HEADER CELL CYCLE/TRANSFERASE 31-JUL-01 1JOW
TITLE CRYSTAL STRUCTURE OF A COMPLEX OF HUMAN CDK6 AND A VIRAL CYCLIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYCLIN HOMOLOG;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: V-CYCLIN;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: CELL DIVISION PROTEIN KINASE 6;
COMPND 8 CHAIN: B;
COMPND 9 FRAGMENT: RESIDUES 1-308;
COMPND 10 SYNONYM: CDK6, SERINE/THREONINE-PROTEIN KINASE PLSTIRE;
COMPND 11 EC: 2.7.1.-;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SAIMIRIINE HERPESVIRUS 2;
SOURCE 3 ORGANISM_COMMON: HERPESVIRUS SAIMIRI;
SOURCE 4 ORGANISM_TAXID: 10381;
SOURCE 5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: SF9;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PFASTBAC HTA DONOR PLASMID;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 GENE: CDK6;
SOURCE 16 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 17 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 18 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 19 EXPRESSION_SYSTEM_CELL_LINE: SF9;
SOURCE 20 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 21 EXPRESSION_SYSTEM_PLASMID: PFASTBAC1 DONOR PLASMID
KEYWDS CDK-CYCLIN COMPLEX, CYCLIN FOLD, CELL CYCLE-TRANSFERASE COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR U.SCHULZE-GAHMEN,S.H.KIM
REVDAT 3 07-FEB-24 1JOW 1 REMARK
REVDAT 2 24-FEB-09 1JOW 1 VERSN
REVDAT 1 27-FEB-02 1JOW 0
JRNL AUTH U.SCHULZE-GAHMEN,S.H.KIM
JRNL TITL STRUCTURAL BASIS FOR CDK6 ACTIVATION BY A VIRUS-ENCODED
JRNL TITL 2 CYCLIN.
JRNL REF NAT.STRUCT.BIOL. V. 9 177 2002
JRNL REFN ISSN 1072-8368
JRNL PMID 11828325
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH U.SCHULZE-GAHMEN,S.H.KIM
REMARK 1 TITL CRYSTALLIZATION OF A COMPLEX BETWEEN HUMAN CDK6 AND A
REMARK 1 TITL 2 VIRUS-ENCODED CYCLIN IS CRITICALLY DEPENDENT ON THE ADDITION
REMARK 1 TITL 3 OF SMALL CHARGED ORGANIC MOLECULES
REMARK 1 REF TO BE PUBLISHED
REMARK 1 REFN
REMARK 2
REMARK 2 RESOLUTION. 3.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.93
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 2293632.740
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 97.9
REMARK 3 NUMBER OF REFLECTIONS : 12629
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) : 0.266
REMARK 3 FREE R VALUE : 0.323
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.600
REMARK 3 FREE R VALUE TEST SET COUNT : 959
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.010
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.29
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 87.60
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1675
REMARK 3 BIN R VALUE (WORKING SET) : 0.3850
REMARK 3 BIN FREE R VALUE : 0.4510
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 7.80
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 141
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.038
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3986
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) : 73.30
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 10.00000
REMARK 3 B22 (A**2) : 10.00000
REMARK 3 B33 (A**2) : -19.99000
REMARK 3 B12 (A**2) : 16.11000
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) : 0.47
REMARK 3 ESD FROM SIGMAA (A) : 0.61
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.65
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.78
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 1.500
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 21.50
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.930
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 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.27
REMARK 3 BSOL : 29.99
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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1JOW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-AUG-01.
