HEADER TRANSFERASE 15-JUL-19 6KHF
TITLE CRYSTAL STRUCTURE OF CLK3 IN COMPLEX WITH CX-4945
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DUAL SPECIFICITY PROTEIN KINASE CLK3;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CDC-LIKE KINASE 3;
COMPND 5 EC: 2.7.12.1;
COMPND 6 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: CLK3;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS CDC2-LIKE KINASE, CASEIN KINASE, CX-4945, ALTERNATIVE SPLICING,
KEYWDS 2 SPLICING, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.Y.LEE,J.S.YUN,H.JIN,J.H.CHANG
REVDAT 2 22-NOV-23 6KHF 1 REMARK
REVDAT 1 02-OCT-19 6KHF 0
JRNL AUTH J.Y.LEE,J.S.YUN,W.K.KIM,H.S.CHUN,H.JIN,S.CHO,J.H.CHANG
JRNL TITL STRUCTURAL BASIS FOR THE SELECTIVE INHIBITION OF CDC2-LIKE
JRNL TITL 2 KINASES BY CX-4945.
JRNL REF BIOMED RES INT V.2019 25068 2019
JRNL REFN ESSN 2314-6141
JRNL PMID 31531359
JRNL DOI 10.1155/2019/6125068
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.36
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.380
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 3 NUMBER OF REFLECTIONS : 17642
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.229
REMARK 3 R VALUE (WORKING SET) : 0.223
REMARK 3 FREE R VALUE : 0.284
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1764
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 24.3590 - 6.0799 1.00 1316 146 0.1967 0.2529
REMARK 3 2 6.0799 - 4.8382 1.00 1262 140 0.2056 0.3081
REMARK 3 3 4.8382 - 4.2303 1.00 1241 139 0.1681 0.2536
REMARK 3 4 4.2303 - 3.8451 1.00 1225 136 0.1879 0.2461
REMARK 3 5 3.8451 - 3.5704 1.00 1242 138 0.2041 0.2573
REMARK 3 6 3.5704 - 3.3605 1.00 1219 135 0.2186 0.2671
REMARK 3 7 3.3605 - 3.1926 1.00 1223 135 0.2323 0.2632
REMARK 3 8 3.1926 - 3.0539 1.00 1214 135 0.2531 0.3017
REMARK 3 9 3.0539 - 2.9365 1.00 1194 133 0.2691 0.3445
REMARK 3 10 2.9365 - 2.8353 1.00 1223 136 0.2956 0.3414
REMARK 3 11 2.8353 - 2.7468 1.00 1214 135 0.2821 0.3398
REMARK 3 12 2.7468 - 2.6684 1.00 1215 135 0.3296 0.3221
REMARK 3 13 2.6684 - 2.5982 0.91 1090 121 0.3470 0.3920
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.390
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.460
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 49.96
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.010 2786
REMARK 3 ANGLE : 1.379 3761
REMARK 3 CHIRALITY : 0.056 394
REMARK 3 PLANARITY : 0.007 482
REMARK 3 DIHEDRAL : 17.158 1030
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6KHF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 16-JUL-19.
REMARK 100 THE DEPOSITION ID IS D_1300012943.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-NOV-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PAL/PLS
REMARK 200 BEAMLINE : 7A (6B, 6C1)
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 270
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17648
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.598
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 6.100
REMARK 200 R MERGE (I) : 0.15400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.69
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 5.20
REMARK 200 R MERGE FOR SHELL (I) : 0.67200
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: PHASER
REMARK 200 STARTING MODEL: 2EU9
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.65
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 60% (V/V) TACSIMATE PH 7.0, 0.025%
REMARK 280 DICHLOROMETHANE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
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 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 30.90950
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 57.48900
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 79.14200
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 30.90950
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 57.48900
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 79.14200
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 30.90950
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 57.48900
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 79.14200
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 30.90950
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 57.48900
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 79.14200
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A1127 LIES ON A SPECIAL POSITION.
