HEADER TRANSFERASE 08-JUN-15 5BX7
TITLE PKA IN COMPLEX WITH A BENZOTHIOPHENE FRAGMENT COMPOUND.
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 ALPHA;
COMPND 9 CHAIN: B;
COMPND 10 FRAGMENT: UNP RESIDUES 6-25;
COMPND 11 SYNONYM: PKI-ALPHA,CAMP-DEPENDENT PROTEIN KINASE INHIBITOR,
COMPND 12 MUSCLE/BRAIN ISOFORM;
COMPND 13 ENGINEERED: YES;
COMPND 14 OTHER_DETAILS: UNP RESIDUES 6-25
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: PRKACA, PKACA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: PRAR;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28B;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 14 ORGANISM_COMMON: HUMAN;
SOURCE 15 ORGANISM_TAXID: 9606
KEYWDS INHIBITOR, PROTEIN KINASE, STRUCTURE-GUIDED, FRAGMENT-BASED,
KEYWDS 2 TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.NARAYANAN,K.A.ALAM,R.A.ENGH
REVDAT 2 10-JAN-24 5BX7 1 REMARK
REVDAT 1 14-SEP-16 5BX7 0
JRNL AUTH D.NARAYANAN,O.A.GANI,K.A.ALAM,R.A.ENGH
JRNL TITL PKA BASED STUDIES OF LIGAND INTERACTIONS WITH A METHIONINE
JRNL TITL 2 GATEKEEPER.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.89 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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.89
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.71
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 3 NUMBER OF REFLECTIONS : 35516
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.178
REMARK 3 R VALUE (WORKING SET) : 0.175
REMARK 3 FREE R VALUE : 0.226
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.180
REMARK 3 FREE R VALUE TEST SET COUNT : 1838
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 37.7100 - 4.4391 0.96 2717 145 0.1417 0.1603
REMARK 3 2 4.4391 - 3.5243 0.98 2669 132 0.1401 0.2117
REMARK 3 3 3.5243 - 3.0790 0.99 2601 158 0.1764 0.2232
REMARK 3 4 3.0790 - 2.7976 0.99 2571 162 0.1782 0.2252
REMARK 3 5 2.7976 - 2.5971 0.99 2628 125 0.1886 0.2246
REMARK 3 6 2.5971 - 2.4440 0.99 2561 173 0.1793 0.2337
REMARK 3 7 2.4440 - 2.3216 1.00 2608 159 0.1857 0.2704
REMARK 3 8 2.3216 - 2.2206 0.99 2581 150 0.1824 0.2325
REMARK 3 9 2.2206 - 2.1351 0.99 2593 128 0.1921 0.2364
REMARK 3 10 2.1351 - 2.0614 0.99 2609 135 0.2053 0.2687
REMARK 3 11 2.0614 - 1.9970 0.99 2585 133 0.2255 0.2896
REMARK 3 12 1.9970 - 1.9399 0.99 2562 128 0.2450 0.3132
REMARK 3 13 1.9399 - 1.8888 0.91 2393 110 0.2486 0.3188
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) : 0.220
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.510
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 : 0.007 3146
REMARK 3 ANGLE : 1.059 4245
REMARK 3 CHIRALITY : 0.042 441
REMARK 3 PLANARITY : 0.005 539
REMARK 3 DIHEDRAL : 14.830 1177
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 5 THROUGH 54 )
REMARK 3 ORIGIN FOR THE GROUP (A): -36.2835 6.0184 -9.4256
REMARK 3 T TENSOR
REMARK 3 T11: 0.0925 T22: 0.2421
REMARK 3 T33: 0.2266 T12: 0.0101
REMARK 3 T13: -0.0177 T23: 0.0061
REMARK 3 L TENSOR
REMARK 3 L11: 1.0601 L22: 1.9225
REMARK 3 L33: 2.4642 L12: -0.1760
REMARK 3 L13: -0.1065 L23: 0.4232
REMARK 3 S TENSOR
REMARK 3 S11: -0.0119 S12: 0.0222 S13: -0.1276
REMARK 3 S21: -0.0822 S22: -0.0212 S23: 0.2528
REMARK 3 S31: 0.2243 S32: -0.2817 S33: 0.0172
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 55 THROUGH 81 )
