HEADER TRANSCRIPTION 03-SEP-15 5AN3
TITLE STRUCTURE OF AN SGT1-SKP1 COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SGT1;
COMPND 3 CHAIN: A, B, C;
COMPND 4 FRAGMENT: TPR DOMAIN, UNP RESIDUES 1-150;
COMPND 5 SYNONYM: SUPPRESSOR OF G2 ALLELE OF SKP1;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: SUPPRESSOR OF KINETOCHORE PROTEIN 1;
COMPND 9 CHAIN: D;
COMPND 10 FRAGMENT: BTBPOZ DOMAIN, UNP RESIDUES 1-35,65-158;
COMPND 11 SYNONYM: CENTROMERE DNA-BINDING PROTEIN COMPLEX CBF3 SUBUNIT D, E3
COMPND 12 UBIQUITIN LIGASE COMPLEX SCF SUBUNIT SKP1, SKP1;
COMPND 13 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 4932;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: T7 EXPRESS LYSY/IQ;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR: PRSET A;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 13 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 14 ORGANISM_TAXID: 4932;
SOURCE 15 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 16 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 17 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 18 EXPRESSION_SYSTEM_VARIANT: T7 EXPRESS LYSY/IQ;
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_VECTOR: PRSET A
KEYWDS TRANSCRIPTION
EXPDTA X-RAY DIFFRACTION
AUTHOR O.WILLHOFT,C.K.VAUGHAN
REVDAT 2 15-FEB-17 5AN3 1 JRNL
REVDAT 1 08-FEB-17 5AN3 0
JRNL AUTH O.WILLHOFT,R.KERR,D.PATEL,W.ZHANG,C.AL-JASSAR,T.DAVITER,
JRNL AUTH 2 S.H.MILLSON,K.THALASSINOS,C.K.VAUGHAN
JRNL TITL THE CRYSTAL STRUCTURE OF THE SGT1-SKP1 COMPLEX: THE LINK
JRNL TITL 2 BETWEEN HSP90 AND BOTH SCF E3 UBIQUITIN LIGASES AND
JRNL TITL 3 KINETOCHORES.
JRNL REF SCI REP V. 7 41626 2017
JRNL REFN ESSN 2045-2322
JRNL PMID 28139700
JRNL DOI 10.1038/SREP41626
REMARK 2
REMARK 2 RESOLUTION. 2.82 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.10.0
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.82
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.88
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 15739
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) : 0.204
REMARK 3 R VALUE (WORKING SET) : 0.202
REMARK 3 FREE R VALUE : 0.241
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 6.150
REMARK 3 FREE R VALUE TEST SET COUNT : 968
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 8
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.82
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 3.02
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.98
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2793
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2450
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2618
REMARK 3 BIN R VALUE (WORKING SET) : 0.2421
REMARK 3 BIN FREE R VALUE : 0.2858
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 6.27
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 175
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3707
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 22
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 86.92
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 70.85
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -4.43230
REMARK 3 B22 (A**2) : -4.43230
