIS E 48 42.89 -142.60
REMARK 500 LEU E 94 60.10 -68.11
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 MET A 142 GLY A 143 75.50
REMARK 500 ILE A 226 ASN A 227 133.24
REMARK 500 ASN A 267 ASN A 268 -132.25
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 101.6
REMARK 620 3 CYS A 96 SG 115.6 99.7
REMARK 620 4 CYS A 99 SG 113.8 107.2 116.2
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 110.6
REMARK 620 3 CYS A 68 SG 109.8 118.3
REMARK 620 4 HIS A 73 ND1 104.1 113.2 99.6
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 120.0
REMARK 620 3 HIS A 77 NE2 112.8 103.3
REMARK 620 4 HIS A 83 ND1 94.1 116.8 109.8
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 98.6
REMARK 620 3 CYS A 182 SG 103.6 113.2
REMARK 620 4 CYS A 185 SG 121.0 104.9 114.8
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 105.2
REMARK 620 3 CYS A 273 SG 118.1 114.8
REMARK 620 4 HIS A 276 ND1 99.8 111.5 106.4
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 119.2
REMARK 620 3 CYS A 336 SG 103.1 109.5
REMARK 620 4 CYS A 339 SG 109.2 102.6 113.6
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 CYS C 73 SG
REMARK 620 2 CYS C 76 SG 111.8
REMARK 620 3 HIS C 88 NE2 109.5 106.3
REMARK 620 4 CYS C 92 SG 113.4 106.3 109.2
REMARK 620 N 1 2 3
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 119.2
REMARK 620 3 HIS E 93 NE2 105.2 117.0
REMARK 620 N 1 2
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 GOL A 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 508
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN E 101
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4FIP RELATED DB: PDB
REMARK 900 SGF11 (1-72), UBP8 (S144N)
REMARK 900 RELATED ID: 4FJC RELATED DB: PDB
REMARK 900 SGF11 (1-72)
DBREF 4FK5 A 1 471 UNP P50102 UBP8_YEAST 1 471
DBREF 4FK5 B 1 96 UNP Q6WNK7 SUS1_YEAST 1 96
DBREF 4FK5 C 1 99 UNP Q03067 SGF11_YEAST 1 99
DBREF 4FK5 E 1 96 UNP P53165 SGF73_YEAST 1 96
SEQADV 4FK5 GLY A -4 UNP P50102 EXPRESSION TAG
SEQADV 4FK5 ALA A -3 UNP P50102 EXPRESSION TAG
SEQADV 4FK5 ALA A -2 UNP P50102 EXPRESSION TAG
SEQADV 4FK5 ALA A -1 UNP P50102 EXPRESSION TAG
SEQADV 4FK5 ALA A 0 UNP P50102 EXPRESSION TAG
SEQADV 4FK5 ASN A 144 UNP P50102 SER 144 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 ASN 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 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
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 GOL A 507 6
HET EDO A 508 4
HET ZN C 101 1
HET GOL C 102 6
HET ZN E 101 1
HETNAM ZN ZINC ION
HETNAM GOL GLYCEROL
HETNAM EDO 1,2-ETHANEDIOL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 5 ZN 8(ZN 2+)
FORMUL 11 GOL 2(C3 H8 O3)
FORMUL 12 EDO C2 H6 O2
FORMUL 16 HOH *396(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 THR A 145 HIS A 157 1 13
HELIX 9 9 ASN A 158 SER A 167 1 10
HELIX 10 10 GLN A 168 CYS A 174 1 7
HELIX 11 11 CYS A 182 GLY A 196 1 15
HELIX 12 12 GLN A 213 ASN A 227 1 15
HELIX 13 13 ASP A 237 LEU A 257 1 21
HELIX 14 14 ASN A 259 ASN A 268 1 10
HELIX 15 15 CYS A 273 PHE A 279 1 7
HELIX 16 16 LYS A 315 HIS A 324 1 10
HELIX 17 17 LYS A 389 CYS A 392 5 4
HELIX 18 18 SER A 451 LEU A 456 1 6
HELIX 19 19 GLN B 7 SER B 19 1 13
HELIX 20 20 GLY B 20 GLU B 36 1 17
HELIX 21 21 GLY B 37 GLU B 54 1 18
HELIX 22 22 ASN B 57 VAL B 73 1 17
HELIX 23 23 SER B 74 GLU B 91 1 18
HELIX 24 24 THR C 7 TYR C 42 1 36
HELIX 25 25 GLN C 65 SER C 68 5 4
HELIX 26 26 ARG C 84 ARG C 95 1 12
HELIX 27 27 LYS E 12 TYR E 19 1 8
HELIX 28 28 SER E 31 SER E 34 5 4
