HEADER TRANSFERASE 12-SEP-17 6EH3
TITLE CRYSTAL STRUCTURE OF THE PROTEIN-KINASE A CATALYTIC SUBUNIT FROM
TITLE 2 CRITECULUS GRISEUS IN COMPLEX WITH COMPOUNDS RKP120 AND RKP190
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CAMP-DEPENDENT PROTEIN KINASE CATALYTIC SUBUNIT ALPHA;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PKA C-ALPHA;
COMPND 5 EC: 2.7.11.11;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: CAMP-DEPENDENT PROTEIN KINASE INHIBITOR;
COMPND 9 CHAIN: C;
COMPND 10 ENGINEERED: YES;
COMPND 11 OTHER_DETAILS: PKI 5-22 WITH N16RBS MUTATION
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CRICETULUS GRISEUS;
SOURCE 3 ORGANISM_COMMON: CHINESE HAMSTER;
SOURCE 4 ORGANISM_TAXID: 10029;
SOURCE 5 ORGAN: OVARY;
SOURCE 6 TISSUE: OVARY;
SOURCE 7 GENE: PRKACA;
SOURCE 8 EXPRESSION_SYSTEM: ESCHERICHIA COLI 'BL21-GOLD(DE3)PLYSS AG';
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 866768;
SOURCE 10 MOL_ID: 2;
SOURCE 11 SYNTHETIC: YES;
SOURCE 12 ORGANISM_SCIENTIFIC: CRICETULUS GRISEUS;
SOURCE 13 ORGANISM_TAXID: 10029
KEYWDS COMPLEX, PEPTIDIC LIGAND, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.M.MUELLER,A.HEINE,G.KLEBE
REVDAT 1 10-OCT-18 6EH3 0
JRNL AUTH J.M.MUELLER,R.KIRSCHNER,A.HEINE,A.GEYER,G.KLEBE
JRNL TITL CRYSTAL STRUCTURE OF THE PROTEIN-KINASE A CATALYTIC SUBUNIT
JRNL TITL 2 FROM CRITECULUS GRISEUS IN COMPLEX WITH COMPOUNDS RKP120 AND
JRNL TITL 3 RKP190
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.95 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.10.1_2155: ???)
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) : 1.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.87
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.370
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 3 NUMBER OF REFLECTIONS : 34587
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.175
REMARK 3 R VALUE (WORKING SET) : 0.173
REMARK 3 FREE R VALUE : 0.219
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1730
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 45.8788 - 4.4578 0.98 2888 152 0.1520 0.1913
REMARK 3 2 4.4578 - 3.5387 0.99 2795 148 0.1451 0.1906
REMARK 3 3 3.5387 - 3.0915 0.99 2748 144 0.1839 0.2242
REMARK 3 4 3.0915 - 2.8089 1.00 2775 146 0.1883 0.2409
REMARK 3 5 2.8089 - 2.6076 0.99 2751 145 0.1822 0.2213
REMARK 3 6 2.6076 - 2.4538 0.99 2720 143 0.1700 0.1976
REMARK 3 7 2.4538 - 2.3310 0.99 2714 143 0.1724 0.2047
REMARK 3 8 2.3310 - 2.2295 0.99 2716 143 0.1697 0.2355
REMARK 3 9 2.2295 - 2.1437 1.00 2727 144 0.1796 0.2687
REMARK 3 10 2.1437 - 2.0697 0.99 2725 143 0.1919 0.2182
REMARK 3 11 2.0697 - 2.0050 0.98 2675 141 0.2284 0.3062
REMARK 3 12 2.0050 - 1.9477 0.96 2623 138 0.2632 0.3137
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) : 0.220
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.040
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 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 : 0.011 3059
