HEADER TRANSFERASE 14-DEC-15 5FBQ
TITLE PI4KB IN COMPLEX WITH RAB11 AND THE MI358 INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHOSPHATIDYLINOSITOL 4-KINASE BETA,PHOSPHATIDYLINOSITOL 4-
COMPND 3 KINASE BETA;
COMPND 4 CHAIN: A;
COMPND 5 FRAGMENT: UNP RESIDUES 128-422, 523-799;
COMPND 6 SYNONYM: PTDINS 4-KINASE BETA,NPIK,PI4K92,PI4KB,PTDINS 4-KINASE BETA,
COMPND 7 NPIK,PI4K92,PI4KB;
COMPND 8 EC: 2.7.1.67,2.7.1.67;
COMPND 9 ENGINEERED: YES;
COMPND 10 MOL_ID: 2;
COMPND 11 MOLECULE: RAS-RELATED PROTEIN RAB-11A;
COMPND 12 CHAIN: B;
COMPND 13 SYNONYM: RAB-11,YL8;
COMPND 14 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: PI4KB, PIK4CB;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 10 ORGANISM_COMMON: HUMAN;
SOURCE 11 ORGANISM_TAXID: 9606;
SOURCE 12 GENE: RAB11A, RAB11;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS INHIBITOR, COMPLEX, KINASE, LIPID, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.CHALUPSKA,I.MEJDROVA,R.NENCKA,E.BOURA
REVDAT 2 10-JAN-24 5FBQ 1 REMARK
REVDAT 1 28-DEC-16 5FBQ 0
JRNL AUTH D.CHALUPSKA,I.MEJDROVA,R.NENCKA,E.BOURA
JRNL TITL PI4KB IN COMPLEX WITH RAB11 AND THE MI358 INHIBITOR
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 3.79 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) : 3.79
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.85
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.1
REMARK 3 NUMBER OF REFLECTIONS : 9439
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.251
REMARK 3 R VALUE (WORKING SET) : 0.248
REMARK 3 FREE R VALUE : 0.302
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.990
REMARK 3 FREE R VALUE TEST SET COUNT : 471
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 48.8534 - 5.4636 0.96 3105 163 0.2214 0.2910
REMARK 3 2 5.4636 - 4.3375 0.97 2972 157 0.2604 0.3185
REMARK 3 3 4.3375 - 3.7894 0.95 2891 151 0.3048 0.3049
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) : 0.440
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 33.270
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 : 0.003 5125
REMARK 3 ANGLE : 0.890 6944
REMARK 3 CHIRALITY : 0.030 797
REMARK 3 PLANARITY : 0.008 868
REMARK 3 DIHEDRAL : 15.600 1876
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 5FBQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-DEC-15.
REMARK 100 THE DEPOSITION ID IS D_1000216343.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-MAY-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
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) : 0.9796
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 : 9508
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.780
REMARK 200 RESOLUTION RANGE LOW (A) : 48.850
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.3
REMARK 200 DATA REDUNDANCY : 5.400
REMARK 200 R MERGE (I) : 0.21100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.3300
