HEADER TRANSFERASE 27-JAN-16 5HU3
TITLE DROSOPHILA CAMKII-D136N IN COMPLEX WITH A PHOSPHORYLATED FRAGMENT OF
TITLE 2 THE EAG POTASSIUM CHANNEL AND MG2+/ADP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CALCIUM/CALMODULIN-DEPENDENT PROTEIN KINASE TYPE II ALPHA
COMPND 3 CHAIN;
COMPND 4 CHAIN: A;
COMPND 5 FRAGMENT: UNP RESIDUES 1-283;
COMPND 6 SYNONYM: CAM-KINASE II ALPHA CHAIN;
COMPND 7 EC: 2.7.11.17;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: YES;
COMPND 10 OTHER_DETAILS: CONSTITUTIVELY ACTIVE CAMKII KINASE DOMAIN CONSTRUCT;
COMPND 11 MOL_ID: 2;
COMPND 12 MOLECULE: POTASSIUM VOLTAGE-GATED CHANNEL PROTEIN EAG;
COMPND 13 CHAIN: B;
COMPND 14 FRAGMENT: UNP RESIDUES 768-820;
COMPND 15 SYNONYM: ETHER-A-GO-GO PROTEIN;
COMPND 16 ENGINEERED: YES;
COMPND 17 OTHER_DETAILS: EAG CONSTRUCT INCLUDING THE CAMKII-BINDING MOTIF
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;
SOURCE 3 ORGANISM_COMMON: FRUIT FLY;
SOURCE 4 ORGANISM_TAXID: 7227;
SOURCE 5 GENE: CAMKII, CAM, CG18069;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PETM-11;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;
SOURCE 12 ORGANISM_COMMON: FRUIT FLY;
SOURCE 13 ORGANISM_TAXID: 7227;
SOURCE 14 GENE: EAG, CG10952;
SOURCE 15 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 16 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 18 EXPRESSION_SYSTEM_VECTOR: PRSFDUET
KEYWDS PROTEIN KINASE, POTASSIUM CHANNEL, COMPLEX, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.F.CASTRO-RODRIGUES,J.H.MORAIS-CABRAL
REVDAT 2 13-NOV-19 5HU3 1 JRNL
REVDAT 1 01-FEB-17 5HU3 0
JRNL AUTH A.F.CASTRO-RODRIGUES,Y.ZHAO,F.FONSECA,G.GABANT,M.CADENE,
JRNL AUTH 2 G.A.ROBERTSON,J.H.MORAIS-CABRAL
JRNL TITL THE INTERACTION BETWEEN THE DROSOPHILA EAG POTASSIUM CHANNEL
JRNL TITL 2 AND THE PROTEIN KINASE CAMKII INVOLVES AN EXTENSIVE
JRNL TITL 3 INTERFACE AT THE ACTIVE SITE OF THE KINASE.
