HEADER TRANSFERASE 08-APR-15 4Z83
TITLE PKAB3 IN COMPLEX WITH PYRROLIDINE INHIBITOR 47A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CAMP-DEPENDENT PROTEIN KINASE CATALYTIC SUBUNIT ALPHA;
COMPND 3 CHAIN: E;
COMPND 4 SYNONYM: PKA C-ALPHA;
COMPND 5 EC: 2.7.11.11;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: CAMP-DEPENDENT PROTEIN KINASE INHIBITOR ALPHA;
COMPND 10 CHAIN: I;
COMPND 11 SYNONYM: PKI-ALPHA,CAMP-DEPENDENT PROTEIN KINASE INHIBITOR,
COMPND 12 MUSCLE/BRAIN ISOFORM;
COMPND 13 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: BOVINE;
SOURCE 4 ORGANISM_TAXID: 9913;
SOURCE 5 GENE: PRKACA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PT7-7;
SOURCE 9 MOL_ID: 2;
SOURCE 10 SYNTHETIC: YES;
SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 12 ORGANISM_COMMON: HUMAN;
SOURCE 13 ORGANISM_TAXID: 9606
KEYWDS INHIBITOR, PROTEIN KINASE, STRUCTURE-GUIDED, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR B.A.LUND,K.A.ALAM,R.A.ENGH
REVDAT 3 10-JAN-24 4Z83 1 REMARK
REVDAT 2 27-JAN-16 4Z83 1 JRNL
REVDAT 1 02-DEC-15 4Z83 0
JRNL AUTH B.S.LAUBER,L.A.HARDEGGER,A.K.ASRAFUL,B.A.LUND,O.DUMELE,
JRNL AUTH 2 M.HARDER,B.KUHN,R.A.ENGH,F.DIEDERICH
JRNL TITL ADDRESSING THE GLYCINE-RICH LOOP OF PROTEIN KINASES BY A
JRNL TITL 2 MULTI-FACETTED INTERACTION NETWORK: INHIBITION OF PKA AND A
JRNL TITL 3 PKB MIMIC.
JRNL REF CHEMISTRY V. 22 211 2016
JRNL REFN ISSN 0947-6539
JRNL PMID 26578105
JRNL DOI 10.1002/CHEM.201503552
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.8.4_1496
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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.61
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.8
REMARK 3 NUMBER OF REFLECTIONS : 68972
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.182
REMARK 3 R VALUE (WORKING SET) : 0.180
REMARK 3 FREE R VALUE : 0.218
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.250
REMARK 3 FREE R VALUE TEST SET COUNT : 3620
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 35.6209 - 5.3254 0.87 2277 131 0.1786 0.2244
REMARK 3 2 5.3254 - 4.2291 0.89 2344 129 0.1347 0.1468
REMARK 3 3 4.2291 - 3.6952 0.90 2335 138 0.1351 0.1688
REMARK 3 4 3.6952 - 3.3576 0.92 2424 131 0.1550 0.2054
REMARK 3 5 3.3576 - 3.1171 0.95 2500 122 0.1591 0.1923
REMARK 3 6 3.1171 - 2.9334 0.96 2503 143 0.1633 0.2004
REMARK 3 7 2.9334 - 2.7866 0.97 2558 140 0.1664 0.2157
REMARK 3 8 2.7866 - 2.6653 0.98 2577 148 0.1760 0.2244
REMARK 3 9 2.6653 - 2.5627 0.98 2565 150 0.1699 0.2357
REMARK 3 10 2.5627 - 2.4743 0.99 2576 149 0.1635 0.2115
REMARK 3 11 2.4743 - 2.3970 0.99 2598 139 0.1640 0.2015