REMARK 3 ORIGIN FOR THE GROUP (A): -30.2551 19.5913 0.0214
REMARK 3 T TENSOR
REMARK 3 T11: 0.1456 T22: 0.2030
REMARK 3 T33: 0.2008 T12: 0.0290
REMARK 3 T13: -0.0139 T23: -0.0166
REMARK 3 L TENSOR
REMARK 3 L11: 3.6246 L22: 1.0820
REMARK 3 L33: 3.2999 L12: 0.7462
REMARK 3 L13: -2.3171 L23: -0.6305
REMARK 3 S TENSOR
REMARK 3 S11: 0.0611 S12: -0.1903 S13: 0.3389
REMARK 3 S21: 0.1550 S22: 0.0383 S23: 0.0586
REMARK 3 S31: -0.3311 S32: -0.0778 S33: -0.0366
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 82 THROUGH 160 )
REMARK 3 ORIGIN FOR THE GROUP (A): -30.3411 4.4105 -2.2068
REMARK 3 T TENSOR
REMARK 3 T11: 0.0975 T22: 0.1626
REMARK 3 T33: 0.1475 T12: -0.0051
REMARK 3 T13: 0.0011 T23: -0.0245
REMARK 3 L TENSOR
REMARK 3 L11: 0.5211 L22: 1.0801
REMARK 3 L33: 1.4094 L12: -0.3069
REMARK 3 L13: -0.0980 L23: -0.4296
REMARK 3 S TENSOR
REMARK 3 S11: -0.0505 S12: -0.0260 S13: 0.0143
REMARK 3 S21: 0.0449 S22: 0.0482 S23: 0.0877
REMARK 3 S31: 0.0757 S32: -0.2028 S33: -0.0025
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 161 THROUGH 316 )
REMARK 3 ORIGIN FOR THE GROUP (A): -23.4602 -8.2721 -2.4403
REMARK 3 T TENSOR
REMARK 3 T11: 0.2067 T22: 0.1150
REMARK 3 T33: 0.1259 T12: -0.0099
REMARK 3 T13: 0.0129 T23: -0.0183
REMARK 3 L TENSOR
REMARK 3 L11: 1.4077 L22: 1.5372
REMARK 3 L33: 2.2195 L12: -0.0577
REMARK 3 L13: -0.0411 L23: -0.5516
REMARK 3 S TENSOR
REMARK 3 S11: -0.0111 S12: 0.0100 S13: -0.1943
REMARK 3 S21: 0.0000 S22: -0.0223 S23: -0.0079
REMARK 3 S31: 0.4584 S32: -0.0320 S33: 0.0273
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 317 THROUGH 350 )
REMARK 3 ORIGIN FOR THE GROUP (A): -26.8480 19.9224 1.6561
REMARK 3 T TENSOR
REMARK 3 T11: 0.1527 T22: 0.2359
REMARK 3 T33: 0.2574 T12: 0.0262
REMARK 3 T13: -0.0245 T23: -0.0416
REMARK 3 L TENSOR
REMARK 3 L11: 0.6742 L22: 2.9899
REMARK 3 L33: 3.5471 L12: -0.2338
REMARK 3 L13: -0.2609 L23: -1.5419
REMARK 3 S TENSOR
REMARK 3 S11: 0.0189 S12: -0.1808 S13: 0.1704
REMARK 3 S21: 0.3708 S22: -0.0024 S23: -0.1546
REMARK 3 S31: -0.4450 S32: 0.0318 S33: -0.0205
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 5 THROUGH 11 )
REMARK 3 ORIGIN FOR THE GROUP (A): -13.0323 -8.1762 16.1225
REMARK 3 T TENSOR
REMARK 3 T11: 0.1849 T22: 0.2134
REMARK 3 T33: 0.1340 T12: 0.0426
REMARK 3 T13: 0.0435 T23: -0.0190
REMARK 3 L TENSOR
REMARK 3 L11: 3.2529 L22: 9.7732
REMARK 3 L33: 3.3809 L12: 0.0369
REMARK 3 L13: 2.3722 L23: -2.4415
REMARK 3 S TENSOR
REMARK 3 S11: -0.0839 S12: 0.0856 S13: 0.0111
REMARK 3 S21: 0.1939 S22: -0.2072 S23: 0.3416
REMARK 3 S31: 0.1951 S32: -0.1564 S33: 0.3369
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 12 THROUGH 24 )
REMARK 3 ORIGIN FOR THE GROUP (A): -13.8860 3.7237 4.4123
REMARK 3 T TENSOR
REMARK 3 T11: 0.2604 T22: 0.1251
REMARK 3 T33: 0.1794 T12: -0.0098
REMARK 3 T13: 0.0042 T23: -0.0042
REMARK 3 L TENSOR
REMARK 3 L11: 5.9296 L22: 3.5050
REMARK 3 L33: 4.7494 L12: -1.4354
REMARK 3 L13: 1.7670 L23: 0.4066
REMARK 3 S TENSOR
REMARK 3 S11: -0.1963 S12: 0.1173 S13: 0.4157
REMARK 3 S21: -0.3186 S22: 0.0326 S23: -0.4431
REMARK 3 S31: -0.5366 S32: 0.0782 S33: 0.1647
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 5BX7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 09-JUN-15.