JRNL REF J.MOL.BIOL. V. 430 5029 2018
JRNL REFN ESSN 1089-8638
JRNL PMID 30381148
JRNL DOI 10.1016/J.JMB.2018.10.015
REMARK 2
REMARK 2 RESOLUTION. 1.89 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.8.2_1309
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) : 30.08
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 3 NUMBER OF REFLECTIONS : 24034
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.194
REMARK 3 R VALUE (WORKING SET) : 0.192
REMARK 3 FREE R VALUE : 0.228
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.040
REMARK 3 FREE R VALUE TEST SET COUNT : 1211
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 30.0783 - 3.9184 0.96 2534 136 0.1451 0.1826
REMARK 3 2 3.9184 - 3.1112 0.99 2574 132 0.1669 0.2116
REMARK 3 3 3.1112 - 2.7182 1.00 2573 146 0.1893 0.2032
REMARK 3 4 2.7182 - 2.4698 1.00 2533 146 0.2096 0.2497
REMARK 3 5 2.4698 - 2.2928 1.00 2559 130 0.2137 0.2299
REMARK 3 6 2.2928 - 2.1577 0.97 2511 132 0.2548 0.3035
REMARK 3 7 2.1577 - 2.0497 0.99 2517 131 0.2835 0.3176
REMARK 3 8 2.0497 - 1.9605 0.99 2560 132 0.2771 0.3528
REMARK 3 9 1.9605 - 1.8850 0.96 2462 126 0.3974 0.4201
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) : 0.260
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.820
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 31.38
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 48.66
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 : 0.017 2376
REMARK 3 ANGLE : 1.347 3241
REMARK 3 CHIRALITY : 0.081 348
REMARK 3 PLANARITY : 0.007 414
REMARK 3 DIHEDRAL : 16.628 878
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 7 THROUGH 130 )
REMARK 3 ORIGIN FOR THE GROUP (A): 1.8805 9.5317 -6.3974
REMARK 3 T TENSOR
REMARK 3 T11: 0.1690 T22: 0.3329
REMARK 3 T33: 0.3171 T12: -0.0505
REMARK 3 T13: 0.0317 T23: 0.0411
REMARK 3 L TENSOR
REMARK 3 L11: 0.8850 L22: 5.1651
REMARK 3 L33: 5.3543 L12: -0.0002
REMARK 3 L13: 0.5042 L23: 0.1322
REMARK 3 S TENSOR
REMARK 3 S11: 0.0219 S12: -0.1962 S13: -0.0729
REMARK 3 S21: 0.5870 S22: -0.3379 S23: -0.1882
REMARK 3 S31: 0.0476 S32: 0.1123 S33: 0.2241
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 131 THROUGH 272 )
REMARK 3 ORIGIN FOR THE GROUP (A): -4.6424 13.1823 -26.2282
REMARK 3 T TENSOR
REMARK 3 T11: 0.4514 T22: 0.3007
REMARK 3 T33: 0.3368 T12: 0.0641
REMARK 3 T13: -0.1215 T23: -0.0516
REMARK 3 L TENSOR
REMARK 3 L11: 1.8787 L22: 4.7842
REMARK 3 L33: 5.2232 L12: 0.8567
REMARK 3 L13: -0.6401 L23: 0.2006
REMARK 3 S TENSOR
REMARK 3 S11: -0.1286 S12: 0.1116 S13: 0.0388
REMARK 3 S21: -1.3099 S22: -0.2053 S23: 0.5514
REMARK 3 S31: -0.2218 S32: -0.5361 S33: 0.2158
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 780 THROUGH 795 )
REMARK 3 ORIGIN FOR THE GROUP (A): 6.0651 17.9011 -20.3317
REMARK 3 T TENSOR
REMARK 3 T11: 0.3094 T22: 0.3365
REMARK 3 T33: 0.3605 T12: -0.0644
REMARK 3 T13: 0.0016 T23: 0.1306
REMARK 3 L TENSOR
REMARK 3 L11: 4.4333 L22: 9.6319
REMARK 3 L33: 7.3255 L12: -0.3829
REMARK 3 L13: -1.0987 L23: 3.8833
REMARK 3 S TENSOR
REMARK 3 S11: 0.0820 S12: -0.4258 S13: 0.0259
REMARK 3 S21: -0.4274 S22: -0.1316 S23: -0.9392
REMARK 3 S31: -0.8249 S32: 0.6240 S33: 0.0447
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 5HU3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 27-JAN-16.