REMARK 3 ANGLE : 1.009 4156
REMARK 3 CHIRALITY : 0.060 440
REMARK 3 PLANARITY : 0.007 554
REMARK 3 DIHEDRAL : 15.514 1805
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 7
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 11 THROUGH 31 )
REMARK 3 ORIGIN FOR THE GROUP (A): -14.1326 -6.2597 6.8562
REMARK 3 T TENSOR
REMARK 3 T11: 0.2496 T22: 0.1904
REMARK 3 T33: 0.2206 T12: 0.0658
REMARK 3 T13: -0.0210 T23: 0.0048
REMARK 3 L TENSOR
REMARK 3 L11: 0.0414 L22: 0.0653
REMARK 3 L33: 0.0996 L12: 0.0407
REMARK 3 L13: 0.0222 L23: 0.0664
REMARK 3 S TENSOR
REMARK 3 S11: -0.1120 S12: -0.0233 S13: 0.1538
REMARK 3 S21: -0.0818 S22: 0.0772 S23: 0.1070
REMARK 3 S31: -0.1901 S32: 0.0776 S33: -0.0021
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 32 THROUGH 54 )
REMARK 3 ORIGIN FOR THE GROUP (A): -25.1465 -20.6804 30.9685
REMARK 3 T TENSOR
REMARK 3 T11: 0.1613 T22: 0.3915
REMARK 3 T33: 0.5341 T12: 0.0243
REMARK 3 T13: 0.0376 T23: 0.0737
REMARK 3 L TENSOR
REMARK 3 L11: 0.1843 L22: 0.9213
REMARK 3 L33: 0.3432 L12: -0.0628
REMARK 3 L13: 0.1818 L23: 0.3187
REMARK 3 S TENSOR
REMARK 3 S11: 0.1300 S12: -0.2020 S13: 0.0427
REMARK 3 S21: 0.1937 S22: -0.0050 S23: -0.0155
REMARK 3 S31: -0.0114 S32: -0.1432 S33: 0.0740
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 55 THROUGH 81 )
REMARK 3 ORIGIN FOR THE GROUP (A): -23.6100 -22.1131 31.5009
REMARK 3 T TENSOR
REMARK 3 T11: 0.3024 T22: 0.3892
REMARK 3 T33: 0.2543 T12: -0.0271
REMARK 3 T13: 0.0607 T23: 0.0363
REMARK 3 L TENSOR
REMARK 3 L11: 0.5161 L22: 0.3082
REMARK 3 L33: 0.0948 L12: -0.3795
REMARK 3 L13: 0.2134 L23: -0.1469
REMARK 3 S TENSOR
REMARK 3 S11: 0.1758 S12: -0.1541 S13: -0.1166
REMARK 3 S21: 0.1605 S22: 0.0355 S23: 0.2191
REMARK 3 S31: -0.2630 S32: -0.0363 S33: 0.0466
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 82 THROUGH 160 )
REMARK 3 ORIGIN FOR THE GROUP (A): -12.1068 -20.1988 20.6906
REMARK 3 T TENSOR
REMARK 3 T11: 0.1025 T22: 0.1263
REMARK 3 T33: 0.1311 T12: -0.0162
REMARK 3 T13: 0.0245 T23: 0.0086
REMARK 3 L TENSOR
REMARK 3 L11: 0.2982 L22: 0.3120
REMARK 3 L33: 0.0992 L12: 0.0099
REMARK 3 L13: 0.0761 L23: -0.1603
REMARK 3 S TENSOR
REMARK 3 S11: 0.0659 S12: -0.0416 S13: -0.0956
REMARK 3 S21: 0.0255 S22: -0.0349 S23: 0.1787
REMARK 3 S31: 0.0392 S32: -0.1186 S33: 0.1477
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 161 THROUGH 252 )
REMARK 3 ORIGIN FOR THE GROUP (A): 1.1634 -16.3856 22.4256
REMARK 3 T TENSOR
REMARK 3 T11: 0.1587 T22: 0.1323
REMARK 3 T33: 0.1489 T12: -0.0117
REMARK 3 T13: -0.0086 T23: -0.0073
REMARK 3 L TENSOR
REMARK 3 L11: 0.0841 L22: 0.3306
REMARK 3 L33: 0.2378 L12: -0.0694
REMARK 3 L13: 0.0674 L23: -0.1510
REMARK 3 S TENSOR
REMARK 3 S11: -0.0002 S12: -0.0696 S13: 0.0045
REMARK 3 S21: 0.0939 S22: -0.0318 S23: -0.0168
REMARK 3 S31: -0.0566 S32: 0.0002 S33: 0.0000
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 253 THROUGH 297 )
REMARK 3 ORIGIN FOR THE GROUP (A): 8.7458 -17.5577 9.0247
