HEADER SIGNALING PROTEIN 24-JUN-15 5C79
TITLE PH DOMAIN OF ASAP1 IN COMPLEX WITH DIC4-PTDINS(4,5)P2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ARF-GAP;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: PH DOMAIN;
COMPND 5 SYNONYM: 130 KDA PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE-DEPENDENT ARF1
COMPND 6 GTPASE-ACTIVATING PROTEIN,ADP-RIBOSYLATION FACTOR-DIRECTED GTPASE-
COMPND 7 ACTIVATING PROTEIN 1,ARF GTPASE-ACTIVATING PROTEIN 1,DEVELOPMENT AND
COMPND 8 DIFFERENTIATION-ENHANCING FACTOR 1,DIFFERENTIATION-ENHANCING FACTOR
COMPND 9 1,PIP2-DEPENDENT ARF1 GAP;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: ASAP1, DDEF1, KIAA1249, SHAG1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PH DOMAIN, DIC4-PTDINS(4, 5)P2, SIGNALING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR D.XIA,W.K.TANG
REVDAT 4 06-MAR-24 5C79 1 COMPND REMARK HETNAM
REVDAT 3 16-MAR-16 5C79 1 REMARK
REVDAT 2 18-NOV-15 5C79 1 JRNL
REVDAT 1 07-OCT-15 5C79 0
JRNL AUTH X.JIAN,W.K.TANG,P.ZHAI,N.S.ROY,R.LUO,J.M.GRUSCHUS,M.E.YOHE,
JRNL AUTH 2 P.W.CHEN,Y.LI,R.A.BYRD,D.XIA,P.A.RANDAZZO
JRNL TITL MOLECULAR BASIS FOR COOPERATIVE BINDING OF ANIONIC
JRNL TITL 2 PHOSPHOLIPIDS TO THE PH DOMAIN OF THE ARF GAP ASAP1.
JRNL REF STRUCTURE V. 23 1977 2015
JRNL REFN ISSN 0969-2126
JRNL PMID 26365802
JRNL DOI 10.1016/J.STR.2015.08.008
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0107
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.21
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.1
REMARK 3 NUMBER OF REFLECTIONS : 26014
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.200
REMARK 3 R VALUE (WORKING SET) : 0.198
REMARK 3 FREE R VALUE : 0.233
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1373
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.64
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1447
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 72.67
REMARK 3 BIN R VALUE (WORKING SET) : 0.4740
REMARK 3 BIN FREE R VALUE SET COUNT : 79
REMARK 3 BIN FREE R VALUE : 0.4860
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1665
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 118
REMARK 3 SOLVENT ATOMS : 222
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.52
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.27000
REMARK 3 B22 (A**2) : 0.43000
REMARK 3 B33 (A**2) : -0.09000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.32000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.109
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.106
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.085
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.556
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.960
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.947
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1810 ; 0.012 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 1730 ; 0.007 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2442 ; 1.889 ; 2.019
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4006 ; 1.309 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 205 ; 6.924 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 80 ;35.358 ;24.750
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 334 ;13.832 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 10 ;14.760 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 268 ; 0.091 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1919 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 391 ; 0.006 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 826 ; 2.258 ; 2.531
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 825 ; 2.257 ; 2.528
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1029 ; 3.694 ; 3.785
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1030 ; 3.692 ; 3.788
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 984 ; 2.829 ; 3.026
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 985 ; 2.828 ; 3.028
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 1414 ; 4.489 ; 4.390
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 2110 ; 6.731 ;21.465
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 1996 ; 6.686 ;21.059
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 1
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 334 435 B 334 435 10734 0.17 0.05
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 5C79 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-JUN-15.
