HEADER PROTEIN BINDING 10-MAR-03 1OQP
TITLE STRUCTURE OF THE CA2+/C-TERMINAL DOMAIN OF CALTRACTIN IN COMPLEX WITH
TITLE 2 THE CDC31P-BINDING DOMAIN FROM KAR1P
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CALTRACTIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CENTRIN, 20 KDA CALCIUM-BINDING PROTEIN;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: CELL DIVISION CONTROL PROTEIN KAR1;
COMPND 8 CHAIN: B;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CHLAMYDOMONAS REINHARDTII;
SOURCE 3 ORGANISM_TAXID: 3055;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET;
SOURCE 9 MOL_ID: 2;
SOURCE 10 SYNTHETIC: YES;
SOURCE 11 OTHER_DETAILS: THE PEPTIDE CONSISTS OF THE CDC31P-BINDING DOMAIN
SOURCE 12 FROM KAR1P, RESIDUES 239-257, AND HAS BEEN CHEMICALLY SYNTHESIZED
SOURCE 13 USING SOLID PHASE F-MOC CHEMISTRY. THE SEQUENCE IS NATURALLY FOUND
SOURCE 14 IN SACCHAROMYCES CEREVISIAE (BAKER'S YEAST).
KEYWDS PROTEIN-PEPTIDE COMPLEX, CALTRACTIN, KAR1P, CALCIUM-BINDING, PROTEIN
KEYWDS 2 BINDING
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR H.T.HU,W.J.CHAZIN
REVDAT 3 23-FEB-22 1OQP 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1OQP 1 VERSN
REVDAT 1 24-JUN-03 1OQP 0
JRNL AUTH H.T.HU,W.J.CHAZIN
JRNL TITL UNIQUE FEATURES IN THE C-TERMINAL DOMAIN PROVIDE CALTRACTIN
JRNL TITL 2 WITH TARGET SPECIFICITY
JRNL REF J.MOL.BIOL. V. 330 473 2003
JRNL REFN ISSN 0022-2836
JRNL PMID 12842464
JRNL DOI 10.1016/S0022-2836(03)00619-3
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.6, AMBER 7.0
REMARK 3 AUTHORS : BRUKER (XWINNMR), PEARLMAN, D.A., CASE, D.A.,
REMARK 3 CALDWELL, J.W., ROSS, W.S., CHEATHAM III, T.E.,
REMARK 3 DEBOLT, S., FERGUSON, D., SEIBEL, G., KOLLMAN, P.
REMARK 3 (AMBER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURES ARE BASED ON A TOTAL OF 1827 CONSTRAINTS, 1641 ARE
REMARK 3 NOE-DERIVED
REMARK 3 DISTANCE CONSTRAINTS, 134 DIHEDRAL ANGLE CONSTRAINTS, 52 DISTANCE
REMARK 3 CONSTRAINTS
REMARK 3 FROM HYDROGEN BONDS.
REMARK 4
REMARK 4 1OQP COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-MAR-03.
REMARK 100 THE DEPOSITION ID IS D_1000018573.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 50MM KCL, 5MM CACL2
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM CRC-C U-15N,13C; 1.2MM K19
REMARK 210 UNLABELED.; 1MM CRC-C U-15N,13C;
REMARK 210 1.2MM K19 UNLABELED.; 1MM CRC-C
REMARK 210 UNLABELED; 1.2 MM K19 UNLABELED.
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY; 4D_13C-
REMARK 210 SEPARATED_NOESY; 2D NOESY; 3D
REMARK 210 13C-F1-EDITED, 13C-F3-FILTERED
REMARK 210 NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : FELIX 2000, DYANA 1.5
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 60
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : 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: NULL
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: DIMERIC
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 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 3 ARG B 241 NE - CZ - NH2 ANGL. DEV. = -3.3 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 1 PHE B 253 37.82 -77.66
REMARK 500 1 ASP B 255 79.10 -67.89
REMARK 500 1 LYS B 256 -70.63 66.49
REMARK 500 2 ASP A 98 -137.11 43.92
REMARK 500 2 ASN A 149 -57.33 172.13
REMARK 500 2 ASP A 150 57.00 79.60
REMARK 500 2 ASN A 152 -8.69 75.57