REMARK 100 THE DEPOSITION ID IS D_1000217616.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-JAN-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.0 - 5.5
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) : 0.97625
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.20
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26540
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.820
REMARK 200 RESOLUTION RANGE LOW (A) : 30.075
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.9
REMARK 200 DATA REDUNDANCY : 3.300
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.03400
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 19.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.82
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.88
REMARK 200 COMPLETENESS FOR SHELL (%) : 91.0
REMARK 200 DATA REDUNDANCY IN SHELL : 2.40
REMARK 200 R MERGE FOR SHELL (I) : 0.57200
REMARK 200 R SYM FOR SHELL (I) : 0.57200
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: REFMAC
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.35
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.38
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 19% PEG 4000, 0.1 M SODIUM CITRATE PH
REMARK 280 5.0, 0.2 M AMMONIUM ACETATE, 5 MM MAGNESIUM CHLORIDE, 0.8 MM ADP,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293.15K
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 29.60850
REMARK 290 SMTRY3 2 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: 3000 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12920 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -31.0 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 GLY A -1
REMARK 465 ALA A 0
REMARK 465 MET A 1
REMARK 465 ALA A 2
REMARK 465 ALA A 3
REMARK 465 PRO A 4
REMARK 465 ALA A 5
REMARK 465 ALA A 6
REMARK 465 CYS A 273
REMARK 465 GLN A 274
REMARK 465 ARG A 275
REMARK 465 GLU A 276
REMARK 465 ARG A 277
REMARK 465 VAL A 278
REMARK 465 ALA A 279
REMARK 465 SER A 280
REMARK 465 VAL A 281
REMARK 465 VAL A 282
REMARK 465 HIS A 283
REMARK 465 GLY B 767
REMARK 465 VAL B 768
REMARK 465 LEU B 769
REMARK 465 PRO B 770
REMARK 465 LYS B 771
REMARK 465 ALA B 772
REMARK 465 PRO B 773
REMARK 465 LYS B 774
REMARK 465 LEU B 775
REMARK 465 GLN B 776
REMARK 465 ALA B 777
REMARK 465 SER B 778
REMARK 465 GLN B 779
REMARK 465 SER B 796
REMARK 465 SER B 797
REMARK 465 PRO B 798
REMARK 465 PRO B 799
REMARK 465 SER B 800
REMARK 465 ARG B 801
REMARK 465 ASP B 802
REMARK 465 SER B 803
REMARK 465 ARG B 804
REMARK 465 VAL B 805
REMARK 465 VAL B 806
REMARK 465 ILE B 807
REMARK 465 GLU B 808
REMARK 465 GLY B 809
REMARK 465 ALA B 810
REMARK 465 ALA B 811
REMARK 465 VAL B 812
REMARK 465 SER B 813
REMARK 465 SER B 814
REMARK 465 ALA B 815
REMARK 465 THR B 816
REMARK 465 VAL B 817
REMARK 465 GLY B 818
REMARK 465 PRO B 819
REMARK 465 SER B 820
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 17 -129.46 -119.75
REMARK 500 HIS A 70 146.34 177.94
REMARK 500 GLU A 106 -52.25 70.49
REMARK 500 ARG A 135 -1.26 74.57
REMARK 500 ASN A 136 42.94 -145.79
REMARK 500 ASP A 157 73.58 57.54
REMARK 500 LEU A 253 50.73 -90.49
REMARK 500
REMARK 500 REMARK: NULL
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 MG A 302 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 141 OD1
REMARK 620 2 ASP A 157 OD2 87.7
REMARK 620 3 TPO B 787 O1P 104.7 81.9
REMARK 620 4 ADP A 301 O1B 166.5 85.1 85.5
REMARK 620 5 ADP A 301 O1A 99.2 81.6 150.2 68.5
REMARK 620 6 HOH A 457 O 98.3 167.1 85.6 91.2 108.5
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ADP A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 302
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5FG8 RELATED DB: PDB
REMARK 900 5FG8 CONTAINS THE SAME PROTEIN (WT-VERSION) COMPLEXED WITH THE SAME
REMARK 900 EAG FRAGMENT (BUT NOT PHOSPHORYLATED) AND MG2+/ADP.
REMARK 900 RELATED ID: 5H9B RELATED DB: PDB
REMARK 900 5FG9 CONTAINS THE SAME PROTEIN (WT-VERSION) COMPLEXED WITH THE SAME
REMARK 900 EAG FRAGMENT (BUT NOT PHOSPHORYLATED) AND MG2+/AMPPN.