REMARK 100 THE DEPOSITION ID IS D_1000211131.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-JUL-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 27403
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
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 (%) : 97.6
REMARK 200 DATA REDUNDANCY : 3.200
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
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: NULL
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 20.96
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.56
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES, PH 7.5, 15% PEG 3350,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 294K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 32.34850
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 302
REMARK 465 GLY A 303
REMARK 465 HIS A 304
REMARK 465 HIS A 305
REMARK 465 HIS A 306
REMARK 465 HIS A 307
REMARK 465 HIS A 308
REMARK 465 HIS A 309
REMARK 465 HIS A 310
REMARK 465 HIS A 311
REMARK 465 HIS A 312
REMARK 465 HIS A 313
REMARK 465 SER A 314
REMARK 465 SER A 315
REMARK 465 GLY A 316
REMARK 465 HIS A 317
REMARK 465 ILE A 318
REMARK 465 ASP A 319
REMARK 465 ASP A 320
REMARK 465 ASP A 321
REMARK 465 LYS A 322
REMARK 465 HIS A 323
REMARK 465 MET A 324
REMARK 465 GLY A 325
REMARK 465 GLY A 326
REMARK 465 TYR A 327
REMARK 465 SER A 328
REMARK 465 MET A 329
REMARK 465 HIS A 330
REMARK 465 GLN A 331
REMARK 465 LEU A 332
REMARK 465 GLN A 333
REMARK 465 PHE A 438
REMARK 465 ARG A 439
REMARK 465 GLY A 440
REMARK 465 GLU A 441
REMARK 465 GLN A 442
REMARK 465 SER A 443
REMARK 465 THR A 444
REMARK 465 GLY A 445
REMARK 465 GLU A 446
REMARK 465 ASN A 447
REMARK 465 SER A 448
REMARK 465 LEU A 449
REMARK 465 GLU A 450
REMARK 465 ASP A 451
REMARK 465 MET B 302
REMARK 465 GLY B 303
REMARK 465 HIS B 304
REMARK 465 HIS B 305
REMARK 465 HIS B 306
REMARK 465 HIS B 307
REMARK 465 HIS B 308
REMARK 465 HIS B 309
REMARK 465 HIS B 310
REMARK 465 HIS B 311
REMARK 465 HIS B 312
REMARK 465 HIS B 313
REMARK 465 SER B 314
REMARK 465 SER B 315
REMARK 465 GLY B 316
REMARK 465 HIS B 317
REMARK 465 ILE B 318
REMARK 465 ASP B 319
REMARK 465 ASP B 320
REMARK 465 ASP B 321
REMARK 465 LYS B 322
REMARK 465 HIS B 323
REMARK 465 MET B 324
REMARK 465 GLY B 325
REMARK 465 GLY B 326
REMARK 465 TYR B 327
REMARK 465 SER B 328
REMARK 465 MET B 329
REMARK 465 HIS B 330
REMARK 465 GLN B 331
REMARK 465 LEU B 332
