Header list of 1r2a.pdb file
Complete list - r 2 2 Bytes
HEADER TRANSFERASE 07-DEC-98 1R2A
TITLE THE MOLECULAR BASIS FOR PROTEIN KINASE A ANCHORING REVEALED BY
TITLE 2 SOLUTION NMR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (CAMP-DEPENDENT PROTEIN KINASE TYPE II REGULATORY
COMPND 3 SUBUNIT);
COMPND 4 CHAIN: A, B;
COMPND 5 FRAGMENT: DIMERIZATION-ANCHORING DOMAIN;
COMPND 6 SYNONYM: RIIA(1-44);
COMPND 7 EC: 2.7.1.37;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: RIIA(1-44);
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET-16B
KEYWDS REGULATORY SUBUNIT, ANCHORING, FOUR-HELIX BUNDLE, TRANSFERASE
EXPDTA SOLUTION NMR
NUMMDL 17
AUTHOR M.G.NEWLON,M.ROY,D.MORIKIS,Z.E.HAUSKEN,V.COGHLAN,J.D.SCOTT,
AUTHOR 2 P.A.JENNINGS
REVDAT 4 02-MAR-22 1R2A 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1R2A 1 VERSN
REVDAT 2 29-DEC-99 1R2A 4 HEADER COMPND REMARK JRNL
REVDAT 2 2 4 ATOM SOURCE SEQRES
REVDAT 1 16-DEC-98 1R2A 0
JRNL AUTH M.G.NEWLON,M.ROY,D.MORIKIS,Z.E.HAUSKEN,V.COGHLAN,J.D.SCOTT,
JRNL AUTH 2 P.A.JENNINGS
JRNL TITL THE MOLECULAR BASIS FOR PROTEIN KINASE A ANCHORING REVEALED
JRNL TITL 2 BY SOLUTION NMR.
JRNL REF NAT.STRUCT.BIOL. V. 6 222 1999
JRNL REFN ISSN 1072-8368
JRNL PMID 10074940
JRNL DOI 10.1038/6663
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.NILGES
REMARK 1 TITL A CALCULATION STRATEGY FOR THE STRUCTURE DETERMINATION OF
REMARK 1 TITL 2 SYMMETRIC DIMERS BY 1H NMR
REMARK 1 REF PROTEINS V. 17 297 1993
REMARK 1 REFN ISSN 0887-3585
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN THE
REMARK 3 JRNL CITATIONS ABOVE
REMARK 4
REMARK 4 1R2A COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-DEC-98.
REMARK 100 THE DEPOSITION ID IS D_1000000230.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 4.0
REMARK 210 IONIC STRENGTH : 0.012 MM
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D NOESY-HSQC; 3D TOCSY-HMQC;
REMARK 210 CBCA(CO)NH; HNCA; HN(CO)CA; 13C
REMARK 210 FILTERED NOESY; HNHA; 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : DMX500
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XPLOR
REMARK 210 METHOD USED : DISTANCE GEOMETRY-SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 49
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 17
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 10
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY ON 13C, 15N-LABELED RIIALPHA(1-44). 13C FILTERED
REMARK 210 EXPERIMENTS ON A 50% 13C,15N LABELED, 50% UNLABELED RIIALPHA(1-
REMARK 210 44) SAMPLE WERE USED TO OBTAIN INTERMOLECULAR CONTACTS OF THE
REMARK 210 HOMODIMER.
