Header list of 1zxa.pdb file
Complete list - r 2 2 Bytes
HEADER TRANSFERASE 07-JUN-05 1ZXA
TITLE SOLUTION STRUCTURE OF THE COILED-COIL DOMAIN OF CGMP-DEPENDENT PROTEIN
TITLE 2 KINASE IA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CGMP-DEPENDENT PROTEIN KINASE 1, ALPHA ISOZYME;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: N-TERMINAL COILED-COIL DOMAIN, RESIDUES 1-58;
COMPND 5 SYNONYM: CGK 1 ALPHA, CGKI-ALPHA;
COMPND 6 EC: 2.7.1.37;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: PRKG1, PRKGR1A;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX-2T
KEYWDS PARALLEL COILED COIL DIMER, TRANSFERASE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR J.R.SCHNELL,G.P.ZHOU,M.ZWECKSTETTER,A.C.RIGBY,J.J.CHOU
REVDAT 3 02-MAR-22 1ZXA 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1ZXA 1 VERSN
REVDAT 1 13-SEP-05 1ZXA 0
JRNL AUTH J.R.SCHNELL,G.P.ZHOU,M.ZWECKSTETTER,A.C.RIGBY,J.J.CHOU
JRNL TITL RAPID AND ACCURATE STRUCTURE DETERMINATION OF COILED-COIL
JRNL TITL 2 DOMAINS USING NMR DIPOLAR COUPLINGS: APPLICATION TO
JRNL TITL 3 CGMP-DEPENDENT PROTEIN KINASE I{ALPHA}
JRNL REF PROTEIN SCI. V. 14 2421 2005
JRNL REFN ISSN 0961-8368
JRNL PMID 16131665
JRNL DOI 10.1110/PS.051528905
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 3.5, XPLOR-NIH 2.9.9
REMARK 3 AUTHORS : BRUKER (XWINNMR),
REMARK 3 C.D.SCHWIETERS,J.J.KUSZEWSKI,N.TJANDRA,G.M.CLORE
REMARK 3 (XPLOR-NIH)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 STRUCTURE DETERMINATION CONSISTS OF FIVE STEPS.
REMARK 3
REMARK 3 1. MEASURE RDCS IN PF1 ALIGNMENT MEDIUM.
REMARK 3 2. IDENTIFY THE COILED-COIL MOTIF BY RDC-BASED MOLECULAR
REMARK 3 REPLACEMENT ANALYSIS.
REMARK 3 3) DEFINE THE SUBTLE CURVATURE AND SUPER-COILING OF THE
REMARK 3 CONSTITUENT HELICES BY RDC REFINEMENT
REMARK 3 4) ASSEMBLE PARALLEL AND ANTI-PARALLEL MODELS OF THE COILED-COIL
REMARK 3 DIMER USING KNOWLEDGE-BASED INTER-MOLECULAR DISTANCE RESTRAINTS.
REMARK 3 5) DERIVE THE CORRECT MONOMER-MONOMER ORIENTATION BY COMPARING
REMARK 3 EXPERIMENTAL RDCS WITH THOSE PREDICTED FROM THE 3D CHARGE
REMARK 3 DISTRIBUTION AND SHAPE OF THE ALTERNATIVE STRUCTURAL MODELS.
REMARK 4
REMARK 4 1ZXA COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-JUN-05.
