HEADER TRANSFERASE, PLANT PROTEIN 23-JAN-04 1S6J
TITLE N-TERMINAL REGION OF THE CA2+-SATURATED CALCIUM REGULATORY DOMAIN
TITLE 2 (CLD) FROM SOYBEAN CALCIUM-DEPENDENT PROTEIN KINASE-ALPHA (CDPK)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CALCIUM-DEPENDENT PROTEIN KINASE SK5;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: N-TERMINAL REGION OF CALMODULIN-LIKE DOMAIN (CLD);
COMPND 5 SYNONYM: CDPK; CALCIUM-DEPENDENT PROTEIN KINASE-ALPHA;
COMPND 6 EC: 2.7.1.-;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GLYCINE MAX;
SOURCE 3 ORGANISM_COMMON: SOYBEAN;
SOURCE 4 ORGANISM_TAXID: 3847;
SOURCE 5 GENE: CDPK SK5;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET-19B;
SOURCE 11 OTHER_DETAILS: 13 RESIDUES FROM AN N-TERMINAL HIS-TAG, AND THE N-
SOURCE 12 TERMINAL DOMAIN OF THE CA2+-REGULATORY REGION
KEYWDS EF-HAND; HELIX-LOOP-HELIX; CALCIUM-BINDING; CALMODULIN SUPERFAMILY,
KEYWDS 2 TRANSFERASE, PLANT PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 15
AUTHOR A.M.WELJIE,H.J.VOGEL
REVDAT 3 02-MAR-22 1S6J 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 1S6J 1 VERSN
REVDAT 1 21-DEC-04 1S6J 0
JRNL AUTH A.M.WELJIE,S.M.GAGNE,H.J.VOGEL
JRNL TITL SOLUTION STRUCTURE AND BACKBONE DYNAMICS OF THE N-TERMINAL
JRNL TITL 2 REGION OF THE CALCIUM REGULATORY DOMAIN FROM SOYBEAN
JRNL TITL 3 CALCIUM-DEPENDENT PROTEIN KINASE ALPHA
JRNL REF BIOCHEMISTRY V. 42 15131 2004
JRNL REFN ISSN 0006-2960
JRNL PMID 15568805
JRNL DOI 10.1021/BI048751R
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH A.M.WELJIE,K.M.ROBERTSON,H.J.VOGEL
REMARK 1 TITL CONFORMATIONAL CHANGES IN THE CA2+-REGULATORY REGION FROM
REMARK 1 TITL 2 SOYBEAN CALCIUM-DEPENDENT PROTEIN KINASE-ALPHA: FLUORESCENCE
REMARK 1 TITL 3 RESONANCE ENERGY TRANSFER STUDIES
REMARK 1 REF J.BIOL.CHEM. V. 278 43764 2003
REMARK 1 REFN ISSN 0021-9258
REMARK 1 REFERENCE 2
REMARK 1 AUTH A.M.WELJIE,H.J.VOGEL
REMARK 1 TITL UNEXPECTED STRUCTURE OF THE CA2+-REGULATORY REGION FROM
REMARK 1 TITL 2 SOYBEAN CALCIUM-DEPENDENT PROTEIN KINASE-ALPHA
REMARK 1 REF J.BIOL.CHEM. V. 279 35494 2004
REMARK 1 REFN ISSN 0021-9258
REMARK 1 PMID 15155727
REMARK 1 DOI 10.1074/JBC.M311520200
REMARK 1 REFERENCE 3
REMARK 1 AUTH J.F.HARPER,M.R.SUSSMAN,G.E.SCHALLER,C.PUTNAM-EVANS,
REMARK 1 AUTH 2 H.CHARBONNEAU,A.C.HARMON
REMARK 1 TITL A CALCIUM-DEPENDENT PROTEIN KINASE WITH A REGULATORY DOMAIN
REMARK 1 TITL 2 SIMILAR TO CALMODULIN
REMARK 1 REF SCIENCE V. 252 951 1991
REMARK 1 REFN ISSN 0036-8075
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.6, CNS 1.1
REMARK 3 AUTHORS : BRUKER (XWINNMR), BRUNGER (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 BASED ON 765 UNAMBIGUOUS NOE-DERIVED RESTRAINTS, 118 AMBIGUOUS NOE-
REMARK 3 DERIVED
REMARK 3 RESTRAINTS, 130 DIHEDRAL ANGLE RESTRAINTS (CSI AND TALOS DERIVED)
REMARK 4
REMARK 4 1S6J COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-JAN-04.