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 HIS A 2
REMARK 465 HIS A 3
REMARK 465 CYS A 4
REMARK 465 LYS A 5
REMARK 465 ARG A 6
REMARK 465 TYR A 7
REMARK 465 ARG A 8
REMARK 465 SER A 9
REMARK 465 PRO A 10
REMARK 465 GLU A 11
REMARK 465 PRO A 12
REMARK 465 ASP A 13
REMARK 465 PRO A 14
REMARK 465 TYR A 15
REMARK 465 LEU A 16
REMARK 465 SER A 17
REMARK 465 TYR A 18
REMARK 465 ARG A 19
REMARK 465 TRP A 20
REMARK 465 LYS A 21
REMARK 465 ARG A 22
REMARK 465 ARG A 23
REMARK 465 ARG A 24
REMARK 465 SER A 25
REMARK 465 TYR A 26
REMARK 465 SER A 27
REMARK 465 ARG A 28
REMARK 465 GLU A 29
REMARK 465 HIS A 30
REMARK 465 GLU A 31
REMARK 465 GLY A 32
REMARK 465 ARG A 33
REMARK 465 LEU A 34
REMARK 465 ARG A 35
REMARK 465 TYR A 36
REMARK 465 PRO A 37
REMARK 465 SER A 38
REMARK 465 ARG A 39
REMARK 465 ARG A 40
REMARK 465 GLU A 41
REMARK 465 PRO A 42
REMARK 465 PRO A 43
REMARK 465 PRO A 44
REMARK 465 ARG A 45
REMARK 465 ARG A 46
REMARK 465 SER A 47
REMARK 465 ARG A 48
REMARK 465 SER A 49
REMARK 465 ARG A 50
REMARK 465 SER A 51
REMARK 465 HIS A 52
REMARK 465 ASP A 53
REMARK 465 ARG A 54
REMARK 465 LEU A 55
REMARK 465 PRO A 56
REMARK 465 TYR A 57
REMARK 465 GLN A 58
REMARK 465 ARG A 59
REMARK 465 ARG A 60
REMARK 465 TYR A 61
REMARK 465 ARG A 62
REMARK 465 GLU A 63
REMARK 465 ARG A 64
REMARK 465 ARG A 65
REMARK 465 ASP A 66
REMARK 465 SER A 67
REMARK 465 ASP A 68
REMARK 465 THR A 69
REMARK 465 TYR A 70
REMARK 465 ARG A 71
REMARK 465 CYS A 72
REMARK 465 GLU A 73
REMARK 465 GLU A 74
REMARK 465 ARG A 75
REMARK 465 SER A 76
REMARK 465 PRO A 77
REMARK 465 SER A 78
REMARK 465 PHE A 79
REMARK 465 GLY A 80
REMARK 465 GLU A 81
REMARK 465 ASP A 82
REMARK 465 TYR A 83
REMARK 465 TYR A 84
REMARK 465 GLY A 85
REMARK 465 PRO A 86
REMARK 465 SER A 87
REMARK 465 ARG A 88
REMARK 465 SER A 89
REMARK 465 ARG A 90
REMARK 465 HIS A 91
REMARK 465 ARG A 92
REMARK 465 ARG A 93
REMARK 465 ARG A 94
REMARK 465 SER A 95
REMARK 465 ARG A 96
REMARK 465 GLU A 97
REMARK 465 ARG A 98
REMARK 465 GLY A 99
REMARK 465 PRO A 100
REMARK 465 TYR A 101
REMARK 465 ARG A 102
REMARK 465 THR A 103
REMARK 465 ARG A 104
REMARK 465 LYS A 105
REMARK 465 HIS A 106
REMARK 465 ALA A 107
REMARK 465 HIS A 108
REMARK 465 HIS A 109
REMARK 465 CYS A 110
REMARK 465 HIS A 111
REMARK 465 LYS A 112
REMARK 465 ARG A 113
REMARK 465 ARG A 114
REMARK 465 THR A 115
REMARK 465 ARG A 116
REMARK 465 SER A 117
REMARK 465 CYS A 118
REMARK 465 SER A 119
REMARK 465 SER A 120
REMARK 465 ALA A 121
REMARK 465 SER A 122
REMARK 465 SER A 123
REMARK 465 ARG A 124
REMARK 465 SER A 125
REMARK 465 GLN A 126
REMARK 465 GLN A 127
REMARK 465 SER A 128
REMARK 465 SER A 129
REMARK 465 LYS A 130
REMARK 465 ARG A 131
REMARK 465 SER A 132
REMARK 465 SER A 133
REMARK 465 ARG A 134
REMARK 465 SER A 135
REMARK 465 VAL A 136
REMARK 465 GLU A 137
REMARK 465 ASP A 138
REMARK 465 ASP A 139
REMARK 465 LYS A 140
REMARK 465 GLU A 141
REMARK 465 GLU A 297
REMARK 465 THR A 298
REMARK 465 LEU A 299
REMARK 465 TYR A 300
