HEADER TRANSFERASE 12-JUN-12 4AXC
TITLE INOSITOL 1,3,4,5,6-PENTAKISPHOSPHATE 2-KINASE APO FORM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INOSITOL-PENTAKISPHOSPHATE 2-KINASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: INOSITOL-1\,3\,4\,5\,6-PENTAKISPHOSPHATE 2-KINASE, INS(1\,
COMPND 5 3\,4\,5\,6)P5 2-KINASE, ATIPK1, INSP5 2-KINASE;
COMPND 6 EC: 2.7.1.158;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;
SOURCE 3 ORGANISM_COMMON: THALE CRESS;
SOURCE 4 ORGANISM_TAXID: 3702;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: ROSETTA PLYSS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PKLSLT
KEYWDS TRANSFERASE, PHYTIC ACID, PROTEIN KINASE, INOSITIDE SIGNALLING
EXPDTA X-RAY DIFFRACTION
AUTHOR J.I BANOS-SANZ,J.SANZ-APARICIO,B.GONZALEZ
REVDAT 3 20-DEC-23 4AXC 1 REMARK LINK
REVDAT 2 05-SEP-12 4AXC 1 JRNL
REVDAT 1 04-JUL-12 4AXC 0
JRNL AUTH J.I.BANOS-SANZ,J.SANZ-APARICIO,H.WHITFIELD,C.HAMILTON,
JRNL AUTH 2 C.A.BREARLEY,B.GONZALEZ
JRNL TITL CONFORMATIONAL CHANGES UNDERGONE BY INOSITOL
JRNL TITL 2 1,3,4,5,6-PENTAKISPHOSPHATE 2-KINASE UPON SUBSTRATE BINDING:
JRNL TITL 3 THE ROLE OF N-LOBE AND ENANTIOMERIC SUBSTRATE PREFERENCE
JRNL REF J.BIOL.CHEM. V. 287 29237 2012
JRNL REFN ISSN 0021-9258
JRNL PMID 22745128
JRNL DOI 10.1074/JBC.M112.363671
REMARK 2
REMARK 2 RESOLUTION. 2.25 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
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) : 2.25
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 66.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 22011
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) : 0.243
REMARK 3 R VALUE (WORKING SET) : 0.242
REMARK 3 FREE R VALUE : 0.278
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1192
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) : 2.25
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.31
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1460
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2950
REMARK 3 BIN FREE R VALUE SET COUNT : 78
REMARK 3 BIN FREE R VALUE : 0.3800
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3143
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 27
REMARK 3 SOLVENT ATOMS : 74
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 56.51
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.89000
REMARK 3 B22 (A**2) : -1.40000
REMARK 3 B33 (A**2) : -0.49000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.333
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.245
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.203
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 14.591
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.934
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.906
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3229 ; 0.008 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4354 ; 1.700 ; 1.984
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 391 ; 5.954 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 146 ;34.950 ;24.452
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 599 ;19.258 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 19 ;21.082 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 491 ; 0.202 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2372 ; 0.004 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
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 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 9 A 46
REMARK 3 RESIDUE RANGE : A 103 A 148
REMARK 3 ORIGIN FOR THE GROUP (A): -15.7835 -4.2762 -13.1449
REMARK 3 T TENSOR
REMARK 3 T11: 0.2493 T22: 0.0888
REMARK 3 T33: 0.2082 T12: -0.0066
REMARK 3 T13: -0.1245 T23: 0.0437
REMARK 3 L TENSOR
REMARK 3 L11: 4.4212 L22: 9.9819
REMARK 3 L33: 2.3382 L12: 1.0337
REMARK 3 L13: -0.3295 L23: 3.9655
REMARK 3 S TENSOR
REMARK 3 S11: -0.2532 S12: 0.1114 S13: 0.0777
REMARK 3 S21: 0.7050 S22: 0.2517 S23: -0.6914
REMARK 3 S31: 0.3059 S32: 0.2009 S33: 0.0015
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 160 A 378
REMARK 3 RESIDUE RANGE : A 388 A 430
REMARK 3 ORIGIN FOR THE GROUP (A): -34.3878 6.9788 -30.4394
REMARK 3 T TENSOR
REMARK 3 T11: 0.0820 T22: 0.0608
REMARK 3 T33: 0.0790 T12: 0.0090
REMARK 3 T13: -0.0562 T23: 0.0357
REMARK 3 L TENSOR
REMARK 3 L11: 2.7621 L22: 2.2164
REMARK 3 L33: 4.8952 L12: 0.6580
REMARK 3 L13: -2.1330 L23: -0.9559
REMARK 3 S TENSOR
REMARK 3 S11: 0.1427 S12: -0.0371 S13: -0.1897
REMARK 3 S21: -0.0194 S22: -0.3602 S23: -0.2569
REMARK 3 S31: 0.0699 S32: 0.0765 S33: 0.2174
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 4AXC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-JUN-12.
