HEADER TRANSFERASE 02-SEP-14 4R8Q
TITLE STRUCTURE AND SUBSTRATE RECRUITMENT OF THE HUMAN SPINDLE CHECKPOINT
TITLE 2 KINASE BUB1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MITOTIC CHECKPOINT SERINE/THREONINE-PROTEIN KINASE BUB1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: KINASE DOMAIN, UNP RESIDUES 724-1085;
COMPND 5 SYNONYM: HBUB1, BUB1A;
COMPND 6 EC: 2.7.11.1;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: BUB1, BUB1L;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PBAC2
KEYWDS SPINDLE ASSEMBLY CHECKPOINT, MITOSIS, KINASE, ACTIVATION, KEN BOX,
KEYWDS 2 CDC20, ATP-BINDING, CELL CYCLE, CELL DIVISION, DISEASE MUTATION,
KEYWDS 3 NUCLEOTIDE-BINDING, NUCLEUS, PHOSPHOPROTEIN, SERINE/THREONINE-
KEYWDS 4 PROTEIN KINASE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.R.TOMCHICK,H.YU
REVDAT 3 28-FEB-24 4R8Q 1 REMARK SEQADV LINK
REVDAT 2 22-NOV-17 4R8Q 1 REMARK
REVDAT 1 12-NOV-14 4R8Q 0
SPRSDE 12-NOV-14 4R8Q 3E7E
JRNL AUTH J.KANG,M.YANG,B.LI,W.QI,C.ZHANG,K.M.SHOKAT,D.R.TOMCHICK,
JRNL AUTH 2 M.MACHIUS,H.YU
JRNL TITL STRUCTURE AND SUBSTRATE RECRUITMENT OF THE HUMAN SPINDLE
JRNL TITL 2 CHECKPOINT KINASE BUB1.
JRNL REF MOL.CELL V. 32 394 2008
JRNL REFN ISSN 1097-2765
JRNL PMID 18995837
JRNL DOI 10.1016/J.MOLCEL.2008.09.017
REMARK 2
REMARK 2 RESOLUTION. 2.31 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.8.4_1496
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.31
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 32.51
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.1
REMARK 3 NUMBER OF REFLECTIONS : 16638
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.226
REMARK 3 R VALUE (WORKING SET) : 0.222
REMARK 3 FREE R VALUE : 0.264
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.740
REMARK 3 FREE R VALUE TEST SET COUNT : 1288
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 32.5091 - 4.8010 0.96 1813 143 0.1867 0.2113
REMARK 3 2 4.8010 - 3.8126 0.99 1760 148 0.1646 0.2118
REMARK 3 3 3.8126 - 3.3312 0.84 1484 123 0.2359 0.2778
REMARK 3 4 3.3312 - 3.0269 1.00 1735 149 0.2447 0.2781
REMARK 3 5 3.0269 - 2.8101 1.00 1750 149 0.2507 0.2783
REMARK 3 6 2.8101 - 2.6445 1.00 1714 146 0.2522 0.2931
REMARK 3 7 2.6445 - 2.5121 1.00 1748 139 0.2581 0.3283
REMARK 3 8 2.5121 - 2.4028 1.00 1720 140 0.2778 0.3387
REMARK 3 9 2.4028 - 2.3103 0.95 1626 151 0.3227 0.3762
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.290
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.620
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 30.06
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 48.18
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.005 2805
REMARK 3 ANGLE : 0.822 3774
REMARK 3 CHIRALITY : 0.030 405
REMARK 3 PLANARITY : 0.003 470
REMARK 3 DIHEDRAL : 13.394 1038
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 7
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 736 THROUGH 766 )
REMARK 3 ORIGIN FOR THE GROUP (A): -9.7893 27.8955 -11.6253
REMARK 3 T TENSOR
REMARK 3 T11: 0.1472 T22: 0.1961
REMARK 3 T33: 0.5283 T12: -0.0258
REMARK 3 T13: -0.0956 T23: -0.0687
REMARK 3 L TENSOR
REMARK 3 L11: 0.2127 L22: 0.1800
REMARK 3 L33: 0.9896 L12: -0.0120
REMARK 3 L13: 0.3476 L23: -0.1465
REMARK 3 S TENSOR
REMARK 3 S11: -0.0540 S12: 0.1864 S13: 0.6417
REMARK 3 S21: -0.1355 S22: -0.0594 S23: 0.1436