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.78
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.92
REMARK 200 COMPLETENESS FOR SHELL (%) : 91.5
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 : 1.450
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASES
REMARK 200 STARTING MODEL: 4D0L
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.32
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.58
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M MAGNESIUM CHLORIDE, 0.1M TRIS
REMARK 280 PH=7, 10% (W/V) PEG 8000, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 291K
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 24.37950
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 94.24300
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 50.57750
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 94.24300
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 24.37950
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 50.57750
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: 2120 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 29840 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 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 ASP A 222
REMARK 465 MET A 223
REMARK 465 HIS A 224
REMARK 465 ILE A 225
REMARK 465 SER A 226
REMARK 465 THR A 227
REMARK 465 GLN A 228
REMARK 465 ARG A 229
REMARK 465 HIS A 230
REMARK 465 SER A 231
REMARK 465 LEU A 244A
REMARK 465 LYS A 244B
REMARK 465 PRO A 244C
REMARK 465 ALA A 244D
REMARK 465 HIS A 244E
REMARK 465 ARG A 244F
REMARK 465 LYS A 244G
REMARK 465 ARG A 244H
REMARK 465 GLU A 244I
REMARK 465 LEU A 244J
REMARK 465 PRO A 244K
REMARK 465 SER A 244L
REMARK 465 LEU A 244M
REMARK 465 SER A 244N
REMARK 465 PRO A 244O
REMARK 465 ALA A 244P
REMARK 465 PRO A 244Q
REMARK 465 ASP A 244R
REMARK 465 THR A 244S
REMARK 465 GLY A 244T
REMARK 465 LEU A 244U
REMARK 465 SER A 244V
REMARK 465 PRO A 244W
REMARK 465 SER A 244X
REMARK 465 LYS A 244Y
REMARK 465 ARG A 244Z
REMARK 465 THR A 245A
REMARK 465 HIS A 245B
REMARK 465 GLN A 245C
REMARK 465 ARG A 245D
REMARK 465 SER A 245E
REMARK 465 LYS A 245F
REMARK 465 SER A 245G
REMARK 465 ASP A 245H
REMARK 465 ALA A 245I
REMARK 465 THR A 245J
REMARK 465 ALA A 245K
REMARK 465 SER A 245L
REMARK 465 ILE A 245M
REMARK 465 SER A 245N
REMARK 465 LEU A 245O
REMARK 465 SER A 245P
REMARK 465 SER A 245Q
REMARK 465 ASN A 245R
REMARK 465 LEU A 245S
REMARK 465 LYS A 245T
REMARK 465 ARG A 245U
REMARK 465 THR A 245V
REMARK 465 ALA A 245W
REMARK 465 SER A 245X
REMARK 465 ASN A 245Y
REMARK 465 PRO A 245Z
REMARK 465 LYS A 246A
REMARK 465 VAL A 246B
REMARK 465 GLU A 246C
REMARK 465 ASN A 246D
REMARK 465 GLU A 246E
REMARK 465 ASP A 246F
REMARK 465 GLU A 246G
REMARK 465 GLU A 246H
REMARK 465 LEU A 246I
REMARK 465 SER A 246J
REMARK 465 SER A 246K