REMARK 3 12 2.3970 - 2.3285 0.99 2590 154 0.1689 0.2056
REMARK 3 13 2.3285 - 2.2672 0.99 2631 144 0.1726 0.2173
REMARK 3 14 2.2672 - 2.2119 0.89 2338 128 0.2054 0.2809
REMARK 3 15 2.2119 - 2.1616 0.98 2561 141 0.2135 0.2053
REMARK 3 16 2.1616 - 2.1156 1.00 2554 149 0.1928 0.2201
REMARK 3 17 2.1156 - 2.0733 0.99 2683 123 0.2026 0.2923
REMARK 3 18 2.0733 - 2.0342 0.98 2568 137 0.2240 0.2481
REMARK 3 19 2.0342 - 1.9978 1.00 2575 159 0.2243 0.2484
REMARK 3 20 1.9978 - 1.9640 1.00 2640 131 0.2455 0.2901
REMARK 3 21 1.9640 - 1.9323 0.98 2554 153 0.2897 0.3373
REMARK 3 22 1.9323 - 1.9026 0.91 2402 138 0.3175 0.3460
REMARK 3 23 1.9026 - 1.8746 0.98 2534 126 0.3330 0.3153
REMARK 3 24 1.8746 - 1.8482 0.99 2637 155 0.3274 0.3850
REMARK 3 25 1.8482 - 1.8232 0.99 2580 133 0.3552 0.3354
REMARK 3 26 1.8232 - 1.7995 0.85 2248 129 0.3203 0.3792
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
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) : 0.250
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.090
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 : 0.026 2996
REMARK 3 ANGLE : 1.013 4055
REMARK 3 CHIRALITY : 0.038 426
REMARK 3 PLANARITY : 0.007 545
REMARK 3 DIHEDRAL : 12.336 1113
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 12
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 14 THROUGH 54 )
REMARK 3 ORIGIN FOR THE GROUP (A): -3.7919 -12.7561 -5.1847
REMARK 3 T TENSOR
REMARK 3 T11: 0.2131 T22: 0.2928
REMARK 3 T33: 0.2841 T12: 0.0685
REMARK 3 T13: 0.0222 T23: 0.0227
REMARK 3 L TENSOR
REMARK 3 L11: 1.2457 L22: 1.4513
REMARK 3 L33: 1.8309 L12: -0.2918
REMARK 3 L13: -0.6978 L23: 0.8480
REMARK 3 S TENSOR
REMARK 3 S11: -0.1966 S12: -0.0495 S13: -0.2463
REMARK 3 S21: -0.1362 S22: 0.0391 S23: -0.3332
REMARK 3 S31: 0.3644 S32: 0.3978 S33: 0.0519
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 55 THROUGH 81 )
REMARK 3 ORIGIN FOR THE GROUP (A): -9.1991 -20.4054 4.1462
REMARK 3 T TENSOR
REMARK 3 T11: 0.4073 T22: 0.2625
REMARK 3 T33: 0.3448 T12: 0.1272
REMARK 3 T13: 0.0388 T23: 0.0689
REMARK 3 L TENSOR
REMARK 3 L11: 2.1755 L22: 1.6852
REMARK 3 L33: 1.9073 L12: 0.0054
REMARK 3 L13: 0.4094 L23: 0.1407
REMARK 3 S TENSOR
REMARK 3 S11: -0.0730 S12: -0.2365 S13: -0.5118
REMARK 3 S21: 0.3226 S22: 0.0822 S23: -0.1727
REMARK 3 S31: 0.7837 S32: 0.2775 S33: 0.0268
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 82 THROUGH 179 )
REMARK 3 ORIGIN FOR THE GROUP (A): -8.5478 -4.5896 1.9666
REMARK 3 T TENSOR
REMARK 3 T11: 0.1861 T22: 0.2342
REMARK 3 T33: 0.2056 T12: 0.0160
REMARK 3 T13: -0.0021 T23: 0.0424
