HEADER CELL CYCLE 23-JAN-09 2W9F
TITLE CRYSTAL STRUCTURE OF CDK4 IN COMPLEX WITH A D-TYPE CYCLIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: G1/S-SPECIFIC CYCLIN-D1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: D-TYPE CYCLIN, PRAD1 ONCOGENE;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: CELL DIVISION PROTEIN KINASE 4;
COMPND 8 CHAIN: B;
COMPND 9 FRAGMENT: KINASE DOMAIN, RESIDUES 1-44,48-303;
COMPND 10 SYNONYM: CDK4, CYCLIN-DEPENDENT KINASE 4, PSK-J3;
COMPND 11 EC: 2.7.11.22;
COMPND 12 ENGINEERED: YES;
COMPND 13 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 7 EXPRESSION_SYSTEM_CELL_LINE: SF21;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 11 ORGANISM_COMMON: HUMAN;
SOURCE 12 ORGANISM_TAXID: 9606;
SOURCE 13 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 15 EXPRESSION_SYSTEM_CELL_LINE: SF21;
SOURCE 16 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS
KEYWDS SERINE/THREONINE-PROTEIN KINASE, CHROMOSOMAL REARRANGEMENT, ATP-
KEYWDS 2 BINDING, TRANSFERASE, POLYMORPHISM, CELL DIVISION, PROTO-ONCOGENE,
KEYWDS 3 PHOSPHOPROTEIN, DISEASE MUTATION, NUCLEOTIDE-BINDING, CYCLIN
KEYWDS 4 DEPENDENT KINASE, KINASE, CYCLIN, ONCOLOGY, CELL CYCLE, DRUG DESGN
EXPDTA X-RAY DIFFRACTION
AUTHOR P.J.DAY,A.CLEASBY,I.J.TICKLE,M.O.REILLY,J.E.COYLE,F.P.HOLDING,
AUTHOR 2 R.L.MCMENAMIN,J.YON,R.CHOPRA,C.LENGAUER,H.JHOTI
REVDAT 4 13-DEC-23 2W9F 1 REMARK
REVDAT 3 24-APR-19 2W9F 1 SOURCE
REVDAT 2 31-MAR-09 2W9F 1 JRNL
REVDAT 1 10-MAR-09 2W9F 0
JRNL AUTH P.J.DAY,A.CLEASBY,I.J.TICKLE,M.O'REILLY,J.E.COYLE,
JRNL AUTH 2 F.P.HOLDING,R.L.MCMENAMIN,J.YON,R.CHOPRA,C.LENGAUER,H.JHOTI
JRNL TITL CRYSTAL STRUCTURE OF HUMAN CDK4 IN COMPLEX WITH A D-TYPE
JRNL TITL 2 CYCLIN.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 106 4166 2009
JRNL REFN ISSN 0027-8424
JRNL PMID 19237565
JRNL DOI 10.1073/PNAS.0809645106
REMARK 2
REMARK 2 RESOLUTION. 2.85 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER-TNT
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SMART,VONRHEIN,WOMACK,
REMARK 3 : MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 93.66
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 3 NUMBER OF REFLECTIONS : 16778
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) : 0.229
REMARK 3 R VALUE (WORKING SET) : 0.225
REMARK 3 FREE R VALUE : 0.300
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 801
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 : 9
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.85
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 3.02
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.97
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2673
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2111
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2539
REMARK 3 BIN R VALUE (WORKING SET) : 0.2093
REMARK 3 BIN FREE R VALUE : 0.2439
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.01
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 134
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 : 3966
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 70
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 82.07
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 84.35
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -5.34606
REMARK 3 B22 (A**2) : 14.77175
REMARK 3 B33 (A**2) : -9.42569
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) : NULL
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL
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 : NULL
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : NULL
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : NULL ; NULL ; NULL
REMARK 3 BOND ANGLES : NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES : NULL ; NULL ; NULL
REMARK 3 TRIGONAL CARBON PLANES : NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES : NULL ; NULL ; NULL
REMARK 3 ISOTROPIC THERMAL FACTORS : NULL ; NULL ; NULL
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 : NULL ; NULL ; NULL
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 : NULL ; NULL ; NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : NULL
REMARK 3 OTHER TORSION ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS. DISORDERED RESIDUES WERE MODELLED STEREOCHEMICALLY
REMARK 3 WHEN POSSIBLE
REMARK 4
REMARK 4 2W9F COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 23-JAN-09.