REMARK 3 B33 (A**2) : 8.86460
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.441
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 1.105
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.322
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 1.211
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.330
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.934
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.900
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 3790 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 5166 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 1658 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 68 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 576 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 3790 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 515 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 4425 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 0.98
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.52
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 2.65
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 27.8230 20.2942 26.5189
REMARK 3 T TENSOR
REMARK 3 T11: -0.1539 T22: -0.4565
REMARK 3 T33: -0.3453 T12: -0.1309
REMARK 3 T13: -0.0076 T23: 0.0441
REMARK 3 L TENSOR
REMARK 3 L11: 9.6123 L22: 5.4894
REMARK 3 L33: 7.7882 L12: 2.3624
REMARK 3 L13: -4.7353 L23: -2.7079
REMARK 3 S TENSOR
REMARK 3 S11: -0.1269 S12: 0.0708 S13: -0.0052
REMARK 3 S21: -0.6368 S22: -0.1398 S23: -0.9116
REMARK 3 S31: -0.1434 S32: 0.7701 S33: 0.2667
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: { B|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 20.7565 5.4369 48.8887
REMARK 3 T TENSOR
REMARK 3 T11: -0.2208 T22: -0.3177
REMARK 3 T33: -0.2216 T12: -0.0157
REMARK 3 T13: -0.0447 T23: 0.0415
REMARK 3 L TENSOR
REMARK 3 L11: 1.9862 L22: 6.5327
REMARK 3 L33: 6.2140 L12: 0.6654
REMARK 3 L13: -1.5475 L23: -3.6289
REMARK 3 S TENSOR
REMARK 3 S11: -0.0441 S12: -0.0951 S13: 0.2058
REMARK 3 S21: 0.4242 S22: -0.1197 S23: 0.0510
REMARK 3 S31: -0.4052 S32: 0.3212 S33: 0.1638
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: { C|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 4.8971 33.5432 29.2299
REMARK 3 T TENSOR
REMARK 3 T11: -0.2394 T22: -0.2063
REMARK 3 T33: -0.2349 T12: -0.0364
REMARK 3 T13: 0.0032 T23: 0.0210
REMARK 3 L TENSOR
REMARK 3 L11: 2.5823 L22: 4.6573
REMARK 3 L33: 2.6695 L12: 0.5365
REMARK 3 L13: 0.8827 L23: 0.5270
REMARK 3 S TENSOR
REMARK 3 S11: 0.1367 S12: -0.1063 S13: 0.2749
REMARK 3 S21: 0.2660 S22: -0.1070 S23: 0.0358
REMARK 3 S31: -0.0146 S32: -0.2883 S33: -0.0297
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: { D|* }
REMARK 3 ORIGIN FOR THE GROUP (A): -10.8393 48.2766 45.8423
REMARK 3 T TENSOR
REMARK 3 T11: -0.1711 T22: -0.0876
REMARK 3 T33: -0.1430 T12: -0.0389
REMARK 3 T13: 0.0185 T23: -0.2805
REMARK 3 L TENSOR
REMARK 3 L11: 7.6982 L22: 6.0854
REMARK 3 L33: 6.0337 L12: -5.8916
REMARK 3 L13: -5.0148 L23: 3.9068
REMARK 3 S TENSOR
REMARK 3 S11: -0.3412 S12: 0.2631 S13: -0.1185
REMARK 3 S21: 0.5598 S22: -0.2410 S23: 0.3021
REMARK 3 S31: 0.1492 S32: -0.5882 S33: 0.5822
