HEADER TRANSFERASE 21-JUL-02 1H1S
TITLE STRUCTURE OF HUMAN THR160-PHOSPHO CDK2/CYCLIN A COMPLEXED
TITLE 2 WITH THE INHIBITOR NU6102
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CELL DIVISION PROTEIN KINASE 2;
COMPND 3 CHAIN: A, C;
COMPND 4 SYNONYM: CYCLIN-DEPENDENT KINASE 2, P33 PROTEIN KINASE;
COMPND 5 EC: 2.7.1.-;
COMPND 6 ENGINEERED: YES;
COMPND 7 OTHER_DETAILS: PHOSPHORYLATED ON THR160;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: CYCLIN A2;
COMPND 10 CHAIN: B, D;
COMPND 11 SYNONYM: CYCLIN A, CYCLIN A3;
COMPND 12 ENGINEERED: 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: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 MOL_ID: 2;
SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 9 ORGANISM_COMMON: HUMAN;
SOURCE 10 ORGANISM_TAXID: 9606;
SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 12 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS KINASE, TRANSFERASE, SERINE/THREONINE-PROTEIN KINASE, ATP-
KEYWDS 2 BINDING, CELL CYCLE, CELL DIVISION, MITOSIS,
KEYWDS 3 PHOSPHORYLATION
EXPDTA X-RAY DIFFRACTION
AUTHOR T.G.DAVIES,M.E.M.NOBLE,J.A.ENDICOTT,L.N.JOHNSON
REVDAT 2 24-FEB-09 1H1S 1 VERSN
REVDAT 1 19-SEP-02 1H1S 0
JRNL AUTH T.G.DAVIES,J.BENTLEY,C.E.ARRIS,F.T.BOYLE,
JRNL AUTH 2 N.J.CURTIN,J.A.ENDICOTT,A.E.GIBSON,B.T.GOLDING,
JRNL AUTH 3 R.J.GRIFFIN,I.R.HARDCASTLE,P.JEWSBURY,L.N.JOHNSON,
JRNL AUTH 4 V.MESGUICHE,D.R.NEWELL,M.E.M.NOBLE,J.A.TUCKER,
JRNL AUTH 5 L.WANG,H.J.WHITFIELD
JRNL TITL STRUCTURE-BASED DESIGN OF A POTENT PURINE-BASED
JRNL TITL 2 CYCLIN-DEPENDENT KINASE INHIBITOR
JRNL REF NAT.STRUCT.BIOL. V. 9 745 2002
JRNL REFN ISSN 1072-8368
JRNL PMID 12244298
JRNL DOI 10.1038/NSB842
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.5
REMARK 3 NUMBER OF REFLECTIONS : 101670
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) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.236
REMARK 3 FREE R VALUE : 0.286
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.0
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8920
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 78
REMARK 3 SOLVENT ATOMS : 703
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): NULL
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : NULL ; NULL
REMARK 3 ANGLE DISTANCE (A) : NULL ; NULL
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : NULL ; NULL
REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : NULL ; NULL
REMARK 3 STAGGERED (DEGREES) : NULL ; NULL
REMARK 3 TRANSVERSE (DEGREES) : NULL ; 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 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1H1S COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 22-JUL-02.
REMARK 100 THE PDBE ID CODE IS EBI-11153.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.00
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-4
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9789
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 101670
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.5
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.07900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.04
REMARK 200 COMPLETENESS FOR SHELL (%) : 61.2
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.28900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.8
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.75