REMARK 465 ASN A 301
REMARK 465 GLU A 302
REMARK 465 HIS A 303
REMARK 465 LYS A 304
REMARK 465 SER A 305
REMARK 465 CYS A 306
REMARK 465 GLU A 307
REMARK 465 GLU A 308
REMARK 465 LYS A 309
REMARK 465 PHE A 482
REMARK 465 HIS A 483
REMARK 465 THR A 484
REMARK 465 SER A 485
REMARK 465 ARG A 486
REMARK 465 ASN A 487
REMARK 465 PRO A 488
REMARK 465 SER A 489
REMARK 465 ARG A 490
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 HIS A 176 CG ND1 CD2 CE1 NE2
REMARK 470 HIS A 231 CG ND1 CD2 CE1 NE2
REMARK 470 PHE A 296 CG CD1 CD2 CE1 CE2 CZ
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 201 O HOH A 1101 1.89
REMARK 500 NZ LYS A 285 O HOH A 1102 2.03
REMARK 500 O THR A 166 NH1 ARG A 189 2.03
REMARK 500 OG1 THR A 337 O HOH A 1102 2.13
REMARK 500 OG1 THR A 337 O HOH A 1103 2.15
REMARK 500 OG SER A 310 O HOH A 1104 2.19
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 HIS A 143 -141.48 -95.03
REMARK 500 GLN A 153 15.66 44.96
REMARK 500 LYS A 180 1.01 80.61
REMARK 500 ARG A 189 174.24 -58.51
REMARK 500 ASP A 212 69.72 -55.19
REMARK 500 LYS A 213 -73.89 -49.63
REMARK 500 ASN A 227 66.93 -103.50
REMARK 500 ASP A 283 44.15 -145.92
REMARK 500 LYS A 285 142.60 176.07
REMARK 500 SER A 294 48.26 -104.52
REMARK 500 VAL A 335 -24.13 -140.37
REMARK 500 ALA A 352 -137.62 -155.62
REMARK 500 SER A 439 -176.60 -62.67
REMARK 500 LEU A 468 41.42 -107.68
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 3NG A 1000
DBREF 6KHF A 1 490 UNP P49761 CLK3_HUMAN 1 490
SEQADV 6KHF ASP A 155 UNP P49761 ARG 155 CONFLICT
SEQRES 1 A 490 MET HIS HIS CYS LYS ARG TYR ARG SER PRO GLU PRO ASP
SEQRES 2 A 490 PRO TYR LEU SER TYR ARG TRP LYS ARG ARG ARG SER TYR
SEQRES 3 A 490 SER ARG GLU HIS GLU GLY ARG LEU ARG TYR PRO SER ARG
SEQRES 4 A 490 ARG GLU PRO PRO PRO ARG ARG SER ARG SER ARG SER HIS
SEQRES 5 A 490 ASP ARG LEU PRO TYR GLN ARG ARG TYR ARG GLU ARG ARG
SEQRES 6 A 490 ASP SER ASP THR TYR ARG CYS GLU GLU ARG SER PRO SER
SEQRES 7 A 490 PHE GLY GLU ASP TYR TYR GLY PRO SER ARG SER ARG HIS
SEQRES 8 A 490 ARG ARG ARG SER ARG GLU ARG GLY PRO TYR ARG THR ARG
SEQRES 9 A 490 LYS HIS ALA HIS HIS CYS HIS LYS ARG ARG THR ARG SER
SEQRES 10 A 490 CYS SER SER ALA SER SER ARG SER GLN GLN SER SER LYS
SEQRES 11 A 490 ARG SER SER ARG SER VAL GLU ASP ASP LYS GLU GLY HIS
SEQRES 12 A 490 LEU VAL CYS ARG ILE GLY ASP TRP LEU GLN GLU ASP TYR
SEQRES 13 A 490 GLU ILE VAL GLY ASN LEU GLY GLU GLY THR PHE GLY LYS
SEQRES 14 A 490 VAL VAL GLU CYS LEU ASP HIS ALA ARG GLY LYS SER GLN
SEQRES 15 A 490 VAL ALA LEU LYS ILE ILE ARG ASN VAL GLY LYS TYR ARG
SEQRES 16 A 490 GLU ALA ALA ARG LEU GLU ILE ASN VAL LEU LYS LYS ILE
SEQRES 17 A 490 LYS GLU LYS ASP LYS GLU ASN LYS PHE LEU CYS VAL LEU
SEQRES 18 A 490 MET SER ASP TRP PHE ASN PHE HIS GLY HIS MET CYS ILE
SEQRES 19 A 490 ALA PHE GLU LEU LEU GLY LYS ASN THR PHE GLU PHE LEU
SEQRES 20 A 490 LYS GLU ASN ASN PHE GLN PRO TYR PRO LEU PRO HIS VAL
SEQRES 21 A 490 ARG HIS MET ALA TYR GLN LEU CYS HIS ALA LEU ARG PHE
