HEADER CELL CYCLE, SIGNALING PROTEIN 24-OCT-00 1G3N
TITLE STRUCTURE OF A P18(INK4C)-CDK6-K-CYCLIN TERNARY COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYCLIN-DEPENDENT KINASE 6;
COMPND 3 CHAIN: A, E;
COMPND 4 SYNONYM: CELL DIVISION PROTEIN KINASE 6, PROTEIN KINASE CDK6;
COMPND 5 EC: 2.7.1.37;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: CYCLIN-DEPENDENT KINASE 6 INHIBITOR;
COMPND 9 CHAIN: B, F;
COMPND 10 SYNONYM: P18(INK4C), CYCLIN-DEPENDENT KINASE INHIBITOR 2C, P18,
COMPND 11 INHIBITS CDK4, CYCLIN-DEPENDENT KINASE 4 INHIBITOR C, P18-INK4C;
COMPND 12 ENGINEERED: YES;
COMPND 13 MOL_ID: 3;
COMPND 14 MOLECULE: V-CYCLIN;
COMPND 15 CHAIN: C, G;
COMPND 16 SYNONYM: K-CYCLIN, FUNCTIONAL CYCLIN D HOMOLOG;
COMPND 17 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: CYCLIN-DEPENDENT KINASE 6;
SOURCE 6 EXPRESSION_SYSTEM: UNIDENTIFIED BACULOVIRUS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 10469;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: HI5;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 11 ORGANISM_COMMON: HUMAN;
SOURCE 12 ORGANISM_TAXID: 9606;
SOURCE 13 GENE: P18(INK4C);
SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 16 MOL_ID: 3;
SOURCE 17 ORGANISM_SCIENTIFIC: HUMAN HERPESVIRUS 8;
SOURCE 18 ORGANISM_TAXID: 37296;
SOURCE 19 GENE: K-CYCLIN (VIRAL CYCLIND HOMOLOG);
SOURCE 20 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 21 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS CYCLIN-DEPENDENT KINASE, INK4 INHIBITOR, VIRAL CYCLIN, CELL CYCLE,
KEYWDS 2 SIGNALING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR P.D.JEFFREY,L.TONG,N.P.PAVLETICH
REVDAT 6 07-FEB-24 1G3N 1 SEQADV
REVDAT 5 04-APR-18 1G3N 1 REMARK
REVDAT 4 04-OCT-17 1G3N 1 REMARK
REVDAT 3 24-FEB-09 1G3N 1 VERSN
REVDAT 2 01-APR-03 1G3N 1 JRNL
REVDAT 1 10-JAN-01 1G3N 0
JRNL AUTH P.D.JEFFREY,L.TONG,N.P.PAVLETICH
JRNL TITL STRUCTURAL BASIS OF INHIBITION OF CDK-CYCLIN COMPLEXES BY
JRNL TITL 2 INK4 INHIBITORS.
JRNL REF GENES DEV. V. 14 3115 2000
JRNL REFN ISSN 0890-9369
JRNL PMID 11124804
JRNL DOI 10.1101/GAD.851100
REMARK 2
REMARK 2 RESOLUTION. 2.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
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 : CNS
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 15.00
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) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 33824
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) : 0.224
REMARK 3 FREE R VALUE : 0.262
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1905
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 : 10644
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) : 55.00
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) : 0.013
REMARK 3 BOND ANGLES (DEGREES) : 1.760
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
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 : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 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 1G3N COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-NOV-00.