REMARK 3 T TENSOR
REMARK 3 T11: 0.1803 T22: 0.1598
REMARK 3 T33: 0.1966 T12: 0.0008
REMARK 3 T13: 0.0246 T23: 0.0279
REMARK 3 L TENSOR
REMARK 3 L11: 0.0839 L22: 0.0758
REMARK 3 L33: 0.1176 L12: -0.0648
REMARK 3 L13: -0.0683 L23: 0.0009
REMARK 3 S TENSOR
REMARK 3 S11: -0.0034 S12: 0.0768 S13: 0.1244
REMARK 3 S21: -0.1231 S22: -0.0530 S23: -0.1977
REMARK 3 S31: -0.1073 S32: 0.1651 S33: -0.0000
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 298 THROUGH 350 )
REMARK 3 ORIGIN FOR THE GROUP (A): -16.6207 -23.9442 22.8889
REMARK 3 T TENSOR
REMARK 3 T11: 0.2148 T22: 0.2137
REMARK 3 T33: 0.2189 T12: 0.0103
REMARK 3 T13: 0.0287 T23: 0.0118
REMARK 3 L TENSOR
REMARK 3 L11: 0.4431 L22: 0.2962
REMARK 3 L33: 0.0226 L12: 0.2311
REMARK 3 L13: 0.0338 L23: -0.0358
REMARK 3 S TENSOR
REMARK 3 S11: 0.1272 S12: -0.1082 S13: -0.0535
REMARK 3 S21: 0.0696 S22: 0.0105 S23: 0.1982
REMARK 3 S31: -0.0052 S32: 0.0045 S33: 0.1699
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 6EH3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 13-SEP-17.
REMARK 100 THE DEPOSITION ID IS D_1200006620.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-NOV-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.9
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : BESSY
REMARK 200 BEAMLINE : 14.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9184
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 34590
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.950
REMARK 200 RESOLUTION RANGE LOW (A) : 45.866
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 200 DATA REDUNDANCY : 4.370
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.05400
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 21.9600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.1
REMARK 200 DATA REDUNDANCY IN SHELL : 4.17
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.49800
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.170
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.83
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.92
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM MES-BIS-TRIS, 75 MM LITHIUM
REMARK 280 CHLORIDE, 1 MM DTT, 0.1 MM SODIUM EDTA, 0.25 MM MEGA 8, 0.7 MM
REMARK 280 PEPTIDIC LIGAND, 5 MM RKP190, 19% V/V METHANOL/WATER IN
REMARK 280 RESERVOIR, PH 6.9, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 277.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 29.34200
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 54.20750
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 36.76300
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 54.20750
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 29.34200
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 36.76300
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1680 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16860 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -1.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 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 LYS A 21 CD CE NZ