DBREF 5HU3 A 1 283 UNP Q00168 KCC2A_DROME 1 283
DBREF 5HU3 B 768 820 UNP Q02280 KCNAE_DROME 768 820
SEQADV 5HU3 GLY A -1 UNP Q00168 EXPRESSION TAG
SEQADV 5HU3 ALA A 0 UNP Q00168 EXPRESSION TAG
SEQADV 5HU3 ASN A 136 UNP Q00168 ASP 136 ENGINEERED MUTATION
SEQADV 5HU3 GLY B 767 UNP Q02280 EXPRESSION TAG
SEQADV 5HU3 LEU B 769 UNP Q02280 PHE 769 CONFLICT
SEQRES 1 A 285 GLY ALA MET ALA ALA PRO ALA ALA CYS THR ARG PHE SER
SEQRES 2 A 285 ASP ASN TYR ASP ILE LYS GLU GLU LEU GLY LYS GLY ALA
SEQRES 3 A 285 PHE SER ILE VAL LYS ARG CYS VAL GLN LYS SER THR GLY
SEQRES 4 A 285 PHE GLU PHE ALA ALA LYS ILE ILE ASN THR LYS LYS LEU
SEQRES 5 A 285 THR ALA ARG ASP PHE GLN LYS LEU GLU ARG GLU ALA ARG
SEQRES 6 A 285 ILE CYS ARG LYS LEU HIS HIS PRO ASN ILE VAL ARG LEU
SEQRES 7 A 285 HIS ASP SER ILE GLN GLU GLU ASN TYR HIS TYR LEU VAL
SEQRES 8 A 285 PHE ASP LEU VAL THR GLY GLY GLU LEU PHE GLU ASP ILE
SEQRES 9 A 285 VAL ALA ARG GLU PHE TYR SER GLU ALA ASP ALA SER HIS
SEQRES 10 A 285 CYS ILE GLN GLN ILE LEU GLU SER VAL ASN HIS CYS HIS
SEQRES 11 A 285 GLN ASN GLY VAL VAL HIS ARG ASN LEU LYS PRO GLU ASN
SEQRES 12 A 285 LEU LEU LEU ALA SER LYS ALA LYS GLY ALA ALA VAL LYS
SEQRES 13 A 285 LEU ALA ASP PHE GLY LEU ALA ILE GLU VAL GLN GLY ASP
SEQRES 14 A 285 HIS GLN ALA TRP PHE GLY PHE ALA GLY THR PRO GLY TYR
SEQRES 15 A 285 LEU SER PRO GLU VAL LEU LYS LYS GLU PRO TYR GLY LYS
SEQRES 16 A 285 SER VAL ASP ILE TRP ALA CYS GLY VAL ILE LEU TYR ILE
SEQRES 17 A 285 LEU LEU VAL GLY TYR PRO PRO PHE TRP ASP GLU ASP GLN
SEQRES 18 A 285 HIS ARG LEU TYR SER GLN ILE LYS ALA GLY ALA TYR ASP
SEQRES 19 A 285 TYR PRO SER PRO GLU TRP ASP THR VAL THR PRO GLU ALA
SEQRES 20 A 285 LYS ASN LEU ILE ASN GLN MET LEU THR VAL ASN PRO ASN
SEQRES 21 A 285 LYS ARG ILE THR ALA ALA GLU ALA LEU LYS HIS PRO TRP
SEQRES 22 A 285 ILE CYS GLN ARG GLU ARG VAL ALA SER VAL VAL HIS
SEQRES 1 B 54 GLY VAL LEU PRO LYS ALA PRO LYS LEU GLN ALA SER GLN
SEQRES 2 B 54 ALA THR LEU ALA ARG GLN ASP TPO ILE ASP GLU GLY GLY
SEQRES 3 B 54 GLU VAL ASP SER SER PRO PRO SER ARG ASP SER ARG VAL
SEQRES 4 B 54 VAL ILE GLU GLY ALA ALA VAL SER SER ALA THR VAL GLY
SEQRES 5 B 54 PRO SER
MODRES 5HU3 TPO B 787 THR MODIFIED RESIDUE
HET TPO B 787 11
HET ADP A 301 27
HET MG A 302 1