REMARK 100 THE DEPOSITION ID IS D_1290052764.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-DEC-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-4
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97940
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 24181
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.250
REMARK 200 RESOLUTION RANGE LOW (A) : 47.440
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 7.300
REMARK 200 R MERGE (I) : 0.07000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.25
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.31
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.40
REMARK 200 R MERGE FOR SHELL (I) : 0.52000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 2XAN
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.41
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M LITHIUM SULFATE 0.1 M TRIS HCL
REMARK 280 PH 8.0 AND 29%(W/V) PEG 4000, PH 5.6
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 52.90000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 34.11500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 52.90000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 34.11500
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 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 A -4
REMARK 465 GLU A -3
REMARK 465 PHE A -2
REMARK 465 GLU A -1
REMARK 465 LEU A 0
REMARK 465 MET A 1
REMARK 465 GLU A 2
REMARK 465 ASN A 47
REMARK 465 ASP A 48
REMARK 465 LYS A 49
REMARK 465 ALA A 50
REMARK 465 ILE A 51
REMARK 465 LYS A 52
REMARK 465 ASN A 53
REMARK 465 SER A 54
REMARK 465 ASN A 55
REMARK 465 GLY A 56
REMARK 465 VAL A 57
REMARK 465 VAL A 58
REMARK 465 SER A 59
REMARK 465 VAL A 60
REMARK 465 PHE A 152
REMARK 465 SER A 153
REMARK 465 GLN A 154
REMARK 465 GLY A 155
REMARK 465 ILE A 156
REMARK 465 THR A 157
REMARK 465 SER A 158
REMARK 465 GLY A 159
REMARK 465 GLY A 160
REMARK 465 ASP A 161
REMARK 465 LYS A 334
REMARK 465 GLU A 335
REMARK 465 GLY A 336
REMARK 465 ARG A 337
REMARK 465 PRO A 338
REMARK 465 LEU A 339
REMARK 465 GLU A 340
REMARK 465 ALA A 341
REMARK 465 ASP A 382
REMARK 465 SER A 383
REMARK 465 GLU A 384
REMARK 465 PRO A 385
REMARK 465 SER A 386
REMARK 465 GLY A 387
REMARK 465 LYS A 435
REMARK 465 ALA A 436
REMARK 465 GLU A 437
REMARK 465 ASN A 438
REMARK 465 THR A 439
REMARK 465 ALA A 440
REMARK 465 GLU A 441
REMARK 465 GLN A 442
REMARK 465 ILE A 443
REMARK 465 GLY A 444
REMARK 465 ASN A 445
REMARK 465 SER A 446
REMARK 465 LYS A 447
REMARK 465 PRO A 448
REMARK 465 SER A 449
REMARK 465 HIS A 450
REMARK 465 SER A 451
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 23 CA - CB - CG ANGL. DEV. = 15.2 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 ARG A 70 -35.50 -35.04
REMARK 500 LYS A 170 -161.72 66.78
REMARK 500 GLN A 237 -124.08 44.32
REMARK 500 ARG A 259 131.51 -38.71
REMARK 500 ASP A 314 149.14 74.17
REMARK 500 ALA A 380 -29.90 -39.49
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 A2073 DISTANCE = 7.36 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A1435 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 320 ND1
REMARK 620 2 CYS A 330 SG 111.2
REMARK 620 3 CYS A 333 SG 95.5 112.8
REMARK 620 4 HIS A 346 NE2 109.6 118.3 107.0
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1435
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1436
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1437
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1438
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1439
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2XAL RELATED DB: PDB
REMARK 900 LEAD DERIVATIVE OF INOSITOL 1,3,4,5,6- PENTAKISPHOSPHATE 2-KINASE
REMARK 900 FROM A. THALIANA IN COMPLEX WITH ADP AND IP6.