REMARK 100 THE DEPOSITION ID IS D_1290038621.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-JUN-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.931
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 16778
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.850
REMARK 200 RESOLUTION RANGE LOW (A) : 60.900
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 200 DATA REDUNDANCY : 3.100
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.85
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.3
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.41000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 1BLX
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.94
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.09
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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 29.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 93.80850
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 32.13850
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 93.80850
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 29.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 32.13850
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 2250 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 28910 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.7 KCAL/MOL
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 400
REMARK 400 COMPOUND
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, GLY 43 TO GLU
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, GLY 44 TO GLU
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, THR 172 TO PHE
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 HIS A 3
REMARK 465 GLN A 4
REMARK 465 LEU A 5
REMARK 465 LEU A 6
REMARK 465 CYS A 7
REMARK 465 CYS A 8
REMARK 465 GLU A 9
REMARK 465 VAL A 10
REMARK 465 GLU A 11
REMARK 465 THR A 12
REMARK 465 ILE A 13
REMARK 465 ARG A 14
REMARK 465 ARG A 15
REMARK 465 ALA A 16
REMARK 465 TYR A 17
REMARK 465 PRO A 18
REMARK 465 ASP A 19
REMARK 465 ALA A 20
REMARK 465 ASN A 21
REMARK 465 LEU A 22
REMARK 465 LEU A 23
REMARK 465 ASN A 24
REMARK 465 ALA A 262
REMARK 465 GLN A 263
REMARK 465 GLN A 264
REMARK 465 ASN A 265
REMARK 465 MET A 266
REMARK 465 ASP A 267
REMARK 465 PRO A 268
REMARK 465 LYS A 269
REMARK 465 ALA A 270
REMARK 465 ALA A 271
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 THR B 3
REMARK 465 SER B 4
REMARK 465 LEU B 171
REMARK 465 PHE B 172
REMARK 465 PRO B 173
REMARK 465 VAL B 174
REMARK 465 VAL B 175
REMARK 465 VAL B 176
REMARK 465 LEU B 232
REMARK 465 PRO B 233
REMARK 465 PRO B 234
REMARK 465 GLU B 235
REMARK 465 ASP B 236
REMARK 465 ASP B 237