REMARK 465 SER A 246L
REMARK 465 THR A 246M
REMARK 465 GLU A 246N
REMARK 465 SER A 246O
REMARK 465 ILE A 246P
REMARK 465 ASP A 246Q
REMARK 465 ASN A 246R
REMARK 465 SER A 246S
REMARK 465 PHE A 246T
REMARK 465 SER A 246U
REMARK 465 SER A 246V
REMARK 465 PRO A 246W
REMARK 465 VAL A 246X
REMARK 465 ARG A 522
REMARK 465 ARG A 523
REMARK 465 ASP A 524
REMARK 465 PRO A 525
REMARK 465 GLU A 526
REMARK 465 ASP A 527
REMARK 465 PRO A 528
REMARK 465 SER A 529
REMARK 465 ALA A 530
REMARK 465 PRO A 698
REMARK 465 ARG A 699
REMARK 465 ASN A 700
REMARK 465 LEU A 701
REMARK 465 GLY A 702
REMARK 465 PHE A 703
REMARK 465 GLU A 704
REMARK 465 THR A 705
REMARK 465 SER A 706
REMARK 465 ALA A 707
REMARK 465 GLY B -4
REMARK 465 ALA B -3
REMARK 465 MET B -2
REMARK 465 GLY B -1
REMARK 465 SER B 0
REMARK 465 MET B 1
REMARK 465 GLY B 2
REMARK 465 THR B 3
REMARK 465 ARG B 4
REMARK 465 ASP B 5
REMARK 465 ASP B 6
REMARK 465 GLU B 7
REMARK 465 TYR B 8
REMARK 465 ALA B 68
REMARK 465 GLY B 69
REMARK 465 GLN B 70
REMARK 465 GLU B 71
REMARK 465 ARG B 72
REMARK 465 TYR B 73
REMARK 465 SER B 177
REMARK 465 GLN B 178
REMARK 465 LYS B 179
REMARK 465 GLN B 180
REMARK 465 MET B 181
REMARK 465 SER B 182
REMARK 465 ASP B 183
REMARK 465 ARG B 184
REMARK 465 ARG B 185
REMARK 465 GLU B 186
REMARK 465 ASN B 187
REMARK 465 ASP B 188
REMARK 465 MET B 189
REMARK 465 SER B 190
REMARK 465 PRO B 191
REMARK 465 SER B 192
REMARK 465 ASN B 193
REMARK 465 ASN B 194
REMARK 465 VAL B 195
REMARK 465 VAL B 196
REMARK 465 PRO B 197
REMARK 465 ILE B 198
REMARK 465 HIS B 199
REMARK 465 VAL B 200
REMARK 465 PRO B 201
REMARK 465 PRO B 202
REMARK 465 THR B 203
REMARK 465 THR B 204
REMARK 465 GLU B 205
REMARK 465 ASN B 206
REMARK 465 LYS B 207
REMARK 465 PRO B 208
REMARK 465 LYS B 209
REMARK 465 VAL B 210
REMARK 465 GLN B 211
REMARK 465 CYS B 212
REMARK 465 CYS B 213
REMARK 465 GLN B 214
REMARK 465 ASN B 215
REMARK 465 ILE B 216
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 ASP A 243 CG OD1 OD2
REMARK 470 GLU A 244 CG CD OE1 OE2
REMARK 470 ASN A 406 CG OD1 ND2
REMARK 470 GLU A 587 CG CD OE1 OE2
REMARK 470 ASP A 606 CG OD1 OD2
REMARK 470 TYR B 10 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS B 24 CG CD CE NZ
REMARK 470 ARG B 30 CG CD NE CZ NH1 NH2
REMARK 470 PHE B 31 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU B 35 CG CD OE1 OE2
REMARK 470 LYS B 41 CG CD CE NZ
REMARK 470 ARG B 74 CG CD NE CZ NH1 NH2
REMARK 470 TYR B 81 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU B 103 CG CD OE1 OE2
REMARK 470 ARG B 104 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 125 CG CD CE NZ
REMARK 470 ARG B 129 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 144 CG CD OE1 OE2
REMARK 470 LYS B 145 CG CD CE NZ
REMARK 470 ASP B 157 CG OD1 OD2
REMARK 470 ARG B 174 CG CD NE CZ NH1 NH2
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 OH TYR A 598 O ILE A 688 2.19