REMARK 900 RELATED ID: 2XAM RELATED DB: PDB
REMARK 900 INOSITOL 1,3,4,5,6-PENTAKISPHOSPHATE 2-KINASE FROM A. THALIANA IN
REMARK 900 COMPLEX WITH ADP AND IP6.
REMARK 900 RELATED ID: 2XAN RELATED DB: PDB
REMARK 900 INOSITOL 1,3,4,5,6-PENTAKISPHOSPHATE 2-KINASE FROM A. THALIANA IN
REMARK 900 COMPLEX WITH AMP PNP AND IP5
REMARK 900 RELATED ID: 2XAO RELATED DB: PDB
REMARK 900 INOSITOL 1,3,4,5,6-PENTAKISPHOSPHATE 2-KINASE FROM A. THALIANA IN
REMARK 900 COMPLEX WITH IP5
REMARK 900 RELATED ID: 2XAR RELATED DB: PDB
REMARK 900 INOSITOL 1,3,4,5,6-PENTAKISPHOSPHATE 2-KINASE FROM A. THALIANA IN
REMARK 900 COMPLEX WITH IP6.
REMARK 900 RELATED ID: 4AQK RELATED DB: PDB
REMARK 900 INOSITOL 1,3,4,5,6-PENTAKISPHOSPHATE 2-KINASE IN COMPLEX WITH ADP
REMARK 900 AND IP6
REMARK 900 RELATED ID: 4AXD RELATED DB: PDB
REMARK 900 INOSITOL 1,3,4,5,6-PENTAKISPHOSPHATE 2-KINASE IN COMPLEX WITH AMPPNP
REMARK 900 RELATED ID: 4AXE RELATED DB: PDB
REMARK 900 INOSITOL 1,3,4,5,6-PENTAKISPHOSPHATE 2-KINASE IN COMPLEX WITH ADP
REMARK 900 RELATED ID: 4AXF RELATED DB: PDB
REMARK 900 INSP5 2-K IN COMPLEX WITH INS(3,4,5,6)P4 PLUS AMPPNP
DBREF 4AXC A 1 451 UNP Q93YN9 IPPK_ARATH 1 451
SEQADV 4AXC GLY A -4 UNP Q93YN9 EXPRESSION TAG
SEQADV 4AXC GLU A -3 UNP Q93YN9 EXPRESSION TAG
SEQADV 4AXC PHE A -2 UNP Q93YN9 EXPRESSION TAG
SEQADV 4AXC GLU A -1 UNP Q93YN9 EXPRESSION TAG
SEQADV 4AXC LEU A 0 UNP Q93YN9 EXPRESSION TAG
SEQADV 4AXC SER A 54 UNP Q93YN9 ALA 54 CONFLICT
SEQADV 4AXC GLN A 90 UNP Q93YN9 LYS 90 CONFLICT
SEQADV 4AXC ALA A 129 UNP Q93YN9 TRP 129 CONFLICT
SEQADV 4AXC THR A 157 UNP Q93YN9 SER 157 CONFLICT
SEQADV 4AXC ILE A 204 UNP Q93YN9 ASN 204 CONFLICT
SEQADV 4AXC ARG A 224 UNP Q93YN9 SER 224 CONFLICT
SEQADV 4AXC CYS A 321 UNP Q93YN9 SER 321 CONFLICT
SEQADV 4AXC ILE A 325 UNP Q93YN9 LEU 325 CONFLICT
SEQADV 4AXC ARG A 337 UNP Q93YN9 LYS 337 CONFLICT
SEQRES 1 A 456 GLY GLU PHE GLU LEU MET GLU MET ILE LEU GLU GLU LYS
SEQRES 2 A 456 ASP ALA SER ASP TRP ILE TYR ARG GLY GLU GLY GLY ALA
SEQRES 3 A 456 ASN LEU VAL LEU ALA TYR ALA GLY SER SER PRO LEU PHE
SEQRES 4 A 456 VAL GLY LYS VAL ILE ARG ILE GLN LYS ALA ARG ARG ASN
SEQRES 5 A 456 ASP LYS ALA ILE LYS ASN SER ASN GLY VAL VAL SER VAL