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: IDEAL-DIST CONTACT TERM CONTACT SETUP.
REMARK 3 ALL ATOMS HAVE CCP4 ATOM TYPE FROM LIBRARY
REMARK 4
REMARK 4 5AN3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-SEP-15.
REMARK 100 THE PDBE ID CODE IS EBI-64889.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I04
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979494
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD (ADSC Q105)
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XIA2
REMARK 200 DATA SCALING SOFTWARE : XIA2
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 15826
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.820
REMARK 200 RESOLUTION RANGE LOW (A) : 81.890
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 21.50
REMARK 200 R MERGE (I) : 0.09000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 29.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.82
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.89
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 21.90
REMARK 200 R MERGE FOR SHELL (I) : 0.83000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: AUTORICKSHAW
REMARK 200 STARTING MODEL: NONE
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.84
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.72
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.325 M MGCL2, 22.5% PEG-6000, 0.1 M
REMARK 280 TRIS-HCL PH 8
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 81.99333
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 40.99667
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 40.99667
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 81.99333
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 MET A 1
REMARK 465 PRO A 2
REMARK 465 ARG A 81
REMARK 465 GLY A 82
REMARK 465 LEU A 135
REMARK 465 ASN A 136
REMARK 465 LYS A 137
REMARK 465 LYS A 138
REMARK 465 ASN A 139
REMARK 465 LYS A 140
REMARK 465 LYS A 141
REMARK 465 GLN A 142
REMARK 465 LYS A 143
REMARK 465 ASP A 144
REMARK 465 SER A 145
REMARK 465 THR A 146
REMARK 465 ASN A 147
REMARK 465 LYS A 148
REMARK 465 HIS A 149
REMARK 465 THR A 150
REMARK 465 MET B 1
REMARK 465 LYS B 138
REMARK 465 ASN B 139
REMARK 465 LYS B 140
REMARK 465 LYS B 141
REMARK 465 GLN B 142
REMARK 465 LYS B 143
REMARK 465 ASP B 144
REMARK 465 SER B 145
REMARK 465 THR B 146
REMARK 465 ASN B 147
REMARK 465 LYS B 148
REMARK 465 HIS B 149
REMARK 465 THR B 150
REMARK 465 MET C 1
REMARK 465 LYS C 137
REMARK 465 LYS C 138
REMARK 465 ASN C 139
REMARK 465 LYS C 140
REMARK 465 LYS C 141
REMARK 465 GLN C 142
REMARK 465 LYS C 143
REMARK 465 ASP C 144
REMARK 465 SER C 145
REMARK 465 THR C 146
REMARK 465 ASN C 147
REMARK 465 LYS C 148
REMARK 465 HIS C 149
REMARK 465 THR C 150
REMARK 465 MET D 1
REMARK 465 VAL D 2
REMARK 465 SER D 37
REMARK 465 GLY D 65
REMARK 465 ASP D 66
REMARK 465 ASP D 67
REMARK 465 ASP D 68
REMARK 465 ASP D 69
REMARK 465 GLU D 70
REMARK 465 ASP D 71
REMARK 465 ASP D 72
REMARK 465 ASP D 73
REMARK 465 ASN D 101
REMARK 465 PHE D 102
REMARK 465 PRO D 103
REMARK 465 ASP D 104
REMARK 465 GLU D 105
REMARK 465 ASP D 106
REMARK 465 ASP D 107
REMARK 465 ASP D 108