REMARK 3 L TENSOR
REMARK 3 L11: 0.7145 L22: 1.2266
REMARK 3 L33: 1.4816 L12: -0.0738
REMARK 3 L13: -0.2058 L23: 0.5721
REMARK 3 S TENSOR
REMARK 3 S11: -0.0744 S12: -0.0671 S13: -0.0922
REMARK 3 S21: 0.0495 S22: -0.0027 S23: -0.1060
REMARK 3 S31: 0.1591 S32: 0.2499 S33: 0.0682
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 180 THROUGH 198 )
REMARK 3 ORIGIN FOR THE GROUP (A): -15.3184 -2.3949 -7.9210
REMARK 3 T TENSOR
REMARK 3 T11: 0.2535 T22: 0.1981
REMARK 3 T33: 0.1891 T12: -0.0210
REMARK 3 T13: -0.0013 T23: 0.0157
REMARK 3 L TENSOR
REMARK 3 L11: 2.3224 L22: 1.7088
REMARK 3 L33: 2.0169 L12: -0.1823
REMARK 3 L13: 0.0715 L23: 0.4660
REMARK 3 S TENSOR
REMARK 3 S11: 0.0003 S12: 0.1087 S13: -0.0381
REMARK 3 S21: -0.1138 S22: -0.0983 S23: -0.0539
REMARK 3 S31: 0.0239 S32: 0.0975 S33: 0.1224
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 199 THROUGH 233 )
REMARK 3 ORIGIN FOR THE GROUP (A): -19.7058 6.6594 -0.9401
REMARK 3 T TENSOR
REMARK 3 T11: 0.1502 T22: 0.1540
REMARK 3 T33: 0.1783 T12: 0.0087
REMARK 3 T13: -0.0275 T23: 0.0257
REMARK 3 L TENSOR
REMARK 3 L11: 1.7734 L22: 2.3558
REMARK 3 L33: 2.9970 L12: 0.6883
REMARK 3 L13: -0.1474 L23: 1.3513
REMARK 3 S TENSOR
REMARK 3 S11: -0.0128 S12: 0.0157 S13: -0.0162
REMARK 3 S21: -0.0258 S22: -0.0062 S23: 0.1180
REMARK 3 S31: -0.0503 S32: -0.1069 S33: 0.0202
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 234 THROUGH 252 )
REMARK 3 ORIGIN FOR THE GROUP (A): -28.8789 7.5353 6.6205
REMARK 3 T TENSOR
REMARK 3 T11: 0.2063 T22: 0.3506
REMARK 3 T33: 0.2786 T12: -0.0086
REMARK 3 T13: 0.0237 T23: -0.0365
REMARK 3 L TENSOR
REMARK 3 L11: 3.2681 L22: 3.0009
REMARK 3 L33: 4.4513 L12: 0.2146
REMARK 3 L13: 0.3586 L23: 0.7013
REMARK 3 S TENSOR
REMARK 3 S11: -0.0555 S12: -0.1076 S13: -0.1006
REMARK 3 S21: 0.1559 S22: -0.1350 S23: 0.5691
REMARK 3 S31: 0.0911 S32: -0.9422 S33: 0.1532
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 253 THROUGH 279 )
REMARK 3 ORIGIN FOR THE GROUP (A): -17.7724 18.5321 3.9825
REMARK 3 T TENSOR
REMARK 3 T11: 0.2527 T22: 0.1848
REMARK 3 T33: 0.2825 T12: -0.0004
REMARK 3 T13: -0.0284 T23: -0.0080
REMARK 3 L TENSOR
REMARK 3 L11: 3.1181 L22: 2.6854
REMARK 3 L33: 4.3655 L12: -0.3094
REMARK 3 L13: 0.0639 L23: 0.5868
REMARK 3 S TENSOR
REMARK 3 S11: -0.0454 S12: 0.0458 S13: 0.2949
REMARK 3 S21: -0.1175 S22: -0.1053 S23: 0.1822
REMARK 3 S31: -0.5385 S32: -0.1600 S33: 0.0876
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 280 THROUGH 307 )
REMARK 3 ORIGIN FOR THE GROUP (A): -3.8066 14.6753 -1.3402
REMARK 3 T TENSOR
REMARK 3 T11: 0.2155 T22: 0.2662