REMARK 465 GLN B 333
REMARK 465 ALA B 437
REMARK 465 PHE B 438
REMARK 465 ARG B 439
REMARK 465 GLY B 440
REMARK 465 GLU B 441
REMARK 465 GLN B 442
REMARK 465 SER B 443
REMARK 465 THR B 444
REMARK 465 GLY B 445
REMARK 465 GLU B 446
REMARK 465 ASN B 447
REMARK 465 SER B 448
REMARK 465 LEU B 449
REMARK 465 GLU B 450
REMARK 465 ASP B 451
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 GLU A 395 -51.16 -129.85
REMARK 500 ASN B 335 109.14 -161.54
REMARK 500 GLU B 395 -58.95 -138.94
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 PBU A 800
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PBU B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PBU B 503
DBREF 5C79 A 325 451 UNP Q9QWY8 ASAP1_MOUSE 325 451
DBREF 5C79 B 325 451 UNP Q9QWY8 ASAP1_MOUSE 325 451
SEQADV 5C79 MET A 302 UNP Q9QWY8 EXPRESSION TAG
SEQADV 5C79 GLY A 303 UNP Q9QWY8 EXPRESSION TAG
SEQADV 5C79 HIS A 304 UNP Q9QWY8 EXPRESSION TAG
SEQADV 5C79 HIS A 305 UNP Q9QWY8 EXPRESSION TAG
SEQADV 5C79 HIS A 306 UNP Q9QWY8 EXPRESSION TAG
SEQADV 5C79 HIS A 307 UNP Q9QWY8 EXPRESSION TAG
SEQADV 5C79 HIS A 308 UNP Q9QWY8 EXPRESSION TAG
SEQADV 5C79 HIS A 309 UNP Q9QWY8 EXPRESSION TAG
SEQADV 5C79 HIS A 310 UNP Q9QWY8 EXPRESSION TAG
SEQADV 5C79 HIS A 311 UNP Q9QWY8 EXPRESSION TAG
SEQADV 5C79 HIS A 312 UNP Q9QWY8 EXPRESSION TAG
SEQADV 5C79 HIS A 313 UNP Q9QWY8 EXPRESSION TAG
SEQADV 5C79 SER A 314 UNP Q9QWY8 EXPRESSION TAG
SEQADV 5C79 SER A 315 UNP Q9QWY8 EXPRESSION TAG
SEQADV 5C79 GLY A 316 UNP Q9QWY8 EXPRESSION TAG
SEQADV 5C79 HIS A 317 UNP Q9QWY8 EXPRESSION TAG
SEQADV 5C79 ILE A 318 UNP Q9QWY8 EXPRESSION TAG
SEQADV 5C79 ASP A 319 UNP Q9QWY8 EXPRESSION TAG
SEQADV 5C79 ASP A 320 UNP Q9QWY8 EXPRESSION TAG
SEQADV 5C79 ASP A 321 UNP Q9QWY8 EXPRESSION TAG
SEQADV 5C79 LYS A 322 UNP Q9QWY8 EXPRESSION TAG
SEQADV 5C79 HIS A 323 UNP Q9QWY8 EXPRESSION TAG
SEQADV 5C79 MET A 324 UNP Q9QWY8 EXPRESSION TAG
SEQADV 5C79 MET B 302 UNP Q9QWY8 EXPRESSION TAG
SEQADV 5C79 GLY B 303 UNP Q9QWY8 EXPRESSION TAG
SEQADV 5C79 HIS B 304 UNP Q9QWY8 EXPRESSION TAG
SEQADV 5C79 HIS B 305 UNP Q9QWY8 EXPRESSION TAG
SEQADV 5C79 HIS B 306 UNP Q9QWY8 EXPRESSION TAG
SEQADV 5C79 HIS B 307 UNP Q9QWY8 EXPRESSION TAG
SEQADV 5C79 HIS B 308 UNP Q9QWY8 EXPRESSION TAG
SEQADV 5C79 HIS B 309 UNP Q9QWY8 EXPRESSION TAG
SEQADV 5C79 HIS B 310 UNP Q9QWY8 EXPRESSION TAG
SEQADV 5C79 HIS B 311 UNP Q9QWY8 EXPRESSION TAG
SEQADV 5C79 HIS B 312 UNP Q9QWY8 EXPRESSION TAG