REMARK 465 ASP D 109
REMARK 465 SER D 110
REMARK 465 ARG D 111
REMARK 465 LYS D 112
REMARK 465 SER D 113
REMARK 465 ALA D 114
REMARK 465 PRO D 115
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 GLU A 4 CG CD OE1 OE2
REMARK 470 LYS A 5 CG CD CE NZ
REMARK 470 ASP A 6 CG OD1 OD2
REMARK 470 LYS A 8 CG CD CE NZ
REMARK 470 LYS A 12 CG CD CE NZ
REMARK 470 LYS A 18 CE NZ
REMARK 470 GLU A 19 CG CD OE1 OE2
REMARK 470 LYS A 22 CG CD CE NZ
REMARK 470 LEU A 26 CD1 CD2
REMARK 470 ILE A 30 CD1
REMARK 470 THR A 36 OG1 CG2
REMARK 470 LEU A 38 CG CD1 CD2
REMARK 470 LEU A 41 CD1 CD2
REMARK 470 ILE A 42 CD1
REMARK 470 LYS A 50 NZ
REMARK 470 LYS A 68 CD CE NZ
REMARK 470 LYS A 73 CD CE NZ
REMARK 470 LEU A 75 CD1 CD2
REMARK 470 MET A 76 CG SD CE
REMARK 470 GLU A 79 CG CD OE1 OE2
REMARK 470 ASP A 83 CG OD1 OD2
REMARK 470 ARG A 84 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 86 CG CD CE NZ
REMARK 470 ILE A 87 CG1 CG2 CD1
REMARK 470 PHE A 99 CD1 CD2 CE1 CE2 CZ
REMARK 470 ILE A 101 CG1 CG2 CD1
REMARK 470 LYS A 102 CG CD CE NZ
REMARK 470 TYR A 104 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU A 105 CG CD OE1 OE2
REMARK 470 LEU A 106 CD1 CD2
REMARK 470 GLN A 108 CG CD OE1 NE2
REMARK 470 LYS A 112 CG CD CE NZ
REMARK 470 LYS A 113 CD CE NZ
REMARK 470 LYS A 115 CG CD CE NZ
REMARK 470 ASN A 116 CG OD1 ND2
REMARK 470 LEU A 117 CG CD1 CD2
REMARK 470 VAL A 120 CG1 CG2
REMARK 470 ASP A 122 CG OD1 OD2
REMARK 470 LEU A 124 CG CD1 CD2
REMARK 470 LEU A 126 CG CD1 CD2
REMARK 470 GLU A 128 CG CD OE1 OE2
REMARK 470 ASP A 129 CG OD1 OD2
REMARK 470 GLU A 132 CG CD OE1 OE2
REMARK 470 LYS A 134 CG CD CE NZ
REMARK 470 GLU B 4 CG CD OE1 OE2
REMARK 470 LYS B 5 CG CD CE NZ
REMARK 470 LYS B 8 CG CD CE NZ
REMARK 470 LYS B 12 CG CD CE NZ
REMARK 470 ASP B 16 CG OD1 OD2
REMARK 470 LYS B 18 CE NZ
REMARK 470 GLU B 19 CD OE1 OE2
REMARK 470 LYS B 22 CG CD CE NZ
REMARK 470 ASP B 28 OD1 OD2
REMARK 470 GLU B 29 CG CD OE1 OE2
REMARK 470 LYS B 32 CG CD CE NZ
REMARK 470 LYS B 50 NZ
REMARK 470 GLU B 65 CG CD OE1 OE2
REMARK 470 LYS B 68 CD CE NZ
REMARK 470 GLU B 69 CG CD OE1 OE2
REMARK 470 LYS B 73 CD CE NZ
REMARK 470 MET B 76 CE
REMARK 470 LYS B 86 CD CE NZ
REMARK 470 LYS B 102 CE NZ
REMARK 470 GLU B 105 CG CD OE1 OE2
REMARK 470 GLN B 108 CG CD OE1 NE2
REMARK 470 SER B 109 OG
REMARK 470 PHE B 111 CD2 CE1 CE2 CZ
REMARK 470 LYS B 112 CG CD CE NZ
REMARK 470 LYS B 113 CD CE NZ
REMARK 470 LYS B 115 CG CD CE NZ
REMARK 470 VAL B 120 CG1 CG2
REMARK 470 ASP B 122 CG OD1 OD2
REMARK 470 LEU B 126 CG CD1 CD2
REMARK 470 GLU B 128 CD OE1 OE2
REMARK 470 ASP B 129 CG OD1 OD2
REMARK 470 ARG B 130 NE CZ NH1 NH2
REMARK 470 GLU B 132 CG CD OE1 OE2
REMARK 470 THR B 133 OG1 CG2
REMARK 470 LYS B 134 CE NZ
REMARK 470 LEU B 135 CG CD1 CD2
REMARK 470 ASN B 136 OD1 ND2
REMARK 470 LYS B 137 CG CD CE NZ
REMARK 470 GLU C 4 CG CD OE1 OE2
REMARK 470 LYS C 5 CG CD CE NZ
REMARK 470 LYS C 8 CE NZ
REMARK 470 LYS C 12 CG CD CE NZ
REMARK 470 LYS C 18 CE NZ
REMARK 470 LYS C 22 CE NZ
REMARK 470 LYS C 32 NZ
REMARK 470 LYS C 73 CE NZ
REMARK 470 LYS C 102 CG CD CE NZ
REMARK 470 GLU C 105 CG CD OE1 OE2
REMARK 470 GLN C 108 CG CD OE1 NE2
REMARK 470 LYS C 112 CE NZ
REMARK 470 LYS C 115 CD CE NZ