REMARK 500 2 GLU B 242 -52.28 -29.56
REMARK 500 3 GLU A 132 92.07 -66.58
REMARK 500 3 HIS B 254 -47.41 -170.11
REMARK 500 3 ASP B 255 -139.52 46.29
REMARK 500 3 LYS B 256 -62.72 69.09
REMARK 500 4 ASP A 98 -135.48 36.95
REMARK 500 4 ASP A 150 42.72 74.59
REMARK 500 4 ASN A 152 -3.71 76.44
REMARK 500 4 GLU B 242 -89.17 -103.56
REMARK 500 4 PHE B 253 36.14 -75.66
REMARK 500 4 LYS B 256 72.80 -69.17
REMARK 500 5 ASP A 150 38.01 76.02
REMARK 500 5 ASN A 152 32.82 71.21
REMARK 500 6 ASP A 150 33.14 75.91
REMARK 500 7 SER A 94 -60.43 69.91
REMARK 500 7 GLU A 96 93.94 -67.54
REMARK 500 7 ASP A 98 -75.52 -115.14
REMARK 500 7 ASP A 150 15.13 59.26
REMARK 500 7 ASN A 152 -15.35 83.70
REMARK 500 7 HIS B 254 -112.98 33.44
REMARK 500 8 SER A 99 -42.13 -27.82
REMARK 500 8 GLU A 132 91.28 -66.22
REMARK 500 8 ASN A 149 -49.72 165.51
REMARK 500 8 ASP A 150 59.39 74.45
REMARK 500 8 LYS B 240 -40.64 74.54
REMARK 500 8 ASP B 255 -124.06 -175.56
REMARK 500 9 SER A 94 -72.92 -71.08
REMARK 500 9 ASP A 98 -68.39 -151.36
REMARK 500 9 GLU A 132 90.82 -62.86
REMARK 500 9 ASN A 149 -109.99 175.62
REMARK 500 9 ASP A 150 27.05 -172.64
REMARK 500 9 ARG B 241 103.63 96.54
REMARK 500 10 SER A 94 49.70 -75.38
REMARK 500 10 GLU A 132 97.56 -60.00
REMARK 500 10 ASP A 150 35.37 74.67
REMARK 500 10 ARG B 241 -44.60 -172.06
REMARK 500 11 SER A 94 40.35 -73.40
REMARK 500 11 ASN A 152 -5.10 85.65
REMARK 500 12 SER A 99 -56.43 71.12
REMARK 500 12 ASP A 150 51.23 29.62
REMARK 500 12 ASN A 152 -15.70 79.63
REMARK 500 12 LEU B 252 -72.99 -93.73
REMARK 500 12 LYS B 256 -65.66 66.79
REMARK 500
REMARK 500 THIS ENTRY HAS 81 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 1 ARG A 124 0.10 SIDE CHAIN
REMARK 500 1 ARG B 241 0.09 SIDE CHAIN
REMARK 500 3 ARG B 250 0.09 SIDE CHAIN
REMARK 500 4 ARG A 125 0.08 SIDE CHAIN
REMARK 500 6 ARG A 124 0.09 SIDE CHAIN
REMARK 500 6 HIS B 249 0.10 SIDE CHAIN
REMARK 500 7 HIS B 249 0.08 SIDE CHAIN
REMARK 500 8 ARG A 125 0.08 SIDE CHAIN
REMARK 500 8 ARG B 241 0.10 SIDE CHAIN
REMARK 500 10 ARG A 124 0.10 SIDE CHAIN
REMARK 500 12 PHE B 253 0.08 SIDE CHAIN
REMARK 500 13 ARG A 97 0.13 SIDE CHAIN
REMARK 500 13 ARG A 124 0.10 SIDE CHAIN
REMARK 500 16 HIS B 249 0.11 SIDE CHAIN
REMARK 500 17 ARG A 125 0.08 SIDE CHAIN
REMARK 500 19 HIS B 249 0.08 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1OQP A 95 169 UNP P05434 CATR_CHLRE 95 169
DBREF 1OQP B 239 257 UNP P11927 KAR1_YEAST 239 257
SEQADV 1OQP GLY A 93 UNP P05434 EXPRESSION TAG
SEQADV 1OQP SER A 94 UNP P05434 EXPRESSION TAG
SEQRES 1 A 77 GLY SER GLY GLU ARG ASP SER ARG GLU GLU ILE LEU LYS
SEQRES 2 A 77 ALA PHE ARG LEU PHE ASP ASP ASP ASN SER GLY THR ILE
SEQRES 3 A 77 THR ILE LYS ASP LEU ARG ARG VAL ALA LYS GLU LEU GLY
SEQRES 4 A 77 GLU ASN LEU THR GLU GLU GLU LEU GLN GLU MET ILE ALA
SEQRES 5 A 77 GLU ALA ASP ARG ASN ASP ASP ASN GLU ILE ASP GLU ASP
SEQRES 6 A 77 GLU PHE ILE ARG ILE MET LYS LYS THR SER LEU PHE
SEQRES 1 B 19 LYS LYS ARG GLU LEU ILE GLU SER LYS TRP HIS ARG LEU
SEQRES 2 B 19 LEU PHE HIS ASP LYS LYS
HELIX 1 1 ASP A 98 ASP A 111 1 14
HELIX 2 2 ILE A 120 GLY A 131 1 12
HELIX 3 3 THR A 135 ASP A 147 1 13
HELIX 4 4 ASP A 155 THR A 166 1 12
HELIX 5 5 LYS B 239 PHE B 253 1 15
SHEET 1 A 2 ILE A 118 THR A 119 0
SHEET 2 A 2 GLU A 153 ILE A 154 -1 O ILE A 154 N ILE A 118
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