SEQADV 5C79 HIS B 313 UNP Q9QWY8 EXPRESSION TAG
SEQADV 5C79 SER B 314 UNP Q9QWY8 EXPRESSION TAG
SEQADV 5C79 SER B 315 UNP Q9QWY8 EXPRESSION TAG
SEQADV 5C79 GLY B 316 UNP Q9QWY8 EXPRESSION TAG
SEQADV 5C79 HIS B 317 UNP Q9QWY8 EXPRESSION TAG
SEQADV 5C79 ILE B 318 UNP Q9QWY8 EXPRESSION TAG
SEQADV 5C79 ASP B 319 UNP Q9QWY8 EXPRESSION TAG
SEQADV 5C79 ASP B 320 UNP Q9QWY8 EXPRESSION TAG
SEQADV 5C79 ASP B 321 UNP Q9QWY8 EXPRESSION TAG
SEQADV 5C79 LYS B 322 UNP Q9QWY8 EXPRESSION TAG
SEQADV 5C79 HIS B 323 UNP Q9QWY8 EXPRESSION TAG
SEQADV 5C79 MET B 324 UNP Q9QWY8 EXPRESSION TAG
SEQRES 1 A 150 MET GLY HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS SER
SEQRES 2 A 150 SER GLY HIS ILE ASP ASP ASP LYS HIS MET GLY GLY TYR
SEQRES 3 A 150 SER MET HIS GLN LEU GLN GLY ASN LYS GLU TYR GLY SER
SEQRES 4 A 150 GLU LYS LYS GLY PHE LEU LEU LYS LYS SER ASP GLY ILE
SEQRES 5 A 150 ARG LYS VAL TRP GLN ARG ARG LYS CYS ALA VAL LYS ASN
SEQRES 6 A 150 GLY ILE LEU THR ILE SER HIS ALA THR SER ASN ARG GLN
SEQRES 7 A 150 PRO ALA LYS LEU ASN LEU LEU THR CYS GLN VAL LYS PRO
SEQRES 8 A 150 ASN ALA GLU ASP LYS LYS SER PHE ASP LEU ILE SER HIS
SEQRES 9 A 150 ASN ARG THR TYR HIS PHE GLN ALA GLU ASP GLU GLN ASP
SEQRES 10 A 150 TYR ILE ALA TRP ILE SER VAL LEU THR ASN SER LYS GLU
SEQRES 11 A 150 GLU ALA LEU THR MET ALA PHE ARG GLY GLU GLN SER THR
SEQRES 12 A 150 GLY GLU ASN SER LEU GLU ASP
SEQRES 1 B 150 MET GLY HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS SER
SEQRES 2 B 150 SER GLY HIS ILE ASP ASP ASP LYS HIS MET GLY GLY TYR
SEQRES 3 B 150 SER MET HIS GLN LEU GLN GLY ASN LYS GLU TYR GLY SER
SEQRES 4 B 150 GLU LYS LYS GLY PHE LEU LEU LYS LYS SER ASP GLY ILE
SEQRES 5 B 150 ARG LYS VAL TRP GLN ARG ARG LYS CYS ALA VAL LYS ASN
SEQRES 6 B 150 GLY ILE LEU THR ILE SER HIS ALA THR SER ASN ARG GLN
SEQRES 7 B 150 PRO ALA LYS LEU ASN LEU LEU THR CYS GLN VAL LYS PRO
SEQRES 8 B 150 ASN ALA GLU ASP LYS LYS SER PHE ASP LEU ILE SER HIS
SEQRES 9 B 150 ASN ARG THR TYR HIS PHE GLN ALA GLU ASP GLU GLN ASP
SEQRES 10 B 150 TYR ILE ALA TRP ILE SER VAL LEU THR ASN SER LYS GLU
SEQRES 11 B 150 GLU ALA LEU THR MET ALA PHE ARG GLY GLU GLN SER THR
SEQRES 12 B 150 GLY GLU ASN SER LEU GLU ASP
HET PBU A 800 39
HET CL B 501 1
HET PBU B 502 39
HET PBU B 503 39
HETNAM PBU (2R)-3-{[(R)-HYDROXY{[(1R,2R,3S,4R,5R,6S)-2,3,6-
HETNAM 2 PBU TRIHYDROXY-4,5-BIS(PHOSPHONOOXY)
HETNAM 3 PBU CYCLOHEXYL]OXY}PHOSPHORYL]OXY}PROPANE-1 ,2-DIYL