REMARK 100 THE DEPOSITION ID IS D_1000210670.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-JUN-13
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) : 0.9184
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 : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 35516
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.890
REMARK 200 RESOLUTION RANGE LOW (A) : 37.710
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 200 DATA REDUNDANCY : 3.400
REMARK 200 R MERGE (I) : 0.06700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.89
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.93
REMARK 200 COMPLETENESS FOR SHELL (%) : 90.1
REMARK 200 DATA REDUNDANCY IN SHELL : 2.70
REMARK 200 R MERGE FOR SHELL (I) : 0.53800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP 11.0
REMARK 200 STARTING MODEL: 3VQH
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.33
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.53
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: THE DROPLETS, CONTAINING 10 MG/ML PKA.
REMARK 280 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, HANGING 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 36.32650
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 40.27000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 37.70850
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 40.27000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 36.32650
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 37.70850
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 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2940 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16700 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 KCAL/MOL
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 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 0
REMARK 465 GLY A 1
REMARK 465 ASN A 2
REMARK 465 ALA A 3
REMARK 465 ALA A 4
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH B 211 O HOH B 216 2.07
REMARK 500 O1P SEP A 10 O HOH A 501 2.11
REMARK 500 NH2 ARG A 308 O HOH A 502 2.13
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 A 594 O HOH A 601 3454 2.14
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 LEU A 82 CA - CB - CG ANGL. DEV. = -14.8 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 LYS A 47 148.21 -174.79
REMARK 500 ASP A 166 41.66 -144.37
REMARK 500 ASP A 184 95.24 66.40
REMARK 500 ASN A 216 -155.87 -142.03
REMARK 500 LYS A 319 63.17 -103.51
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 4W1 A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD B 101
DBREF 5BX7 A 0 349 UNP P17612 KAPCA_HUMAN 1 350
DBREF 5BX7 B 5 24 UNP P61925 IPKA_HUMAN 6 25
SEQADV 5BX7 PHE A 350 UNP P17612 EXPRESSION TAG
SEQRES 1 A 351 MET GLY ASN ALA ALA ALA ALA LYS LYS GLY SEP GLU GLN
SEQRES 2 A 351 GLU SER VAL LYS GLU PHE LEU ALA LYS ALA LYS GLU ASP
SEQRES 3 A 351 PHE LEU LYS LYS TRP GLU SER PRO ALA GLN ASN THR ALA
SEQRES 4 A 351 HIS LEU ASP GLN PHE GLU ARG ILE LYS THR LEU GLY THR
SEQRES 5 A 351 GLY SER PHE GLY ARG VAL MET LEU VAL LYS HIS LYS GLU
SEQRES 6 A 351 THR GLY ASN HIS TYR ALA MET LYS ILE LEU ASP LYS GLN
SEQRES 7 A 351 LYS VAL VAL LYS LEU LYS GLN ILE GLU HIS THR LEU ASN
SEQRES 8 A 351 GLU LYS ARG ILE LEU GLN ALA VAL ASN PHE PRO PHE LEU