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 37.11500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 74.23000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 67.67500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 74.23000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 37.11500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 67.67500
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
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 GENERATING THE BIOMOLECULE
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: PQS
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 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A -4
REMARK 465 PRO A -3
REMARK 465 LEU A -2
REMARK 465 GLY A -1
REMARK 465 ARG A 297
REMARK 465 LEU A 298
REMARK 465 GLY C -4
REMARK 465 PRO C -3
REMARK 465 LEU C -2
REMARK 465 GLY C -1
REMARK 465 ARG C 297
REMARK 465 LEU C 298
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 OE2 GLU A 28 - O HOH A 2029 2.13
REMARK 500 OG1 THR A 72 - O HOH A 2083 2.08
REMARK 500 O ALA A 95 - NH1 ARG A 199 2.16
REMARK 500 OD2 ASP A 247 - OG SER A 249 2.09
REMARK 500 N TYR B 178 - O HOH B 2028 2.13
REMARK 500 OD1 ASP B 345 - O HOH B 2130 2.18
REMARK 500 CB LEU B 423 - O HOH B 2176 1.88
REMARK 500 CG LEU B 423 - O HOH B 2176 2.14
REMARK 500 OH TYR C 15 - OE1 GLU C 51 2.20
REMARK 500 OE1 GLU C 40 - O HOH C 2031 1.81
REMARK 500 OE2 GLU C 40 - O HOH C 2031 2.16
REMARK 500 OG SER C 46 - O HOH C 2034 2.20
REMARK 500 OG SER C 94 - O HOH C 2059 2.12
REMARK 500 O ILE D 270 - O HOH D 2048 1.93
REMARK 500 O HOH A 2034 - O HOH A 2126 2.04
REMARK 500 O HOH A 2070 - O HOH A 2196 2.13
REMARK 500 O HOH A 2122 - O HOH A 2265 2.17
REMARK 500 O HOH A 2258 - O HOH A 2260 2.14
REMARK 500 O HOH C 2004 - O HOH B 2097 1.94
REMARK 500 O HOH D 2034 - O HOH D 2047 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500
REMARK 500 NH2 ARG A 199 OE2 GLU B 374 4456 2.18
REMARK 500 OE2 GLU B 374 NH2 ARG A 199 4556 2.18
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 SER A 120 CB SER A 120 OG -0.083
REMARK 500 TYR A 159 C TPO A 160 N 0.169
REMARK 500 TYR C 159 C TPO C 160 N 0.154
REMARK 500 TPO C 160 C HIS C 161 N 0.182
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 ARG A 36 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 ARG A 36 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 ASP A 38 N - CA - C ANGL. DEV. = 19.6 DEGREES
REMARK 500 ASP A 92 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ASP A 145 CB - CG - OD2 ANGL. DEV. = 5.9 DEGREES
REMARK 500 ARG A 157 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 VAL A 163 CG1 - CB - CG2 ANGL. DEV. = 10.3 DEGREES
REMARK 500 VAL A 163 N - CA - CB ANGL. DEV. = -14.0 DEGREES
REMARK 500 ASP A 210 CB - CG - OD1 ANGL. DEV. = 7.6 DEGREES
REMARK 500 VAL A 230 CB - CA - C ANGL. DEV. = -18.5 DEGREES
REMARK 500 ASP A 247 CB - CG - OD2 ANGL. DEV. = 6.6 DEGREES
REMARK 500 ASP A 256 CB - CG - OD2 ANGL. DEV. = 6.6 DEGREES
REMARK 500 ARG A 260 NE - CZ - NH1 ANGL. DEV. = 4.9 DEGREES
REMARK 500 ARG A 260 NE - CZ - NH2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 PRO B 176 N - CA - C ANGL. DEV. = 16.1 DEGREES
REMARK 500 PRO B 176 N - CA - CB ANGL. DEV. = 16.1 DEGREES
REMARK 500 PRO B 176 N - CD - CG ANGL. DEV. = 16.1 DEGREES
REMARK 500 ASP B 205 CB - CG - OD2 ANGL. DEV. = 6.3 DEGREES
REMARK 500 ASP B 284 CB - CG - OD2 ANGL. DEV. = 7.6 DEGREES
REMARK 500 ARG B 293 NE - CZ - NH1 ANGL. DEV. = 5.4 DEGREES
REMARK 500 ARG B 293 NE - CZ - NH2 ANGL. DEV. = -4.6 DEGREES
REMARK 500 ASP B 343 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 LEU B 423 CB - CA - C ANGL. DEV. = 11.5 DEGREES