HETNAM 4 PBU DIBUTANOATE
HETNAM CL CHLORIDE ION
HETSYN PBU DI-BUTANOYL L-ALPHA-PHOSPHATIDYL-D-MYO-INOSITOL 4,5-
HETSYN 2 PBU BISPHOSPHATE; DI-C4-PIP2
FORMUL 3 PBU 3(C17 H33 O19 P3)
FORMUL 4 CL CL 1-
FORMUL 7 HOH *222(H2 O)
HELIX 1 AA1 GLY A 334 TYR A 338 5 5
HELIX 2 AA2 LEU A 386 CYS A 388 5 3
HELIX 3 AA3 ASP A 415 ALA A 437 1 23
HELIX 4 AA4 LEU B 386 CYS B 388 5 3
HELIX 5 AA5 ASP B 415 MET B 436 1 22
SHEET 1 AA1 7 ALA A 381 ASN A 384 0
SHEET 2 AA1 7 ILE A 368 ILE A 371 -1 N LEU A 369 O LEU A 383
SHEET 3 AA1 7 TRP A 357 LYS A 365 -1 N ALA A 363 O THR A 370
SHEET 4 AA1 7 LYS A 342 LYS A 349 -1 N LEU A 346 O ARG A 360
SHEET 5 AA1 7 ARG A 407 GLN A 412 -1 O GLN A 412 N LEU A 347
SHEET 6 AA1 7 SER A 399 SER A 404 -1 N LEU A 402 O TYR A 409
SHEET 7 AA1 7 GLN A 389 PRO A 392 -1 N GLN A 389 O ILE A 403
SHEET 1 AA2 7 ALA B 381 ASN B 384 0
SHEET 2 AA2 7 ILE B 368 ILE B 371 -1 N LEU B 369 O LEU B 383
SHEET 3 AA2 7 TRP B 357 LYS B 365 -1 N ALA B 363 O THR B 370
SHEET 4 AA2 7 LYS B 342 LYS B 349 -1 N LEU B 346 O ARG B 360
SHEET 5 AA2 7 ARG B 407 GLN B 412 -1 O GLN B 412 N LEU B 347
SHEET 6 AA2 7 SER B 399 SER B 404 -1 N LEU B 402 O TYR B 409
SHEET 7 AA2 7 GLN B 389 PRO B 392 -1 N GLN B 389 O ILE B 403
SITE 1 AC1 21 LYS A 348 SER A 350 ASP A 351 ILE A 353
SITE 2 AC1 21 ARG A 354 GLN A 358 ARG A 360 HIS A 373
SITE 3 AC1 21 ALA A 374 GLN A 389 ARG A 407 HOH A 904
SITE 4 AC1 21 HOH A 905 HOH A 932 HOH A 960 HOH A 962
SITE 5 AC1 21 GLY B 334 LYS B 430 GLU B 431 LEU B 434
SITE 6 AC1 21 PBU B 502
SITE 1 AC2 6 LEU A 386 CYS A 388 LYS A 430 LEU B 386
SITE 2 AC2 6 CYS B 388 LYS B 430
SITE 1 AC3 19 GLN A 389 PRO A 392 LYS A 397 PBU A 800
SITE 2 AC3 19 LYS B 348 SER B 350 ASP B 351 GLY B 352
SITE 3 AC3 19 ILE B 353 GLN B 358 ARG B 360 HIS B 373
SITE 4 AC3 19 ALA B 374 ARG B 378 ARG B 407 HOH B 607
SITE 5 AC3 19 HOH B 648 HOH B 659 HOH B 662
SITE 1 AC4 20 GLY A 334 TRP A 357 ARG A 359 GLU A 414
SITE 2 AC4 20 HOH A 918 HOH A 999 LYS B 349 LYS B 355
SITE 3 AC4 20 TRP B 357 GLN B 412 HOH B 613 HOH B 629
SITE 4 AC4 20 HOH B 638 HOH B 640 HOH B 644 HOH B 660
SITE 5 AC4 20 HOH B 663 HOH B 675 HOH B 683 HOH B 695
CRYST1 37.543 64.697 44.428 90.00 95.63 90.00 P 1 21 1 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 0.026636 0.000000 0.002626 0.00000
SCALE2 0.000000 0.015457 0.000000 0.00000
SCALE3 0.000000 0.000000 0.022617 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