REMARK 3 S31: -0.0251 S32: 0.4207 S33: -0.1618
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 767 THROUGH 804 )
REMARK 3 ORIGIN FOR THE GROUP (A): -16.8543 16.7489 -31.8366
REMARK 3 T TENSOR
REMARK 3 T11: 0.3596 T22: 1.0014
REMARK 3 T33: -0.4053 T12: -0.0259
REMARK 3 T13: -0.0845 T23: 0.0433
REMARK 3 L TENSOR
REMARK 3 L11: 0.3333 L22: 0.0218
REMARK 3 L33: 0.0237 L12: 0.0168
REMARK 3 L13: -0.1260 L23: -0.0140
REMARK 3 S TENSOR
REMARK 3 S11: -0.1653 S12: 0.9438 S13: -0.1394
REMARK 3 S21: -0.5239 S22: 0.2180 S23: 0.0776
REMARK 3 S31: 0.0890 S32: 0.3107 S33: 0.1038
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 805 THROUGH 866 )
REMARK 3 ORIGIN FOR THE GROUP (A): -16.0104 16.0500 -17.3741
REMARK 3 T TENSOR
REMARK 3 T11: 0.2094 T22: 0.2117
REMARK 3 T33: 0.2234 T12: 0.0384
REMARK 3 T13: -0.0935 T23: 0.0140
REMARK 3 L TENSOR
REMARK 3 L11: 0.4762 L22: 0.3599
REMARK 3 L33: 0.4246 L12: 0.1310
REMARK 3 L13: 0.3265 L23: 0.2339
REMARK 3 S TENSOR
REMARK 3 S11: -0.0618 S12: 0.2296 S13: -0.2633
REMARK 3 S21: 0.1188 S22: 0.3115 S23: -0.5893
REMARK 3 S31: 0.1740 S32: 0.5333 S33: 0.1532
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 867 THROUGH 952 )
REMARK 3 ORIGIN FOR THE GROUP (A): -33.0046 14.7615 -12.9896
REMARK 3 T TENSOR
REMARK 3 T11: 0.2330 T22: 0.1519
REMARK 3 T33: 0.1656 T12: -0.0089
REMARK 3 T13: -0.0758 T23: 0.0229
REMARK 3 L TENSOR
REMARK 3 L11: 0.6285 L22: 0.2383
REMARK 3 L33: 0.2919 L12: -0.1255
REMARK 3 L13: -0.4539 L23: 0.1649
REMARK 3 S TENSOR
REMARK 3 S11: -0.0499 S12: -0.0400 S13: -0.0687
REMARK 3 S21: 0.0346 S22: 0.0172 S23: -0.0205
REMARK 3 S31: 0.0816 S32: 0.0573 S33: -0.1537
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 953 THROUGH 1036 )
REMARK 3 ORIGIN FOR THE GROUP (A): -36.8508 28.1196 -4.5012
REMARK 3 T TENSOR
REMARK 3 T11: 0.1359 T22: 0.1526
REMARK 3 T33: 0.3583 T12: 0.0070
REMARK 3 T13: -0.0708 T23: -0.0914
REMARK 3 L TENSOR
REMARK 3 L11: 0.3655 L22: 0.2610
REMARK 3 L33: 0.2917 L12: 0.1692
REMARK 3 L13: -0.2440 L23: 0.0465
REMARK 3 S TENSOR
REMARK 3 S11: -0.0236 S12: -0.1450 S13: 0.8979
REMARK 3 S21: 0.0431 S22: 0.1389 S23: 0.1256
REMARK 3 S31: 0.0258 S32: 0.1154 S33: 0.3376
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1037 THROUGH 1065 )
REMARK 3 ORIGIN FOR THE GROUP (A): -38.8503 14.7656 2.4269
REMARK 3 T TENSOR
REMARK 3 T11: 0.4151 T22: 0.3798
REMARK 3 T33: 0.2893 T12: 0.0797
REMARK 3 T13: -0.0943 T23: 0.0973
REMARK 3 L TENSOR
REMARK 3 L11: 0.9409 L22: 0.1016
REMARK 3 L33: 0.3869 L12: -0.2863
REMARK 3 L13: -0.5578 L23: 0.1444
REMARK 3 S TENSOR
REMARK 3 S11: -0.4565 S12: -1.0247 S13: -0.1476
REMARK 3 S21: 0.1174 S22: 0.4004 S23: 0.2673
REMARK 3 S31: 0.1841 S32: 0.2823 S33: 0.0721
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1066 THROUGH 1083 )
REMARK 3 ORIGIN FOR THE GROUP (A): -41.1481 4.5665 -21.8397
REMARK 3 T TENSOR
REMARK 3 T11: 0.5823 T22: 0.2172
REMARK 3 T33: 0.7130 T12: 0.0785
REMARK 3 T13: 0.0324 T23: -0.3530
REMARK 3 L TENSOR
REMARK 3 L11: 0.2087 L22: 0.0352
REMARK 3 L33: 0.0914 L12: -0.0078
REMARK 3 L13: 0.0281 L23: 0.0268
REMARK 3 S TENSOR
REMARK 3 S11: -0.0806 S12: 0.2584 S13: -0.2243
REMARK 3 S21: 0.2875 S22: 0.1759 S23: 0.2323
REMARK 3 S31: 0.2302 S32: 0.2914 S33: 0.0211
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4R8Q COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-SEP-14.