REMARK 3 T33: 0.2757 T12: -0.0780
REMARK 3 T13: 0.0085 T23: 0.0371
REMARK 3 L TENSOR
REMARK 3 L11: 2.7869 L22: 2.5061
REMARK 3 L33: 1.2041 L12: -0.3728
REMARK 3 L13: -0.6793 L23: 0.8086
REMARK 3 S TENSOR
REMARK 3 S11: -0.0236 S12: 0.0239 S13: 0.3761
REMARK 3 S21: -0.2188 S22: 0.0182 S23: -0.4088
REMARK 3 S31: -0.3430 S32: 0.3397 S33: -0.0545
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 308 THROUGH 327 )
REMARK 3 ORIGIN FOR THE GROUP (A): -0.1050 -3.9528 15.6060
REMARK 3 T TENSOR
REMARK 3 T11: 0.3934 T22: 0.5333
REMARK 3 T33: 0.3772 T12: 0.0446
REMARK 3 T13: -0.1106 T23: 0.0559
REMARK 3 L TENSOR
REMARK 3 L11: 1.0443 L22: 1.8046
REMARK 3 L33: 0.5473 L12: 0.6047
REMARK 3 L13: -0.5553 L23: 0.2842
REMARK 3 S TENSOR
REMARK 3 S11: 0.0878 S12: -0.4723 S13: -0.1898
REMARK 3 S21: 0.9119 S22: -0.1075 S23: -0.6815
REMARK 3 S31: 0.1360 S32: 0.6756 S33: 0.1838
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 328 THROUGH 350 )
REMARK 3 ORIGIN FOR THE GROUP (A): -17.1206 -24.3874 -0.1482
REMARK 3 T TENSOR
REMARK 3 T11: 0.4635 T22: 0.2558
REMARK 3 T33: 0.4527 T12: 0.0060
REMARK 3 T13: 0.1315 T23: 0.0273
REMARK 3 L TENSOR
REMARK 3 L11: 0.4618 L22: 2.7186
REMARK 3 L33: 0.9279 L12: 0.1445
REMARK 3 L13: 0.1539 L23: 1.1943
REMARK 3 S TENSOR
REMARK 3 S11: -0.1623 S12: -0.0645 S13: -0.3729
REMARK 3 S21: 0.2252 S22: -0.1964 S23: 0.3150
REMARK 3 S31: 0.6440 S32: -0.1822 S33: 0.3317
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'I' AND (RESID 1 THROUGH 8 )
REMARK 3 ORIGIN FOR THE GROUP (A): -25.7089 8.2256 19.4900
REMARK 3 T TENSOR
REMARK 3 T11: 0.2898 T22: 0.2660
REMARK 3 T33: 0.1853 T12: -0.0140
REMARK 3 T13: -0.0193 T23: 0.0278
REMARK 3 L TENSOR
REMARK 3 L11: 2.1036 L22: 5.5062
REMARK 3 L33: 3.2319 L12: -0.3335
REMARK 3 L13: 0.0576 L23: 1.4945
REMARK 3 S TENSOR
REMARK 3 S11: -0.1600 S12: 0.0821 S13: 0.2116
REMARK 3 S21: 0.4523 S22: 0.0773 S23: -0.2450
REMARK 3 S31: -0.1044 S32: 0.0048 S33: 0.0544
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'I' AND (RESID 9 THROUGH 20 )
REMARK 3 ORIGIN FOR THE GROUP (A): -24.5927 -3.4436 7.6144
REMARK 3 T TENSOR
REMARK 3 T11: 0.3386 T22: 0.2945
REMARK 3 T33: 0.2462 T12: -0.0513
REMARK 3 T13: -0.0155 T23: 0.0012
REMARK 3 L TENSOR
REMARK 3 L11: 3.6232 L22: 2.7319
REMARK 3 L33: 3.0591 L12: -1.4438
REMARK 3 L13: -0.8755 L23: -1.1727
REMARK 3 S TENSOR
REMARK 3 S11: 0.0908 S12: 0.2876 S13: -0.3231
REMARK 3 S21: -0.3753 S22: 0.0147 S23: 0.1965
REMARK 3 S31: 0.4069 S32: -0.3609 S33: 0.0320
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 4Z83 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 08-APR-15.