REMARK 500 VAL C 17 CB - CA - C ANGL. DEV. = -16.7 DEGREES
REMARK 500 ARG C 36 CD - NE - CZ ANGL. DEV. = 14.1 DEGREES
REMARK 500 ARG C 36 CG - CD - NE ANGL. DEV. = 21.7 DEGREES
REMARK 500 ARG C 36 NE - CZ - NH1 ANGL. DEV. = -8.8 DEGREES
REMARK 500 ARG C 36 NE - CZ - NH2 ANGL. DEV. = 9.4 DEGREES
REMARK 500 LEU C 76 CA - CB - CG ANGL. DEV. = 14.5 DEGREES
REMARK 500 ASP C 86 CB - CG - OD2 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ARG C 122 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG C 122 NE - CZ - NH2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 ARG C 126 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ASP C 145 CB - CG - OD2 ANGL. DEV. = 8.6 DEGREES
REMARK 500 ARG C 157 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ASP C 206 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ARG C 214 NE - CZ - NH1 ANGL. DEV. = -3.6 DEGREES
REMARK 500 VAL C 230 CB - CA - C ANGL. DEV. = -14.0 DEGREES
REMARK 500 ASP C 247 CB - CG - OD2 ANGL. DEV. = 9.9 DEGREES
REMARK 500 ASP C 270 CB - CG - OD2 ANGL. DEV. = 6.2 DEGREES
REMARK 500 ASP D 181 CB - CG - OD2 ANGL. DEV. = 7.0 DEGREES
REMARK 500 ARG D 250 NE - CZ - NH1 ANGL. DEV. = 6.6 DEGREES
REMARK 500 ARG D 250 NE - CZ - NH2 ANGL. DEV. = -5.4 DEGREES
REMARK 500 ASP D 283 CB - CG - OD2 ANGL. DEV. = 7.0 DEGREES
REMARK 500 ARG D 293 NE - CZ - NH1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 ARG D 293 NE - CZ - NH2 ANGL. DEV. = -5.6 DEGREES
REMARK 500 ASP D 343 CB - CG - OD2 ANGL. DEV. = 5.9 DEGREES
REMARK 500 ASP D 393 CB - CG - OD2 ANGL. DEV. = 7.0 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 51 ANGLE DEVIATIONS
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 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 ASP A 38 -34.15 -155.42
REMARK 500 THR A 39 162.14 94.51
REMARK 500 GLU A 40 33.67 35.71
REMARK 500 THR A 41 -128.07 -145.54
REMARK 500 LEU A 96 -74.03 -79.19
REMARK 500 ASP A 127 38.83 -153.17
REMARK 500 ASP A 145 75.94 54.47
REMARK 500 VAL A 164 132.64 77.73
REMARK 500 SER A 181 -152.83 -142.84
REMARK 500 LYS A 242 78.81 -108.92
REMARK 500 THR A 290 -167.68 -129.57
REMARK 500 HIS A 295 62.44 -68.99
REMARK 500 PRO B 176 1.49 -34.12
REMARK 500 ASP B 283 55.99 34.53
REMARK 500 TRP B 372 111.58 -31.42
REMARK 500 GLU C 40 -1.56 53.98
REMARK 500 THR C 41 -113.70 -113.63
REMARK 500 LEU C 96 -113.53 -72.58
REMARK 500 ASP C 127 40.48 -161.75
REMARK 500 THR C 137 42.38 -90.64
REMARK 500 ASP C 145 76.48 46.77
REMARK 500 VAL C 164 136.91 78.40
REMARK 500 SER C 181 -153.78 -159.06
REMARK 500 ASP C 256 -177.86 -47.44
REMARK 500 PRO D 176 10.00 -45.66
REMARK 500 ASP D 283 63.98 33.07
REMARK 500 ASP D 284 46.92 39.83
REMARK 500 TRP D 372 94.55 -19.37
REMARK 500 ASN D 415 157.61 -42.46
REMARK 500 ASN D 431 64.01 71.06
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 ASP A 38 19.9 L L OUTSIDE RANGE
REMARK 500 TYR B 347 24.8 L L OUTSIDE RANGE
REMARK 500 LEU B 423 23.7 L L OUTSIDE RANGE
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 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 4SP A1298
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 4SP C1298
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1AQ1 RELATED DB: PDB
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED
REMARK 900 WITH THE INHIBITOR STAUROSPORINE
REMARK 900 RELATED ID: 1B38 RELATED DB: PDB
REMARK 900 HUMAN CYCLIN-DEPENDENT KINASE 2
REMARK 900 RELATED ID: 1B39 RELATED DB: PDB