REMARK 100 THE DEPOSITION ID IS D_1000014015.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-DEC-00
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.99999
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 12783
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.100
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 1.0
REMARK 200 DATA REDUNDANCY : 7.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.05700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 29.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.19
REMARK 200 COMPLETENESS FOR SHELL (%) : 0.8
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.29000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.78
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: TRIS/HCL, SODIUM CHLORIDE, PEG 3350,
REMARK 280 CALCIUM ACETATE, PH 8.0, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 295.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2
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 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
REMARK 290 7555 Y,X,-Z+2/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+1/3
REMARK 290 10555 -Y,-X,-Z+1/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+5/6
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 299.18000
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 149.59000
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 224.38500
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 74.79500
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 373.97500
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 299.18000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 149.59000
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 74.79500
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 224.38500
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 373.97500
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS THE HETERODIMER IN THE
REMARK 300 ASYMMETRIC UNIT
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4000 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22020 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 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 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 ALA A 2
REMARK 465 ASP A 3
REMARK 465 SER A 4
REMARK 465 PRO A 5
REMARK 465 ASN A 6
REMARK 465 ARG A 7
REMARK 465 LEU A 8
REMARK 465 CYS A 124
REMARK 465 ASP A 125
REMARK 465 CYS A 126
REMARK 465 MET B 1
REMARK 465 GLU B 2
REMARK 465 LYS B 3
REMARK 465 ASP B 4
REMARK 465 GLY B 5
REMARK 465 LEU B 6
REMARK 465 CYS B 7
REMARK 465 ARG B 8
REMARK 465 ALA B 9
REMARK 465 ALA B 17
REMARK 465 GLU B 18
REMARK 465 ILE B 19
REMARK 465 GLY B 20
REMARK 465 GLU B 21
REMARK 465 GLY B 22
REMARK 465 ALA B 23
REMARK 465 ARG B 245
REMARK 465 ASP B 246
REMARK 465 VAL B 247
REMARK 465 ALA B 248
REMARK 465 LEU B 249
REMARK 465 PRO B 250
REMARK 465 ARG B 251
REMARK 465 GLN B 301