REMARK 100 THE DEPOSITION ID IS D_1000087040.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-APR-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.29
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97954
REMARK 200 MONOCHROMATOR : SAGITALLY FOCUSED SI(111)
REMARK 200 OPTICS : MONOCHROMATOR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 16738
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.310
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.7
REMARK 200 DATA REDUNDANCY : 5.400
REMARK 200 R MERGE (I) : 0.03700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.32
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.36
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.60
REMARK 200 R MERGE FOR SHELL (I) : 0.73100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SHELXS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.66
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.26
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: TO 15 MG/ML BUB1, ATP WAS ADDED TO A
REMARK 280 FINAL CONCENTRATION OF 10 MM. SITTING DROPS WERE MADE BY MIXING
REMARK 280 1.5 MICROLITERS PROTEIN WITH 1.5 MICROLITERS CRYSTALLIZATION
REMARK 280 SOLUTION (20% W/V PEG 3350, 0.1 M SODIUM FORMATE PH 6.29, 25 MM
REMARK 280 DTT) AND EQUILIBRATING AGAINST 200 MICROLITERS OF RESERVOIR
REMARK 280 SOLUTION. LARGE SINGLE CRYSTALS WERE OBTAINED BY REPEATED
REMARK 280 SEEDING. THE CRYSTALS WERE CRYO-PROTECTED IN RESERVOIR SOLUTION
REMARK 280 SUPPLEMENTED WITH 18% V/V GLYCEROL AND THEN FLASH-COOLED IN
REMARK 280 LIQUID PROPANE, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K,
REMARK 280 VAPOR DIFFUSION, SITTING DROP
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 23.59800
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 23.59800
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 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 54.38400
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 73.81600
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 54.38400
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 73.81600
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 23.59800
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 54.38400
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 73.81600
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 23.59800
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 54.38400
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 73.81600
REMARK 290 SMTRY3 8 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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 721
REMARK 465 SER A 722
REMARK 465 PRO A 723
REMARK 465 GLN A 724
REMARK 465 MET A 725
REMARK 465 SER A 726
REMARK 465 SER A 727
REMARK 465 LEU A 728
REMARK 465 GLY A 729
REMARK 465 THR A 730
REMARK 465 VAL A 731
REMARK 465 ASP A 732
REMARK 465 ALA A 733
REMARK 465 PRO A 734
REMARK 465 ASN A 735
REMARK 465 GLY A 807
REMARK 465 ASP A 808
REMARK 465 LEU A 809
REMARK 465 ASN A 810
REMARK 465 ASP A 811
REMARK 465 ALA A 812
REMARK 465 LYS A 813
REMARK 465 ASN A 814
REMARK 465 LYS A 815
REMARK 465 GLN A 932
REMARK 465 ASP A 933