REMARK 465 LEU B 244
REMARK 465 PRO B 245
REMARK 465 ARG B 246
REMARK 465 GLY B 247
REMARK 465 ALA B 248
REMARK 465 PHE B 249
REMARK 465 PRO B 250
REMARK 465 PRO B 251
REMARK 465 ARG B 252
REMARK 465 GLY B 253
REMARK 465 PRO B 254
REMARK 465 ARG B 255
REMARK 465 PRO B 256
REMARK 465 VAL B 257
REMARK 465 GLN B 258
REMARK 465 HIS B 296
REMARK 465 LYS B 297
REMARK 465 ASP B 298
REMARK 465 GLU B 299
REMARK 465 GLY B 300
REMARK 465 ASN B 301
REMARK 465 PRO B 302
REMARK 465 GLU B 303
REMARK 465 HIS B 304
REMARK 465 HIS B 305
REMARK 465 HIS B 306
REMARK 465 HIS B 307
REMARK 465 HIS B 308
REMARK 465 HIS B 309
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 PRO B 108 C - N - CA ANGL. DEV. = 12.2 DEGREES
REMARK 500 PRO B 108 C - N - CD ANGL. DEV. = -16.1 DEGREES
REMARK 500 PRO B 113 C - N - CA ANGL. DEV. = 15.0 DEGREES
REMARK 500 PRO B 113 C - N - CD ANGL. DEV. = -14.8 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ARG A 26 -54.30 -134.18
REMARK 500 LEU A 91 -4.95 -145.38
REMARK 500 LYS A 96 -15.47 -48.25
REMARK 500 PRO A 134 -35.52 -37.71
REMARK 500 PRO A 169 82.36 -68.26
REMARK 500 GLN A 213 -72.23 -59.37
REMARK 500 LYS A 238 77.78 63.80
REMARK 500 ARG A 260 -32.53 -39.73
REMARK 500 VAL B 9 42.56 -167.87
REMARK 500 ALA B 10 -178.46 166.38
REMARK 500 TYR B 21 -161.37 -71.96
REMARK 500 PRO B 26 -60.28 -29.42
REMARK 500 HIS B 30 159.34 -44.69
REMARK 500 ILE B 51 -60.80 -28.97
REMARK 500 ASN B 70 40.27 -91.27
REMARK 500 THR B 80 -78.26 -136.33
REMARK 500 ASP B 84 -5.29 -53.10
REMARK 500 ASP B 105 -74.22 -49.11
REMARK 500 LYS B 106 -71.27 -12.73
REMARK 500 ALA B 107 108.21 -23.12
REMARK 500 PRO B 108 113.19 -14.85
REMARK 500 LEU B 112 -138.58 -142.58
REMARK 500 ALA B 114 -42.71 171.88
REMARK 500 GLU B 115 18.24 -69.30
REMARK 500 ARG B 139 -31.56 71.27
REMARK 500 ILE B 146 67.14 -43.41
REMARK 500 SER B 150 65.23 -66.22
REMARK 500 LEU B 156 156.98 -48.37
REMARK 500 TYR B 167 -70.35 -70.23
REMARK 500 GLN B 188 -88.67 -131.49
REMARK 500 SER B 189 4.71 167.67
REMARK 500 THR B 190 -51.82 -15.37
REMARK 500 ALA B 192 -173.14 -69.53
REMARK 500 PHE B 208 -83.86 -75.10
REMARK 500 ARG B 209 -18.09 -46.94
REMARK 500 LYS B 211 164.68 168.27
REMARK 500 ASN B 217 176.60 72.80
REMARK 500 ARG B 240 -121.98 -167.49
REMARK 500 ASP B 241 64.74 -173.88
REMARK 500 MET B 264 -35.40 172.21
REMARK 500 LEU B 276 47.34 -79.59
REMARK 500 TYR B 294 2.84 -66.86
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 LEU B 156 ALA B 157 -143.23
REMARK 500 LYS B 211 PRO B 212 -147.76
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH B2004 DISTANCE = 7.99 ANGSTROMS