REMARK 470 GLU A 24 CG CD OE1 OE2
REMARK 470 GLU A 25 OE1 OE2
REMARK 470 LYS A 28 CD CE NZ
REMARK 470 LYS A 29 CE NZ
REMARK 470 GLU A 31 CG CD OE1 OE2
REMARK 470 SER A 32 OG
REMARK 470 GLN A 35 CG CD OE1 NE2
REMARK 470 ASN A 36 CG OD1 ND2
REMARK 470 ARG A 45 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 47 CD CE NZ
REMARK 470 LYS A 61 CE NZ
REMARK 470 LEU A 74 CD1 CD2
REMARK 470 LYS A 78 CD CE NZ
REMARK 470 LYS A 81 CG CD CE NZ
REMARK 470 LEU A 82 CD1
REMARK 470 LYS A 83 CG CD CE NZ
REMARK 470 LYS A 92 NZ
REMARK 470 GLU A 107 OE1
REMARK 470 GLN A 176 CD OE1 NE2
REMARK 470 LYS A 192 CE NZ
REMARK 470 ILE A 244 CD1
REMARK 470 LYS A 254 CD CE NZ
REMARK 470 ARG A 256 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 285 CG CD CE NZ
REMARK 470 LYS A 317 CG CD CE NZ
REMARK 470 PHE A 318 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS A 319 CG CD CE NZ
REMARK 470 GLU A 331 CG CD OE1 OE2
REMARK 470 GLU A 333 CG CD OE1 OE2
REMARK 470 GLU A 334 CG CD OE1 OE2
REMARK 470 ILE A 335 CG1 CG2 CD1
REMARK 470 ARG A 336 CG CD NE CZ NH1 NH2
REMARK 470 ILE A 339 CG1 CG2 CD1
REMARK 470 LYS A 342 CG CD CE NZ
REMARK 470 LYS A 345 CD CE NZ
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue B4Z A 401
DBREF 6EH3 A 0 350 UNP P25321 KAPCA_CRIGR 1 351
DBREF 6EH3 C 8 25 PDB 6EH3 6EH3 8 25
SEQADV 6EH3 GLY A -2 UNP P25321 EXPRESSION TAG
SEQADV 6EH3 HIS A -1 UNP P25321 EXPRESSION TAG
SEQRES 1 A 353 GLY HIS MET GLY ASN ALA ALA ALA ALA LYS LYS GLY SEP
SEQRES 2 A 353 GLU GLN GLU SER VAL LYS GLU PHE LEU ALA LYS ALA LYS
SEQRES 3 A 353 GLU GLU PHE LEU LYS LYS TRP GLU SER PRO SER GLN ASN
SEQRES 4 A 353 THR ALA GLN LEU ASP HIS PHE ASP ARG ILE LYS THR LEU
SEQRES 5 A 353 GLY THR GLY SER PHE GLY ARG VAL MET LEU VAL LYS HIS
SEQRES 6 A 353 LYS GLU THR GLY ASN HIS TYR ALA MET LYS ILE LEU ASP
SEQRES 7 A 353 LYS GLN LYS VAL VAL LYS LEU LYS GLN ILE GLU HIS THR
SEQRES 8 A 353 LEU ASN GLU LYS ARG ILE LEU GLN ALA VAL ASN PHE PRO
SEQRES 9 A 353 PHE LEU VAL LYS LEU GLU PHE SER PHE LYS ASP ASN SER
SEQRES 10 A 353 ASN LEU TYR MET VAL MET GLU TYR VAL PRO GLY GLY GLU
SEQRES 11 A 353 MET PHE SER HIS LEU ARG ARG ILE GLY ARG PHE SEP GLU
SEQRES 12 A 353 PRO HIS ALA ARG PHE TYR ALA ALA GLN ILE VAL LEU THR
SEQRES 13 A 353 PHE GLU TYR LEU HIS SER LEU ASP LEU ILE TYR ARG ASP
SEQRES 14 A 353 LEU LYS PRO GLU ASN LEU LEU ILE ASP GLN GLN GLY TYR
SEQRES 15 A 353 ILE GLN VAL THR ASP PHE GLY PHE ALA LYS ARG VAL LYS
SEQRES 16 A 353 GLY ARG THR TRP TPO LEU CYS GLY THR PRO GLU TYR LEU
SEQRES 17 A 353 ALA PRO GLU ILE ILE LEU SER LYS GLY TYR ASN LYS ALA
SEQRES 18 A 353 VAL ASP TRP TRP ALA LEU GLY VAL LEU ILE TYR GLU MET
SEQRES 19 A 353 ALA ALA GLY TYR PRO PRO PHE PHE ALA ASP GLN PRO ILE
SEQRES 20 A 353 GLN ILE TYR GLU LYS ILE VAL SER GLY LYS VAL ARG PHE
SEQRES 21 A 353 PRO SER HIS PHE SER SER ASP LEU LYS ASP LEU LEU ARG
