HEADER COMPLEX (KINASE/ANTI-ONCOGENE) 22-JUN-98 1BI7
TITLE MECHANISM OF G1 CYCLIN DEPENDENT KINASE INHIBITION FROM THE STRUCTURE
TITLE 2 OF THE CDK6-P16INK4A TUMOR SUPPRESSOR COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYCLIN-DEPENDENT KINASE 6;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CDK6;
COMPND 5 EC: 2.7.1.-;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: MULTIPLE TUMOR SUPPRESSOR;
COMPND 9 CHAIN: B;
COMPND 10 SYNONYM: P16INK4A, MTS1;
COMPND 11 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 CELL_LINE: SPODOPTERA FRUGIPERDA;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: HI5;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR: BACULOVIRUS;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 CELL_LINE: SPODOPTERA FRUGIPERDA;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: HI5;
SOURCE 19 EXPRESSION_SYSTEM_VECTOR: GLUTATHIONE-S-TRANSFERASE FUSION
KEYWDS CYCLIN DEPENDENT KINASE, CYCLIN DEPENDENT KINASE INHIBITORY PROTEIN,
KEYWDS 2 CDK, INK4, CELL CYCLE, MULTIPLE TUMOR SUPPRESSOR, MTS1, COMPLEX
KEYWDS 3 (KINASE-ANTI-ONCOGENE), COMPLEX (KINASE-ANTI-ONCOGENE) COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR A.A.RUSSO,L.TONG,J.O.LEE,P.D.JEFFREY,N.P.PAVLETICH
REVDAT 4 07-FEB-24 1BI7 1 SEQADV
REVDAT 3 24-FEB-09 1BI7 1 VERSN
REVDAT 2 16-FEB-99 1BI7 1 SOURCE COMPND REMARK DBREF
REVDAT 2 2 1 SEQADV KEYWDS HEADER
REVDAT 1 13-JAN-99 1BI7 0
JRNL AUTH A.A.RUSSO,L.TONG,J.O.LEE,P.D.JEFFREY,N.P.PAVLETICH
JRNL TITL STRUCTURAL BASIS FOR INHIBITION OF THE CYCLIN-DEPENDENT
JRNL TITL 2 KINASE CDK6 BY THE TUMOUR SUPPRESSOR P16INK4A.
JRNL REF NATURE V. 395 237 1998
JRNL REFN ISSN 0028-0836
JRNL PMID 9751050
JRNL DOI 10.1038/26155
REMARK 2
REMARK 2 RESOLUTION. 3.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.8
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 94.7
REMARK 3 NUMBER OF REFLECTIONS : 11109
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 SET) : 0.227
REMARK 3 FREE R VALUE : 0.330
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 562
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 : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
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 : 3087
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.012
REMARK 3 BOND ANGLES (DEGREES) : 1.940
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : GROUP
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1BI7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000171787.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : JAN-97
REMARK 200 TEMPERATURE (KELVIN) : 110
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 2
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CHESS
REMARK 200 BEAMLINE : A1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.908
REMARK 200 MONOCHROMATOR : MIRRORS
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 12443
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.400
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.7
REMARK 200 DATA REDUNDANCY : 5.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06800
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.52