REMARK 525 HOH B2006 DISTANCE = 6.23 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2W99 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CDK4 IN COMPLEX WITH A D-TYPE CYCLIN
REMARK 900 RELATED ID: 2W96 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CDK4 IN COMPLEX WITH A D-TYPE CYCLIN
REMARK 900 RELATED ID: 1LD2 RELATED DB: PDB
REMARK 900 THEORETICAL STRUCTURE OF HUMAN CYCLIN- DEPENDENT KINASE 4(CDK4)
DBREF 2W9F A 1 271 UNP P24385 CCND1_HUMAN 1 271
DBREF 2W9F B 1 44 UNP P11802 CDK4_HUMAN 1 44
DBREF 2W9F B 48 303 UNP P11802 CDK4_HUMAN 48 303
DBREF 2W9F B 304 309 PDB 2W9F 2W9F 304 309
SEQADV 2W9F GLU B 43 UNP P11802 GLY 43 ENGINEERED MUTATION
SEQADV 2W9F GLU B 44 UNP P11802 GLY 44 ENGINEERED MUTATION
SEQADV 2W9F PHE B 172 UNP P11802 THR 172 ENGINEERED MUTATION
SEQRES 1 A 271 MET GLU HIS GLN LEU LEU CYS CYS GLU VAL GLU THR ILE
SEQRES 2 A 271 ARG ARG ALA TYR PRO ASP ALA ASN LEU LEU ASN ASP ARG
SEQRES 3 A 271 VAL LEU ARG ALA MET LEU LYS ALA GLU GLU THR CYS ALA
SEQRES 4 A 271 PRO SER VAL SER TYR PHE LYS CYS VAL GLN LYS GLU VAL
SEQRES 5 A 271 LEU PRO SER MET ARG LYS ILE VAL ALA THR TRP MET LEU
SEQRES 6 A 271 GLU VAL CYS GLU GLU GLN LYS CYS GLU GLU GLU VAL PHE
SEQRES 7 A 271 PRO LEU ALA MET ASN TYR LEU ASP ARG PHE LEU SER LEU
SEQRES 8 A 271 GLU PRO VAL LYS LYS SER ARG LEU GLN LEU LEU GLY ALA
SEQRES 9 A 271 THR CYS MET PHE VAL ALA SER LYS MET LYS GLU THR ILE
SEQRES 10 A 271 PRO LEU THR ALA GLU LYS LEU CYS ILE TYR THR ASP ASN
SEQRES 11 A 271 SER ILE ARG PRO GLU GLU LEU LEU GLN MET GLU LEU LEU
SEQRES 12 A 271 LEU VAL ASN LYS LEU LYS TRP ASN LEU ALA ALA MET THR
SEQRES 13 A 271 PRO HIS ASP PHE ILE GLU HIS PHE LEU SER LYS MET PRO
SEQRES 14 A 271 GLU ALA GLU GLU ASN LYS GLN ILE ILE ARG LYS HIS ALA
SEQRES 15 A 271 GLN THR PHE VAL ALA LEU CYS ALA THR ASP VAL LYS PHE
SEQRES 16 A 271 ILE SER ASN PRO PRO SER MET VAL ALA ALA GLY SER VAL
SEQRES 17 A 271 VAL ALA ALA VAL GLN GLY LEU ASN LEU ARG SER PRO ASN
SEQRES 18 A 271 ASN PHE LEU SER TYR TYR ARG LEU THR ARG PHE LEU SER
SEQRES 19 A 271 ARG VAL ILE LYS CYS ASP PRO ASP CYS LEU ARG ALA CYS
SEQRES 20 A 271 GLN GLU GLN ILE GLU ALA LEU LEU GLU SER SER LEU ARG
SEQRES 21 A 271 GLN ALA GLN GLN ASN MET ASP PRO LYS ALA ALA
SEQRES 1 B 306 MET ALA THR SER ARG TYR GLU PRO VAL ALA GLU ILE GLY
SEQRES 2 B 306 VAL GLY ALA TYR GLY THR VAL TYR LYS ALA ARG ASP PRO
SEQRES 3 B 306 HIS SER GLY HIS PHE VAL ALA LEU LYS SER VAL ARG VAL
SEQRES 4 B 306 PRO ASN GLY GLU GLU GLY LEU PRO ILE SER THR VAL ARG
SEQRES 5 B 306 GLU VAL ALA LEU LEU ARG ARG LEU GLU ALA PHE GLU HIS
SEQRES 6 B 306 PRO ASN VAL VAL ARG LEU MET ASP VAL CYS ALA THR SER
SEQRES 7 B 306 ARG THR ASP ARG GLU ILE LYS VAL THR LEU VAL PHE GLU
SEQRES 8 B 306 HIS VAL ASP GLN ASP LEU ARG THR TYR LEU ASP LYS ALA