REMARK 900 HUMAN CYCLIN-DEPENDENT KINASE 2 PHOSPHORYLATED
REMARK 900 ON THR 160
REMARK 900 RELATED ID: 1BUH RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE HUMAN CDK2 KINASE
REMARK 900 COMPLEX WITHCELL CYCLE-REGULATORY PROTEIN
REMARK 900 CKSHS1
REMARK 900 RELATED ID: 1CKP RELATED DB: PDB
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED
REMARK 900 WITH THE INHIBITOR PURVALANOL B
REMARK 900 RELATED ID: 1DI8 RELATED DB: PDB
REMARK 900 THE STRUCTURE OF CYCLIN-DEPENDENT KINASE 2
REMARK 900 (CDK2) IN COMPLEX WITH 4-[3-
REMARK 900 HYDROXYANILINO]-6,7-DIMETHOXYQUINAZOLINE
REMARK 900 RELATED ID: 1DM2 RELATED DB: PDB
REMARK 900 HUMAN CYCLIN-DEPENDENT KINASE 2 COMPLEXED
REMARK 900 WITH THE INHIBITOR HYMENIALDISINE
REMARK 900 RELATED ID: 1E1V RELATED DB: PDB
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED
REMARK 900 WITH THE INHIBITOR NU2058
REMARK 900 RELATED ID: 1E1X RELATED DB: PDB
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED
REMARK 900 WITH THE INHIBITOR NU6027
REMARK 900 RELATED ID: 1E9H RELATED DB: PDB
REMARK 900 THR 160 PHOSPHORYLATED CDK2 - HUMAN CYCLIN
REMARK 900 A3 COMPLEX WITH THE INHIBITOR INDIRUBIN-5-
REMARK 900 SULPHONATE BOUND
REMARK 900 RELATED ID: 1F5Q RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MURINE GAMMA HERPESVIRUS
REMARK 900 CYCLIN COMPLEXED TO HUMAN CYCLIN DEPENDANT
REMARK 900 KINASE 2
REMARK 900 RELATED ID: 1FIN RELATED DB: PDB
REMARK 900 CYCLIN A - CYCLIN-DEPENDENT KINASE 2 COMPLEX
REMARK 900 RELATED ID: 1FQ1 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF KINASE ASSOCIATED
REMARK 900 PHOSPHATASE (KAP) INCOMPLEX WITH PHOSPHO-CDK2
REMARK 900 RELATED ID: 1FVT RELATED DB: PDB
REMARK 900 THE STRUCTURE OF CYCLIN-DEPENDENT KINASE 2
REMARK 900 (CDK2) INCOMPLEX WITH AN OXINDOLE INHIBITOR
REMARK 900 RELATED ID: 1FVV RELATED DB: PDB
REMARK 900 THE STRUCTURE OF CDK2/CYCLIN A IN COMPLEX
REMARK 900 WITH AN OXINDOLEINHIBITOR
REMARK 900 RELATED ID: 1G5S RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN CYCLIN DEPENDENT
REMARK 900 KINASE 2 (CDK2)IN COMPLEX WITH THE
REMARK 900 INHIBITOR H717
REMARK 900 RELATED ID: 1GIH RELATED DB: PDB
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED
REMARK 900 WITH THE CDK4INHIBITOR
REMARK 900 RELATED ID: 1GII RELATED DB: PDB
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED
REMARK 900 WITH THE CDK4INHIBITOR
REMARK 900 RELATED ID: 1GIJ RELATED DB: PDB
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED
REMARK 900 WITH THE CDK4INHIBITOR
REMARK 900 RELATED ID: 1GY3 RELATED DB: PDB
REMARK 900 PCDK2/CYCLIN A IN COMPLEX WITH MGADP,
REMARK 900 NITRATE AND PEPTIDE SUBSTRATE
REMARK 900 RELATED ID: 1GZ8 RELATED DB: PDB
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED
REMARK 900 WITH THE INHIBITOR 2-AMINO-6-(3'-METHYL-
REMARK 900 2'-OXO)BUTOXYPURINE
REMARK 900 RELATED ID: 1H00 RELATED DB: PDB
REMARK 900 CDK2 IN COMPLEX WITH A DISUBSTITUTED 4, 6
REMARK 900 -BIS ANILINO PYRIMIDINE CDK4 INHIBITOR
REMARK 900 RELATED ID: 1H01 RELATED DB: PDB
REMARK 900 CDK2 IN COMPLEX WITH A DISUBSTITUTED 2, 4
REMARK 900 -BIS ANILINO PYRIMIDINE CDK4 INHIBITOR
REMARK 900 RELATED ID: 1H06 RELATED DB: PDB
REMARK 900 CDK2 IN COMPLEX WITH A DISUBSTITUTED 4, 6
REMARK 900 -BIS ANILINO PYRIMIDINE CDK4 INHIBITOR
REMARK 900 RELATED ID: 1H07 RELATED DB: PDB
REMARK 900 CDK2 IN COMPLEX WITH A DISUBSTITUTED 4, 6
REMARK 900 -BIS ANILINO PYRIMIDINE CDK4 INHIBITOR
REMARK 900 RELATED ID: 1H08 RELATED DB: PDB
REMARK 900 CDK2 IN COMPLEX WITH A DISUBSTITUTED 2, 4