REMARK 500 O PHE B 31 NH1 ARG B 51 2.19
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 PRO A 349 C - N - CD ANGL. DEV. = -26.3 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 347 38.99 -92.14
REMARK 500 LYS A 379 63.42 -114.62
REMARK 500 ARG A 590 66.58 -119.44
REMARK 500 PRO A 592 39.78 -86.37
REMARK 500 ILE A 688 -34.98 -134.45
REMARK 500 PHE A 690 30.97 -92.66
REMARK 500 PHE A 692 70.47 63.91
REMARK 500 LEU A 694 -125.91 59.98
REMARK 500 LEU A 710 78.48 -106.51
REMARK 500 LYS B 125 45.44 73.03
REMARK 500 ASN B 146 -163.18 -110.70
REMARK 500 TYR B 173 -15.70 -48.55
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLU B 47 PHE B 48 148.59
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 5W6 A 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GDP B 301
DBREF 5FBQ A 128 522 UNP Q9UBF8 PI4KB_HUMAN 128 422
DBREF 5FBQ A 523 799 UNP Q9UBF8 PI4KB_HUMAN 523 799
DBREF 5FBQ B 1 216 UNP P62491 RB11A_HUMAN 1 216
SEQADV 5FBQ GLY B -4 UNP P62491 EXPRESSION TAG
SEQADV 5FBQ ALA B -3 UNP P62491 EXPRESSION TAG
SEQADV 5FBQ MET B -2 UNP P62491 EXPRESSION TAG
SEQADV 5FBQ GLY B -1 UNP P62491 EXPRESSION TAG
SEQADV 5FBQ SER B 0 UNP P62491 EXPRESSION TAG
SEQRES 1 A 572 SER TRP LEU LEU ARG LEU PHE GLU SER LYS LEU PHE ASP
SEQRES 2 A 572 ILE SER MET ALA ILE SER TYR LEU TYR ASN SER LYS GLU
SEQRES 3 A 572 PRO GLY VAL GLN ALA TYR ILE GLY ASN ARG LEU PHE CYS
SEQRES 4 A 572 PHE ARG ASN GLU ASP VAL ASP PHE TYR LEU PRO GLN LEU
SEQRES 5 A 572 LEU ASN MET TYR ILE HIS MET ASP GLU ASP VAL GLY ASP
SEQRES 6 A 572 ALA ILE LYS PRO TYR ILE VAL HIS ARG CYS ARG GLN SER
SEQRES 7 A 572 ILE ASN PHE SER LEU GLN CYS ALA LEU LEU LEU GLY ALA
SEQRES 8 A 572 TYR SER SER ASP MET HIS ILE SER THR GLN ARG HIS SER
SEQRES 9 A 572 ARG GLY THR LYS LEU ARG LYS LEU ILE LEU SER ASP GLU
SEQRES 10 A 572 LEU LYS PRO ALA HIS ARG LYS ARG GLU LEU PRO SER LEU
SEQRES 11 A 572 SER PRO ALA PRO ASP THR GLY LEU SER PRO SER LYS ARG
SEQRES 12 A 572 THR HIS GLN ARG SER LYS SER ASP ALA THR ALA SER ILE
SEQRES 13 A 572 SER LEU SER SER ASN LEU LYS ARG THR ALA SER ASN PRO
SEQRES 14 A 572 LYS VAL GLU ASN GLU ASP GLU GLU LEU SER SER SER THR
SEQRES 15 A 572 GLU SER ILE ASP ASN SER PHE SER SER PRO VAL ARG LEU
SEQRES 16 A 572 ALA PRO GLU ARG GLU PHE ILE LYS SER LEU MET ALA ILE
SEQRES 17 A 572 GLY LYS ARG LEU ALA THR LEU PRO THR LYS GLU GLN LYS
SEQRES 18 A 572 THR GLN ARG LEU ILE SER GLU LEU SER LEU LEU ASN HIS
SEQRES 19 A 572 LYS LEU PRO ALA ARG VAL TRP LEU PRO THR ALA GLY PHE
SEQRES 20 A 572 ASP HIS HIS VAL VAL ARG VAL PRO HIS THR GLN ALA VAL
SEQRES 21 A 572 VAL LEU ASN SER LYS ASP LYS ALA PRO TYR LEU ILE TYR
SEQRES 22 A 572 VAL GLU VAL LEU GLU CYS GLU ASN PHE ASP THR THR SER
SEQRES 23 A 572 VAL PRO ALA ARG ILE PRO GLU ASN ARG ARG ASP PRO GLU
SEQRES 24 A 572 ASP PRO SER ALA VAL ALA LEU LYS GLU PRO TRP GLN GLU