REMARK 100 THE DEPOSITION ID IS D_1000012192.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-MAR-99
REMARK 200 TEMPERATURE (KELVIN) : 113
REMARK 200 PH : 7.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : MIRROR, YALE DESIGN
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : R-AXIS
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 40272
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900
REMARK 200 RESOLUTION RANGE LOW (A) : 100.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.0
REMARK 200 DATA REDUNDANCY : 3.300
REMARK 200 R MERGE (I) : 0.05700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 91.9
REMARK 200 DATA REDUNDANCY IN SHELL : 2.50
REMARK 200 R MERGE FOR SHELL (I) : 0.29900
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: 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 (%): 56.51
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.83
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: (NH4)2SO4, DIOXANE, TRIS-HCL, PH 7.6,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
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 38.89000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 82.41000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 73.47500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 82.41000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 38.89000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 73.47500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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 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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4150 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 29470 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, G
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: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7650 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 44560 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -39.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, E, G
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: 4
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5850 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 39050 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, E, F
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 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 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 ALA B 2
REMARK 465 GLU B 3
REMARK 465 PRO B 4
REMARK 465 TRP B 5
REMARK 465 ALA B 161
REMARK 465 GLY B 162
REMARK 465 GLY B 163
REMARK 465 ALA B 164
REMARK 465 THR B 165
REMARK 465 ASN B 166
REMARK 465 LEU B 167
REMARK 465 GLN B 168
REMARK 465 MET C 1
REMARK 465 ALA C 2
REMARK 465 THR C 3
REMARK 465 ALA C 4
REMARK 465 ASN C 5
REMARK 465 ASN C 6
REMARK 465 PRO C 7
REMARK 465 PRO C 8
REMARK 465 SER C 9
REMARK 465 GLY C 10
REMARK 465 LEU C 11
REMARK 465 LEU C 12
REMARK 465 ASP C 13
REMARK 465 PRO C 14
REMARK 465 THR C 15
REMARK 465 ASP C 214
REMARK 465 THR C 215
REMARK 465 HIS C 216
REMARK 465 SER C 217
REMARK 465 GLY C 218
REMARK 465 LEU C 254
REMARK 465 ASP C 255
REMARK 465 SER C 256
REMARK 465 TYR C 257
REMARK 465 MET E 1
REMARK 465 GLU E 2
REMARK 465 LYS E 3
REMARK 465 ASP E 4
REMARK 465 GLY E 5
REMARK 465 LEU E 6
REMARK 465 CYS E 7
REMARK 465 ARG E 8
REMARK 465 ASP E 302
REMARK 465 LEU E 303
REMARK 465 GLU E 304
REMARK 465 ARG E 305
REMARK 465 CYS E 306
REMARK 465 LYS E 307
REMARK 465 GLU E 308
REMARK 465 ASN E 309
REMARK 465 LEU E 310
REMARK 465 ASP E 311
REMARK 465 SER E 312
REMARK 465 HIS E 313
REMARK 465 LEU E 314
REMARK 465 PRO E 315
REMARK 465 PRO E 316
REMARK 465 SER E 317
REMARK 465 GLN E 318
REMARK 465 ASN E 319
REMARK 465 THR E 320
REMARK 465 SER E 321
REMARK 465 GLU E 322
REMARK 465 LEU E 323
REMARK 465 ASN E 324
REMARK 465 THR E 325
REMARK 465 ALA E 326
REMARK 465 MET F 1
REMARK 465 ALA F 2
REMARK 465 GLU F 3
REMARK 465 PRO F 4
REMARK 465 TRP F 5
REMARK 465 ALA F 161
REMARK 465 GLY F 162
REMARK 465 GLY F 163
REMARK 465 ALA F 164
REMARK 465 THR F 165
REMARK 465 ASN F 166
REMARK 465 LEU F 167
REMARK 465 GLN F 168
REMARK 465 MET G 1
REMARK 465 ALA G 2
REMARK 465 THR G 3
REMARK 465 ALA G 4
REMARK 465 ASN G 5
REMARK 465 ASN G 6
REMARK 465 PRO G 7
REMARK 465 PRO G 8
REMARK 465 SER G 9
REMARK 465 GLY G 10
REMARK 465 LEU G 11
REMARK 465 LEU G 12
REMARK 465 ASP G 13
REMARK 465 PRO G 14
REMARK 465 THR G 15
REMARK 465 ASP G 214
REMARK 465 THR G 215
REMARK 465 HIS G 216
REMARK 465 SER G 217
REMARK 465 GLY G 218
REMARK 465 LEU G 254
REMARK 465 ASP G 255
REMARK 465 SER G 256
REMARK 465 TYR G 257
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 LEU B 25 NH1 ARG B 59 2.09
REMARK 500 O LEU F 25 NH1 ARG F 59 2.14
REMARK 500 NE2 GLN A 252 OE2 GLU E 21 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 LYS A 147 CD LYS A 147 CE 0.153
REMARK 500 LYS A 147 CE LYS A 147 NZ 0.151
REMARK 500 LYS E 147 CD LYS E 147 CE 0.172
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 LYS A 147 CD - CE - NZ ANGL. DEV. = 18.6 DEGREES