REMARK 900 -BIS ANILINO PYRIMIDINE CDK4 INHIBITOR
REMARK 900 RELATED ID: 1H0U RELATED DB: PDB
REMARK 900 M. SMEGMATIS ARYLAMINE N-ACETYL TRANSFERASE
REMARK 900 RELATED ID: 1H0V RELATED DB: PDB
REMARK 900 HUMAN CYCLIN DEPENDENT PROTEIN KINASE 2 IN
REMARK 900 COMPLEX WITH THE INHIBITOR 2-AMINO-6-[(R
REMARK 900 )-PYRROLIDINO-5'-YL]METHOXYPURINE
REMARK 900 RELATED ID: 1H0W RELATED DB: PDB
REMARK 900 HUMAN CYCLIN DEPENDENT PROTEIN KINASE 2 IN
REMARK 900 COMPLEX WITH THE INHIBITOR 2-AMINO-6-[
REMARK 900 CYCLOHEX-3-ENYL]METHOXYPURINE
REMARK 900 RELATED ID: 1H1P RELATED DB: PDB
REMARK 900 STRUCTURE OF HUMAN THR160-PHOSPHO CDK2/CYCLIN A
REMARK 900 COMPLEXED WITH THE INHIBITOR NU2058
REMARK 900 RELATED ID: 1H1Q RELATED DB: PDB
REMARK 900 STRUCTURE OF HUMAN THR160-PHOSPHO CDK2/CYCLIN A
REMARK 900 COMPLEXED WITH THE INHIBITOR NU6094
REMARK 900 RELATED ID: 1H1R RELATED DB: PDB
REMARK 900 STRUCTURE OF HUMAN THR160-PHOSPHO CDK2/CYCLIN A
REMARK 900 COMPLEXED WITH THE INHIBITOR NU6086
REMARK 900 RELATED ID: 1HCK RELATED DB: PDB
REMARK 900 HUMAN CYCLIN-DEPENDENT KINASE 2
REMARK 900 RELATED ID: 1HCL RELATED DB: PDB
REMARK 900 HUMAN CYCLIN-DEPENDENT KINASE 2
REMARK 900 RELATED ID: 1JST RELATED DB: PDB
REMARK 900 PHOSPHORYLATED CYCLIN-DEPENDENT KINASE-2 BOUND
REMARK 900 TO CYCLIN A
REMARK 900 RELATED ID: 1JSU RELATED DB: PDB
REMARK 900 P27(KIP1)/CYCLIN A/CDK2 COMPLEX
REMARK 900 RELATED ID: 1JSV RELATED DB: PDB
REMARK 900 THE STRUCTURE OF CYCLIN-DEPENDENT KINASE 2
REMARK 900 (CDK2) INCOMPLEX WITH 4-[(6-AMINO-4-
REMARK 900 PYRIMIDINYL)AMINO]BENZENESULFONAMIDE
REMARK 900 RELATED ID: 1JVP RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN CDK2 (
REMARK 900 UNPHOSPHORYLATED) INCOMPLEX WITH PKF049-365
REMARK 900 RELATED ID: 1KE5 RELATED DB: PDB
REMARK 900 CDK2 COMPLEXED WITH N-METHYL-4-{[(2-OXO-
REMARK 900 1,2-DIHYDRO-3H-INDOL-3-YLIDENE)METHYL]
REMARK 900 AMINO}BENZENESULFONAMIDE
REMARK 900 RELATED ID: 1KE6 RELATED DB: PDB
REMARK 900 CYCLIN-DEPENDENT KINASE 2 (CDK2) COMPLEXED
REMARK 900 WITH N-METHYL-{4-[2-(7-OXO-6,7-DIHYDRO
REMARK 900 -8H-[1,3]THIAZOLO[5,4-E]INDOL-8-
REMARK 900 YLIDENE)HYDRAZINO]PHENYL}METHANESULFONAMIDE
REMARK 900 RELATED ID: 1KE7 RELATED DB: PDB
REMARK 900 CYCLIN-DEPENDENT KINASE 2 (CDK2) COMPLEXED
REMARK 900 WITH 3-{[(2,2-DIOXIDO-1,3-DIHYDRO-2-
REMARK 900 BENZOTHIEN-5-YL)AMINO]METHYLENE}-5-(1,3-
REMARK 900 OXAZOL-5-YL)-1,3-DIHYDRO-2H-INDOL-2-
REMARK 900 ONE
REMARK 900 RELATED ID: 1KE8 RELATED DB: PDB
REMARK 900 CYCLIN-DEPENDENT KINASE 2 (CDK2) COMPLEXED
REMARK 900 WITH 4-{[(2-OXO-1,2-DIHYDRO-3H-INDOL-3
REMARK 900 -YLIDENE)METHYL]AMINO}-N-(1,3-THIAZOL-2-
REMARK 900 YL)BENZENESULFONAMIDE
REMARK 900 RELATED ID: 1KE9 RELATED DB: PDB
REMARK 900 CYCLIN-DEPENDENT KINASE 2 (CDK2) COMPLEXED
REMARK 900 WITH 3-{[4-({[AMINO(IMINO)METHYL]
REMARK 900 AMINOSULFONYL)ANILINO]METHYLENE}-2-OXO-2,3-
REMARK 900 DIHYDRO-1H-INDOLE
REMARK 900 RELATED ID: 1QMZ RELATED DB: PDB
REMARK 900 PHOSPHORYLATED CDK2-CYCLYIN A-SUBSTRATE
REMARK 900 PEPTIDE COMPLEX
DBREF 1H1S A -4 0 PDB 1H1S 1H1S -4 0
DBREF 1H1S A 1 298 UNP P24941 CDK2_HUMAN 1 298
DBREF 1H1S B 175 432 UNP P20248 CGA2_HUMAN 175 432
DBREF 1H1S C -4 0 PDB 1H1S 1H1S -4 0
DBREF 1H1S C 1 298 UNP P24941 CDK2_HUMAN 1 298
DBREF 1H1S D 175 432 UNP P20248 CGA2_HUMAN 175 432
SEQRES 1 A 303 GLY PRO LEU GLY SER MET GLU ASN PHE GLN LYS VAL GLU
SEQRES 2 A 303 LYS ILE GLY GLU GLY THR TYR GLY VAL VAL TYR LYS ALA
SEQRES 3 A 303 ARG ASN LYS LEU THR GLY GLU VAL VAL ALA LEU LYS LYS