SEQRES 9 A 351 VAL LYS LEU GLU PHE SER PHE LYS ASP ASN SER ASN LEU
SEQRES 10 A 351 TYR MET VAL MET GLU TYR VAL PRO GLY GLY GLU MET PHE
SEQRES 11 A 351 SER HIS LEU ARG ARG ILE GLY ARG PHE SER GLU PRO HIS
SEQRES 12 A 351 ALA ARG PHE TYR ALA ALA GLN ILE VAL LEU THR PHE GLU
SEQRES 13 A 351 TYR LEU HIS SER LEU ASP LEU ILE TYR ARG ASP LEU LYS
SEQRES 14 A 351 PRO GLU ASN LEU LEU ILE ASP GLN GLN GLY TYR ILE GLN
SEQRES 15 A 351 VAL THR ASP PHE GLY PHE ALA LYS ARG VAL LYS GLY ARG
SEQRES 16 A 351 THR TRP TPO LEU CYS GLY THR PRO GLU TYR LEU ALA PRO
SEQRES 17 A 351 GLU ILE ILE LEU SER LYS GLY TYR ASN LYS ALA VAL ASP
SEQRES 18 A 351 TRP TRP ALA LEU GLY VAL LEU ILE TYR GLU MET ALA ALA
SEQRES 19 A 351 GLY TYR PRO PRO PHE PHE ALA ASP GLN PRO ILE GLN ILE
SEQRES 20 A 351 TYR GLU LYS ILE VAL SER GLY LYS VAL ARG PHE PRO SER
SEQRES 21 A 351 HIS PHE SER SER ASP LEU LYS ASP LEU LEU ARG ASN LEU
SEQRES 22 A 351 LEU GLN VAL ASP LEU THR LYS ARG PHE GLY ASN LEU LYS
SEQRES 23 A 351 ASN GLY VAL ASN ASP ILE LYS ASN HIS LYS TRP PHE ALA
SEQRES 24 A 351 THR THR ASP TRP ILE ALA ILE TYR GLN ARG LYS VAL GLU
SEQRES 25 A 351 ALA PRO PHE ILE PRO LYS PHE LYS GLY PRO GLY ASP THR
SEQRES 26 A 351 SER ASN PHE ASP ASP TYR GLU GLU GLU GLU ILE ARG VAL
SEQRES 27 A 351 SEP ILE ASN GLU LYS CYS GLY LYS GLU PHE SER GLU PHE
SEQRES 1 B 20 THR THR TYR ALA ASP PHE ILE ALA SER GLY ARG THR GLY
SEQRES 2 B 20 ARG ARG ASN ALA ILE HIS ASP
MODRES 5BX7 SEP A 10 SER MODIFIED RESIDUE
MODRES 5BX7 TPO A 197 THR MODIFIED RESIDUE
MODRES 5BX7 SEP A 338 SER MODIFIED RESIDUE
HET SEP A 10 10
HET TPO A 197 11
HET SEP A 338 10
HET 4W1 A 401 11
HET MPD A 402 8
HET EDO A 403 4
HET MPD B 101 8
HETNAM SEP PHOSPHOSERINE
HETNAM TPO PHOSPHOTHREONINE
HETNAM 4W1 1-BENZOTHIOPHEN-3-YLMETHANOL
HETNAM MPD (4S)-2-METHYL-2,4-PENTANEDIOL
HETNAM EDO 1,2-ETHANEDIOL
HETSYN SEP PHOSPHONOSERINE
HETSYN TPO PHOSPHONOTHREONINE
HETSYN EDO ETHYLENE GLYCOL
FORMUL 1 SEP 2(C3 H8 N O6 P)
FORMUL 1 TPO C4 H10 N O6 P
FORMUL 3 4W1 C9 H8 O S
FORMUL 4 MPD 2(C6 H14 O2)
FORMUL 5 EDO C2 H6 O2
FORMUL 7 HOH *202(H2 O)
HELIX 1 AA1 SEP A 10 SER A 32 1 23
HELIX 2 AA2 HIS A 39 ASP A 41 5 3
HELIX 3 AA3 LYS A 76 LEU A 82 1 7
HELIX 4 AA4 GLN A 84 GLN A 96 1 13
HELIX 5 AA5 GLU A 127 GLY A 136 1 10
HELIX 6 AA6 SER 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 GLY A 253 1 12
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 B 6 ALA B 12 1 7
SHEET 1 AA1 5 PHE A 43 THR A 51 0
SHEET 2 AA1 5 GLY A 55 HIS A 62 -1 O LEU A 59 N LYS A 47
SHEET 3 AA1 5 HIS A 68 ASP A 75 -1 O ILE A 73 N ARG A 56
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 GLU A 107 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 1.34
LINK C SEP A 10 N GLU A 11 1555 1555 1.33
LINK C TRP A 196 N TPO A 197 1555 1555 1.33
LINK C TPO A 197 N LEU A 198 1555 1555 1.33
LINK C VAL A 337 N SEP A 338 1555 1555 1.33
LINK C SEP A 338 N ILE A 339 1555 1555 1.33
SITE 1 AC1 6 VAL A 57 ALA A 70 GLU A 121 VAL A 123
SITE 2 AC1 6 GLU A 127 LEU A 173
SITE 1 AC2 3 ARG A 134 ASN A 326 ASP A 328
SITE 1 AC3 1 GLU A 155
SITE 1 AC4 3 GLU A 86 ALA A 233 TYR B 7
CRYST1 72.653 75.417 80.540 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 0.013764 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013260 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012416 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