SEQRES 25 A 572 LYS VAL ARG ARG ILE ARG GLU GLY SER PRO TYR GLY HIS
SEQRES 26 A 572 LEU PRO ASN TRP ARG LEU LEU SER VAL ILE VAL LYS CYS
SEQRES 27 A 572 GLY ASP ASP LEU ARG GLN GLU LEU LEU ALA PHE GLN VAL
SEQRES 28 A 572 LEU LYS GLN LEU GLN SER ILE TRP GLU GLN GLU ARG VAL
SEQRES 29 A 572 PRO LEU TRP ILE LYS PRO TYR LYS ILE LEU VAL ILE SER
SEQRES 30 A 572 ALA ASP SER GLY MET ILE GLU PRO VAL VAL ASN ALA VAL
SEQRES 31 A 572 SER ILE HIS GLN VAL LYS LYS GLN SER GLN LEU SER LEU
SEQRES 32 A 572 LEU ASP TYR PHE LEU GLN GLU HIS GLY SER TYR THR THR
SEQRES 33 A 572 GLU ALA PHE LEU SER ALA GLN ARG ASN PHE VAL GLN SER
SEQRES 34 A 572 CYS ALA GLY TYR CYS LEU VAL CYS TYR LEU LEU GLN VAL
SEQRES 35 A 572 LYS ASP ARG HIS ASN GLY ASN ILE LEU LEU ASP ALA GLU
SEQRES 36 A 572 GLY HIS ILE ILE HIS ILE ASP PHE GLY PHE ILE LEU SER
SEQRES 37 A 572 SER SER PRO ARG ASN LEU GLY PHE GLU THR SER ALA PHE
SEQRES 38 A 572 LYS LEU THR THR GLU PHE VAL ASP VAL MET GLY GLY LEU
SEQRES 39 A 572 ASP GLY ASP MET PHE ASN TYR TYR LYS MET LEU MET LEU
SEQRES 40 A 572 GLN GLY LEU ILE ALA ALA ARG LYS HIS MET ASP LYS VAL
SEQRES 41 A 572 VAL GLN ILE VAL GLU ILE MET GLN GLN GLY SER GLN LEU
SEQRES 42 A 572 PRO CYS PHE HIS GLY SER SER THR ILE ARG ASN LEU LYS
SEQRES 43 A 572 GLU ARG PHE HIS MET SER MET THR GLU GLU GLN LEU GLN
SEQRES 44 A 572 LEU LEU VAL GLU GLN MET VAL ASP GLY SER MET ARG SER
SEQRES 1 B 221 GLY ALA MET GLY SER MET GLY THR ARG ASP ASP GLU TYR
SEQRES 2 B 221 ASP TYR LEU PHE LYS VAL VAL LEU ILE GLY ASP SER GLY
SEQRES 3 B 221 VAL GLY LYS SER ASN LEU LEU SER ARG PHE THR ARG ASN
SEQRES 4 B 221 GLU PHE ASN LEU GLU SER LYS SER THR ILE GLY VAL GLU
SEQRES 5 B 221 PHE ALA THR ARG SER ILE GLN VAL ASP GLY LYS THR ILE
SEQRES 6 B 221 LYS ALA GLN ILE TRP ASP THR ALA GLY GLN GLU ARG TYR
SEQRES 7 B 221 ARG ALA ILE THR SER ALA TYR TYR ARG GLY ALA VAL GLY
SEQRES 8 B 221 ALA LEU LEU VAL TYR ASP ILE ALA LYS HIS LEU THR TYR
SEQRES 9 B 221 GLU ASN VAL GLU ARG TRP LEU LYS GLU LEU ARG ASP HIS
SEQRES 10 B 221 ALA ASP SER ASN ILE VAL ILE MET LEU VAL GLY ASN LYS
SEQRES 11 B 221 SER ASP LEU ARG HIS LEU ARG ALA VAL PRO THR ASP GLU
SEQRES 12 B 221 ALA ARG ALA PHE ALA GLU LYS ASN GLY LEU SER PHE ILE
SEQRES 13 B 221 GLU THR SER ALA LEU ASP SER THR ASN VAL GLU ALA ALA
SEQRES 14 B 221 PHE GLN THR ILE LEU THR GLU ILE TYR ARG ILE VAL SER
SEQRES 15 B 221 GLN LYS GLN MET SER ASP ARG ARG GLU ASN ASP MET SER
SEQRES 16 B 221 PRO SER ASN ASN VAL VAL PRO ILE HIS VAL PRO PRO THR
SEQRES 17 B 221 THR GLU ASN LYS PRO LYS VAL GLN CYS CYS GLN ASN ILE
HET 5W6 A 801 37
HET GDP B 301 40
HETNAM 5W6 ~{N}-[2-[[6-CHLORANYL-3-[3-[4-(HYDROXYMETHYL)PIPERIDIN-
HETNAM 2 5W6 1-YL]SULFONYL-4-METHOXY-PHENYL]-2-METHYL-IMIDAZO[1,2-
HETNAM 3 5W6 B]PYRIDAZIN-8-YL]AMINO]ETHYL]ETHANAMIDE
HETNAM GDP GUANOSINE-5'-DIPHOSPHATE
FORMUL 3 5W6 C24 H31 CL N6 O5 S
FORMUL 4 GDP C10 H15 N5 O11 P2
