Header list of 1jo6.pdb file
Complete list - b 23 2 Bytes
HEADER METAL TRANSPORT, MEMBRANE PROTEIN 27-JUL-01 1JO6
TITLE SOLUTION STRUCTURE OF THE CYTOPLASMIC N-TERMINUS OF THE BK BETA-
TITLE 2 SUBUNIT KCNMB2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POTASSIUM LARGE CONDUCTANCE CALCIUM-ACTIVATED CHANNEL,
COMPND 3 SUBFAMILY M, BETA MEMBER 2;
COMPND 4 CHAIN: A;
COMPND 5 FRAGMENT: CYTOPLASMIC N-TERMINUS OF KCNMB2, RESIDUES 1-45;
COMPND 6 SYNONYM: KCNMB2; MAXIK CHANNEL BETA 2 SUBUNIT; LARGE CONDUCTANCE
COMPND 7 CALCIUM-ACTIVATED POTASSIUM CHANNEL BETA2 SUBUNIT;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THE 45-RESIDUE PEPTIDE WAS SYNTHESIZED BY STANDARD
SOURCE 4 SOLID-PHASE SYNTHESIS. THE SEQUENCE OCCURS NATURALLY IN HUMANS.
KEYWDS HELIX, ION CHANNEL, CYTOPLASMIC PART OF, METAL TRANSPORT, MEMBRANE
KEYWDS 2 PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 24
AUTHOR D.BENTROP,M.BEYERMANN,R.WISSMANN,B.FAKLER
REVDAT 4 23-FEB-22 1JO6 1 REMARK
REVDAT 3 24-FEB-09 1JO6 1 VERSN
REVDAT 2 01-APR-03 1JO6 1 JRNL
REVDAT 1 16-NOV-01 1JO6 0
JRNL AUTH D.BENTROP,M.BEYERMANN,R.WISSMANN,B.FAKLER
JRNL TITL NMR STRUCTURE OF THE "BALL-AND-CHAIN" DOMAIN OF KCNMB2, THE
JRNL TITL 2 BETA 2-SUBUNIT OF LARGE CONDUCTANCE CA2+- AND
JRNL TITL 3 VOLTAGE-ACTIVATED POTASSIUM CHANNELS.
JRNL REF J.BIOL.CHEM. V. 276 42116 2001
JRNL REFN ISSN 0021-9258
JRNL PMID 11517232
JRNL DOI 10.1074/JBC.M107118200
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.WALLNER,P.MEERA,L.TORO
REMARK 1 TITL MOLECULAR BASIS OF FAST INACTIVATION IN VOLTAGE AND
REMARK 1 TITL 2 CA2+-ACTIVATED K+ CHANNELS: A TRANSMEMBRANE BETA-SUBUNIT
REMARK 1 TITL 3 HOMOLOG
REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 96 4137 1999
REMARK 1 REFN ISSN 0027-8424
REMARK 1 DOI 10.1073/PNAS.96.7.4137
REMARK 1 REFERENCE 2
REMARK 1 AUTH X.M.XIA,J.P.DING,C.J.LINGLE
REMARK 1 TITL MOLECULAR BASIS FOR THE INACTIVATION OF CA2+- AND
REMARK 1 TITL 2 VOLTAGE-DEPENDENT BK CHANNELS IN ADRENAL CHROMAFFIN CELLS
REMARK 1 TITL 3 AND RAT INSULINOMA TUMOR CELLS
REMARK 1 REF J.NEUROSCI. V. 19 5255 1999
REMARK 1 REFN ISSN 0270-6474
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.6, DYANA 1.5
REMARK 3 AUTHORS : BRUKER (XWINNMR), MUMENTHALER, GUENTERT (DYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURES ARE BASED ON 728 NOE-DERIVED DISTANCE CONSTRAINTS
REMARK 3 (486 INTRARESIDUAL, 191 SEQUENTIAL, 51 MEDIUM-RANGE), 5 DIHEDRAL
REMARK 3 ANGLE
REMARK 3 RESTRAINTS, 11 STEREOSPECIFIC ASSIGNMENTS
REMARK 4
REMARK 4 1JO6 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-AUG-01.