REMARK 100 THE DEPOSITION ID IS D_1000021429.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 6.9
REMARK 210 IONIC STRENGTH : 200 MM NACL, 10 MM CACL2
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.5 MM U-15N NTH-CLD; 200 MM
REMARK 210 NACL; 10 MM CACL2; 95% H2O, 5%
REMARK 210 D2O; 0.5 MM U-15N,13C NTH-CLD;
REMARK 210 200 MM NACL; 10 MM CACL2; 95%
REMARK 210 H2O, 5% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA; AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN; BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 2.1, NMRVIEW 5.04, CNS
REMARK 210 1.1, ARIA 1.2, VNMR UNKNOWN
REMARK 210 METHOD USED : SIMULATED ANNEALING; MOLECULAR
REMARK 210 DYNAMICS; MATRIX RELAXATION
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 15
REMARK 210 CONFORMERS, SELECTION CRITERIA : BACK CALCULATED DATA AGREE WITH
REMARK 210 EXPERIMENTAL NOESY SPECTRUM,
REMARK 210 STRUCTURES WITH ACCEPTABLE
REMARK 210 COVALENT GEOMETRY,STRUCTURES
REMARK 210 WITH FAVORABLE NON-BOND ENERGY,
REMARK 210 STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS,STRUCTURES
REMARK 210 WITH THE LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
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 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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
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
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 1 SER A 3 11.82 -148.35
REMARK 500 1 ASP A 7 -74.34 -162.43
REMARK 500 1 GLU A 21 -0.43 -176.03
REMARK 500 1 LYS A 26 -65.94 -90.75
REMARK 500 1 ASN A 36 18.80 55.89
REMARK 500 1 ASP A 47 -16.75 -49.62
REMARK 500 1 SER A 54 -95.63 -91.28
REMARK 500 1 GLU A 55 23.67 -147.95
REMARK 500 1 GLU A 58 -9.60 -54.56
REMARK 500 1 LYS A 72 29.05 44.25
REMARK 500 1 ALA A 84 108.67 -55.47
REMARK 500 1 VAL A 86 84.70 56.91
REMARK 500 2 HIS A 5 -60.51 -109.94
REMARK 500 2 ASP A 7 -71.14 -136.02
REMARK 500 2 ASP A 8 -104.16 -93.63
REMARK 500 2 ASP A 9 20.22 -171.80
REMARK 500 2 ARG A 16 -108.93 -72.12
REMARK 500 2 LYS A 26 -29.83 -38.93
REMARK 500 2 ASN A 36 15.94 55.70
REMARK 500 2 ASP A 47 -16.04 -49.82
REMARK 500 2 SER A 54 -92.36 -68.97
REMARK 500 2 LYS A 72 12.85 56.19
REMARK 500 3 ILE A 6 97.76 -55.61
REMARK 500 3 ASP A 7 -75.14 -169.49
REMARK 500 3 ASP A 8 29.89 -166.57
REMARK 500 3 ASP A 9 -68.50 -121.98
REMARK 500 3 GLU A 15 -87.53 -96.15
REMARK 500 3 GLU A 20 -65.18 -90.79
REMARK 500 3 GLU A 21 -15.94 -175.04
REMARK 500 3 ASN A 36 16.21 52.54
REMARK 500 3 SER A 54 -97.92 -88.43
REMARK 500 3 GLU A 55 41.83 -141.00
REMARK 500 3 GLU A 58 -9.64 -53.73
REMARK 500 3 ASP A 69 98.64 -54.38
REMARK 500 3 LYS A 72 33.37 34.49
REMARK 500 3 ALA A 84 -80.73 -68.84
REMARK 500 3 VAL A 86 82.77 54.61
REMARK 500 4 HIS A 5 -69.05 -161.75
REMARK 500 4 ASP A 7 -72.78 -167.31
REMARK 500 4 ASP A 8 31.76 -169.53
REMARK 500 4 ASP A 9 -78.68 -101.55
REMARK 500 4 LEU A 25 -25.70 -38.33
REMARK 500 4 LYS A 26 -16.41 -49.42
REMARK 500 4 ASN A 36 13.20 56.04
REMARK 500 4 GLU A 55 33.12 -84.63
REMARK 500 5 ASP A 7 -101.78 -149.53
REMARK 500 5 ASP A 8 54.03 -143.97
REMARK 500 5 ASP A 9 -87.54 -131.56
REMARK 500 5 ARG A 16 -154.57 -67.46
REMARK 500 5 GLU A 21 -15.63 -49.52
REMARK 500
REMARK 500 THIS ENTRY HAS 163 RAMACHANDRAN OUTLIERS.