REMARK 500 LYS E 147 CD - CE - NZ ANGL. DEV. = 16.5 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 GLN A 11 -7.07 -176.21
REMARK 500 ASN A 35 44.42 -144.08
REMARK 500 ARG A 87 -80.35 -70.24
REMARK 500 THR A 88 -155.98 -125.91
REMARK 500 ARG A 90 -15.99 -48.96
REMARK 500 ASP A 102 39.89 -77.45
REMARK 500 ASP A 110 38.27 -77.33
REMARK 500 PRO A 113 175.71 -52.09
REMARK 500 ARG A 144 -4.18 66.22
REMARK 500 ASP A 145 46.15 -146.21
REMARK 500 ASP A 163 74.07 -168.57
REMARK 500 GLN A 173 -80.70 -44.76
REMARK 500 SER A 194 -121.65 -114.87
REMARK 500 HIS A 255 172.64 -57.54
REMARK 500 SER A 258 -97.68 -64.20
REMARK 500 ALA A 259 80.04 153.83
REMARK 500 LEU A 281 44.53 -75.49
REMARK 500 PRO A 298 -2.32 -57.76
REMARK 500 LYS B 46 92.60 -66.49
REMARK 500 ASP B 100 -157.03 -81.54
REMARK 500 ASN B 129 89.59 -66.77
REMARK 500 ARG B 149 48.81 -67.09
REMARK 500 SER B 154 -72.98 -47.75
REMARK 500 GLU C 29 -67.63 -12.81
REMARK 500 PHE C 39 -91.94 -37.33
REMARK 500 THR C 41 -81.62 -125.05
REMARK 500 GLN C 44 -63.17 76.01
REMARK 500 SER C 60 -74.48 -58.07
REMARK 500 CYS C 62 -80.99 -70.96
REMARK 500 GLU C 64 -70.15 -82.34
REMARK 500 TYR C 65 21.27 -58.63
REMARK 500 THR C 111 60.22 -108.09
REMARK 500 TRP C 144 12.58 55.68
REMARK 500 LEU C 162 -67.88 -93.86
REMARK 500 HIS C 168 -33.00 86.25
REMARK 500 PRO C 212 177.49 -45.14
REMARK 500 ASP C 250 107.15 -163.55
REMARK 500 LEU C 251 12.59 -61.83
REMARK 500 GLN E 11 -5.76 -178.23
REMARK 500 ASN E 35 45.07 -144.30
REMARK 500 GLU E 72 56.86 39.63
REMARK 500 ARG E 87 -76.43 -71.18
REMARK 500 THR E 88 -157.40 -130.43
REMARK 500 ASP E 102 33.35 -75.62
REMARK 500 ASP E 110 33.91 -85.96
REMARK 500 SER E 138 -16.70 -49.19
REMARK 500 ARG E 144 -5.97 72.24
REMARK 500 ASP E 145 49.28 -145.32
REMARK 500 ASP E 163 69.19 -172.45
REMARK 500 GLN E 173 -83.81 -44.02
REMARK 500
REMARK 500 THIS ENTRY HAS 81 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1BI7 RELATED DB: PDB
REMARK 900 P16(INK4A)-CDK6 BINARY COMPLEX
REMARK 900 RELATED ID: 1BI8 RELATED DB: PDB
REMARK 900 P19(INK4D)-CDK6 BINARY COMPLEX
DBREF 1G3N A 1 326 UNP Q00534 CDK6_HUMAN 1 326
DBREF 1G3N E 1 326 UNP Q00534 CDK6_HUMAN 1 326
DBREF 1G3N B 1 168 UNP P42773 CDN2C_HUMAN 1 168
DBREF 1G3N F 1 168 UNP P42773 CDN2C_HUMAN 1 168
DBREF 1G3N C 1 257 UNP O40946 O40946_HHV8 1 257
DBREF 1G3N G 1 257 UNP O40946 O40946_HHV8 1 257
SEQADV 1G3N VAL C 163 UNP O40946 LEU 163 CONFLICT
SEQADV 1G3N LEU C 188 UNP O40946 LYS 188 CONFLICT
SEQADV 1G3N VAL G 163 UNP O40946 LEU 163 CONFLICT
SEQADV 1G3N LEU G 188 UNP O40946 LYS 188 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 168 MET ALA GLU PRO TRP GLY ASN GLU LEU ALA SER ALA ALA