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: 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 GLN A 6 50.27 -152.02
REMARK 500 1 ARG A 24 -62.59 -92.49
REMARK 500 1 ALA A 44 -65.32 -92.98
REMARK 500 1 ARG A 45 106.39 -47.79
REMARK 500 1 GLN B 6 50.34 -152.04
REMARK 500 1 ARG B 24 -62.41 -92.65
REMARK 500 1 ALA B 44 -65.41 -92.73
REMARK 500 1 ARG B 45 106.34 -47.74
REMARK 500 2 HIS A 4 -50.57 -134.65
REMARK 500 2 GLN A 6 38.65 -141.13
REMARK 500 2 ALA A 44 -71.86 -60.74
REMARK 500 2 HIS B 4 -50.72 -134.75
REMARK 500 2 GLN B 6 38.59 -140.90
REMARK 500 2 ALA B 44 -71.81 -61.00
REMARK 500 3 MET A 2 76.81 -159.42
REMARK 500 3 ILE A 7 58.32 -146.83
REMARK 500 3 ARG A 45 160.58 -48.96
REMARK 500 3 MET B 2 76.72 -159.45
REMARK 500 3 ILE B 7 58.54 -146.84
REMARK 500 3 ARG B 45 160.66 -49.10
REMARK 500 4 MET A 2 34.23 -152.40
REMARK 500 4 ILE A 5 60.10 -100.26
REMARK 500 4 GLN A 26 71.30 51.97
REMARK 500 4 MET B 2 34.13 -152.33
REMARK 500 4 ILE B 5 59.97 -100.22
REMARK 500 4 GLN B 26 71.15 52.21
REMARK 500 5 MET A 2 -43.89 -134.66
REMARK 500 5 ILE A 5 62.36 -112.46
REMARK 500 5 GLN A 6 41.14 -109.23
REMARK 500 5 GLN A 26 77.42 53.80
REMARK 500 5 ALA A 44 -63.21 -90.09
REMARK 500 5 MET B 2 -43.98 -134.88
REMARK 500 5 ILE B 5 62.25 -112.56
REMARK 500 5 GLN B 6 41.12 -109.17
REMARK 500 5 GLN B 26 77.44 53.89
REMARK 500 6 ARG A 45 -81.95 -50.88
REMARK 500 6 ARG B 45 -81.97 -51.00
REMARK 500 7 HIS A 4 37.20 -155.85
REMARK 500 7 GLN A 6 53.48 -156.33
REMARK 500 7 PRO A 9 -169.63 -73.84
REMARK 500 7 GLN A 26 96.09 -39.35
REMARK 500 7 HIS B 4 36.98 -155.89
REMARK 500 7 GLN B 6 53.43 -156.35
REMARK 500 7 PRO B 9 -169.53 -73.87
REMARK 500 7 GLN B 26 95.98 -39.25
REMARK 500 8 MET A 2 20.54 -141.93
REMARK 500 8 MET B 2 20.54 -141.74
REMARK 500 9 ARG A 45 -71.44 -49.73
REMARK 500 9 ARG B 45 -71.22 -49.97
REMARK 500 10 MET A 2 76.73 53.11
REMARK 500
REMARK 500 THIS ENTRY HAS 95 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 24 0.22 SIDE CHAIN
REMARK 500 1 ARG A 40 0.31 SIDE CHAIN
REMARK 500 1 ARG A 42 0.22 SIDE CHAIN
REMARK 500 1 ARG A 45 0.32 SIDE CHAIN
REMARK 500 1 ARG A 46 0.26 SIDE CHAIN
REMARK 500 1 ARG B 24 0.22 SIDE CHAIN
REMARK 500 1 ARG B 40 0.31 SIDE CHAIN
REMARK 500 1 ARG B 42 0.22 SIDE CHAIN
REMARK 500 1 ARG B 45 0.32 SIDE CHAIN
REMARK 500 1 ARG B 46 0.26 SIDE CHAIN
REMARK 500 2 ARG A 24 0.23 SIDE CHAIN
REMARK 500 2 ARG A 40 0.24 SIDE CHAIN
REMARK 500 2 ARG A 42 0.30 SIDE CHAIN
REMARK 500 2 ARG A 45 0.24 SIDE CHAIN
REMARK 500 2 ARG A 46 0.31 SIDE CHAIN
REMARK 500 2 ARG B 24 0.23 SIDE CHAIN