REMARK 465 ASP A 934
REMARK 465 GLU A 935
REMARK 465 ASP A 936
REMARK 465 ASP A 937
REMARK 465 LEU A 938
REMARK 465 ARG A 1084
REMARK 465 LYS A 1085
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 GLN A 768 58.29 -95.31
REMARK 500 HIS A 790 -116.08 -88.89
REMARK 500 ASN A 883 32.11 -94.21
REMARK 500 LYS A 887 -42.38 64.42
REMARK 500 ASP A 917 45.95 -152.91
REMARK 500 ASP A 946 90.85 66.73
REMARK 500 SER A 969 18.96 -140.38
REMARK 500 ASN A 983 -84.38 -133.22
REMARK 500 ASN A1037 69.24 -119.21
REMARK 500 HIS A1043 59.85 -117.21
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 MG A1502 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 922 OD1
REMARK 620 2 ASP A 946 OD2 95.4
REMARK 620 3 ADP A1501 O1B 167.4 79.1
REMARK 620 4 ADP A1501 O2A 99.3 87.7 69.4
REMARK 620 5 HOH A1601 O 88.4 173.5 96.1 86.4
REMARK 620 6 HOH A1602 O 90.3 89.9 100.9 170.3 95.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1503 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 946 OD1
REMARK 620 2 ASP A 946 OD2 62.5
REMARK 620 3 ADP A1501 O3B 85.9 80.2
REMARK 620 4 HOH A1603 O 90.5 89.5 169.6
REMARK 620 5 HOH A1604 O 96.7 149.7 76.4 113.7
REMARK 620 6 HOH A1605 O 161.0 98.6 93.1 87.2 101.5
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 1501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1503
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4QPM RELATED DB: PDB
REMARK 900 PHOSPHORYLATED VERSION OF BUB1
DBREF 4R8Q A 724 1085 UNP O43683 BUB1_HUMAN 724 1085
SEQADV 4R8Q GLY A 721 UNP O43683 EXPRESSION TAG
SEQADV 4R8Q SER A 722 UNP O43683 EXPRESSION TAG
SEQADV 4R8Q PRO A 723 UNP O43683 EXPRESSION TAG
SEQRES 1 A 365 GLY SER PRO GLN MET SER SER LEU GLY THR VAL ASP ALA
SEQRES 2 A 365 PRO ASN PHE ILE VAL GLY ASN PRO TRP ASP ASP LYS LEU
SEQRES 3 A 365 ILE PHE LYS LEU LEU SER GLY LEU SER LYS PRO VAL SER
SEQRES 4 A 365 SER TYR PRO ASN THR PHE GLU TRP GLN CYS LYS LEU PRO
SEQRES 5 A 365 ALA ILE LYS PRO LYS THR GLU PHE GLN LEU GLY SER LYS
SEQRES 6 A 365 LEU VAL TYR VAL HIS HIS LEU LEU GLY GLU GLY ALA PHE
SEQRES 7 A 365 ALA GLN VAL TYR GLU ALA THR GLN GLY ASP LEU ASN ASP
SEQRES 8 A 365 ALA LYS ASN LYS GLN LYS PHE VAL LEU LYS VAL GLN LYS
SEQRES 9 A 365 PRO ALA ASN PRO TRP GLU PHE TYR ILE GLY THR GLN LEU
SEQRES 10 A 365 MET GLU ARG LEU LYS PRO SER MET GLN HIS MET PHE MET
SEQRES 11 A 365 LYS PHE TYR SER ALA HIS LEU PHE GLN ASN GLY SER VAL
SEQRES 12 A 365 LEU VAL GLY GLU LEU TYR SER TYR GLY THR LEU LEU ASN
SEQRES 13 A 365 ALA ILE ASN LEU TYR LYS ASN THR PRO GLU LYS VAL MET
SEQRES 14 A 365 PRO GLN GLY LEU VAL ILE SER PHE ALA MET ARG MET LEU
SEQRES 15 A 365 TYR MET ILE GLU GLN VAL HIS ASP CYS GLU ILE ILE HIS
SEQRES 16 A 365 GLY ASP ILE LYS PRO ASP ASN PHE ILE LEU GLY ASN GLY
SEQRES 17 A 365 PHE LEU GLU GLN ASP ASP GLU ASP ASP LEU SER ALA GLY
SEQRES 18 A 365 LEU ALA LEU ILE ASP LEU GLY GLN SER ILE ASP MET LYS
SEQRES 19 A 365 LEU PHE PRO LYS GLY THR ILE PHE THR ALA LYS CYS GLU
SEQRES 20 A 365 THR SER GLY PHE GLN CYS VAL GLU MET LEU SER ASN LYS
SEQRES 21 A 365 PRO TRP ASN TYR GLN ILE ASP TYR PHE GLY VAL ALA ALA
SEQRES 22 A 365 THR VAL TYR CYS MET LEU PHE GLY THR TYR MET LYS VAL