SEQRES 4 A 303 ILE ARG LEU ASP THR GLU THR GLU GLY VAL PRO SER THR
SEQRES 5 A 303 ALA ILE ARG GLU ILE SER LEU LEU LYS GLU LEU ASN HIS
SEQRES 6 A 303 PRO ASN ILE VAL LYS LEU LEU ASP VAL ILE HIS THR GLU
SEQRES 7 A 303 ASN LYS LEU TYR LEU VAL PHE GLU PHE LEU HIS GLN ASP
SEQRES 8 A 303 LEU LYS LYS PHE MET ASP ALA SER ALA LEU THR GLY ILE
SEQRES 9 A 303 PRO LEU PRO LEU ILE LYS SER TYR LEU PHE GLN LEU LEU
SEQRES 10 A 303 GLN GLY LEU ALA PHE CYS HIS SER HIS ARG VAL LEU HIS
SEQRES 11 A 303 ARG ASP LEU LYS PRO GLN ASN LEU LEU ILE ASN THR GLU
SEQRES 12 A 303 GLY ALA ILE LYS LEU ALA ASP PHE GLY LEU ALA ARG ALA
SEQRES 13 A 303 PHE GLY VAL PRO VAL ARG THR TYR TPO HIS GLU VAL VAL
SEQRES 14 A 303 THR LEU TRP TYR ARG ALA PRO GLU ILE LEU LEU GLY CYS
SEQRES 15 A 303 LYS TYR TYR SER THR ALA VAL ASP ILE TRP SER LEU GLY
SEQRES 16 A 303 CYS ILE PHE ALA GLU MET VAL THR ARG ARG ALA LEU PHE
SEQRES 17 A 303 PRO GLY ASP SER GLU ILE ASP GLN LEU PHE ARG ILE PHE
SEQRES 18 A 303 ARG THR LEU GLY THR PRO ASP GLU VAL VAL TRP PRO GLY
SEQRES 19 A 303 VAL THR SER MET PRO ASP TYR LYS PRO SER PHE PRO LYS
SEQRES 20 A 303 TRP ALA ARG GLN ASP PHE SER LYS VAL VAL PRO PRO LEU
SEQRES 21 A 303 ASP GLU ASP GLY ARG SER LEU LEU SER GLN MET LEU HIS
SEQRES 22 A 303 TYR ASP PRO ASN LYS ARG ILE SER ALA LYS ALA ALA LEU
SEQRES 23 A 303 ALA HIS PRO PHE PHE GLN ASP VAL THR LYS PRO VAL PRO
SEQRES 24 A 303 HIS LEU ARG LEU
SEQRES 1 B 258 VAL PRO ASP TYR HIS GLU ASP ILE HIS THR TYR LEU ARG
SEQRES 2 B 258 GLU MET GLU VAL LYS CYS LYS PRO LYS VAL GLY TYR MET
SEQRES 3 B 258 LYS LYS GLN PRO ASP ILE THR ASN SER MET ARG ALA ILE
SEQRES 4 B 258 LEU VAL ASP TRP LEU VAL GLU VAL GLY GLU GLU TYR LYS
SEQRES 5 B 258 LEU GLN ASN GLU THR LEU HIS LEU ALA VAL ASN TYR ILE
SEQRES 6 B 258 ASP ARG PHE LEU SER SER MET SER VAL LEU ARG GLY LYS
SEQRES 7 B 258 LEU GLN LEU VAL GLY THR ALA ALA MET LEU LEU ALA SER
SEQRES 8 B 258 LYS PHE GLU GLU ILE TYR PRO PRO GLU VAL ALA GLU PHE
SEQRES 9 B 258 VAL TYR ILE THR ASP ASP THR TYR THR LYS LYS GLN VAL
SEQRES 10 B 258 LEU ARG MET GLU HIS LEU VAL LEU LYS VAL LEU THR PHE
SEQRES 11 B 258 ASP LEU ALA ALA PRO THR VAL ASN GLN PHE LEU THR GLN
SEQRES 12 B 258 TYR PHE LEU HIS GLN GLN PRO ALA ASN CYS LYS VAL GLU
SEQRES 13 B 258 SER LEU ALA MET PHE LEU GLY GLU LEU SER LEU ILE ASP
SEQRES 14 B 258 ALA ASP PRO TYR LEU LYS TYR LEU PRO SER VAL ILE ALA
SEQRES 15 B 258 GLY ALA ALA PHE HIS LEU ALA LEU TYR THR VAL THR GLY
SEQRES 16 B 258 GLN SER TRP PRO GLU SER LEU ILE ARG LYS THR GLY TYR
SEQRES 17 B 258 THR LEU GLU SER LEU LYS PRO CYS LEU MET ASP LEU HIS
SEQRES 18 B 258 GLN THR TYR LEU LYS ALA PRO GLN HIS ALA GLN GLN SER
SEQRES 19 B 258 ILE ARG GLU LYS TYR LYS ASN SER LYS TYR HIS GLY VAL
SEQRES 20 B 258 SER LEU LEU ASN PRO PRO GLU THR LEU ASN LEU
SEQRES 1 C 303 GLY PRO LEU GLY SER MET GLU ASN PHE GLN LYS VAL GLU
SEQRES 2 C 303 LYS ILE GLY GLU GLY THR TYR GLY VAL VAL TYR LYS ALA
SEQRES 3 C 303 ARG ASN LYS LEU THR GLY GLU VAL VAL ALA LEU LYS LYS
SEQRES 4 C 303 ILE ARG LEU ASP THR GLU THR GLU GLY VAL PRO SER THR
SEQRES 5 C 303 ALA ILE ARG GLU ILE SER LEU LEU LYS GLU LEU ASN HIS
SEQRES 6 C 303 PRO ASN ILE VAL LYS LEU LEU ASP VAL ILE HIS THR GLU
SEQRES 7 C 303 ASN LYS LEU TYR LEU VAL PHE GLU PHE LEU HIS GLN ASP
SEQRES 8 C 303 LEU LYS LYS PHE MET ASP ALA SER ALA LEU THR GLY ILE
SEQRES 9 C 303 PRO LEU PRO LEU ILE LYS SER TYR LEU PHE GLN LEU LEU
SEQRES 10 C 303 GLN GLY LEU ALA PHE CYS HIS SER HIS ARG VAL LEU HIS
SEQRES 11 C 303 ARG ASP LEU LYS PRO GLN ASN LEU LEU ILE ASN THR GLU