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.2
REMARK 200 DATA REDUNDANCY IN SHELL : 4.10
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.33000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 6.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR, MAD
REMARK 200 SOFTWARE USED: X-PLOR 3.8
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 69.08
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.98
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 2 2
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 -Y,X,Z+1/4
REMARK 290 4555 Y,-X,Z+3/4
REMARK 290 5555 -X,Y,-Z
REMARK 290 6555 X,-Y,-Z+1/2
REMARK 290 7555 Y,X,-Z+3/4
REMARK 290 8555 -Y,-X,-Z+1/4
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 56.25000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 28.12500
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 84.37500
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 0.00000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 56.25000
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 84.37500
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 28.12500
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 APPLY THE FOLLOWING TO CHAINS: A, B
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 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 123.10000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 168.75000
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 GLU A 2
REMARK 465 LYS A 3
REMARK 465 ASP A 4
REMARK 465 GLY A 5
REMARK 465 LEU A 6
REMARK 465 CYS A 7
REMARK 465 ARG A 8
REMARK 465 ALA A 9
REMARK 465 THR A 49
REMARK 465 GLY A 50
REMARK 465 GLU A 51
REMARK 465 GLU A 52
REMARK 465 GLY A 53
REMARK 465 MET A 54
REMARK 465 PRO A 55
REMARK 465 LEU A 56
REMARK 465 SER A 57
REMARK 465 THR A 58
REMARK 465 ILE A 59
REMARK 465 ARG A 60
REMARK 465 GLU A 61
REMARK 465 VAL A 62
REMARK 465 ALA A 63
REMARK 465 VAL A 64
REMARK 465 LEU A 65
REMARK 465 ARG A 66
REMARK 465 HIS A 67
REMARK 465 LEU A 68
REMARK 465 GLU A 69
REMARK 465 THR A 70
REMARK 465 PHE A 71
REMARK 465 ASP A 302
REMARK 465 LEU A 303
REMARK 465 GLU A 304
REMARK 465 ARG A 305
REMARK 465 CYS A 306
REMARK 465 LYS A 307
REMARK 465 GLU A 308
REMARK 465 ASN A 309
REMARK 465 LEU A 310
REMARK 465 ASP A 311
REMARK 465 SER A 312
REMARK 465 HIS A 313
REMARK 465 LEU A 314
REMARK 465 PRO A 315
REMARK 465 PRO A 316
REMARK 465 SER A 317
REMARK 465 GLN A 318
REMARK 465 ASN A 319
REMARK 465 THR A 320
REMARK 465 SER A 321
REMARK 465 GLU A 322
REMARK 465 LEU A 323
REMARK 465 ASN A 324
REMARK 465 THR A 325
REMARK 465 ALA A 326
REMARK 465 MET B 1
REMARK 465 GLU B 2
REMARK 465 PRO B 3
REMARK 465 ALA B 4
REMARK 465 ALA B 5
REMARK 465 GLY B 6
REMARK 465 SER B 7
REMARK 465 SER B 8
REMARK 465 MET B 9
REMARK 465 GLY B 135
REMARK 465 GLY B 136
REMARK 465 THR B 137
REMARK 465 ARG B 138
REMARK 465 GLY B 139
REMARK 465 SER B 140
REMARK 465 ASN B 141
REMARK 465 HIS B 142
REMARK 465 ALA B 143
REMARK 465 ARG B 144
REMARK 465 ILE B 145
REMARK 465 ASP B 146
REMARK 465 ALA B 147
REMARK 465 ALA B 148
REMARK 465 GLU B 149
REMARK 465 GLY B 150
REMARK 465 PRO B 151
REMARK 465 SER B 152