HELIX 1 AA1 SER A 128 GLU A 135 1 8
HELIX 2 AA2 ASP A 140 SER A 151 1 12
HELIX 3 AA3 GLU A 153 LEU A 164 1 12
HELIX 4 AA4 PHE A 165 PHE A 167 5 3
HELIX 5 AA5 ARG A 168 PHE A 174 1 7
HELIX 6 AA6 TYR A 175 MET A 186 1 12
HELIX 7 AA7 ASP A 187 SER A 205 1 19
HELIX 8 AA8 SER A 205 TYR A 219 1 15
HELIX 9 AA9 GLY A 233 SER A 242 1 10
HELIX 10 AB1 LEU A 307 LEU A 324 1 18
HELIX 11 AB2 ALA A 325 LEU A 327 5 3
HELIX 12 AB3 THR A 329 LYS A 347 1 19
HELIX 13 AB4 PRO A 367 ALA A 371 5 5
HELIX 14 AB5 ASN A 393 THR A 397 5 5
HELIX 15 AB6 PRO A 536 SER A 548 1 13
HELIX 16 AB7 PRO A 549 LEU A 553 5 5
HELIX 17 AB8 LEU A 569 GLU A 589 1 21
HELIX 18 AB9 ILE A 619 GLN A 627 1 9
HELIX 19 AC1 SER A 629 GLY A 639 1 11
HELIX 20 AC2 THR A 643 LEU A 667 1 25
HELIX 21 AC3 THR A 711 MET A 718 1 8
HELIX 22 AC4 GLY A 723 LYS A 742 1 20
HELIX 23 AC5 HIS A 743 GLN A 755 1 13
HELIX 24 AC6 LEU A 760 HIS A 764 5 5
HELIX 25 AC7 SER A 767 ARG A 775 1 9
HELIX 26 AC8 THR A 781 ARG A 798 1 18
HELIX 27 AC9 GLY B 23 ASN B 34 1 12
HELIX 28 AD1 THR B 77 ARG B 82 5 6
HELIX 29 AD2 LYS B 95 ASN B 101 1 7
HELIX 30 AD3 ASN B 101 ALA B 113 1 13
HELIX 31 AD4 LEU B 128 ARG B 132 5 5
HELIX 32 AD5 PRO B 135 ASN B 146 1 12
HELIX 33 AD6 ASN B 160 ARG B 174 1 15
SHEET 1 AA1 3 HIS A 361 ARG A 365 0
SHEET 2 AA1 3 TYR A 382 GLU A 390 -1 O GLU A 387 N ARG A 365
SHEET 3 AA1 3 VAL A 372 VAL A 373 -1 N VAL A 372 O LEU A 383
SHEET 1 AA2 5 HIS A 361 ARG A 365 0
SHEET 2 AA2 5 TYR A 382 GLU A 390 -1 O GLU A 387 N ARG A 365
SHEET 3 AA2 5 TRP A 556 LYS A 564 -1 O LEU A 559 N VAL A 386
SHEET 4 AA2 5 GLY A 608 ILE A 610 -1 O ILE A 610 N ILE A 562
SHEET 5 AA2 5 ILE A 600 VAL A 602 -1 N LEU A 601 O MET A 609
SHEET 1 AA3 3 ALA A 616 SER A 618 0
SHEET 2 AA3 3 ILE A 677 ASP A 680 -1 O LEU A 679 N VAL A 617
SHEET 3 AA3 3 ILE A 685 HIS A 687 -1 O ILE A 686 N LEU A 678
SHEET 1 AA4 6 GLU B 47 VAL B 55 0
SHEET 2 AA4 6 LYS B 58 ASP B 66 -1 O ASP B 66 N GLU B 47
SHEET 3 AA4 6 TYR B 10 ILE B 17 1 N VAL B 14 O GLN B 63
SHEET 4 AA4 6 GLY B 86 ASP B 92 1 O VAL B 90 N ILE B 17
SHEET 5 AA4 6 VAL B 118 ASN B 124 1 O VAL B 122 N TYR B 91
SHEET 6 AA4 6 SER B 149 THR B 153 1 O SER B 149 N LEU B 121
SITE 1 AC1 15 LEU A 374 TYR A 385 TRP A 537 ILE A 562
SITE 2 AC1 15 LYS A 564 TYR A 598 ILE A 610 GLU A 611
SITE 3 AC1 15 PRO A 612 VAL A 613 VAL A 614 ALA A 616
SITE 4 AC1 15 GLY A 675 ASN A 676 ILE A 688
SITE 1 AC2 16 GLY A 155 GLY B 21 VAL B 22 GLY B 23
SITE 2 AC2 16 LYS B 24 SER B 25 ASN B 26 PHE B 36
SITE 3 AC2 16 LEU B 38 SER B 40 ASN B 124 ASP B 127
SITE 4 AC2 16 LEU B 128 SER B 154 ALA B 155 LEU B 156
CRYST1 48.759 101.155 188.486 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 0.020509 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009886 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005305 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