REMARK 465 ASP B 302
REMARK 465 LEU B 303
REMARK 465 GLU B 304
REMARK 465 ARG B 305
REMARK 465 CYS B 306
REMARK 465 LYS B 307
REMARK 465 GLU B 308
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 ASN A 9 CG OD1 ND2
REMARK 470 ARG A 10 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 12 CG CD CE NZ
REMARK 470 THR A 17 OG1 CG2
REMARK 470 MET A 18 CG SD CE
REMARK 470 GLU A 42 CG CD OE1 OE2
REMARK 470 LYS A 92 CG CD CE NZ
REMARK 470 SER A 123 OG
REMARK 470 ASP A 210 CG OD1 OD2
REMARK 470 ASN A 211 CG OD1 ND2
REMARK 470 THR A 212 OG1 CG2
REMARK 470 ASN A 213 CG OD1 ND2
REMARK 470 ARG A 215 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 221 CG CD1 CD2
REMARK 470 ASP B 10 CG OD1 OD2
REMARK 470 GLN B 11 CG CD OE1 NE2
REMARK 470 GLN B 12 CG CD OE1 NE2
REMARK 470 GLU B 14 CG CD OE1 OE2
REMARK 470 CYS B 15 SG
REMARK 470 VAL B 16 CG1 CG2
REMARK 470 LYS B 26 CG CD CE NZ
REMARK 470 LYS B 29 CG CD CE NZ
REMARK 470 ARG B 31 CG CD NE CZ NH1 NH2
REMARK 470 ASP B 32 CG OD1 OD2
REMARK 470 LEU B 33 CG CD1 CD2
REMARK 470 ASN B 35 CG OD1 ND2
REMARK 470 ARG B 38 CG CD NE CZ NH1 NH2
REMARK 470 VAL B 40 CG1 CG2
REMARK 470 ARG B 44 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 46 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 51 CG CD OE1 OE2
REMARK 470 ARG B 78 CG CD NE CZ NH1 NH2
REMARK 470 CYS B 83 SG
REMARK 470 ARG B 87 CG CD NE CZ NH1 NH2
REMARK 470 THR B 88 OG1 CG2
REMARK 470 ARG B 90 CG CD NE CZ NH1 NH2
REMARK 470 THR B 92 OG1 CG2
REMARK 470 LYS B 93 CG CD CE NZ
REMARK 470 THR B 95 OG1 CG2
REMARK 470 GLN B 103 CG CD OE1 NE2
REMARK 470 LYS B 111 CG CD CE NZ
REMARK 470 LEU B 183 CG CD1 CD2
REMARK 470 GLU B 189 CG CD OE1 OE2
REMARK 470 GLN B 252 CG CD OE1 NE2
REMARK 470 GLN B 260 CG CD OE1 NE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O ARG B 214 N LYS B 216 2.12
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 PRO B 217 C - N - CA ANGL. DEV. = 9.9 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 LYS A 12 122.84 -39.73
REMARK 500 SER A 15 66.21 -173.78
REMARK 500 THR A 16 -38.48 -25.88
REMARK 500 THR A 17 35.26 -76.91
REMARK 500 MET A 18 -1.94 -172.98
REMARK 500 ARG A 22 78.84 -51.49
REMARK 500 LEU A 32 18.42 -63.06
REMARK 500 GLU A 46 -45.31 -132.75
REMARK 500 LEU A 84 35.86 -80.98
REMARK 500 LYS A 86 -70.55 -66.64
REMARK 500 ILE A 97 -78.56 -45.82
REMARK 500 ILE A 108 -77.41 -72.73
REMARK 500 ASN A 129 2.64 -63.17
REMARK 500 TRP A 145 4.10 50.55
REMARK 500 THR A 147 -64.55 -97.05
REMARK 500 GLU A 148 152.59 -35.20
REMARK 500 GLU A 167 -39.27 -32.35
REMARK 500 LEU A 185 -19.41 -46.56
REMARK 500 GLU A 208 58.38 -93.75
REMARK 500 THR A 209 91.15 -161.35
REMARK 500 ASP A 210 95.30 65.48
REMARK 500 ASN A 211 -36.38 -31.76
REMARK 500 ASN A 213 7.38 86.16
REMARK 500 TRP A 217 -35.71 -34.44
REMARK 500 ASN A 229 72.98 70.69
REMARK 500 LEU A 248 0.97 -54.16
REMARK 500 GLN B 12 65.58 -103.74
REMARK 500 LYS B 34 -83.00 -54.70
REMARK 500 ASN B 35 163.02 -47.20