SEQRES 9 B 306 PRO PRO PRO GLY LEU PRO ALA GLU THR ILE LYS ASP LEU
SEQRES 10 B 306 MET ARG GLN PHE LEU ARG GLY LEU ASP PHE LEU HIS ALA
SEQRES 11 B 306 ASN CYS ILE VAL HIS ARG ASP LEU LYS PRO GLU ASN ILE
SEQRES 12 B 306 LEU VAL THR SER GLY GLY THR VAL LYS LEU ALA ASP PHE
SEQRES 13 B 306 GLY LEU ALA ARG ILE TYR SER TYR GLN MET ALA LEU PHE
SEQRES 14 B 306 PRO VAL VAL VAL THR LEU TRP TYR ARG ALA PRO GLU VAL
SEQRES 15 B 306 LEU LEU GLN SER THR TYR ALA THR PRO VAL ASP MET TRP
SEQRES 16 B 306 SER VAL GLY CYS ILE PHE ALA GLU MET PHE ARG ARG LYS
SEQRES 17 B 306 PRO LEU PHE CYS GLY ASN SER GLU ALA ASP GLN LEU GLY
SEQRES 18 B 306 LYS ILE PHE ASP LEU ILE GLY LEU PRO PRO GLU ASP ASP
SEQRES 19 B 306 TRP PRO ARG ASP VAL SER LEU PRO ARG GLY ALA PHE PRO
SEQRES 20 B 306 PRO ARG GLY PRO ARG PRO VAL GLN SER VAL VAL PRO GLU
SEQRES 21 B 306 MET GLU GLU SER GLY ALA GLN LEU LEU LEU GLU MET LEU
SEQRES 22 B 306 THR PHE ASN PRO HIS LYS ARG ILE SER ALA PHE ARG ALA
SEQRES 23 B 306 LEU GLN HIS SER TYR LEU HIS LYS ASP GLU GLY ASN PRO
SEQRES 24 B 306 GLU HIS HIS HIS HIS HIS HIS
FORMUL 3 HOH *70(H2 O)
HELIX 1 1 VAL A 27 CYS A 38 1 12
HELIX 2 2 SER A 43 VAL A 48 1 6
HELIX 3 3 LEU A 53 GLN A 71 1 19
HELIX 4 4 GLU A 76 LEU A 89 1 14
HELIX 5 5 ARG A 98 GLU A 115 1 18
HELIX 6 6 THR A 120 TYR A 127 1 8
HELIX 7 7 ARG A 133 LEU A 148 1 16
HELIX 8 8 THR A 156 SER A 166 1 11
HELIX 9 9 ALA A 171 THR A 191 1 21
HELIX 10 10 VAL A 193 ASN A 198 1 6
HELIX 11 11 PRO A 199 SER A 219 1 21
HELIX 12 12 PHE A 223 TYR A 227 5 5
HELIX 13 13 ARG A 228 LYS A 238 1 11
HELIX 14 14 ASP A 240 SER A 257 1 18
HELIX 15 15 PRO B 50 LEU B 63 1 14
HELIX 16 16 GLU B 64 GLU B 67 5 4
HELIX 17 17 ASP B 99 ALA B 107 1 9
HELIX 18 18 THR B 116 ASN B 134 1 19
HELIX 19 19 GLY B 160 ILE B 164 5 5
HELIX 20 20 PRO B 194 MET B 207 1 14
HELIX 21 21 SER B 218 ILE B 230 1 13
HELIX 22 22 GLU B 266 LEU B 276 1 11
HELIX 23 23 SER B 285 GLN B 291 1 7
SHEET 1 BA 5 GLU B 7 GLY B 15 0
SHEET 2 BA 5 GLY B 18 ARG B 24 -1 O GLY B 18 N GLY B 15
SHEET 3 BA 5 PHE B 31 VAL B 39 -1 O VAL B 32 N ALA B 23
SHEET 4 BA 5 ILE B 87 GLU B 94 -1 O ILE B 87 N VAL B 39
SHEET 5 BA 5 ASP B 76 ALA B 79 -1 O ASP B 76 N VAL B 92
SHEET 1 BB 2 LEU B 147 VAL B 148 0
SHEET 2 BB 2 VAL B 154 LYS B 155 -1 O LYS B 155 N LEU B 147
CISPEP 1 PRO B 109 PRO B 110 0 4.04
CISPEP 2 LEU B 112 PRO B 113 0 0.82
CISPEP 3 VAL B 185 LEU B 186 0 -21.66
CRYST1 58.000 64.277 187.617 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 0.017241 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015558 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005330 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