REMARK 470 GLU C 128 OE1 OE2
REMARK 470 GLU C 132 CG CD OE1 OE2
REMARK 470 LYS C 134 O CD CE NZ
REMARK 470 LEU C 135 CG CD1 CD2
REMARK 470 ASN C 136 CG OD1 ND2
REMARK 470 THR D 3 N CA O CB OG1 CG2
REMARK 470 SER D 4 OG
REMARK 470 ASN D 5 CG OD1 ND2
REMARK 470 GLU D 12 CD OE1 OE2
REMARK 470 LYS D 20 CG CD CE NZ
REMARK 470 LYS D 21 CD CE NZ
REMARK 470 LEU D 27 CD1 CD2
REMARK 470 GLU D 74 CG CD OE1 OE2
REMARK 470 ILE D 75 CD1
REMARK 470 ASN D 81 CG OD1 ND2
REMARK 470 ARG D 83 CD NE CZ NH1 NH2
REMARK 470 LYS D 89 CE NZ
REMARK 470 GLU D 95 OE1 OE2
REMARK 470 ARG D 98 CG CD NE CZ NH1 NH2
REMARK 470 ASP D 99 CG OD1 OD2
REMARK 470 SER D 100 C O
REMARK 470 LYS D 125 CG CD CE NZ
REMARK 470 GLN D 128 CG CD OE1 NE2
REMARK 470 GLU D 129 OE1 OE2
REMARK 470 LEU D 131 CD1 CD2
REMARK 470 TYR D 132 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU D 133 OE1 OE2
REMARK 470 ILE D 135 CG1 CG2 CD1
REMARK 470 LEU D 136 CG CD1 CD2
REMARK 470 LYS D 144 CG CD CE NZ
REMARK 470 ASP D 148 CG OD1 OD2
REMARK 470 LYS D 152 CG CD CE NZ
REMARK 470 VAL D 153 CG1 CG2
REMARK 470 VAL D 154 CG1 CG2
REMARK 470 GLU D 156 CG CD OE1 OE2
REMARK 470 MET D 157 CG SD CE
REMARK 470 ILE D 158 CG1 CG2 CD1
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 LYS A 102 0.06 53.97
REMARK 500 ASN D 81 4.10 -66.87
REMARK 500 HIS D 97 37.44 -97.52
REMARK 500 ASP D 99 76.71 -108.00
REMARK 500
REMARK 500 REMARK: NULL
DBREF 5AN3 A 1 150 UNP Q08446 SGT1_YEAST 1 150
DBREF 5AN3 B 1 150 UNP Q08446 SGT1_YEAST 1 150
DBREF 5AN3 C 1 150 UNP Q08446 SGT1_YEAST 1 150
DBREF 5AN3 D 1 35 UNP P52286 SKP1_YEAST 1 35
DBREF 5AN3 D 65 158 UNP P52286 SKP1_YEAST 65 158
SEQADV 5AN3 ALA D 36 UNP P52286 LINKER
SEQADV 5AN3 SER D 37 UNP P52286 LINKER
SEQRES 1 A 150 MET PRO VAL GLU LYS ASP LEU LYS THR ALA TYR LYS ALA
SEQRES 2 A 150 LEU TYR ASP GLU LYS GLU PRO LEU LYS ALA LEU HIS LEU
SEQRES 3 A 150 TYR ASP GLU ILE LEU LYS GLY SER PRO THR ASN LEU THR
SEQRES 4 A 150 ALA LEU ILE PHE LYS ALA ALA CYS LEU GLU LYS LEU TYR
SEQRES 5 A 150 PHE GLY PHE SER ASP TRP HIS SER ASP ALA THR MET GLU
SEQRES 6 A 150 ASN ALA LYS GLU LEU LEU ASP LYS ALA LEU MET THR ALA
SEQRES 7 A 150 GLU GLY ARG GLY ASP ARG SER LYS ILE GLY LEU VAL ASN
SEQRES 8 A 150 PHE ARG TYR PHE VAL HIS PHE PHE ASN ILE LYS ASP TYR
SEQRES 9 A 150 GLU LEU ALA GLN SER TYR PHE LYS LYS ALA LYS ASN LEU
SEQRES 10 A 150 GLY TYR VAL ASP ASP THR LEU PRO LEU TRP GLU ASP ARG
SEQRES 11 A 150 LEU GLU THR LYS LEU ASN LYS LYS ASN LYS LYS GLN LYS
SEQRES 12 A 150 ASP SER THR ASN LYS HIS THR
SEQRES 1 B 150 MET PRO VAL GLU LYS ASP LEU LYS THR ALA TYR LYS ALA
SEQRES 2 B 150 LEU TYR ASP GLU LYS GLU PRO LEU LYS ALA LEU HIS LEU
SEQRES 3 B 150 TYR ASP GLU ILE LEU LYS GLY SER PRO THR ASN LEU THR
SEQRES 4 B 150 ALA LEU ILE PHE LYS ALA ALA CYS LEU GLU LYS LEU TYR
SEQRES 5 B 150 PHE GLY PHE SER ASP TRP HIS SER ASP ALA THR MET GLU
SEQRES 6 B 150 ASN ALA LYS GLU LEU LEU ASP LYS ALA LEU MET THR ALA
SEQRES 7 B 150 GLU GLY ARG GLY ASP ARG SER LYS ILE GLY LEU VAL ASN
SEQRES 8 B 150 PHE ARG TYR PHE VAL HIS PHE PHE ASN ILE LYS ASP TYR
SEQRES 9 B 150 GLU LEU ALA GLN SER TYR PHE LYS LYS ALA LYS ASN LEU
SEQRES 10 B 150 GLY TYR VAL ASP ASP THR LEU PRO LEU TRP GLU ASP ARG