REMARK 100 THE DEPOSITION ID IS D_1000033226.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303; 303
REMARK 210 PH : 7.0; 7.0
REMARK 210 IONIC STRENGTH : 30 MM SALT; 30 MM SALT
REMARK 210 PRESSURE : AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 1 MM CGK1A(1-59) U-15N,13C, 85%
REMARK 210 -2H, 20 MM PHOSPHATE BUFFER NA,
REMARK 210 10 MM NACL, 1 MM EDTA, 5 MM DTT,
REMARK 210 1 MM AZIDE, 95% H2O, 5% D2O; 1
REMARK 210 MM CGK1A(1-59) U-15N,13C, 85%-2H,
REMARK 210 20 MM PHOSPHATE BUFFER NA, 10
REMARK 210 MM NACL, 1 MM EDTA, 5 MM DTT, 1
REMARK 210 MM AZIDE, 15 MG/ML PF1, 95% H2O,
REMARK 210 5% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : TROSY VERSION OF HNCA, HNCACB,
REMARK 210 HNCACO; 2D 1H-15N SPIN ECHO
REMARK 210 DIFFERENCE EXPERIMENTS FOR 3-
REMARK 210 BOND JCC AND JNC MEASUREMENT;
REMARK 210 STANDARD HNCO-BASED 3D
REMARK 210 EXPERIMENTS FOR MEASURING ONE-
REMARK 210 BOND J(NH), J(NC'), AND J(C'CA);
REMARK 210 STANDARD HNCO-BASED 3D
REMARK 210 EXPERIMENTS FOR MEASURING ONE-
REMARK 210 BOND D(NH), D(NC'), AND D(C'CA);
REMARK 210 STANDARD 2D EXPERIMENTS FOR
REMARK 210 MEASURING 15N T1 AND T2
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE; DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 2.2, PALES 1
REMARK 210 METHOD USED : SIMULATED ANNEALING, RDC
REMARK 210 REFINEMENT AND ANALYSIS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 20
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : ALL CALCULATED STRUCTURES
REMARK 210 SUBMITTED
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 20
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-20
REMARK 465 RES C SSSEQI
REMARK 465 GLY A -7
REMARK 465 SER A -6
REMARK 465 PRO A -5
REMARK 465 GLY A -4
REMARK 465 ILE A -3
REMARK 465 PRO A -2
REMARK 465 GLY A -1
REMARK 465 SER A 0
REMARK 465 THR A 1
REMARK 465 SER A 2
REMARK 465 GLU A 3
REMARK 465 LEU A 4
REMARK 465 GLU A 5
REMARK 465 GLU A 6
REMARK 465 ASP A 7
REMARK 465 PHE A 8
REMARK 465 SER A 45
REMARK 465 VAL A 46
REMARK 465 LEU A 47
REMARK 465 PRO A 48
REMARK 465 VAL A 49
REMARK 465 PRO A 50
REMARK 465 SER A 51
REMARK 465 THR A 52
REMARK 465 HIS A 53
REMARK 465 ILE A 54
REMARK 465 GLY A 55
REMARK 465 PRO A 56
REMARK 465 ARG A 57
REMARK 465 THR A 58
REMARK 465 THR A 59
REMARK 465 GLY B -7
REMARK 465 SER B -6
REMARK 465 PRO B -5
REMARK 465 GLY B -4
REMARK 465 ILE B -3
REMARK 465 PRO B -2
REMARK 465 GLY B -1
REMARK 465 SER B 0
REMARK 465 THR B 1
REMARK 465 SER B 2
REMARK 465 GLU B 3
REMARK 465 LEU B 4
REMARK 465 GLU B 5
REMARK 465 GLU B 6
REMARK 465 ASP B 7
REMARK 465 PHE B 8
REMARK 465 SER B 45
REMARK 465 VAL B 46