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 CA A 88 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 33 OD1
REMARK 620 2 ASP A 33 OD2 39.9
REMARK 620 3 ASP A 35 OD2 109.8 120.5
REMARK 620 4 SER A 37 OG 105.8 68.8 86.1
REMARK 620 5 THR A 39 O 60.7 54.7 170.1 98.9
REMARK 620 6 GLU A 44 OE1 66.6 105.4 89.6 169.5 84.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 89 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 69 OD1
REMARK 620 2 ASP A 71 OD2 120.4
REMARK 620 3 SER A 73 OG 101.4 71.9
REMARK 620 4 THR A 75 O 68.9 138.8 66.9
REMARK 620 5 ASP A 77 OD2 112.7 123.2 116.5 77.7
REMARK 620 6 GLU A 80 OE2 92.3 78.3 150.2 142.9 81.1
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 CA A 88
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 89
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1S6I RELATED DB: PDB
REMARK 900 CA2+-REGULATORY REGION (CLD) FROM SOYBEAN CALCIUM-DEPENDENT PROTEIN
REMARK 900 KINASE-ALPHA (CDPK) IN THE PRESENCE OF CA2+ AND THE JUNCTION DOMAIN
REMARK 900 (JD)
DBREF 1S6J A 14 87 UNP P28583 CDPK_SOYBN 329 402
SEQADV 1S6J HIS A 1 UNP P28583 EXPRESSION TAG
SEQADV 1S6J SER A 2 UNP P28583 EXPRESSION TAG
SEQADV 1S6J SER A 3 UNP P28583 EXPRESSION TAG
SEQADV 1S6J GLY A 4 UNP P28583 EXPRESSION TAG
SEQADV 1S6J HIS A 5 UNP P28583 EXPRESSION TAG
SEQADV 1S6J ILE A 6 UNP P28583 EXPRESSION TAG
SEQADV 1S6J ASP A 7 UNP P28583 EXPRESSION TAG
SEQADV 1S6J ASP A 8 UNP P28583 EXPRESSION TAG
SEQADV 1S6J ASP A 9 UNP P28583 EXPRESSION TAG
SEQADV 1S6J ASP A 10 UNP P28583 EXPRESSION TAG
SEQADV 1S6J LYS A 11 UNP P28583 EXPRESSION TAG
SEQADV 1S6J HIS A 12 UNP P28583 EXPRESSION TAG
SEQADV 1S6J MET A 13 UNP P28583 EXPRESSION TAG
SEQRES 1 A 87 HIS SER SER GLY HIS ILE ASP ASP ASP ASP LYS HIS MET
SEQRES 2 A 87 ALA GLU ARG LEU SER GLU GLU GLU ILE GLY GLY LEU LYS
SEQRES 3 A 87 GLU LEU PHE LYS MET ILE ASP THR ASP ASN SER GLY THR
SEQRES 4 A 87 ILE THR PHE ASP GLU LEU LYS ASP GLY LEU LYS ARG VAL
SEQRES 5 A 87 GLY SER GLU LEU MET GLU SER GLU ILE LYS ASP LEU MET
SEQRES 6 A 87 ASP ALA ALA ASP ILE ASP LYS SER GLY THR ILE ASP TYR
SEQRES 7 A 87 GLY GLU PHE ILE ALA ALA THR VAL HIS
HET CA A 88 1
HET CA A 89 1
HETNAM CA CALCIUM ION
FORMUL 2 CA 2(CA 2+)
HELIX 1 1 ASP A 8 MET A 13 1 6
HELIX 2 2 GLU A 27 ASP A 33 1 7
HELIX 3 3 PHE A 42 ARG A 51 1 10
HELIX 4 4 MET A 57 ASP A 69 1 13
HELIX 5 5 ASP A 77 ILE A 82 1 6
SHEET 1 A 2 ILE A 40 THR A 41 0
SHEET 2 A 2 THR A 75 ILE A 76 -1 O ILE A 76 N ILE A 40
LINK OD1 ASP A 33 CA CA A 88 1555 1555 3.29
LINK OD2 ASP A 33 CA CA A 88 1555 1555 3.13
LINK OD2 ASP A 35 CA CA A 88 1555 1555 2.96
LINK OG SER A 37 CA CA A 88 1555 1555 2.64
LINK O THR A 39 CA CA A 88 1555 1555 2.34
LINK OE1 GLU A 44 CA CA A 88 1555 1555 2.93
LINK OD1 ASP A 69 CA CA A 89 1555 1555 2.62
LINK OD2 ASP A 71 CA CA A 89 1555 1555 2.85
LINK OG SER A 73 CA CA A 89 1555 1555 2.41
LINK O THR A 75 CA CA A 89 1555 1555 2.82
LINK OD2 ASP A 77 CA CA A 89 1555 1555 3.40
LINK OE2 GLU A 80 CA CA A 89 1555 1555 2.83
SITE 1 AC1 5 ASP A 33 ASP A 35 SER A 37 THR A 39
SITE 2 AC1 5 GLU A 44
SITE 1 AC2 6 ASP A 69 ASP A 71 SER A 73 THR A 75
SITE 2 AC2 6 ASP A 77 GLU A 80
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
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 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
MODEL 1
(ATOM LINES ARE NOT SHOWN.)
END