SEQRES 2 B 168 ALA ARG GLY ASP LEU GLU GLN LEU THR SER LEU LEU GLN
SEQRES 3 B 168 ASN ASN VAL ASN VAL ASN ALA GLN ASN GLY PHE GLY ARG
SEQRES 4 B 168 THR ALA LEU GLN VAL MET LYS LEU GLY ASN PRO GLU ILE
SEQRES 5 B 168 ALA ARG ARG LEU LEU LEU ARG GLY ALA ASN PRO ASP LEU
SEQRES 6 B 168 LYS ASP ARG THR GLY PHE ALA VAL ILE HIS ASP ALA ALA
SEQRES 7 B 168 ARG ALA GLY PHE LEU ASP THR LEU GLN THR LEU LEU GLU
SEQRES 8 B 168 PHE GLN ALA ASP VAL ASN ILE GLU ASP ASN GLU GLY ASN
SEQRES 9 B 168 LEU PRO LEU HIS LEU ALA ALA LYS GLU GLY HIS LEU ARG
SEQRES 10 B 168 VAL VAL GLU PHE LEU VAL LYS HIS THR ALA SER ASN VAL
SEQRES 11 B 168 GLY HIS ARG ASN HIS LYS GLY ASP THR ALA CYS ASP LEU
SEQRES 12 B 168 ALA ARG LEU TYR GLY ARG ASN GLU VAL VAL SER LEU MET
SEQRES 13 B 168 GLN ALA ASN GLY ALA GLY GLY ALA THR ASN LEU GLN
SEQRES 1 C 257 MET ALA THR ALA ASN ASN PRO PRO SER GLY LEU LEU ASP
SEQRES 2 C 257 PRO THR LEU CYS GLU ASP ARG ILE PHE TYR ASN ILE LEU
SEQRES 3 C 257 GLU ILE GLU PRO ARG PHE LEU THR SER ASP SER VAL PHE
SEQRES 4 C 257 GLY THR PHE GLN GLN SER LEU THR SER HIS MET ARG LYS
SEQRES 5 C 257 LEU LEU GLY THR TRP MET PHE SER VAL CYS GLN GLU TYR
SEQRES 6 C 257 ASN LEU GLU PRO ASN VAL VAL ALA LEU ALA LEU ASN LEU
SEQRES 7 C 257 LEU ASP ARG LEU LEU LEU ILE LYS GLN VAL SER LYS GLU
SEQRES 8 C 257 HIS PHE GLN LYS THR GLY SER ALA CYS LEU LEU VAL ALA
SEQRES 9 C 257 SER LYS LEU ARG SER LEU THR PRO ILE SER THR SER SER
SEQRES 10 C 257 LEU CYS TYR ALA ALA ALA ASP SER PHE SER ARG GLN GLU
SEQRES 11 C 257 LEU ILE ASP GLN GLU LYS GLU LEU LEU GLU LYS LEU ALA
SEQRES 12 C 257 TRP ARG THR GLU ALA VAL LEU ALA THR ASP VAL THR SER
SEQRES 13 C 257 PHE LEU LEU LEU LYS LEU VAL GLY GLY SER GLN HIS LEU
SEQRES 14 C 257 ASP PHE TRP HIS HIS GLU VAL ASN THR LEU ILE THR LYS
SEQRES 15 C 257 ALA LEU VAL ASP PRO LEU THR GLY SER LEU PRO ALA SER
SEQRES 16 C 257 ILE ILE SER ALA ALA GLY CYS ALA LEU LEU VAL PRO ALA
SEQRES 17 C 257 ASN VAL ILE PRO GLN ASP THR HIS SER GLY GLY VAL VAL
SEQRES 18 C 257 PRO GLN LEU ALA SER ILE LEU GLY CYS ASP VAL SER VAL
SEQRES 19 C 257 LEU GLN ALA ALA VAL GLU GLN ILE LEU THR SER VAL SER
SEQRES 20 C 257 ASP PHE ASP LEU ARG ILE LEU ASP SER TYR
SEQRES 1 E 326 MET GLU LYS ASP GLY LEU CYS ARG ALA ASP GLN GLN TYR
SEQRES 2 E 326 GLU CYS VAL ALA GLU ILE GLY GLU GLY ALA TYR GLY LYS
SEQRES 3 E 326 VAL PHE LYS ALA ARG ASP LEU LYS ASN GLY GLY ARG PHE
SEQRES 4 E 326 VAL ALA LEU LYS ARG VAL ARG VAL GLN THR GLY GLU GLU
SEQRES 5 E 326 GLY MET PRO LEU SER THR ILE ARG GLU VAL ALA VAL LEU
