Header list of 1bak.pdb file
Complete list - b 16 2 Bytes
HEADER TRANSFERASE 21-NOV-97 1BAK
TITLE SIGNAL TRANSDUCTION PLECKSTRIN HOMOLOGY DOMAIN OF G-PROTEIN COUPLED
TITLE 2 RECEPTOR KINASE 2 (BETA-ADRENERGIC RECEPTOR KINASE 1), C-TERMINAL
TITLE 3 EXTENDED, NMR, 20 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: G-PROTEIN COUPLED RECEPTOR KINASE 2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: C-TERMINAL EXTENDED PLECKSTRIN HOMOLOGY DOMAIN;
COMPND 5 SYNONYM: GRK-2, BETA-ADRENERGIC RECEPTOR KINASE 1, BETA-ARK 1;
COMPND 6 EC: 2.7.1.126;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PLECKSTRIN HOMOLOGY DOMAIN, PH DOMAIN, SIGNAL TRANSDUCTION, G-BETA-
KEYWDS 2 GAMMA BINDING DOMAIN, BETA-ADRENERGIC RECEPTOR KINASE, BETA-ARK, G-
KEYWDS 3 PROTEIN COUPLED RECEPTOR KINASE (GRK-2), TRANSFERASE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR D.FUSHMAN,D.COWBURN
REVDAT 4 16-FEB-22 1BAK 1 REMARK
REVDAT 3 24-FEB-09 1BAK 1 VERSN
REVDAT 2 01-APR-03 1BAK 1 JRNL
REVDAT 1 25-FEB-98 1BAK 0
JRNL AUTH D.FUSHMAN,T.NAJMABADI-HASKE,S.CAHILL,J.ZHENG,H.LEVINE 3RD.,
JRNL AUTH 2 D.COWBURN
JRNL TITL THE SOLUTION STRUCTURE AND DYNAMICS OF THE PLECKSTRIN
JRNL TITL 2 HOMOLOGY DOMAIN OF G PROTEIN-COUPLED RECEPTOR KINASE 2
JRNL TITL 3 (BETA-ADRENERGIC RECEPTOR KINASE 1). A BINDING PARTNER OF
JRNL TITL 4 GBETAGAMMA SUBUNITS.
JRNL REF J.BIOL.CHEM. V. 273 2835 1998
JRNL REFN ISSN 0021-9258
JRNL PMID 9446593
JRNL DOI 10.1074/JBC.273.5.2835
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH D.MAHADEVAN,N.THANKI,J.SINGH,P.MCPHIE,D.ZANGRILLI,L.M.WANG,
REMARK 1 AUTH 2 C.GUERRERO,H.LEVINE III,C.HUMBLET,J.SALDANHA,J.S.GUTKIND,
REMARK 1 AUTH 3 T.NAJMABADI-HASKE
REMARK 1 TITL STRUCTURAL STUDIES ON THE PH DOMAINS OF DBL, SOS1, IRS-1,
REMARK 1 TITL 2 AND BETA ARK1 AND THEIR DIFFERENTIAL BINDING TO G BETA GAMMA
REMARK 1 TITL 3 SUBUNITS
REMARK 1 REF BIOCHEMISTRY V. 34 9111 1995
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 2
REMARK 1 AUTH K.TOUHARA,J.INGLESE,J.A.PITCHER,G.SHAW,R.J.LEFKOWITZ
REMARK 1 TITL BINDING OF G PROTEIN BETA GAMMA-SUBUNITS TO PLECKSTRIN
REMARK 1 TITL 2 HOMOLOGY DOMAINS
REMARK 1 REF J.BIOL.CHEM. V. 269 10217 1994
REMARK 1 REFN ISSN 0021-9258
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR, DYANA
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1BAK COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000171529.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 308
REMARK 210 PH : 4.5
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 1H-15N)HSQC; (1H-13C)HSQC; HSQC
REMARK 210 -J; HTQC; 2D AND 3D 15N-NOESY-
REMARK 210 HMQC (IN H2O; IN D2O) AND HOHAHA-
REMARK 210 HMQC; 13C-NOESY-HMQC; HCCH-TOCSY;
REMARK 210 CBCANH; CBCA(CO)NH; HNCA; HN(CO)
REMARK 210 CA; HNCO; {1H}15N-NOE; H2O-
REMARK 210 SELECTIVE 15N-EDITED NOESY AND
REMARK 210 ROESY; H-D-EXCHANGE
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : DMX500; DMX600
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XEASY, DIANA, DYANA
REMARK 210 METHOD USED : DISTANCE GEOMETRY
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 400
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION
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: 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 O LYS A 644 H ARG A 648 1.47
REMARK 500 O GLU A 610 H LEU A 621 1.50