REMARK 465 ASP B 153
REMARK 465 ILE B 154
REMARK 465 PRO B 155
REMARK 465 ASP B 156
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 MET A 174 CG SD CE
REMARK 470 LEU A 176 CG CD1 CD2
REMARK 470 TYR A 196 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU B 10 CG CD OE1 OE2
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 GLU A 114 N - CA - C ANGL. DEV. = 17.2 DEGREES
REMARK 500 LEU A 202 CA - CB - CG ANGL. DEV. = -17.7 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 CYS A 15 106.99 -57.09
REMARK 500 ALA A 17 149.13 -178.75
REMARK 500 ASN A 35 -166.02 -101.24
REMARK 500 VAL A 47 -120.73 -124.37
REMARK 500 HIS A 73 122.32 61.37
REMARK 500 SER A 86 111.49 -169.63
REMARK 500 ARG A 90 94.74 58.96
REMARK 500 GLU A 91 134.33 143.21
REMARK 500 THR A 95 89.36 -164.20
REMARK 500 GLN A 103 118.10 175.31
REMARK 500 GLU A 114 -37.60 -20.64
REMARK 500 ARG A 140 -8.02 58.25
REMARK 500 ARG A 144 -46.96 63.16
REMARK 500 ASP A 145 61.42 -108.23
REMARK 500 GLN A 149 -0.89 -55.33
REMARK 500 ALA A 167 86.11 70.49
REMARK 500 GLN A 173 72.43 -9.83
REMARK 500 MET A 174 -82.89 47.12
REMARK 500 THR A 177 76.98 -49.69
REMARK 500 VAL A 180 155.05 179.73
REMARK 500 VAL A 181 41.81 -105.22
REMARK 500 THR A 182 88.32 41.63
REMARK 500 GLN A 193 92.93 69.09
REMARK 500 SER A 194 8.00 -159.45
REMARK 500 SER A 195 179.60 171.27
REMARK 500 TYR A 196 60.10 -164.55
REMARK 500 SER A 222 -62.35 -103.89
REMARK 500 VAL A 234 -72.33 -81.25
REMARK 500 GLU A 240 79.31 -62.26
REMARK 500 GLU A 241 -55.02 -164.70
REMARK 500 PRO A 244 170.87 -59.49
REMARK 500 VAL A 247 141.07 -30.29
REMARK 500 ALA A 248 -96.66 -21.90
REMARK 500 PHE A 254 49.89 -100.45
REMARK 500 HIS A 255 121.52 -12.78
REMARK 500 SER A 256 -32.08 -16.33
REMARK 500 LYS A 257 122.38 -20.12
REMARK 500 SER A 258 169.56 91.44
REMARK 500 ALA A 259 45.16 173.87
REMARK 500 ASP A 268 23.06 49.48
REMARK 500 ASP A 275 -78.40 -66.33
REMARK 500 LEU A 281 49.88 -89.50
REMARK 500 TYR A 299 -52.43 -20.07
REMARK 500 PRO B 11 -83.98 -90.20
REMARK 500 SER B 12 -51.06 77.58
REMARK 500 ASP B 14 -41.28 -154.62
REMARK 500 ARG B 29 -71.29 -54.18
REMARK 500 GLU B 33 28.51 -71.09
REMARK 500 PRO B 38 40.64 -78.19
REMARK 500 ASN B 39 -2.66 -165.03
REMARK 500
REMARK 500 THIS ENTRY HAS 67 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 TYR A 170 0.06 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1BI7 A 1 326 UNP Q00534 CDK6_HUMAN 1 326
DBREF 1BI7 B 1 156 UNP P42771 CDN2A_HUMAN 1 156
SEQADV 1BI7 ASN B 37 UNP P42771 LEU 37 CONFLICT
SEQRES 1 A 326 MET GLU LYS ASP GLY LEU CYS ARG ALA ASP GLN GLN TYR
SEQRES 2 A 326 GLU CYS VAL ALA GLU ILE GLY GLU GLY ALA TYR GLY LYS
SEQRES 3 A 326 VAL PHE LYS ALA ARG ASP LEU LYS ASN GLY GLY ARG PHE
SEQRES 4 A 326 VAL ALA LEU LYS ARG VAL ARG VAL GLN THR GLY GLU GLU
SEQRES 5 A 326 GLY MET PRO LEU SER THR ILE ARG GLU VAL ALA VAL LEU
SEQRES 6 A 326 ARG HIS LEU GLU THR PHE GLU HIS PRO ASN VAL VAL ARG
SEQRES 7 A 326 LEU PHE ASP VAL CYS THR VAL SER ARG THR ASP ARG GLU
SEQRES 8 A 326 THR LYS LEU THR LEU VAL PHE GLU HIS VAL ASP GLN ASP
SEQRES 9 A 326 LEU THR THR TYR LEU ASP LYS VAL PRO GLU PRO GLY VAL