REMARK 500 ARG B 38 160.41 -43.33
REMARK 500 THR B 49 60.04 -64.69
REMARK 500 GLU B 51 58.98 -165.49
REMARK 500 GLU B 52 0.51 -150.02
REMARK 500 THR B 58 -2.72 -55.72
REMARK 500 ILE B 59 -64.45 -98.49
REMARK 500 CYS B 83 -71.43 -39.53
REMARK 500 THR B 84 105.15 57.94
REMARK 500 ASP B 89 -88.60 -69.09
REMARK 500 PHE B 98 -162.39 -112.16
REMARK 500 LEU B 105 -17.14 -45.24
REMARK 500 PRO B 113 162.92 -46.78
REMARK 500 THR B 119 -14.46 -49.97
REMARK 500 ASP B 163 74.32 45.68
REMARK 500 LEU B 166 -18.02 -145.66
REMARK 500 GLN B 173 15.47 56.03
REMARK 500 VAL B 181 143.48 72.23
REMARK 500 LEU B 183 -62.69 -5.31
REMARK 500 GLN B 193 15.69 54.24
REMARK 500 ALA B 197 -134.72 -166.47
REMARK 500 PRO B 199 -8.65 -53.28
REMARK 500
REMARK 500 THIS ENTRY HAS 64 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1JST RELATED DB: PDB
REMARK 900 RELATED ID: 1F5Q RELATED DB: PDB
DBREF 1JOW A 1 254 UNP Q01043 CGH2_SHV21 1 254
DBREF 1JOW B 1 308 UNP Q00534 CDK6_HUMAN 1 308
SEQRES 1 A 254 MET ALA ASP SER PRO ASN ARG LEU ASN ARG ALA LYS ILE
SEQRES 2 A 254 ASP SER THR THR MET LYS ASP PRO ARG VAL LEU ASN ASN
SEQRES 3 A 254 LEU LYS LEU ARG GLU LEU LEU LEU PRO LYS PHE THR SER
SEQRES 4 A 254 LEU TRP GLU ILE GLN THR GLU VAL THR VAL ASP ASN ARG
SEQRES 5 A 254 THR ILE LEU LEU THR TRP MET HIS LEU LEU CYS GLU SER
SEQRES 6 A 254 PHE GLU LEU ASP LYS SER VAL PHE PRO LEU SER VAL SER
SEQRES 7 A 254 ILE LEU ASP ARG TYR LEU CYS LYS LYS GLN GLY THR LYS
SEQRES 8 A 254 LYS THR LEU GLN LYS ILE GLY ALA ALA CYS VAL LEU ILE
SEQRES 9 A 254 GLY SER LYS ILE ARG THR VAL LYS PRO MET THR VAL SER
SEQRES 10 A 254 LYS LEU THR TYR LEU SER CYS ASP CYS PHE THR ASN LEU
SEQRES 11 A 254 GLU LEU ILE ASN GLN GLU LYS ASP ILE LEU GLU ALA LEU
SEQRES 12 A 254 LYS TRP ASP THR GLU ALA VAL LEU ALA THR ASP PHE LEU
SEQRES 13 A 254 ILE PRO LEU CYS ASN ALA LEU LYS ILE PRO GLU ASP LEU
SEQRES 14 A 254 TRP PRO GLN LEU TYR GLU ALA ALA SER THR THR ILE CYS
SEQRES 15 A 254 LYS ALA LEU ILE GLN PRO ASN ILE ALA LEU LEU SER PRO
SEQRES 16 A 254 GLY LEU ILE CYS ALA GLY GLY LEU LEU THR THR ILE GLU
SEQRES 17 A 254 THR ASP ASN THR ASN CYS ARG PRO TRP THR CYS TYR LEU
SEQRES 18 A 254 GLU ASP LEU SER SER ILE LEU ASN PHE SER THR ASN THR
SEQRES 19 A 254 VAL ARG THR VAL LYS ASP GLN VAL SER GLU ALA PHE SER
SEQRES 20 A 254 LEU TYR ASP LEU GLU ILE LEU
SEQRES 1 B 308 MET GLU LYS ASP GLY LEU CYS ARG ALA ASP GLN GLN TYR
SEQRES 2 B 308 GLU CYS VAL ALA GLU ILE GLY GLU GLY ALA TYR GLY LYS
SEQRES 3 B 308 VAL PHE LYS ALA ARG ASP LEU LYS ASN GLY GLY ARG PHE
SEQRES 4 B 308 VAL ALA LEU LYS ARG VAL ARG VAL GLN THR GLY GLU GLU
SEQRES 5 B 308 GLY MET PRO LEU SER THR ILE ARG GLU VAL ALA VAL LEU
SEQRES 6 B 308 ARG HIS LEU GLU THR PHE GLU HIS PRO ASN VAL VAL ARG
SEQRES 7 B 308 LEU PHE ASP VAL CYS THR VAL SER ARG THR ASP ARG GLU
SEQRES 8 B 308 THR LYS LEU THR LEU VAL PHE GLU HIS VAL ASP GLN ASP
SEQRES 9 B 308 LEU THR THR TYR LEU ASP LYS VAL PRO GLU PRO GLY VAL