REMARK 100 THE DEPOSITION ID IS D_1000208753.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-NOV-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7
REMARK 200 NUMBER OF CRYSTALS USED : NULL
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) : 0.918410
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS NOVEMBER 11, 2013
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 37443
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 35.614
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 200 DATA REDUNDANCY : 3.900
REMARK 200 R MERGE (I) : 0.08579
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.7800
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.82
REMARK 200 COMPLETENESS FOR SHELL (%) : 0.9
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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 2.5.5
REMARK 200 STARTING MODEL: 1RDQ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.28
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: THE DROPLETS, CONTAINING 16 MG/ML
REMARK 280 PKAB3, 25 MM BIS-TRIS-HCL, PH 7.0, 150 MM KCL, 1.5MM OCTANOYL-N-
REMARK 280 METHYLGLUCAMIDE AND 0.8 MM PKI PEPTIDE, WERE EQUILIBRATED
REMARK 280 AGAINST 12-26 % (V/V) METHANOL., VAPOR DIFFUSION, SITTING DROP,
REMARK 280 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 41.28750
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 39.47400
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 30.74550
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 39.47400
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 41.28750
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 30.74550
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: 1900 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15710 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -3.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, I
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 E 1
REMARK 465 ASN E 2
REMARK 465 ALA E 3
REMARK 465 ALA E 4
REMARK 465 ALA E 5
REMARK 465 ALA E 6
REMARK 465 LYS E 7
REMARK 465 LYS E 8
REMARK 465 GLY E 9
REMARK 465 SER E 10
REMARK 465 GLU E 11
REMARK 465 GLN E 12
REMARK 465 GLU E 13
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 E 16 CG CD CE NZ
REMARK 470 LYS E 21 CG CD CE NZ
REMARK 470 GLU E 24 CD OE1 OE2
REMARK 470 LYS E 81 CD CE NZ
REMARK 470 LYS E 83 CE NZ
REMARK 470 GLN E 176 CG CD OE1 NE2
REMARK 470 LYS E 254 CE NZ
REMARK 470 ARG E 256 CZ NH1 NH2
REMARK 470 LYS E 285 NZ
REMARK 470 LYS E 295 CD CE NZ
REMARK 470 LYS E 317 CG CD CE NZ
REMARK 470 PHE E 318 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS E 319 CG CD CE NZ
REMARK 470 GLU E 333 CD OE1 OE2
REMARK 470 GLU E 334 CG CD OE1 OE2
REMARK 470 ASN I 16 CG OD1 ND2
REMARK 470 ASP I 20 C O
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 GLN E 177 CD
REMARK 480 ARG E 308 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 HD21 ASN E 32 O HOH E 514 1.58
REMARK 500 HE1 TRP E 196 O HOH E 516 1.58
REMARK 500 C5 4L7 E 402 O HOH E 681 1.69
REMARK 500 O HOH E 770 O HOH E 810 1.82