SEQRES 6 A 456 LEU THR SER ASP GLU GLN HIS LEU TRP ARG GLU ASN ASN
SEQRES 7 A 456 GLU LEU ILE SER SER PRO ASN LYS GLU VAL LEU GLU GLN
SEQRES 8 A 456 ARG TYR VAL GLN ASN VAL ILE ILE PRO LEU LEU GLY PRO
SEQRES 9 A 456 LYS HIS VAL ASP ALA GLY VAL ARG VAL SER VAL SER LYS
SEQRES 10 A 456 GLU PHE LEU GLU CYS VAL ASP LYS LYS VAL THR LYS GLN
SEQRES 11 A 456 ARG PRO LEU ALA ARG VAL ASN ALA ALA ASN VAL ASP THR
SEQRES 12 A 456 SER HIS ASP SER ALA LEU ILE LEU ASN ASP HIS SER LEU
SEQRES 13 A 456 PHE SER GLN GLY ILE THR SER GLY GLY ASP CYS ILE SER
SEQRES 14 A 456 VAL GLU ILE LYS PRO LYS CYS GLY PHE LEU PRO THR SER
SEQRES 15 A 456 ARG PHE ILE GLY LYS GLU ASN MET LEU LYS THR SER VAL
SEQRES 16 A 456 SER ARG PHE LYS MET HIS GLN LEU LEU LYS LEU GLU TYR
SEQRES 17 A 456 ILE GLU ILE SER GLU GLU SER GLU TYR ASP PRO LEU ASP
SEQRES 18 A 456 LEU PHE SER GLY SER LYS GLU ARG VAL LEU GLU ALA ILE
SEQRES 19 A 456 LYS ALA LEU TYR SER THR PRO GLN ASN ASN PHE ARG VAL
SEQRES 20 A 456 PHE LEU ASN GLY SER LEU ILE LEU GLY GLY SER GLY GLU
SEQRES 21 A 456 SER THR GLY ARG THR SER PRO GLU ILE GLY TYR ALA PHE
SEQRES 22 A 456 GLU ASP ALA LEU LYS GLY PHE ILE GLN SER GLU ASP GLY
SEQRES 23 A 456 HIS ARG THR GLU CYS PHE LEU GLN LEU VAL SER ASP ALA
SEQRES 24 A 456 VAL TYR GLY SER GLY VAL LEU ASP ARG LEU LEU GLU ILE
SEQRES 25 A 456 GLN LYS LEU ASP LYS LEU ASP ILE GLU GLY ALA ILE HIS
SEQRES 26 A 456 CYS TYR TYR ASP ILE ILE ASN GLN PRO CYS PRO ILE CYS
SEQRES 27 A 456 LYS GLU GLY ARG PRO LEU GLU ALA GLU LEU SER LEU HIS
SEQRES 28 A 456 ALA LEU PRO LEU ASP GLU SER LEU LYS ILE VAL LYS GLU
SEQRES 29 A 456 TYR LEU ILE ALA ALA THR ALA LYS ASP CYS SER ILE MET
SEQRES 30 A 456 ILE SER PHE GLN SER ARG ASN ALA TRP ASP SER GLU PRO
SEQRES 31 A 456 SER GLY ASP TYR VAL SER LEU LYS PRO THR ASN GLN THR
SEQRES 32 A 456 PHE ASP TYR LYS VAL HIS PHE ILE ASP LEU SER LEU LYS
SEQRES 33 A 456 PRO LEU LYS ARG MET GLU SER TYR TYR LYS LEU ASP LYS
SEQRES 34 A 456 LYS ILE ILE SER PHE TYR ASN ARG LYS GLN LYS ALA GLU
SEQRES 35 A 456 ASN THR ALA GLU GLN ILE GLY ASN SER LYS PRO SER HIS
SEQRES 36 A 456 SER
HET ZN A1435 1
HET SO4 A1436 5
HET SO4 A1437 5
HET SO4 A1438 5
HET SO4 A1439 5
HET GOL A1440 6
HETNAM ZN ZINC ION