SEQRES 10 A 326 PRO THR GLU THR ILE LYS ASP MET MET PHE GLN LEU LEU
SEQRES 11 A 326 ARG GLY LEU ASP PHE LEU HIS SER HIS ARG VAL VAL HIS
SEQRES 12 A 326 ARG ASP LEU LYS PRO GLN ASN ILE LEU VAL THR SER SER
SEQRES 13 A 326 GLY GLN ILE LYS LEU ALA ASP PHE GLY LEU ALA ARG ILE
SEQRES 14 A 326 TYR SER PHE GLN MET ALA LEU THR SER VAL VAL VAL THR
SEQRES 15 A 326 LEU TRP TYR ARG ALA PRO GLU VAL LEU LEU GLN SER SER
SEQRES 16 A 326 TYR ALA THR PRO VAL ASP LEU TRP SER VAL GLY CYS ILE
SEQRES 17 A 326 PHE ALA GLU MET PHE ARG ARG LYS PRO LEU PHE ARG GLY
SEQRES 18 A 326 SER SER ASP VAL ASP GLN LEU GLY LYS ILE LEU ASP VAL
SEQRES 19 A 326 ILE GLY LEU PRO GLY GLU GLU ASP TRP PRO ARG ASP VAL
SEQRES 20 A 326 ALA LEU PRO ARG GLN ALA PHE HIS SER LYS SER ALA GLN
SEQRES 21 A 326 PRO ILE GLU LYS PHE VAL THR ASP ILE ASP GLU LEU GLY
SEQRES 22 A 326 LYS ASP LEU LEU LEU LYS CYS LEU THR PHE ASN PRO ALA
SEQRES 23 A 326 LYS ARG ILE SER ALA TYR SER ALA LEU SER HIS PRO TYR
SEQRES 24 A 326 PHE GLN ASP LEU GLU ARG CYS LYS GLU ASN LEU ASP SER
SEQRES 25 A 326 HIS LEU PRO PRO SER GLN ASN THR SER GLU LEU ASN THR
SEQRES 26 A 326 ALA
SEQRES 1 B 156 MET GLU PRO ALA ALA GLY SER SER MET GLU PRO SER ALA
SEQRES 2 B 156 ASP TRP LEU ALA THR ALA ALA ALA ARG GLY ARG VAL GLU
SEQRES 3 B 156 GLU VAL ARG ALA LEU LEU GLU ALA GLY ALA ASN PRO ASN
SEQRES 4 B 156 ALA PRO ASN SER TYR GLY ARG ARG PRO ILE GLN VAL MET
SEQRES 5 B 156 MET MET GLY SER ALA ARG VAL ALA GLU LEU LEU LEU LEU
SEQRES 6 B 156 HIS GLY ALA GLU PRO ASN CYS ALA ASP PRO ALA THR LEU
SEQRES 7 B 156 THR ARG PRO VAL HIS ASP ALA ALA ARG GLU GLY PHE LEU
SEQRES 8 B 156 ASP THR LEU VAL VAL LEU HIS ARG ALA GLY ALA ARG LEU
SEQRES 9 B 156 ASP VAL ARG ASP ALA TRP GLY ARG LEU PRO VAL ASP LEU
SEQRES 10 B 156 ALA GLU GLU LEU GLY HIS ARG ASP VAL ALA ARG TYR LEU
SEQRES 11 B 156 ARG ALA ALA ALA GLY GLY THR ARG GLY SER ASN HIS ALA
SEQRES 12 B 156 ARG ILE ASP ALA ALA GLU GLY PRO SER ASP ILE PRO ASP
HELIX 1 2 LEU A 105 LYS A 111 1 7
HELIX 2 3 THR A 119 HIS A 139 1 21
HELIX 3 4 PRO A 148 ASN A 150 5 3
HELIX 4 5 PRO A 188 LEU A 192 1 5
HELIX 5 6 THR A 198 ARG A 214 5 17
HELIX 6 7 ASP A 224 ILE A 235 1 12
HELIX 7 8 ARG A 251 PHE A 254 5 4
HELIX 8 9 ILE A 262 LYS A 264 5 3
HELIX 9 10 GLU A 271 CYS A 280 1 10
HELIX 10 11 ALA A 291 SER A 296 1 6
HELIX 11 12 TRP B 15 ARG B 22 1 8
HELIX 12 13 VAL B 25 ALA B 34 1 10
HELIX 13 14 ALA B 57 HIS B 66 1 10
HELIX 14 15 PRO B 81 GLU B 88 1 8
HELIX 15 16 LEU B 91 ALA B 100 1 10
HELIX 16 17 PRO B 114 LEU B 121 1 8
HELIX 17 18 ARG B 124 LEU B 130 1 7
SHEET 1 A 5 GLY A 20 GLY A 22 0
SHEET 2 A 5 GLY A 25 ASP A 32 -1 N VAL A 27 O GLY A 20
SHEET 3 A 5 ARG A 38 VAL A 45 -1 N ARG A 44 O LYS A 26
SHEET 4 A 5 LEU A 94 GLU A 99 -1 N PHE A 98 O ALA A 41
SHEET 5 A 5 LEU A 79 THR A 84 -1 N CYS A 83 O THR A 95
SHEET 1 B 2 TYR A 13 GLU A 18 0
SHEET 2 B 2 PHE A 28 ASP A 32 -1 N ARG A 31 O GLU A 14
CRYST1 123.100 123.100 112.500 90.00 90.00 90.00 P 41 2 2 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 0.008123 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008123 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008889 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