SEQRES 6 E 326 ARG HIS LEU GLU THR PHE GLU HIS PRO ASN VAL VAL ARG
SEQRES 7 E 326 LEU PHE ASP VAL CYS THR VAL SER ARG THR ASP ARG GLU
SEQRES 8 E 326 THR LYS LEU THR LEU VAL PHE GLU HIS VAL ASP GLN ASP
SEQRES 9 E 326 LEU THR THR TYR LEU ASP LYS VAL PRO GLU PRO GLY VAL
SEQRES 10 E 326 PRO THR GLU THR ILE LYS ASP MET MET PHE GLN LEU LEU
SEQRES 11 E 326 ARG GLY LEU ASP PHE LEU HIS SER HIS ARG VAL VAL HIS
SEQRES 12 E 326 ARG ASP LEU LYS PRO GLN ASN ILE LEU VAL THR SER SER
SEQRES 13 E 326 GLY GLN ILE LYS LEU ALA ASP PHE GLY LEU ALA ARG ILE
SEQRES 14 E 326 TYR SER PHE GLN MET ALA LEU THR SER VAL VAL VAL THR
SEQRES 15 E 326 LEU TRP TYR ARG ALA PRO GLU VAL LEU LEU GLN SER SER
SEQRES 16 E 326 TYR ALA THR PRO VAL ASP LEU TRP SER VAL GLY CYS ILE
SEQRES 17 E 326 PHE ALA GLU MET PHE ARG ARG LYS PRO LEU PHE ARG GLY
SEQRES 18 E 326 SER SER ASP VAL ASP GLN LEU GLY LYS ILE LEU ASP VAL
SEQRES 19 E 326 ILE GLY LEU PRO GLY GLU GLU ASP TRP PRO ARG ASP VAL
SEQRES 20 E 326 ALA LEU PRO ARG GLN ALA PHE HIS SER LYS SER ALA GLN
SEQRES 21 E 326 PRO ILE GLU LYS PHE VAL THR ASP ILE ASP GLU LEU GLY
SEQRES 22 E 326 LYS ASP LEU LEU LEU LYS CYS LEU THR PHE ASN PRO ALA
SEQRES 23 E 326 LYS ARG ILE SER ALA TYR SER ALA LEU SER HIS PRO TYR
SEQRES 24 E 326 PHE GLN ASP LEU GLU ARG CYS LYS GLU ASN LEU ASP SER
SEQRES 25 E 326 HIS LEU PRO PRO SER GLN ASN THR SER GLU LEU ASN THR
SEQRES 26 E 326 ALA
SEQRES 1 F 168 MET ALA GLU PRO TRP GLY ASN GLU LEU ALA SER ALA ALA
SEQRES 2 F 168 ALA ARG GLY ASP LEU GLU GLN LEU THR SER LEU LEU GLN
SEQRES 3 F 168 ASN ASN VAL ASN VAL ASN ALA GLN ASN GLY PHE GLY ARG
SEQRES 4 F 168 THR ALA LEU GLN VAL MET LYS LEU GLY ASN PRO GLU ILE
SEQRES 5 F 168 ALA ARG ARG LEU LEU LEU ARG GLY ALA ASN PRO ASP LEU
SEQRES 6 F 168 LYS ASP ARG THR GLY PHE ALA VAL ILE HIS ASP ALA ALA
SEQRES 7 F 168 ARG ALA GLY PHE LEU ASP THR LEU GLN THR LEU LEU GLU
SEQRES 8 F 168 PHE GLN ALA ASP VAL ASN ILE GLU ASP ASN GLU GLY ASN
SEQRES 9 F 168 LEU PRO LEU HIS LEU ALA ALA LYS GLU GLY HIS LEU ARG
SEQRES 10 F 168 VAL VAL GLU PHE LEU VAL LYS HIS THR ALA SER ASN VAL
SEQRES 11 F 168 GLY HIS ARG ASN HIS LYS GLY ASP THR ALA CYS ASP LEU
SEQRES 12 F 168 ALA ARG LEU TYR GLY ARG ASN GLU VAL VAL SER LEU MET
SEQRES 13 F 168 GLN ALA ASN GLY ALA GLY GLY ALA THR ASN LEU GLN
SEQRES 1 G 257 MET ALA THR ALA ASN ASN PRO PRO SER GLY LEU LEU ASP
SEQRES 2 G 257 PRO THR LEU CYS GLU ASP ARG ILE PHE TYR ASN ILE LEU
SEQRES 3 G 257 GLU ILE GLU PRO ARG PHE LEU THR SER ASP SER VAL PHE
SEQRES 4 G 257 GLY THR PHE GLN GLN SER LEU THR SER HIS MET ARG LYS