REMARK 500 H THR A 612 O CYS A 619 1.55
REMARK 500 O ASP A 649 H GLU A 653 1.60
REMARK 500 O PRO A 638 H GLN A 642 1.60
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 553 78.62 48.45
REMARK 500 1 HIS A 554 -60.93 -146.82
REMARK 500 1 ASP A 558 -107.68 -77.94
REMARK 500 1 MET A 568 -179.97 157.57
REMARK 500 1 ASN A 570 -59.46 -168.88
REMARK 500 1 ASN A 586 -38.28 -165.58
REMARK 500 1 LEU A 588 119.85 177.72
REMARK 500 1 SER A 599 51.84 -155.08
REMARK 500 1 THR A 602 -159.68 -123.74
REMARK 500 1 GLU A 605 -53.90 -158.05
REMARK 500 1 ILE A 606 136.98 -29.46
REMARK 500 1 SER A 608 134.29 -173.72
REMARK 500 1 LYS A 615 -32.98 82.13
REMARK 500 1 GLU A 616 -50.42 -156.38
REMARK 500 1 LYS A 618 -98.55 -124.29
REMARK 500 1 LEU A 622 89.67 -154.82
REMARK 500 1 GLU A 639 -79.98 -26.95
REMARK 500 1 ARG A 660 65.85 -68.07
REMARK 500 1 MET A 664 85.14 61.64
REMARK 500 1 LYS A 665 -62.66 -151.16
REMARK 500 1 ASN A 666 -58.11 75.95
REMARK 500 1 LYS A 667 91.42 48.07
REMARK 500 1 ARG A 669 153.47 63.04
REMARK 500 2 LYS A 557 -106.46 -130.61
REMARK 500 2 ASP A 558 22.81 -152.49
REMARK 500 2 CYS A 559 128.48 -170.30
REMARK 500 2 THR A 574 -16.50 -158.21
REMARK 500 2 ASN A 586 -41.79 -164.74
REMARK 500 2 LEU A 588 116.61 178.97
REMARK 500 2 GLU A 595 145.99 -175.21
REMARK 500 2 ALA A 596 160.42 177.33
REMARK 500 2 PRO A 597 -163.55 -74.98
REMARK 500 2 THR A 602 -162.72 -114.29
REMARK 500 2 GLU A 605 -53.55 -158.70
REMARK 500 2 ILE A 606 139.41 -32.43
REMARK 500 2 SER A 608 135.24 -174.05
REMARK 500 2 LYS A 615 -32.92 81.51
REMARK 500 2 GLU A 616 -47.95 -156.92
REMARK 500 2 LYS A 618 -98.20 -119.20
REMARK 500 2 LEU A 622 84.60 -160.25
REMARK 500 2 GLU A 639 -83.42 -23.05
REMARK 500 2 ARG A 652 -70.73 -76.57
REMARK 500 2 GLU A 653 -33.17 -36.25
REMARK 500 2 GLN A 659 45.33 -84.79
REMARK 500 2 MET A 664 57.26 -162.56
REMARK 500 2 LYS A 665 62.66 -170.61
REMARK 500 2 ARG A 669 167.25 55.83
REMARK 500 3 SER A 553 117.58 66.02
REMARK 500 3 HIS A 554 72.16 -175.29
REMARK 500 3 LYS A 557 70.45 -152.57
REMARK 500
REMARK 500 THIS ENTRY HAS 424 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1BAK A 556 670 UNP P25098 ARBK1_HUMAN 556 670
SEQRES 1 A 119 GLY SER HIS MET GLY LYS ASP CYS ILE MET HIS GLY TYR
SEQRES 2 A 119 MET SER LYS MET GLY ASN PRO PHE LEU THR GLN TRP GLN
SEQRES 3 A 119 ARG ARG TYR PHE TYR LEU PHE PRO ASN ARG LEU GLU TRP
SEQRES 4 A 119 ARG GLY GLU GLY GLU ALA PRO GLN SER LEU LEU THR MET
SEQRES 5 A 119 GLU GLU ILE GLN SER VAL GLU GLU THR GLN ILE LYS GLU
SEQRES 6 A 119 ARG LYS CYS LEU LEU LEU LYS ILE ARG GLY GLY LYS GLN
SEQRES 7 A 119 PHE ILE LEU GLN CYS ASP SER ASP PRO GLU LEU VAL GLN
SEQRES 8 A 119 TRP LYS LYS GLU LEU ARG ASP ALA TYR ARG GLU ALA GLN
SEQRES 9 A 119 GLN LEU VAL GLN ARG VAL PRO LYS MET LYS ASN LYS PRO
SEQRES 10 A 119 ARG SER
HELIX 1 1 ASP A 637 VAL A 658 1 22
SHEET 1 A 7 ILE A 606 THR A 612 0
SHEET 2 A 7 CYS A 619 ILE A 624 -1 N LYS A 623 O GLN A 607
SHEET 3 A 7 GLN A 629 GLN A 633 -1 N LEU A 632 O LEU A 620
SHEET 4 A 7 MET A 561 MET A 568 -1 N MET A 568 O ILE A 631
SHEET 5 A 7 ARG A 578 LEU A 583 -1 N LEU A 583 O MET A 561
SHEET 6 A 7 ARG A 587 ARG A 591 -1 N ARG A 591 O TYR A 580
SHEET 7 A 7 LEU A 600 THR A 602 -1 N LEU A 601 O LEU A 588
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 - b 16 2 Bytes