SEQRES 12 C 303 GLY ALA ILE LYS LEU ALA ASP PHE GLY LEU ALA ARG ALA
SEQRES 13 C 303 PHE GLY VAL PRO VAL ARG THR TYR TPO HIS GLU VAL VAL
SEQRES 14 C 303 THR LEU TRP TYR ARG ALA PRO GLU ILE LEU LEU GLY CYS
SEQRES 15 C 303 LYS TYR TYR SER THR ALA VAL ASP ILE TRP SER LEU GLY
SEQRES 16 C 303 CYS ILE PHE ALA GLU MET VAL THR ARG ARG ALA LEU PHE
SEQRES 17 C 303 PRO GLY ASP SER GLU ILE ASP GLN LEU PHE ARG ILE PHE
SEQRES 18 C 303 ARG THR LEU GLY THR PRO ASP GLU VAL VAL TRP PRO GLY
SEQRES 19 C 303 VAL THR SER MET PRO ASP TYR LYS PRO SER PHE PRO LYS
SEQRES 20 C 303 TRP ALA ARG GLN ASP PHE SER LYS VAL VAL PRO PRO LEU
SEQRES 21 C 303 ASP GLU ASP GLY ARG SER LEU LEU SER GLN MET LEU HIS
SEQRES 22 C 303 TYR ASP PRO ASN LYS ARG ILE SER ALA LYS ALA ALA LEU
SEQRES 23 C 303 ALA HIS PRO PHE PHE GLN ASP VAL THR LYS PRO VAL PRO
SEQRES 24 C 303 HIS LEU ARG LEU
SEQRES 1 D 258 VAL PRO ASP TYR HIS GLU ASP ILE HIS THR TYR LEU ARG
SEQRES 2 D 258 GLU MET GLU VAL LYS CYS LYS PRO LYS VAL GLY TYR MET
SEQRES 3 D 258 LYS LYS GLN PRO ASP ILE THR ASN SER MET ARG ALA ILE
SEQRES 4 D 258 LEU VAL ASP TRP LEU VAL GLU VAL GLY GLU GLU TYR LYS
SEQRES 5 D 258 LEU GLN ASN GLU THR LEU HIS LEU ALA VAL ASN TYR ILE
SEQRES 6 D 258 ASP ARG PHE LEU SER SER MET SER VAL LEU ARG GLY LYS
SEQRES 7 D 258 LEU GLN LEU VAL GLY THR ALA ALA MET LEU LEU ALA SER
SEQRES 8 D 258 LYS PHE GLU GLU ILE TYR PRO PRO GLU VAL ALA GLU PHE
SEQRES 9 D 258 VAL TYR ILE THR ASP ASP THR TYR THR LYS LYS GLN VAL
SEQRES 10 D 258 LEU ARG MET GLU HIS LEU VAL LEU LYS VAL LEU THR PHE
SEQRES 11 D 258 ASP LEU ALA ALA PRO THR VAL ASN GLN PHE LEU THR GLN
SEQRES 12 D 258 TYR PHE LEU HIS GLN GLN PRO ALA ASN CYS LYS VAL GLU
SEQRES 13 D 258 SER LEU ALA MET PHE LEU GLY GLU LEU SER LEU ILE ASP
SEQRES 14 D 258 ALA ASP PRO TYR LEU LYS TYR LEU PRO SER VAL ILE ALA
SEQRES 15 D 258 GLY ALA ALA PHE HIS LEU ALA LEU TYR THR VAL THR GLY
SEQRES 16 D 258 GLN SER TRP PRO GLU SER LEU ILE ARG LYS THR GLY TYR
SEQRES 17 D 258 THR LEU GLU SER LEU LYS PRO CYS LEU MET ASP LEU HIS
SEQRES 18 D 258 GLN THR TYR LEU LYS ALA PRO GLN HIS ALA GLN GLN SER
SEQRES 19 D 258 ILE ARG GLU LYS TYR LYS ASN SER LYS TYR HIS GLY VAL
SEQRES 20 D 258 SER LEU LEU ASN PRO PRO GLU THR LEU ASN LEU
MODRES 1H1S TPO A 160 THR PHOSPHOTHREONINE
MODRES 1H1S TPO C 160 THR PHOSPHOTHREONINE
HET TPO A 160 11
HET TPO C 160 11
HET 4SP A1298 28
HET 4SP C1298 28
HETNAM TPO PHOSPHOTHREONINE
HETNAM 4SP O6-CYCLOHEXYLMETHOXY-2-(4'-SULPHAMOYLANILINO)
HETNAM 2 4SP PURINE
HETSYN TPO PHOSPHONOTHREONINE
FORMUL 1 TPO 2(C4 H10 N O6 P)
FORMUL 5 4SP 2()
FORMUL 7 HOH *703(H2 O1)
HELIX 1 1 PRO A 45 LEU A 58 1 14
HELIX 2 2 LEU A 87 SER A 94 1 8
HELIX 3 3 PRO A 100 HIS A 121 1 22
HELIX 4 4 LYS A 129 GLN A 131 5 3
HELIX 5 5 ASP A 145 ALA A 149 5 5
HELIX 6 6 THR A 165 ARG A 169 5 5
HELIX 7 7 ALA A 170 LEU A 175 1 6
HELIX 8 8 THR A 182 ARG A 199 1 18
HELIX 9 9 SER A 207 GLY A 220 1 14
HELIX 10 10 GLY A 229 MET A 233 5 5
HELIX 11 11 ASP A 247 VAL A 252 1 6
HELIX 12 12 ASP A 256 LEU A 267 1 12
HELIX 13 13 SER A 276 LEU A 281 1 6
HELIX 14 14 ALA A 282 GLN A 287 5 6
HELIX 15 15 VAL B 175 ASP B 177 5 3
HELIX 16 16 TYR B 178 CYS B 193 1 16
HELIX 17 17 GLY B 198 GLN B 203 5 6
HELIX 18 18 THR B 207 TYR B 225 1 19
HELIX 19 19 GLN B 228 SER B 244 1 17
HELIX 20 20 LYS B 252 GLU B 269 1 18
HELIX 21 21 GLU B 274 THR B 282 1 9
HELIX 22 22 THR B 287 LEU B 302 1 16
HELIX 23 23 THR B 310 LEU B 320 1 11
HELIX 24 24 ASN B 326 ASP B 343 1 18
HELIX 25 25 ASP B 343 LEU B 348 1 6