SEQRES 5 G 257 LEU LEU GLY THR TRP MET PHE SER VAL CYS GLN GLU TYR
SEQRES 6 G 257 ASN LEU GLU PRO ASN VAL VAL ALA LEU ALA LEU ASN LEU
SEQRES 7 G 257 LEU ASP ARG LEU LEU LEU ILE LYS GLN VAL SER LYS GLU
SEQRES 8 G 257 HIS PHE GLN LYS THR GLY SER ALA CYS LEU LEU VAL ALA
SEQRES 9 G 257 SER LYS LEU ARG SER LEU THR PRO ILE SER THR SER SER
SEQRES 10 G 257 LEU CYS TYR ALA ALA ALA ASP SER PHE SER ARG GLN GLU
SEQRES 11 G 257 LEU ILE ASP GLN GLU LYS GLU LEU LEU GLU LYS LEU ALA
SEQRES 12 G 257 TRP ARG THR GLU ALA VAL LEU ALA THR ASP VAL THR SER
SEQRES 13 G 257 PHE LEU LEU LEU LYS LEU VAL GLY GLY SER GLN HIS LEU
SEQRES 14 G 257 ASP PHE TRP HIS HIS GLU VAL ASN THR LEU ILE THR LYS
SEQRES 15 G 257 ALA LEU VAL ASP PRO LEU THR GLY SER LEU PRO ALA SER
SEQRES 16 G 257 ILE ILE SER ALA ALA GLY CYS ALA LEU LEU VAL PRO ALA
SEQRES 17 G 257 ASN VAL ILE PRO GLN ASP THR HIS SER GLY GLY VAL VAL
SEQRES 18 G 257 PRO GLN LEU ALA SER ILE LEU GLY CYS ASP VAL SER VAL
SEQRES 19 G 257 LEU GLN ALA ALA VAL GLU GLN ILE LEU THR SER VAL SER
SEQRES 20 G 257 ASP PHE ASP LEU ARG ILE LEU ASP SER TYR
HELIX 1 1 PRO A 55 PHE A 71 1 17
HELIX 2 2 ASP A 104 ASP A 110 1 7
HELIX 3 3 PRO A 118 HIS A 139 1 22
HELIX 4 4 LYS A 147 GLN A 149 5 3
HELIX 5 5 THR A 182 ARG A 186 5 5
HELIX 6 6 ALA A 187 LEU A 192 1 6
HELIX 7 7 THR A 198 ARG A 215 1 18
HELIX 8 8 SER A 223 GLY A 236 1 14
HELIX 9 9 GLY A 239 TRP A 243 5 5
HELIX 10 10 PRO A 250 PHE A 254 5 5
HELIX 11 11 PRO A 261 PHE A 265 5 5
HELIX 12 12 ASP A 270 LEU A 281 1 12
HELIX 13 13 ASN A 284 ARG A 288 5 5
HELIX 14 14 SER A 290 SER A 296 1 7
HELIX 15 15 HIS A 297 GLN A 301 5 5
HELIX 16 16 GLY B 6 GLY B 16 1 11
HELIX 17 17 ASP B 17 LEU B 25 1 9
HELIX 18 18 THR B 40 MET B 45 1 6
HELIX 19 19 ASN B 49 ARG B 59 1 11
HELIX 20 20 ALA B 72 GLY B 81 1 10
HELIX 21 21 PHE B 82 PHE B 92 1 11
HELIX 22 22 LEU B 105 GLY B 114 1 10
HELIX 23 23 HIS B 115 THR B 126 1 12
HELIX 24 24 THR B 139 GLY B 148 1 10
HELIX 25 25 ARG B 149 GLY B 160 1 12
HELIX 26 26 LEU C 16 GLU C 29 1 14
HELIX 27 27 PRO C 30 LEU C 33 5 4
HELIX 28 28 SER C 35 PHE C 39 5 5
HELIX 29 29 THR C 47 TYR C 65 1 19
HELIX 30 30 GLU C 68 LEU C 83 1 16
HELIX 31 31 SER C 89 SER C 109 1 21
HELIX 32 32 SER C 114 ALA C 122 1 9
HELIX 33 33 SER C 127 LEU C 142 1 16
HELIX 34 34 LEU C 150 VAL C 163 1 14
HELIX 35 35 HIS C 168 VAL C 185 1 18
HELIX 36 36 LEU C 188 LEU C 192 5 5
HELIX 37 37 PRO C 193 VAL C 206 1 14
HELIX 38 38 PRO C 207 ILE C 211 5 5
HELIX 39 39 GLY C 219 GLY C 229 1 11
HELIX 40 40 ASP C 231 PHE C 249 1 19
HELIX 41 41 PRO E 55 PHE E 71 1 17