HETNAM SO4 SULFATE ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 ZN ZN 2+
FORMUL 3 SO4 4(O4 S 2-)
FORMUL 7 GOL C3 H8 O3
FORMUL 8 HOH *74(H2 O)
HELIX 1 1 LYS A 8 SER A 11 5 4
HELIX 2 2 THR A 62 ARG A 70 1 9
HELIX 3 3 ASN A 72 SER A 77 1 6
HELIX 4 4 ASN A 80 VAL A 92 1 13
HELIX 5 5 ILE A 93 GLY A 98 1 6
HELIX 6 6 PRO A 99 VAL A 102 5 4
HELIX 7 7 SER A 111 ARG A 126 1 16
HELIX 8 8 PRO A 127 VAL A 131 5 5
HELIX 9 9 GLY A 181 SER A 189 5 9
HELIX 10 10 SER A 191 TYR A 203 1 13
HELIX 11 11 ASP A 213 PHE A 218 1 6
HELIX 12 12 SER A 221 THR A 235 1 15
HELIX 13 13 SER A 261 LEU A 272 1 12
HELIX 14 14 HIS A 282 GLY A 299 1 18
HELIX 15 15 GLY A 299 LYS A 309 1 11
HELIX 16 16 ASP A 314 ILE A 326 1 13
HELIX 17 17 PRO A 349 CYS A 369 1 21
HELIX 18 18 PRO A 412 LYS A 414 5 3
HELIX 19 19 ARG A 415 GLN A 434 1 20
SHEET 1 AA 5 TRP A 13 GLU A 18 0
SHEET 2 AA 5 ASN A 22 TYR A 27 -1 O VAL A 24 N ARG A 16
SHEET 3 AA 5 LYS A 37 GLN A 42 -1 O LYS A 37 N TYR A 27
SHEET 4 AA 5 SER A 142 ASN A 147 -1 O LEU A 144 N ARG A 40
SHEET 5 AA 5 VAL A 106 SER A 109 -1 O VAL A 106 N ILE A 145
SHEET 1 AB 6 SER A 247 LEU A 250 0
SHEET 2 AB 6 PHE A 240 LEU A 244 -1 O VAL A 242 N ILE A 249
SHEET 3 AB 6 ILE A 163 ILE A 167 -1 O SER A 164 N PHE A 243
SHEET 4 AB 6 SER A 370 ARG A 378 -1 O ILE A 371 N ILE A 167
SHEET 5 AB 6 GLN A 397 ILE A 406 -1 O THR A 398 N ARG A 378
SHEET 6 AB 6 TYR A 389 LEU A 392 -1 O VAL A 390 N PHE A 399
LINK ND1 HIS A 320 ZN ZN A1435 1555 1555 2.26
LINK SG CYS A 330 ZN ZN A1435 1555 1555 2.37
LINK SG CYS A 333 ZN ZN A1435 1555 1555 2.44
LINK NE2 HIS A 346 ZN ZN A1435 1555 1555 2.05
SITE 1 AC1 4 HIS A 320 CYS A 330 CYS A 333 HIS A 346
SITE 1 AC2 5 GLY A 20 LYS A 43 ALA A 133 ALA A 134
SITE 2 AC2 5 LYS A 309
SITE 1 AC3 5 LYS A 168 LYS A 200 ASN A 238 GLU A 255
SITE 2 AC3 5 HOH A2047
SITE 1 AC4 4 GLY A 19 GLY A 20 ALA A 21 ASN A 22
SITE 1 AC5 5 SER A 374 PHE A 375 GLN A 376 ASP A 400
SITE 2 AC5 5 LYS A 402
CRYST1 105.800 68.230 66.000 90.00 90.00 90.00 P 21 21 2 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 0.009452 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014656 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015152 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