REMARK 500 2 ARG B 40 0.24 SIDE CHAIN
REMARK 500 2 ARG B 42 0.30 SIDE CHAIN
REMARK 500 2 ARG B 45 0.25 SIDE CHAIN
REMARK 500 2 ARG B 46 0.31 SIDE CHAIN
REMARK 500 3 ARG A 24 0.31 SIDE CHAIN
REMARK 500 3 ARG A 40 0.20 SIDE CHAIN
REMARK 500 3 ARG A 42 0.22 SIDE CHAIN
REMARK 500 3 ARG A 45 0.24 SIDE CHAIN
REMARK 500 3 ARG A 46 0.32 SIDE CHAIN
REMARK 500 3 ARG B 24 0.31 SIDE CHAIN
REMARK 500 3 ARG B 40 0.20 SIDE CHAIN
REMARK 500 3 ARG B 42 0.22 SIDE CHAIN
REMARK 500 3 ARG B 45 0.24 SIDE CHAIN
REMARK 500 3 ARG B 46 0.32 SIDE CHAIN
REMARK 500 4 ARG A 24 0.26 SIDE CHAIN
REMARK 500 4 ARG A 40 0.31 SIDE CHAIN
REMARK 500 4 ARG A 42 0.26 SIDE CHAIN
REMARK 500 4 ARG A 45 0.31 SIDE CHAIN
REMARK 500 4 ARG A 46 0.26 SIDE CHAIN
REMARK 500 4 ARG B 24 0.26 SIDE CHAIN
REMARK 500 4 ARG B 40 0.31 SIDE CHAIN
REMARK 500 4 ARG B 42 0.26 SIDE CHAIN
REMARK 500 4 ARG B 45 0.31 SIDE CHAIN
REMARK 500 4 ARG B 46 0.26 SIDE CHAIN
REMARK 500 5 ARG A 24 0.32 SIDE CHAIN
REMARK 500 5 ARG A 40 0.23 SIDE CHAIN
REMARK 500 5 ARG A 42 0.32 SIDE CHAIN
REMARK 500 5 ARG A 45 0.24 SIDE CHAIN
REMARK 500 5 ARG A 46 0.31 SIDE CHAIN
REMARK 500 5 ARG B 24 0.32 SIDE CHAIN
REMARK 500 5 ARG B 40 0.23 SIDE CHAIN
REMARK 500 5 ARG B 42 0.32 SIDE CHAIN
REMARK 500 5 ARG B 45 0.23 SIDE CHAIN
REMARK 500 5 ARG B 46 0.31 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 170 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1R2A A 2 46 UNP P12367 KAP2_MOUSE 1 44
DBREF 1R2A B 2 46 UNP P12367 KAP2_MOUSE 1 44
SEQADV 1R2A HIS A 1 UNP P12367 CLONING ARTIFACT
SEQADV 1R2A GLY A 3 UNP P12367 SER 2 CLONING ARTIFACT
SEQADV 1R2A LEU A 23 UNP P12367 INSERTION
SEQADV 1R2A ARG A 24 UNP P12367 GLY 22 VARIANT
SEQADV 1R2A HIS B 1 UNP P12367 CLONING ARTIFACT
SEQADV 1R2A GLY B 3 UNP P12367 SER 2 CLONING ARTIFACT
SEQADV 1R2A LEU B 23 UNP P12367 INSERTION
SEQADV 1R2A ARG B 24 UNP P12367 GLY 22 VARIANT
SEQRES 1 A 46 HIS MET GLY HIS ILE GLN ILE PRO PRO GLY LEU THR GLU
SEQRES 2 A 46 LEU LEU GLN GLY TYR THR VAL GLU VAL LEU ARG GLN GLN
SEQRES 3 A 46 PRO PRO ASP LEU VAL ASP PHE ALA VAL GLU TYR PHE THR
SEQRES 4 A 46 ARG LEU ARG GLU ALA ARG ARG
SEQRES 1 B 46 HIS MET GLY HIS ILE GLN ILE PRO PRO GLY LEU THR GLU
SEQRES 2 B 46 LEU LEU GLN GLY TYR THR VAL GLU VAL LEU ARG GLN GLN
SEQRES 3 B 46 PRO PRO ASP LEU VAL ASP PHE ALA VAL GLU TYR PHE THR
SEQRES 4 B 46 ARG LEU ARG GLU ALA ARG ARG
HELIX 1 1 LEU A 11 ARG A 24 1 14
HELIX 2 2 LEU A 30 ALA A 44 1 15
HELIX 3 3 LEU B 11 ARG B 24 1 14
HELIX 4 4 LEU B 30 ALA B 44 1 15
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
Complete list - r 2 2 Bytes