HETNAM TPO PHOSPHOTHREONINE
HETNAM ADP ADENOSINE-5'-DIPHOSPHATE
HETNAM MG MAGNESIUM ION
HETSYN TPO PHOSPHONOTHREONINE
FORMUL 2 TPO C4 H10 N O6 P
FORMUL 3 ADP C10 H15 N5 O10 P2
FORMUL 4 MG MG 2+
FORMUL 5 HOH *77(H2 O)
HELIX 1 AA1 THR A 8 ASN A 13 1 6
HELIX 2 AA2 THR A 51 LEU A 68 1 18
HELIX 3 AA3 GLU A 97 GLU A 106 1 10
HELIX 4 AA4 SER A 109 GLN A 129 1 21
HELIX 5 AA5 LYS A 138 GLU A 140 5 3
HELIX 6 AA6 THR A 177 LEU A 181 5 5
HELIX 7 AA7 SER A 182 LYS A 187 1 6
HELIX 8 AA8 LYS A 193 GLY A 210 1 18
HELIX 9 AA9 ASP A 218 GLY A 229 1 12
HELIX 10 AB1 THR A 242 LEU A 253 1 12
HELIX 11 AB2 THR A 262 LEU A 267 1 6
SHEET 1 AA1 5 TYR A 14 GLY A 23 0
SHEET 2 AA1 5 SER A 26 GLN A 33 -1 O ARG A 30 N LYS A 17
SHEET 3 AA1 5 GLU A 39 ASN A 46 -1 O ALA A 42 N LYS A 29
SHEET 4 AA1 5 TYR A 85 ASP A 91 -1 O PHE A 90 N ALA A 41
SHEET 5 AA1 5 LEU A 76 GLN A 81 -1 N HIS A 77 O VAL A 89
SHEET 1 AA2 2 VAL A 132 VAL A 133 0
SHEET 2 AA2 2 ILE A 162 GLU A 163 -1 O ILE A 162 N VAL A 133
SHEET 1 AA3 2 LEU A 142 LEU A 144 0
SHEET 2 AA3 2 VAL A 153 LEU A 155 -1 O LYS A 154 N LEU A 143
SHEET 1 AA4 2 ALA A 175 GLY A 176 0
SHEET 2 AA4 2 ILE B 788 ASP B 789 -1 O ILE B 788 N GLY A 176
LINK OD1 ASN A 141 MG MG A 302 1555 1555 2.31
LINK OD2 ASP A 157 MG MG A 302 1555 1555 2.35
LINK C ASP B 786 N TPO B 787 1555 1555 1.32
LINK O1P TPO B 787 MG MG A 302 1555 1555 2.41
LINK C TPO B 787 N ILE B 788 1555 1555 1.34
LINK O1B ADP A 301 MG MG A 302 1555 1555 2.13
LINK O1A ADP A 301 MG MG A 302 1555 1555 2.26
LINK MG MG A 302 O HOH A 457 1555 1555 2.12
CISPEP 1 SER A 235 PRO A 236 0 -0.44
SITE 1 AC1 22 GLY A 21 GLY A 23 ALA A 24 SER A 26
SITE 2 AC1 22 VAL A 28 ALA A 41 LYS A 43 ASP A 91
SITE 3 AC1 22 VAL A 93 GLU A 97 GLU A 140 ASN A 141
SITE 4 AC1 22 LEU A 143 ASP A 157 MG A 302 HOH A 407
SITE 5 AC1 22 HOH A 424 HOH A 427 HOH A 432 HOH A 457
SITE 6 AC1 22 ARG B 784 TPO B 787
SITE 1 AC2 5 ASN A 141 ASP A 157 ADP A 301 HOH A 457
SITE 2 AC2 5 TPO B 787
CRYST1 36.907 59.217 70.301 90.00 96.68 90.00 P 1 21 1 2
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 0.027095 0.000000 0.003171 0.00000
SCALE2 0.000000 0.016887 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014322 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