SEQRES 23 A 365 LYS ASN GLU GLY GLY GLU CYS LYS PRO GLU GLY LEU PHE
SEQRES 24 A 365 ARG ARG LEU PRO HIS LEU ASP MET TRP ASN GLU PHE PHE
SEQRES 25 A 365 HIS VAL MET LEU ASN ILE PRO ASP CYS HIS HIS LEU PRO
SEQRES 26 A 365 SER LEU ASP LEU LEU ARG GLN LYS LEU LYS LYS VAL PHE
SEQRES 27 A 365 GLN GLN HIS TYR THR ASN LYS ILE ARG ALA LEU ARG ASN
SEQRES 28 A 365 ARG LEU ILE VAL LEU LEU LEU GLU CYS LYS ARG SER ARG
SEQRES 29 A 365 LYS
HET ADP A1501 39
HET MG A1502 1
HET MG A1503 1
HETNAM ADP ADENOSINE-5'-DIPHOSPHATE
HETNAM MG MAGNESIUM ION
FORMUL 2 ADP C10 H15 N5 O10 P2
FORMUL 3 MG 2(MG 2+)
FORMUL 5 HOH *16(H2 O)
HELIX 1 1 ASP A 743 GLY A 753 1 11
HELIX 2 2 PRO A 757 TYR A 761 5 5
HELIX 3 3 ASN A 827 LEU A 841 1 15
HELIX 4 4 MET A 845 PHE A 849 5 5
HELIX 5 5 THR A 873 ASN A 883 1 11
HELIX 6 6 PRO A 890 CYS A 911 1 22
HELIX 7 7 LYS A 919 ASP A 921 5 3
HELIX 8 8 ASN A 927 LEU A 930 5 4
HELIX 9 9 LYS A 954 PHE A 956 5 3
HELIX 10 10 CYS A 973 SER A 978 1 6
HELIX 11 11 TYR A 984 GLY A 1001 1 18
HELIX 12 12 HIS A 1024 ASN A 1037 1 14
HELIX 13 13 SER A 1046 TYR A 1062 1 17
HELIX 14 14 LYS A 1065 SER A 1083 1 19
SHEET 1 A 2 ILE A 737 VAL A 738 0
SHEET 2 A 2 ILE A 961 PHE A 962 1 O ILE A 961 N VAL A 738
SHEET 1 B 7 THR A 764 GLU A 766 0
SHEET 2 B 7 PHE A 852 LEU A 857 1 O LEU A 857 N PHE A 765
SHEET 3 B 7 SER A 862 GLY A 866 -1 O VAL A 863 N HIS A 856
SHEET 4 B 7 PHE A 818 GLN A 823 -1 N LYS A 821 O LEU A 864
SHEET 5 B 7 ALA A 799 THR A 805 -1 N GLN A 800 O VAL A 822
SHEET 6 B 7 LYS A 785 GLU A 795 -1 N TYR A 788 O THR A 805
SHEET 7 B 7 THR A 778 LEU A 782 -1 N THR A 778 O VAL A 789
SHEET 1 C 2 ILE A 913 ILE A 914 0
SHEET 2 C 2 ILE A 951 ASP A 952 -1 O ILE A 951 N ILE A 914
SHEET 1 D 2 PHE A 923 LEU A 925 0
SHEET 2 D 2 LEU A 942 LEU A 944 -1 O ALA A 943 N ILE A 924
SHEET 1 E 2 VAL A1006 ASN A1008 0
SHEET 2 E 2 CYS A1013 PRO A1015 -1 O LYS A1014 N LYS A1007
LINK OD1 ASN A 922 MG MG A1502 1555 1555 2.11
LINK OD2 ASP A 946 MG MG A1502 1555 1555 2.12
LINK OD1 ASP A 946 MG MG A1503 1555 1555 2.06
LINK OD2 ASP A 946 MG MG A1503 1555 1555 2.16
LINK O1B ADP A1501 MG MG A1502 1555 1555 1.94
LINK O2A ADP A1501 MG MG A1502 1555 1555 2.07
LINK O3B ADP A1501 MG MG A1503 1555 1555 2.15
LINK MG MG A1502 O HOH A1601 1555 1555 2.08
LINK MG MG A1502 O HOH A1602 1555 1555 2.09
LINK MG MG A1503 O HOH A1603 1555 1555 2.07
LINK MG MG A1503 O HOH A1604 1555 1555 2.07
LINK MG MG A1503 O HOH A1605 1555 1555 2.08
CISPEP 1 LYS A 824 PRO A 825 0 -1.83
SITE 1 AC1 19 GLY A 794 GLY A 796 ALA A 797 PHE A 798
SITE 2 AC1 19 ALA A 799 VAL A 801 LYS A 821 MET A 850
SITE 3 AC1 19 GLU A 867 TYR A 869 THR A 873 ASP A 921
SITE 4 AC1 19 ASN A 922 ASP A 946 MG A1502 MG A1503
SITE 5 AC1 19 HOH A1601 HOH A1604 HOH A1605
SITE 1 AC2 5 ASN A 922 ASP A 946 ADP A1501 HOH A1601
SITE 2 AC2 5 HOH A1602
SITE 1 AC3 5 ASP A 946 ADP A1501 HOH A1603 HOH A1604
SITE 2 AC3 5 HOH A1605
CRYST1 108.768 147.632 47.196 90.00 90.00 90.00 C 2 2 21 8
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 0.009194 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006774 0.000000 0.00000
SCALE3 0.000000 0.000000 0.021188 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