REMARK 465 LEU B 47
REMARK 465 PRO B 48
REMARK 465 VAL B 49
REMARK 465 PRO B 50
REMARK 465 SER B 51
REMARK 465 THR B 52
REMARK 465 HIS B 53
REMARK 465 ILE B 54
REMARK 465 GLY B 55
REMARK 465 PRO B 56
REMARK 465 ARG B 57
REMARK 465 THR B 58
REMARK 465 THR B 59
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 7 ILE A 19 -70.41 -63.22
REMARK 500 9 ILE A 19 -71.66 -64.19
REMARK 500 9 LYS A 20 -39.47 -39.36
REMARK 500 9 ILE B 19 -70.85 -63.20
REMARK 500 10 ILE A 19 -70.78 -64.18
REMARK 500 12 ILE B 19 -71.34 -65.75
REMARK 500 16 ILE A 19 -70.72 -62.16
REMARK 500 16 ILE B 19 -73.34 -62.32
REMARK 500 17 ILE B 19 -70.71 -64.60
REMARK 500 17 LYS B 20 -39.77 -39.05
REMARK 500 18 ILE A 19 -73.15 -63.70
REMARK 500 19 ILE A 19 -71.70 -62.88
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1ZXA A 2 59 UNP Q13976 KGP1A_HUMAN 1 58
DBREF 1ZXA B 2 59 UNP Q13976 KGP1A_HUMAN 1 58
SEQADV 1ZXA GLY A -7 UNP Q13976 CLONING ARTIFACT
SEQADV 1ZXA GLY B -7 UNP Q13976 CLONING ARTIFACT
SEQADV 1ZXA SER A -6 UNP Q13976 CLONING ARTIFACT
SEQADV 1ZXA SER B -6 UNP Q13976 CLONING ARTIFACT
SEQADV 1ZXA PRO A -5 UNP Q13976 CLONING ARTIFACT
SEQADV 1ZXA PRO B -5 UNP Q13976 CLONING ARTIFACT
SEQADV 1ZXA GLY A -4 UNP Q13976 CLONING ARTIFACT
SEQADV 1ZXA GLY B -4 UNP Q13976 CLONING ARTIFACT
SEQADV 1ZXA ILE A -3 UNP Q13976 CLONING ARTIFACT
SEQADV 1ZXA ILE B -3 UNP Q13976 CLONING ARTIFACT
SEQADV 1ZXA PRO A -2 UNP Q13976 CLONING ARTIFACT
SEQADV 1ZXA PRO B -2 UNP Q13976 CLONING ARTIFACT
SEQADV 1ZXA GLY A -1 UNP Q13976 CLONING ARTIFACT
SEQADV 1ZXA GLY B -1 UNP Q13976 CLONING ARTIFACT
SEQADV 1ZXA SER A 0 UNP Q13976 CLONING ARTIFACT
SEQADV 1ZXA SER B 0 UNP Q13976 CLONING ARTIFACT
SEQADV 1ZXA THR A 1 UNP Q13976 CLONING ARTIFACT
SEQADV 1ZXA THR B 1 UNP Q13976 CLONING ARTIFACT
SEQRES 1 A 67 GLY SER PRO GLY ILE PRO GLY SER THR SER GLU LEU GLU
SEQRES 2 A 67 GLU ASP PHE ALA LYS ILE LEU MET LEU LYS GLU GLU ARG
SEQRES 3 A 67 ILE LYS GLU LEU GLU LYS ARG LEU SER GLU LYS GLU GLU
SEQRES 4 A 67 GLU ILE GLN GLU LEU LYS ARG LYS LEU HIS LYS CYS GLN
SEQRES 5 A 67 SER VAL LEU PRO VAL PRO SER THR HIS ILE GLY PRO ARG
SEQRES 6 A 67 THR THR
SEQRES 1 B 67 GLY SER PRO GLY ILE PRO GLY SER THR SER GLU LEU GLU
SEQRES 2 B 67 GLU ASP PHE ALA LYS ILE LEU MET LEU LYS GLU GLU ARG
SEQRES 3 B 67 ILE LYS GLU LEU GLU LYS ARG LEU SER GLU LYS GLU GLU
SEQRES 4 B 67 GLU ILE GLN GLU LEU LYS ARG LYS LEU HIS LYS CYS GLN
SEQRES 5 B 67 SER VAL LEU PRO VAL PRO SER THR HIS ILE GLY PRO ARG
SEQRES 6 B 67 THR THR
HELIX 1 1 ALA A 9 GLN A 44 1 36
HELIX 2 2 ALA B 9 GLN B 44 1 36
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