SEQRES 22 A 353 ASN LEU LEU GLN VAL ASP LEU THR LYS ARG PHE GLY ASN
SEQRES 23 A 353 LEU LYS ASN GLY VAL ASN ASP ILE LYS ASN HIS LYS TRP
SEQRES 24 A 353 PHE ALA THR THR ASP TRP ILE ALA ILE TYR GLN ARG LYS
SEQRES 25 A 353 VAL GLU ALA PRO PHE ILE PRO LYS PHE LYS GLY PRO GLY
SEQRES 26 A 353 ASP THR SER ASN PHE ASP ASP TYR GLU GLU GLU GLU ILE
SEQRES 27 A 353 ARG VAL SEP ILE ASN GLU LYS CYS GLY LYS GLU PHE THR
SEQRES 28 A 353 GLU PHE
SEQRES 1 C 18 THR THR TYR ALA ASP PHE ILE ALA SER GLY ARG THR GLY
SEQRES 2 C 18 ARG ARG SER ALA ILE
MODRES 6EH3 SEP A 10 SER MODIFIED RESIDUE
MODRES 6EH3 SEP A 139 SER MODIFIED RESIDUE
MODRES 6EH3 TPO A 197 THR MODIFIED RESIDUE
MODRES 6EH3 SEP A 338 SER MODIFIED RESIDUE
HET SEP A 10 14
HET SEP A 139 14
HET TPO A 197 17
HET SEP A 338 14
HET B4Z A 401 42
HETNAM SEP PHOSPHOSERINE
HETNAM TPO PHOSPHOTHREONINE
HETNAM B4Z ~{N}-[2-[(PHENYLMETHYL)AMINO]ETHYL]ISOQUINOLINE-5-
HETNAM 2 B4Z SULFONAMIDE
HETSYN SEP PHOSPHONOSERINE
HETSYN TPO PHOSPHONOTHREONINE
FORMUL 1 SEP 3(C3 H8 N O6 P)
FORMUL 1 TPO C4 H10 N O6 P
FORMUL 3 B4Z C18 H19 N3 O2 S
FORMUL 4 HOH *151(H2 O)
HELIX 1 AA1 GLY A 1 SER A 32 1 32
HELIX 2 AA2 GLN A 39 ASP A 41 5 3
HELIX 3 AA3 LYS A 76 LEU A 82 1 7
HELIX 4 AA4 GLN A 84 VAL A 98 1 15
HELIX 5 AA5 GLU A 127 GLY A 136 1 10
HELIX 6 AA6 SEP A 139 LEU A 160 1 22
HELIX 7 AA7 LYS A 168 GLU A 170 5 3
HELIX 8 AA8 THR A 201 LEU A 205 5 5
HELIX 9 AA9 ALA A 206 LEU A 211 1 6
HELIX 10 AB1 LYS A 217 GLY A 234 1 18
HELIX 11 AB2 GLN A 242 SER A 252 1 11
HELIX 12 AB3 SER A 262 LEU A 273 1 12
HELIX 13 AB4 VAL A 288 ASN A 293 1 6
HELIX 14 AB5 HIS A 294 ALA A 298 5 5
HELIX 15 AB6 ASP A 301 GLN A 307 1 7
HELIX 16 AB7 THR C 9 SER C 16 1 8
SHEET 1 AA1 5 PHE A 43 THR A 51 0
SHEET 2 AA1 5 GLY A 55 HIS A 62 -1 O VAL A 57 N LEU A 49
SHEET 3 AA1 5 HIS A 68 ASP A 75 -1 O MET A 71 N MET A 58
SHEET 4 AA1 5 ASN A 115 GLU A 121 -1 O MET A 120 N ALA A 70
SHEET 5 AA1 5 LEU A 106 LYS A 111 -1 N PHE A 108 O VAL A 119
SHEET 1 AA2 2 LEU A 162 ILE A 163 0
SHEET 2 AA2 2 LYS A 189 ARG A 190 -1 O LYS A 189 N ILE A 163
SHEET 1 AA3 2 LEU A 172 ILE A 174 0
SHEET 2 AA3 2 ILE A 180 VAL A 182 -1 O GLN A 181 N LEU A 173
LINK C GLY A 9 N SEP A 10 1555 1555 1.32
LINK C SEP A 10 N GLU A 11 1555 1555 1.34
LINK C PHE A 138 N SEP A 139 1555 1555 1.32
LINK C SEP A 139 N GLU A 140 1555 1555 1.32
LINK C TRP A 196 N TPO A 197 1555 1555 1.34
LINK C TPO A 197 N LEU A 198 1555 1555 1.33
LINK C VAL A 337 N SEP A 338 1555 1555 1.34
LINK C SEP A 338 N ILE A 339 1555 1555 1.34
SITE 1 AC1 14 VAL A 57 ALA A 70 GLU A 121 TYR A 122
SITE 2 AC1 14 VAL A 123 GLU A 127 GLU A 170 ASN A 171
SITE 3 AC1 14 LEU A 173 THR A 183 ASP A 184 PHE A 327
SITE 4 AC1 14 ARG C 21 ARG C 22
CRYST1 58.684 73.526 108.415 90.00 90.00 90.00 P 21 21 21 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.017040 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013601 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009224 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