REMARK 100 THE DEPOSITION ID IS D_1000013996.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 288
REMARK 210 PH : 3.0
REMARK 210 IONIC STRENGTH : 0
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 2MM KCNMB2(RESIDUES 1-45), NA;
REMARK 210 90% H2O, 10% D2O; 2MM
REMARK 210 KCNMB2(RESIDUES 1-45), NA; 99.9%
REMARK 210 D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 1H-1H NOESY (2D); DQF-COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : AURELIA 2.7.5, XEASY 1.3.13
REMARK 210 METHOD USED : SIMULATED ANNEALING, TORSION
REMARK 210 ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 30
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 24
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS,TARGET
REMARK 210 FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING STANDARD 2D HOMONUCLEAR
REMARK 210 TECHNIQUES
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 ASP A 29 H ASP A 32 1.56
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 A 2 -168.87 -61.96
REMARK 500 1 THR A 5 -135.69 -76.27
REMARK 500 1 SER A 6 111.49 173.12
REMARK 500 1 THR A 9 -167.92 -116.71
REMARK 500 1 SER A 11 -96.38 -65.04
REMARK 500 1 HIS A 15 -78.79 -61.50
REMARK 500 1 ASP A 16 133.27 -36.94
REMARK 500 1 VAL A 37 -178.70 -68.12
REMARK 500 1 THR A 38 154.58 -49.80
REMARK 500 1 LEU A 40 91.28 43.53
REMARK 500 1 ALA A 42 135.18 -170.68
REMARK 500 2 PHE A 2 142.74 -177.48
REMARK 500 2 THR A 5 -102.21 -69.69
REMARK 500 2 SER A 6 82.55 178.73
REMARK 500 2 THR A 9 -167.97 -116.71
REMARK 500 2 SER A 12 42.11 -88.30
REMARK 500 2 HIS A 15 -75.53 -59.75
REMARK 500 2 ASP A 16 142.06 -38.88
REMARK 500 2 GLU A 17 -95.67 -85.21
REMARK 500 2 LEU A 31 88.68 38.77
REMARK 500 2 LYS A 35 -94.25 49.50
REMARK 500 2 LYS A 41 175.68 -53.65
REMARK 500 2 GLU A 44 132.00 -179.37
REMARK 500 3 PHE A 2 143.00 -172.33
REMARK 500 3 THR A 9 -158.06 -83.31
REMARK 500 3 SER A 11 -96.24 -60.65
REMARK 500 3 ASP A 16 136.47 -38.80
REMARK 500 3 GLU A 17 -82.98 -86.96
REMARK 500 3 LYS A 35 -90.45 54.35
REMARK 500 3 THR A 36 -169.90 44.95
REMARK 500 3 THR A 38 165.72 -46.80
REMARK 500 3 LYS A 41 174.71 -57.67
REMARK 500 3 ALA A 42 166.60 -48.70
REMARK 500 3 GLU A 44 -59.28 -163.79
REMARK 500 4 PHE A 2 149.16 -174.07
REMARK 500 4 THR A 5 -136.53 -78.59
REMARK 500 4 SER A 6 88.39 40.80
REMARK 500 4 THR A 9 -158.04 -83.70
REMARK 500 4 SER A 11 -96.29 -84.92
REMARK 500 4 GLU A 17 -94.85 -85.17
REMARK 500 4 ARG A 34 -69.26 -130.77
REMARK 500 4 LYS A 35 -97.38 43.60
REMARK 500 4 THR A 36 -176.74 -174.41
REMARK 500 4 THR A 38 170.54 -45.34
REMARK 500 4 LYS A 41 178.02 -51.92
REMARK 500 4 GLU A 44 96.17 -47.41
REMARK 500 5 PHE A 2 138.63 -37.11
REMARK 500 5 THR A 5 -102.19 -51.78
REMARK 500 5 SER A 6 95.69 -164.53
REMARK 500 5 ARG A 8 150.94 -48.68
REMARK 500
REMARK 500 THIS ENTRY HAS 309 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1JO6 A 1 45 UNP Q9Y691 KCMB2_HUMAN 1 45
SEQRES 1 A 45 MET PHE ILE TRP THR SER GLY ARG THR SER SER SER TYR
SEQRES 2 A 45 ARG HIS ASP GLU LYS ARG ASN ILE TYR GLN LYS ILE ARG
SEQRES 3 A 45 ASP HIS ASP LEU LEU ASP LYS ARG LYS THR VAL THR ALA
SEQRES 4 A 45 LEU LYS ALA GLY GLU ASP
HELIX 1 1 ILE A 21 LEU A 30 1 10
CRYST1 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 23 2 Bytes