SEQRES 11 B 150 LEU GLU THR LYS LEU ASN LYS LYS ASN LYS LYS GLN LYS
SEQRES 12 B 150 ASP SER THR ASN LYS HIS THR
SEQRES 1 C 150 MET PRO VAL GLU LYS ASP LEU LYS THR ALA TYR LYS ALA
SEQRES 2 C 150 LEU TYR ASP GLU LYS GLU PRO LEU LYS ALA LEU HIS LEU
SEQRES 3 C 150 TYR ASP GLU ILE LEU LYS GLY SER PRO THR ASN LEU THR
SEQRES 4 C 150 ALA LEU ILE PHE LYS ALA ALA CYS LEU GLU LYS LEU TYR
SEQRES 5 C 150 PHE GLY PHE SER ASP TRP HIS SER ASP ALA THR MET GLU
SEQRES 6 C 150 ASN ALA LYS GLU LEU LEU ASP LYS ALA LEU MET THR ALA
SEQRES 7 C 150 GLU GLY ARG GLY ASP ARG SER LYS ILE GLY LEU VAL ASN
SEQRES 8 C 150 PHE ARG TYR PHE VAL HIS PHE PHE ASN ILE LYS ASP TYR
SEQRES 9 C 150 GLU LEU ALA GLN SER TYR PHE LYS LYS ALA LYS ASN LEU
SEQRES 10 C 150 GLY TYR VAL ASP ASP THR LEU PRO LEU TRP GLU ASP ARG
SEQRES 11 C 150 LEU GLU THR LYS LEU ASN LYS LYS ASN LYS LYS GLN LYS
SEQRES 12 C 150 ASP SER THR ASN LYS HIS THR
SEQRES 1 D 131 MET VAL THR SER ASN VAL VAL LEU VAL SER GLY GLU GLY
SEQRES 2 D 131 GLU ARG PHE THR VAL ASP LYS LYS ILE ALA GLU ARG SER
SEQRES 3 D 131 LEU LEU LEU LYS ASN TYR LEU ASN ASP ALA SER GLY ASP
SEQRES 4 D 131 ASP ASP ASP GLU ASP ASP ASP GLU ILE VAL MET PRO VAL
SEQRES 5 D 131 PRO ASN VAL ARG SER SER VAL LEU GLN LYS VAL ILE GLU
SEQRES 6 D 131 TRP ALA GLU HIS HIS ARG ASP SER ASN PHE PRO ASP GLU
SEQRES 7 D 131 ASP ASP ASP ASP SER ARG LYS SER ALA PRO VAL ASP SER
SEQRES 8 D 131 TRP ASP ARG GLU PHE LEU LYS VAL ASP GLN GLU MET LEU
SEQRES 9 D 131 TYR GLU ILE ILE LEU ALA ALA ASN TYR LEU ASN ILE LYS
SEQRES 10 D 131 PRO LEU LEU ASP ALA GLY CYS LYS VAL VAL ALA GLU MET
SEQRES 11 D 131 ILE
FORMUL 5 HOH *22(H2 O)
HELIX 1 1 VAL A 3 ASP A 16 1 14
HELIX 2 2 GLU A 19 SER A 34 1 16
HELIX 3 3 ASN A 37 PHE A 53 1 17
HELIX 4 4 PHE A 55 HIS A 59 5 5
HELIX 5 5 SER A 60 GLY A 80 1 21
HELIX 6 6 ASP A 83 ILE A 101 1 19
HELIX 7 7 ASP A 103 LEU A 117 1 15
HELIX 8 8 THR A 123 LYS A 134 1 12
HELIX 9 9 PRO B 2 ASP B 16 1 15
HELIX 10 10 GLU B 19 SER B 34 1 16
HELIX 11 11 ASN B 37 PHE B 53 1 17
HELIX 12 12 PHE B 55 HIS B 59 5 5
HELIX 13 13 SER B 60 GLY B 82 1 23
HELIX 14 14 ASP B 83 ILE B 101 1 19
HELIX 15 15 ASP B 103 LEU B 117 1 15
HELIX 16 16 THR B 123 ASN B 136 1 14
HELIX 17 17 PRO C 2 ASP C 16 1 15
HELIX 18 18 GLU C 19 SER C 34 1 16
HELIX 19 19 ASN C 37 PHE C 53 1 17
HELIX 20 20 PHE C 55 HIS C 59 5 5
HELIX 21 21 SER C 60 GLY C 82 1 23
HELIX 22 22 ASP C 83 ILE C 101 1 19
HELIX 23 23 ASP C 103 LEU C 117 1 15
HELIX 24 24 THR C 123 THR C 133 1 11
HELIX 25 25 LYS D 20 GLU D 24 1 5
HELIX 26 26 SER D 26 ASN D 34 1 9
HELIX 27 27 ARG D 83 HIS D 97 1 15
HELIX 28 28 ASP D 117 LEU D 124 1 8
HELIX 29 29 ASP D 127 LEU D 141 1 15
HELIX 30 30 ILE D 143 VAL D 153 1 11
HELIX 31 31 VAL D 153 ILE D 158 1 6
SHEET 1 DA 3 ARG D 15 ASP D 19 0
SHEET 2 DA 3 ASN D 5 VAL D 9 -1 O VAL D 6 N VAL D 18
SHEET 3 DA 3 VAL D 76 PRO D 78 1 O MET D 77 N VAL D 9
CRYST1 94.560 94.560 122.990 90.00 90.00 120.00 P 32 2 1 18
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 0.010575 0.006106 0.000000 0.00000
SCALE2 0.000000 0.012211 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008131 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