REMARK 500 O HOH E 510 O HOH E 743 1.84
REMARK 500 O HOH E 752 O HOH E 792 1.96
REMARK 500 NH2 ARG E 308 O HOH E 501 1.98
REMARK 500 O HOH E 525 O HOH E 629 2.01
REMARK 500 NZ LYS E 279 O HOH E 502 2.02
REMARK 500 O HOH E 511 O HOH E 608 2.07
REMARK 500 O HOH E 595 O HOH E 811 2.10
REMARK 500 NZ LYS E 345 O HOH E 503 2.10
REMARK 500 O HOH E 827 O HOH I 130 2.11
REMARK 500 O HOH E 756 O HOH E 826 2.11
REMARK 500 O HOH E 771 O HOH E 834 2.13
REMARK 500 O HOH E 775 O HOH E 812 2.14
REMARK 500 O HOH E 681 O HOH E 805 2.16
REMARK 500 OG SER E 259 O HOH E 504 2.17
REMARK 500 O HOH E 615 O HOH E 784 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 O HOH E 813 O HOH E 832 4445 1.88
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 ASP E 166 47.25 -145.97
REMARK 500 ASP E 184 73.80 52.50
REMARK 500 LEU E 273 49.76 -83.60
REMARK 500 LYS E 319 47.50 -84.76
REMARK 500 HIS I 19 -1.24 -156.56
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 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH E 841 DISTANCE = 6.15 ANGSTROMS
REMARK 525 HOH E 842 DISTANCE = 6.48 ANGSTROMS
REMARK 525 HOH E 843 DISTANCE = 6.52 ANGSTROMS
REMARK 525 HOH E 844 DISTANCE = 7.29 ANGSTROMS
REMARK 525 HOH E 845 DISTANCE = 7.96 ANGSTROMS
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 4L7 E 402
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 4L7 E 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 4L7 E 402
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1Q61 RELATED DB: PDB
REMARK 900 1Q61 CONTAINS THE APO-FORM
DBREF 4Z83 E 1 350 UNP P00517 KAPCA_BOVIN 2 351
DBREF 4Z83 I 1 20 UNP P61925 IPKA_HUMAN 6 25
SEQADV 4Z83 ALA E 123 UNP P00517 VAL 124 ENGINEERED MUTATION
SEQADV 4Z83 MET E 173 UNP P00517 LEU 174 ENGINEERED MUTATION
SEQADV 4Z83 LYS E 181 UNP P00517 GLN 182 ENGINEERED MUTATION
SEQRES 1 E 350 GLY ASN ALA ALA ALA ALA LYS LYS GLY SER GLU GLN GLU
SEQRES 2 E 350 SER VAL LYS GLU PHE LEU ALA LYS ALA LYS GLU ASP PHE
SEQRES 3 E 350 LEU LYS LYS TRP GLU ASN PRO ALA GLN ASN THR ALA HIS
SEQRES 4 E 350 LEU ASP GLN PHE GLU ARG ILE LYS THR LEU GLY THR GLY
SEQRES 5 E 350 SER PHE GLY ARG VAL MET LEU VAL LYS HIS MET GLU THR
SEQRES 6 E 350 GLY ASN HIS TYR ALA MET LYS ILE LEU ASP LYS GLN LYS
SEQRES 7 E 350 VAL VAL LYS LEU LYS GLN ILE GLU HIS THR LEU ASN GLU
SEQRES 8 E 350 LYS ARG ILE LEU GLN ALA VAL ASN PHE PRO PHE LEU VAL
SEQRES 9 E 350 LYS LEU GLU PHE SER PHE LYS ASP ASN SER ASN LEU TYR
SEQRES 10 E 350 MET VAL MET GLU TYR ALA PRO GLY GLY GLU MET PHE SER
SEQRES 11 E 350 HIS LEU ARG ARG ILE GLY ARG PHE SER GLU PRO HIS ALA
SEQRES 12 E 350 ARG PHE TYR ALA ALA GLN ILE VAL LEU THR PHE GLU TYR
SEQRES 13 E 350 LEU HIS SER LEU ASP LEU ILE TYR ARG ASP LEU LYS PRO
SEQRES 14 E 350 GLU ASN LEU MET ILE ASP GLN GLN GLY TYR ILE LYS VAL
SEQRES 15 E 350 THR ASP PHE GLY PHE ALA LYS ARG VAL LYS GLY ARG THR
SEQRES 16 E 350 TRP TPO LEU CYS GLY THR PRO GLU TYR LEU ALA PRO GLU
SEQRES 17 E 350 ILE ILE LEU SER LYS GLY TYR ASN LYS ALA VAL ASP TRP
SEQRES 18 E 350 TRP ALA LEU GLY VAL LEU ILE TYR GLU MET ALA ALA GLY