SEQRES 22 A 490 LEU HIS GLU ASN GLN LEU THR HIS THR ASP LEU LYS PRO
SEQRES 23 A 490 GLU ASN ILE LEU PHE VAL ASN SER GLU PHE GLU THR LEU
SEQRES 24 A 490 TYR ASN GLU HIS LYS SER CYS GLU GLU LYS SER VAL LYS
SEQRES 25 A 490 ASN THR SER ILE ARG VAL ALA ASP PHE GLY SER ALA THR
SEQRES 26 A 490 PHE ASP HIS GLU HIS HIS THR THR ILE VAL ALA THR ARG
SEQRES 27 A 490 HIS TYR ARG PRO PRO GLU VAL ILE LEU GLU LEU GLY TRP
SEQRES 28 A 490 ALA GLN PRO CYS ASP VAL TRP SER ILE GLY CYS ILE LEU
SEQRES 29 A 490 PHE GLU TYR TYR ARG GLY PHE THR LEU PHE GLN THR HIS
SEQRES 30 A 490 GLU ASN ARG GLU HIS LEU VAL MET MET GLU LYS ILE LEU
SEQRES 31 A 490 GLY PRO ILE PRO SER HIS MET ILE HIS ARG THR ARG LYS
SEQRES 32 A 490 GLN LYS TYR PHE TYR LYS GLY GLY LEU VAL TRP ASP GLU
SEQRES 33 A 490 ASN SER SER ASP GLY ARG TYR VAL LYS GLU ASN CYS LYS
SEQRES 34 A 490 PRO LEU LYS SER TYR MET LEU GLN ASP SER LEU GLU HIS
SEQRES 35 A 490 VAL GLN LEU PHE ASP LEU MET ARG ARG MET LEU GLU PHE
SEQRES 36 A 490 ASP PRO ALA GLN ARG ILE THR LEU ALA GLU ALA LEU LEU
SEQRES 37 A 490 HIS PRO PHE PHE ALA GLY LEU THR PRO GLU GLU ARG SER
SEQRES 38 A 490 PHE HIS THR SER ARG ASN PRO SER ARG
HET 3NG A1000 25
HETNAM 3NG 5-[(3-CHLOROPHENYL)AMINO]BENZO[C][2,6]NAPHTHYRIDINE-8-
HETNAM 2 3NG CARBOXYLIC ACID
FORMUL 2 3NG C19 H12 CL N3 O2
FORMUL 3 HOH *66(H2 O)
HELIX 1 AA1 VAL A 191 ASP A 212 1 22
HELIX 2 AA2 ASN A 242 ASN A 250 1 9
HELIX 3 AA3 PRO A 256 GLU A 276 1 21
HELIX 4 AA4 LYS A 285 GLU A 287 5 3
HELIX 5 AA5 THR A 337 ARG A 341 5 5
HELIX 6 AA6 PRO A 342 LEU A 347 1 6
HELIX 7 AA7 GLN A 353 GLY A 370 1 18
HELIX 8 AA8 GLU A 378 GLY A 391 1 14
HELIX 9 AA9 PRO A 394 ARG A 400 1 7
HELIX 10 AB1 LYS A 403 LYS A 405 5 3
HELIX 11 AB2 SER A 418 CYS A 428 1 11
HELIX 12 AB3 PRO A 430 MET A 435 5 6
HELIX 13 AB4 SER A 439 LEU A 453 1 15
HELIX 14 AB5 THR A 462 LEU A 467 1 6
HELIX 15 AB6 LEU A 468 LEU A 475 5 8
SHEET 1 AA1 2 TRP A 151 LEU A 152 0
SHEET 2 AA1 2 TYR A 156 GLU A 157 -1 O TYR A 156 N LEU A 152
SHEET 1 AA2 5 GLY A 160 GLY A 165 0
SHEET 2 AA2 5 GLY A 168 CYS A 173 -1 O GLU A 172 N GLY A 160
SHEET 3 AA2 5 VAL A 183 ILE A 188 -1 O ILE A 187 N LYS A 169
SHEET 4 AA2 5 HIS A 231 GLU A 237 -1 O PHE A 236 N ALA A 184
SHEET 5 AA2 5 MET A 222 PHE A 228 -1 N SER A 223 O ALA A 235
SHEET 1 AA3 2 LEU A 279 THR A 280 0
SHEET 2 AA3 2 THR A 325 PHE A 326 -1 O THR A 325 N THR A 280
SHEET 1 AA4 2 ILE A 289 PHE A 291 0
SHEET 2 AA4 2 ILE A 316 VAL A 318 -1 O ARG A 317 N LEU A 290
SHEET 1 AA5 2 PHE A 407 TYR A 408 0
SHEET 2 AA5 2 GLY A 411 LEU A 412 -1 O GLY A 411 N TYR A 408
SITE 1 AC1 11 LEU A 162 GLY A 163 GLU A 164 PHE A 167
SITE 2 AC1 11 ALA A 184 LYS A 186 PHE A 236 LEU A 238
SITE 3 AC1 11 LEU A 239 LEU A 290 ASP A 320
CRYST1 61.819 114.978 158.284 90.00 90.00 90.00 I 2 2 2 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.016176 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008697 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006318 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