HELIX 29 29 LEU E 35 THR E 42 1 8
HELIX 30 30 ASN E 50 PHE E 58 1 9
HELIX 31 31 ALA E 89 LEU E 94 1 6
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 TYR A 102 -1 O ASP A 101 N CYS A 96
SHEET 1 B 3 THR A 125 MET A 126 0
SHEET 2 B 3 TYR E 75 CYS E 78 -1 O VAL E 77 N MET A 126
SHEET 3 B 3 PRO E 84 ALA E 86 -1 O LEU E 85 N ARG E 76
SHEET 1 C 3 ASN A 295 PHE A 303 0
SHEET 2 C 3 GLY A 281 VAL A 288 -1 N SER A 285 O THR A 299
SHEET 3 C 3 ILE A 346 LYS A 353 -1 O GLY A 350 N GLU A 284
SHEET 1 D 5 LEU A 306 LEU A 308 0
SHEET 2 D 5 VAL A 357 LEU A 362 1 O GLN A 361 N LEU A 308
SHEET 3 D 5 ALA A 460 VAL A 470 -1 O TYR A 461 N LEU A 362
SHEET 4 D 5 ILE A 409 LYS A 420 -1 N GLU A 412 O THR A 466
SHEET 5 D 5 TYR A 385 ASN A 387 -1 N LEU A 386 O TYR A 411
SHEET 1 E 7 LEU A 306 LEU A 308 0
SHEET 2 E 7 VAL A 357 LEU A 362 1 O GLN A 361 N LEU A 308
SHEET 3 E 7 ALA A 460 VAL A 470 -1 O TYR A 461 N LEU A 362
SHEET 4 E 7 ILE A 409 LYS A 420 -1 N GLU A 412 O THR A 466
SHEET 5 E 7 HIS A 427 LYS A 433 -1 O ILE A 429 N SER A 418
SHEET 6 E 7 TRP A 439 ASN A 443 -1 O PHE A 442 N ALA A 430
SHEET 7 E 7 MET A 446 ILE A 450 -1 O SER A 448 N LYS A 441
SHEET 1 F 2 PHE A 365 HIS A 367 0
SHEET 2 F 2 ASN A 373 LYS A 375 -1 O ARG A 374 N GLU A 366
SHEET 1 G 2 VAL B 93 GLN B 96 0
SHEET 2 G 2 GLU E 7 ILE E 11 -1 O GLY E 10 N ASP B 94
SHEET 1 H 2 TYR C 70 HIS C 72 0
SHEET 2 H 2 ASP C 79 SER C 81 -1 O VAL C 80 N ILE C 71
LINK SG CYS A 4 ZN ZN A 501 1555 1555 2.25
LINK ND1 HIS A 6 ZN ZN A 501 1555 1555 2.18
LINK SG CYS A 46 ZN ZN A 502 1555 1555 2.32
LINK SG CYS A 49 ZN ZN A 502 1555 1555 2.19
LINK SG CYS A 60 ZN ZN A 503 1555 1555 2.37
LINK SG CYS A 63 ZN ZN A 503 1555 1555 2.14
LINK SG CYS A 68 ZN ZN A 502 1555 1555 2.27
LINK ND1 HIS A 73 ZN ZN A 502 1555 1555 2.22
LINK NE2 HIS A 77 ZN ZN A 503 1555 1555 2.03
LINK ND1 HIS A 83 ZN ZN A 503 1555 1555 2.13
LINK SG CYS A 96 ZN ZN A 501 1555 1555 2.26
LINK SG CYS A 99 ZN ZN A 501 1555 1555 2.13
LINK NE2 HIS A 170 ZN ZN A 504 1555 1555 2.04
LINK SG CYS A 174 ZN ZN A 504 1555 1555 2.42
LINK SG CYS A 182 ZN ZN A 504 1555 1555 2.27
LINK SG CYS A 185 ZN ZN A 504 1555 1555 2.09
LINK ND1 HIS A 250 ZN ZN A 505 1555 1555 2.07
LINK SG CYS A 271 ZN ZN A 505 1555 1555 2.35
LINK SG CYS A 273 ZN ZN A 505 1555 1555 2.28
LINK ND1 HIS A 276 ZN ZN A 505 1555 1555 1.99
LINK SG CYS A 289 ZN ZN A 506 1555 1555 2.42
LINK SG CYS A 292 ZN ZN A 506 1555 1555 2.41
LINK SG CYS A 336 ZN ZN A 506 1555 1555 2.44
LINK SG CYS A 339 ZN ZN A 506 1555 1555 2.95
LINK SG CYS C 73 ZN ZN C 101 1555 1555 2.35
LINK SG CYS C 76 ZN ZN C 101 1555 1555 2.29
LINK NE2 HIS C 88 ZN ZN C 101 1555 1555 1.99
LINK SG CYS C 92 ZN ZN C 101 1555 1555 2.46
LINK SG CYS E 78 ZN ZN E 101 1555 1555 2.13
LINK SG CYS E 81 ZN ZN E 101 1555 1555 2.14
LINK NE2 HIS E 93 ZN ZN E 101 1555 1555 1.88
CISPEP 1 GLY A 337 GLU A 338 0 -27.62
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 6 ASN A 387 ASN A 390 HOH A 608 HOH A 839
SITE 2 AC7 6 HOH A 841 GLN B 35
SITE 1 AC8 3 ASN A 25 ALA A 26 HOH A 760
SITE 1 AC9 4 CYS C 73 CYS C 76 HIS C 88 CYS C 92
SITE 1 BC1 7 GLY A 104 THR C 33 GLN C 34 LEU C 37
SITE 2 BC1 7 HOH C 245 LYS E 71 HOH E 253
SITE 1 BC2 3 CYS E 78 CYS E 81 HIS E 93
CRYST1 83.528 104.775 107.018 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 0.011972 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009544 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009344 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