SEQRES 19 E 350 TYR PRO PRO PHE PHE ALA ASP GLN PRO ILE GLN ILE TYR
SEQRES 20 E 350 GLU LYS ILE VAL SER GLY LYS VAL ARG PHE PRO SER HIS
SEQRES 21 E 350 PHE SER SER ASP LEU LYS ASP LEU LEU ARG ASN LEU LEU
SEQRES 22 E 350 GLN VAL ASP LEU THR LYS ARG PHE GLY ASN LEU LYS ASN
SEQRES 23 E 350 GLY VAL ASN ASP ILE LYS ASN HIS LYS TRP PHE ALA THR
SEQRES 24 E 350 THR ASP TRP ILE ALA ILE TYR GLN ARG LYS VAL GLU ALA
SEQRES 25 E 350 PRO PHE ILE PRO LYS PHE LYS GLY PRO GLY ASP THR SER
SEQRES 26 E 350 ASN PHE ASP ASP TYR GLU GLU GLU GLU ILE ARG VAL SEP
SEQRES 27 E 350 ILE ASN GLU LYS CYS GLY LYS GLU PHE SER GLU PHE
SEQRES 1 I 20 THR THR TYR ALA ASP PHE ILE ALA SER GLY ARG THR GLY
SEQRES 2 I 20 ARG ARG ASN ALA ILE HIS ASP
MODRES 4Z83 TPO E 197 THR MODIFIED RESIDUE
MODRES 4Z83 SEP E 338 SER MODIFIED RESIDUE
HET TPO E 197 17
HET SEP E 338 14
HET 4L7 E 401 39
HET 4L7 E 402 11
HETNAM TPO PHOSPHOTHREONINE
HETNAM SEP PHOSPHOSERINE
HETNAM 4L7 7-{(3S,4R)-4-[(5-BROMOTHIOPHEN-2-YL)
HETNAM 2 4L7 CARBONYL]PYRROLIDIN-3-YL}QUINAZOLIN-4(3H)-ONE
HETSYN TPO PHOSPHONOTHREONINE
HETSYN SEP PHOSPHONOSERINE
FORMUL 1 TPO C4 H10 N O6 P
FORMUL 1 SEP C3 H8 N O6 P
FORMUL 3 4L7 2(C17 H14 BR N3 O2 S)
FORMUL 5 HOH *375(H2 O)
HELIX 1 AA1 SER E 14 ASN E 32 1 19
HELIX 2 AA2 HIS E 39 ASP E 41 5 3
HELIX 3 AA3 LYS E 76 LEU E 82 1 7
HELIX 4 AA4 GLN E 84 GLN E 96 1 13
HELIX 5 AA5 GLU E 127 GLY E 136 1 10
HELIX 6 AA6 SER E 139 LEU E 160 1 22
HELIX 7 AA7 LYS E 168 GLU E 170 5 3
HELIX 8 AA8 THR E 201 LEU E 205 5 5
HELIX 9 AA9 ALA E 206 LEU E 211 1 6
HELIX 10 AB1 LYS E 217 GLY E 234 1 18
HELIX 11 AB2 GLN E 242 GLY E 253 1 12
HELIX 12 AB3 SER E 262 LEU E 273 1 12
HELIX 13 AB4 VAL E 288 ASN E 293 1 6
HELIX 14 AB5 HIS E 294 ALA E 298 5 5
HELIX 15 AB6 ASP E 301 GLN E 307 1 7
HELIX 16 AB7 THR I 2 ALA I 8 1 7
SHEET 1 AA1 5 PHE E 43 GLY E 52 0
SHEET 2 AA1 5 GLY E 55 HIS E 62 -1 O VAL E 57 N LEU E 49
SHEET 3 AA1 5 HIS E 68 ASP E 75 -1 O ILE E 73 N ARG E 56
SHEET 4 AA1 5 ASN E 115 GLU E 121 -1 O MET E 118 N LYS E 72
SHEET 5 AA1 5 LEU E 106 LYS E 111 -1 N PHE E 110 O TYR E 117
SHEET 1 AA2 2 LEU E 162 ILE E 163 0
SHEET 2 AA2 2 LYS E 189 ARG E 190 -1 O LYS E 189 N ILE E 163
SHEET 1 AA3 2 LEU E 172 ILE E 174 0
SHEET 2 AA3 2 ILE E 180 VAL E 182 -1 O LYS E 181 N MET E 173
LINK C TRP E 196 N TPO E 197 1555 1555 1.33
LINK C TPO E 197 N LEU E 198 1555 1555 1.32
LINK C VAL E 337 N SEP E 338 1555 1555 1.33
LINK C SEP E 338 N ILE E 339 1555 1555 1.33
SITE 1 AC1 20 GLY E 50 THR E 51 GLY E 52 SER E 53
SITE 2 AC1 20 PHE E 54 GLY E 55 VAL E 57 ALA E 70
SITE 3 AC1 20 LEU E 74 VAL E 104 MET E 120 GLU E 121
SITE 4 AC1 20 TYR E 122 ALA E 123 GLU E 127 GLU E 170
SITE 5 AC1 20 MET E 173 THR E 183 ASP E 184 HOH E 535
SITE 1 AC2 8 VAL E 15 PHE E 18 PHE E 100 LEU E 152
SITE 2 AC2 8 GLU E 155 TYR E 306 HOH E 681 HOH E 805
CRYST1 82.575 61.491 78.948 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 0.012110 0.000000 0.000000 0.00000
SCALE2 0.000000 0.016263 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012667 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