HELIX 42 42 ASP E 104 ASP E 110 1 7
HELIX 43 43 PRO E 118 HIS E 139 1 22
HELIX 44 44 LYS E 147 GLN E 149 5 3
HELIX 45 45 THR E 182 ARG E 186 5 5
HELIX 46 46 ALA E 187 LEU E 192 1 6
HELIX 47 47 THR E 198 ARG E 215 1 18
HELIX 48 48 SER E 223 GLY E 236 1 14
HELIX 49 49 PRO E 250 PHE E 254 5 5
HELIX 50 50 PRO E 261 PHE E 265 5 5
HELIX 51 51 ASP E 270 LEU E 281 1 12
HELIX 52 52 ASN E 284 ARG E 288 5 5
HELIX 53 53 SER E 290 SER E 296 1 7
HELIX 54 54 HIS E 297 GLN E 301 5 5
HELIX 55 55 GLY F 6 GLY F 16 1 11
HELIX 56 56 ASP F 17 LEU F 25 1 9
HELIX 57 57 THR F 40 MET F 45 1 6
HELIX 58 58 ASN F 49 ARG F 59 1 11
HELIX 59 59 ALA F 72 GLY F 81 1 10
HELIX 60 60 PHE F 82 PHE F 92 1 11
HELIX 61 61 LEU F 105 GLY F 114 1 10
HELIX 62 62 HIS F 115 THR F 126 1 12
HELIX 63 63 THR F 139 GLY F 148 1 10
HELIX 64 64 ARG F 149 ALA F 158 1 10
HELIX 65 65 LEU G 16 GLU G 29 1 14
HELIX 66 66 PRO G 30 LEU G 33 5 4
HELIX 67 67 SER G 35 PHE G 39 5 5
HELIX 68 68 THR G 47 TYR G 65 1 19
HELIX 69 69 GLU G 68 LEU G 83 1 16
HELIX 70 70 SER G 89 SER G 109 1 21
HELIX 71 71 SER G 114 ALA G 122 1 9
HELIX 72 72 SER G 127 LEU G 142 1 16
HELIX 73 73 ALA G 151 VAL G 163 1 13
HELIX 74 74 HIS G 168 ASP G 186 1 19
HELIX 75 75 LEU G 188 LEU G 192 5 5
HELIX 76 76 PRO G 193 VAL G 206 1 14
HELIX 77 77 PRO G 207 ILE G 211 5 5
HELIX 78 78 GLY G 219 GLY G 229 1 11
HELIX 79 79 ASP G 231 PHE G 249 1 19
SHEET 1 A 5 TYR A 13 GLY A 22 0
SHEET 2 A 5 GLY A 25 ASP A 32 -1 N GLY A 25 O GLY A 22
SHEET 3 A 5 PHE A 39 GLN A 48 -1 N VAL A 40 O ALA A 30
SHEET 4 A 5 GLU A 91 GLU A 99 -1 O THR A 92 N VAL A 47
SHEET 5 A 5 LEU A 79 SER A 86 -1 N PHE A 80 O VAL A 97
SHEET 1 B 2 ILE A 151 VAL A 153 0
SHEET 2 B 2 ILE A 159 LEU A 161 -1 O LYS A 160 N LEU A 152
SHEET 1 C 2 ILE A 169 PHE A 172 0
SHEET 2 C 2 THR A 177 VAL A 180 -1 O THR A 177 N PHE A 172
SHEET 1 D 5 TYR E 13 GLY E 22 0
SHEET 2 D 5 GLY E 25 ASP E 32 -1 N GLY E 25 O GLY E 22
SHEET 3 D 5 PHE E 39 GLN E 48 -1 O VAL E 40 N ALA E 30
SHEET 4 D 5 GLU E 91 GLU E 99 -1 O THR E 92 N VAL E 47
SHEET 5 D 5 LEU E 79 SER E 86 -1 N PHE E 80 O VAL E 97
SHEET 1 E 2 ILE E 151 VAL E 153 0
SHEET 2 E 2 ILE E 159 LEU E 161 -1 O LYS E 160 N LEU E 152
SHEET 1 F 2 ILE E 169 PHE E 172 0
SHEET 2 F 2 THR E 177 VAL E 180 -1 O THR E 177 N PHE E 172
CRYST1 77.780 146.950 164.820 90.00 90.00 90.00 P 21 21 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 0.012860 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006810 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006070 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