HELIX 26 26 LEU B 351 GLY B 369 1 19
HELIX 27 27 PRO B 373 GLY B 381 1 9
HELIX 28 28 THR B 383 ALA B 401 1 19
HELIX 29 29 PRO B 402 HIS B 404 5 3
HELIX 30 30 GLN B 407 TYR B 413 1 7
HELIX 31 31 LYS B 414 HIS B 419 5 6
HELIX 32 32 GLY B 420 LEU B 424 5 5
HELIX 33 33 PRO C 45 LEU C 58 1 14
HELIX 34 34 LEU C 87 SER C 94 1 8
HELIX 35 35 PRO C 100 HIS C 121 1 22
HELIX 36 36 LYS C 129 GLN C 131 5 3
HELIX 37 37 THR C 165 ARG C 169 5 5
HELIX 38 38 ALA C 170 LEU C 175 1 6
HELIX 39 39 THR C 182 ARG C 199 1 18
HELIX 40 40 SER C 207 GLY C 220 1 14
HELIX 41 41 GLY C 229 MET C 233 5 5
HELIX 42 42 ASP C 247 VAL C 252 1 6
HELIX 43 43 ASP C 256 LEU C 267 1 12
HELIX 44 44 SER C 276 ALA C 282 1 7
HELIX 45 45 HIS C 283 VAL C 289 5 7
HELIX 46 46 TYR D 178 CYS D 193 1 16
HELIX 47 47 TYR D 199 GLN D 203 5 5
HELIX 48 48 THR D 207 TYR D 225 1 19
HELIX 49 49 GLN D 228 MET D 246 1 19
HELIX 50 50 LEU D 249 GLY D 251 5 3
HELIX 51 51 LYS D 252 GLU D 269 1 18
HELIX 52 52 GLU D 274 THR D 282 1 9
HELIX 53 53 THR D 287 LEU D 302 1 16
HELIX 54 54 THR D 310 PHE D 319 1 10
HELIX 55 55 LEU D 320 GLN D 322 5 3
HELIX 56 56 ASN D 326 ASP D 343 1 18
HELIX 57 57 ASP D 343 LEU D 348 1 6
HELIX 58 58 LEU D 351 THR D 368 1 18
HELIX 59 59 PRO D 373 GLY D 381 1 9
HELIX 60 60 THR D 383 ALA D 401 1 19
HELIX 61 61 PRO D 402 HIS D 404 5 3
HELIX 62 62 GLN D 407 TYR D 413 1 7
HELIX 63 63 ASN D 415 HIS D 419 5 5
HELIX 64 64 GLY D 420 LEU D 424 5 5
SHEET 1 AA 5 PHE A 4 GLY A 11 0
SHEET 2 AA 5 VAL A 17 ASN A 23 -1 O VAL A 18 N ILE A 10
SHEET 3 AA 5 VAL A 29 ARG A 36 -1 O VAL A 30 N ALA A 21
SHEET 4 AA 5 LYS A 75 GLU A 81 -1 O LEU A 76 N ILE A 35
SHEET 5 AA 5 LEU A 66 HIS A 71 -1 N LEU A 67 O VAL A 79
SHEET 1 AB 3 GLN A 85 ASP A 86 0
SHEET 2 AB 3 LEU A 133 ILE A 135 -1 N ILE A 135 O GLN A 85
SHEET 3 AB 3 ILE A 141 LEU A 143 -1 O LYS A 142 N LEU A 134
SHEET 1 AC 2 VAL A 123 LEU A 124 0
SHEET 2 AC 2 ARG A 150 ALA A 151 -1 O ARG A 150 N LEU A 124
SHEET 1 CA 5 PHE C 4 GLY C 11 0
SHEET 2 CA 5 VAL C 17 ASN C 23 -1 O VAL C 18 N ILE C 10
SHEET 3 CA 5 VAL C 29 ARG C 36 -1 O VAL C 30 N ALA C 21
SHEET 4 CA 5 LYS C 75 GLU C 81 -1 O LEU C 76 N ILE C 35
SHEET 5 CA 5 LEU C 66 HIS C 71 -1 N LEU C 67 O VAL C 79
SHEET 1 CB 3 GLN C 85 ASP C 86 0
SHEET 2 CB 3 LEU C 133 ILE C 135 -1 O ILE C 135 N GLN C 85
SHEET 3 CB 3 ILE C 141 LEU C 143 -1 O LYS C 142 N LEU C 134
SHEET 1 CC 2 VAL C 123 LEU C 124 0
SHEET 2 CC 2 ARG C 150 ALA C 151 -1 O ARG C 150 N LEU C 124
LINK C TYR A 159 N TPO A 160 1555 1555 1.49
LINK C TPO A 160 N HIS A 161 1555 1555 1.43
LINK C TYR C 159 N TPO C 160 1555 1555 1.48
LINK C TPO C 160 N HIS C 161 1555 1555 1.51
CISPEP 1 VAL A 154 PRO A 155 0 -1.92
CISPEP 2 GLN B 323 PRO B 324 0 -9.60
CISPEP 3 ASP B 345 PRO B 346 0 4.10
CISPEP 4 VAL C 154 PRO C 155 0 -8.26
CISPEP 5 GLN D 323 PRO D 324 0 -9.31
CISPEP 6 ASP D 345 PRO D 346 0 11.04
SITE 1 AC1 14 ILE A 10 GLU A 12 ALA A 31 VAL A 64
SITE 2 AC1 14 PHE A 80 GLU A 81 LEU A 83 HIS A 84
SITE 3 AC1 14 GLN A 85 ASP A 86 LYS A 89 ASN A 132
SITE 4 AC1 14 LEU A 134 HOH A2271
SITE 1 AC2 15 ILE C 10 GLY C 11 GLU C 12 VAL C 18
SITE 2 AC2 15 ALA C 31 VAL C 64 PHE C 80 GLU C 81
SITE 3 AC2 15 LEU C 83 HIS C 84 GLN C 85 ASP C 86
SITE 4 AC2 15 LYS C 89 LEU C 134 HOH C2009
CRYST1 74.230 135.350 148.460 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 0.013472 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007388 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006736 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