SEQRES 10 B 308 PRO THR GLU THR ILE LYS ASP MET MET PHE GLN LEU LEU
SEQRES 11 B 308 ARG GLY LEU ASP PHE LEU HIS SER HIS ARG VAL VAL HIS
SEQRES 12 B 308 ARG ASP LEU LYS PRO GLN ASN ILE LEU VAL THR SER SER
SEQRES 13 B 308 GLY GLN ILE LYS LEU ALA ASP PHE GLY LEU ALA ARG ILE
SEQRES 14 B 308 TYR SER PHE GLN MET ALA LEU THR SER VAL VAL VAL THR
SEQRES 15 B 308 LEU TRP TYR ARG ALA PRO GLU VAL LEU LEU GLN SER SER
SEQRES 16 B 308 TYR ALA THR PRO VAL ASP LEU TRP SER VAL GLY CYS ILE
SEQRES 17 B 308 PHE ALA GLU MET PHE ARG ARG LYS PRO LEU PHE ARG GLY
SEQRES 18 B 308 SER SER ASP VAL ASP GLN LEU GLY LYS ILE LEU ASP VAL
SEQRES 19 B 308 ILE GLY LEU PRO GLY GLU GLU ASP TRP PRO ARG ASP VAL
SEQRES 20 B 308 ALA LEU PRO ARG GLN ALA PHE HIS SER LYS SER ALA GLN
SEQRES 21 B 308 PRO ILE GLU LYS PHE VAL THR ASP ILE ASP GLU LEU GLY
SEQRES 22 B 308 LYS ASP LEU LEU LEU LYS CYS LEU THR PHE ASN PRO ALA
SEQRES 23 B 308 LYS ARG ILE SER ALA TYR SER ALA LEU SER HIS PRO TYR
SEQRES 24 B 308 PHE GLN ASP LEU GLU ARG CYS LYS GLU
HELIX 1 1 SER A 15 ASP A 20 1 6
HELIX 2 2 VAL A 23 LEU A 32 1 10
HELIX 3 3 THR A 48 PHE A 66 1 19
HELIX 4 4 VAL A 72 LYS A 87 1 16
HELIX 5 5 THR A 90 THR A 110 1 21
HELIX 6 6 VAL A 116 TYR A 121 1 6
HELIX 7 7 LEU A 130 LYS A 144 1 15
HELIX 8 8 LEU A 151 ASP A 154 5 4
HELIX 9 9 PHE A 155 LEU A 163 1 9
HELIX 10 10 PRO A 166 ASP A 168 5 3
HELIX 11 11 LEU A 169 LEU A 185 1 17
HELIX 12 12 ASN A 189 LEU A 193 5 5
HELIX 13 13 SER A 194 GLU A 208 1 15
HELIX 14 14 TRP A 217 ASN A 229 1 13
HELIX 15 15 SER A 231 LEU A 248 1 18
HELIX 16 16 ASP A 250 LEU A 254 5 5
HELIX 17 17 LEU B 56 GLU B 69 1 14
HELIX 18 18 THR B 70 GLU B 72 5 3
HELIX 19 19 LEU B 105 LYS B 111 1 7
HELIX 20 20 PRO B 118 HIS B 139 1 22
HELIX 21 21 LYS B 147 GLN B 149 5 3
HELIX 22 22 THR B 182 ARG B 186 5 5
HELIX 23 23 ALA B 187 LEU B 192 1 6
HELIX 24 24 THR B 198 ARG B 214 1 17
HELIX 25 25 SER B 223 GLY B 236 1 14
HELIX 26 26 PRO B 261 PHE B 265 5 5
HELIX 27 27 ASP B 270 LEU B 281 1 12
HELIX 28 28 SER B 290 LEU B 295 1 6
SHEET 1 A 2 ARG A 10 ALA A 11 0
SHEET 2 A 2 ALA B 175 LEU B 176 -1 O LEU B 176 N ARG A 10
SHEET 1 B 2 TYR B 13 GLU B 14 0
SHEET 2 B 2 ARG B 31 ASP B 32 -1 O ARG B 31 N GLU B 14
SHEET 1 C 4 VAL B 27 PHE B 28 0
SHEET 2 C 4 LEU B 42 LYS B 43 -1 O LEU B 42 N PHE B 28
SHEET 3 C 4 LEU B 96 PHE B 98 -1 O LEU B 96 N LYS B 43
SHEET 4 C 4 LEU B 79 VAL B 82 -1 N ASP B 81 O VAL B 97
SHEET 1 D 3 GLN B 103 ASP B 104 0
SHEET 2 D 3 ILE B 151 VAL B 153 -1 O VAL B 153 N GLN B 103
SHEET 3 D 3 ILE B 159 LEU B 161 -1 O LYS B 160 N LEU B 152
SHEET 1 E 2 VAL B 141 VAL B 142 0
SHEET 2 E 2 ARG B 168 ILE B 169 -1 O ARG B 168 N VAL B 142
CISPEP 1 GLU B 114 PRO B 115 0 -0.21
CRYST1 70.140 70.140 448.770 90.00 90.00 120.00 P 65 2 2 12
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 0.014257 0.008231 0.000000 0.00000
SCALE2 0.000000 0.016463 0.000000 0.00000
SCALE3 0.000000 0.000000 0.002228 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
