Header list of 1ujl.pdb file
Complete list - r 2 2 Bytes
HEADER MEMBRANE PROTEIN 05-AUG-03 1UJL
TITLE SOLUTION STRUCTURE OF THE HERG K+ CHANNEL S5-P EXTRACELLULAR LINKER
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POTASSIUM VOLTAGE-GATED CHANNEL SUBFAMILY H MEMBER 2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 1-42;
COMPND 5 SYNONYM: HERG K+ CHANNEL S5-P EXTRACELLULAR LINKER, ETHER-A-GO-GO
COMPND 6 RELATED GENE POTASSIUM CHANNEL 1, H-ERG, ERG1, ETHER-A-GO-GO RELATED
COMPND 7 PROTEIN 1, EAG RELATED PROTEIN 1, EAG HOMOLOG;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THE PEPTIDE WAS CHEMICALLY SYNTHESIZED. THE SEQUENCE
SOURCE 4 OF THE PEPTIDE IS NATURALLY FOUND IN HOMO SAPIENS (HUMAN).
KEYWDS TWO HELICES, AMPHIPHATIC HELIX, MEMBRANE PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR A.M.TORRES,P.S.BANSAL,M.SUNDE,C.E.CLARKE,J.A.BURSILL,D.J.SMITH,
AUTHOR 2 A.BAUSKIN,S.N.BREIT,T.J.CAMPBELL,P.F.ALEWOOD,P.W.KUCHEL,
AUTHOR 3 J.I.VANDENBERG
REVDAT 3 02-MAR-22 1UJL 1 REMARK
REVDAT 2 24-FEB-09 1UJL 1 VERSN
REVDAT 1 04-NOV-03 1UJL 0
JRNL AUTH A.M.TORRES,P.S.BANSAL,M.SUNDE,C.E.CLARKE,J.A.BURSILL,
JRNL AUTH 2 D.J.SMITH,A.BAUSKIN,S.N.BREIT,T.J.CAMPBELL,P.F.ALEWOOD,
JRNL AUTH 3 P.W.KUCHEL,J.I.VANDENBERG
JRNL TITL STRUCTURE OF THE HERG K+ CHANNEL S5P EXTRACELLULAR LINKER:
JRNL TITL 2 ROLE OF AN AMPHIPATHIC ALPHA-HELIX IN C-TYPE INACTIVATION.
JRNL REF J.BIOL.CHEM. V. 278 42136 2003
JRNL REFN ISSN 0021-9258
JRNL PMID 13680209
JRNL DOI 10.1074/JBC.M212824200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 3.1, CNS 1.1
REMARK 3 AUTHORS : BRUKER (XWINNMR), BRUNGER, A. T., ADAMS, P.D.,
REMARK 3 CLORE, G.M., DELANO, W.L., GROS, P., GROSSE-
REMARK 3 KUNSTLEVE, R.W., JIANG, J.S., KUSZEWSKI, J.,
REMARK 3 NILGES, M., PANNU, N.S., READ, R.J., RICE, L.M.,
REMARK 3 SIMONSON, T., WARREN, G.L. (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURES ARE BASED ON A TOTAL OF 430 RESTRAINTS, 416 ARE NOE-
REMARK 3 DERIVED
REMARK 3 DISTANCE CONSTRAINTS, 14 DISTANCE RESTRAINTS FROM HYDROGEN BONDS.
REMARK 4
REMARK 4 1UJL COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 05-AUG-03.
REMARK 100 THE DEPOSITION ID IS D_1000005897.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 3.3
REMARK 210 IONIC STRENGTH : 0
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.4MM S5-P PEPTIDE
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY
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 : XEASY 1.3.13, DYANA 1.5
REMARK 210 METHOD USED : SIMULATED ANNEALING, MOLECULAR
REMARK 210 DYNAMICS, DISTANCE GEOMETRY,
REMARK 210 TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 1600
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 8
REMARK 210
REMARK 210 REMARK: THE STRUCTURES WERE DETERMINED USING STANDARD 2D
REMARK 210 HOMONUCLEAR 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: 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 MET A 5 163.65 -49.53
REMARK 500 1 GLU A 6 65.67 -69.66
REMARK 500 1 PRO A 8 64.29 -69.42
REMARK 500 1 ASP A 11 -74.68 -118.61
REMARK 500 1 ILE A 14 -168.90 43.92
REMARK 500 1 ILE A 24 -67.21 -98.16
REMARK 500 1 TYR A 28 40.12 -159.50
REMARK 500 1 ASN A 29 92.84 49.62
REMARK 500 1 SER A 30 54.58 -140.79
REMARK 500 1 SER A 31 165.37 62.41
REMARK 500 2 ASN A 4 32.11 -161.23
REMARK 500 2 MET A 5 173.69 -48.24
REMARK 500 2 GLU A 6 66.20 -69.75
REMARK 500 2 HIS A 9 79.17 -106.66
REMARK 500 2 ARG A 13 -52.39 -129.62
REMARK 500 2 ILE A 14 -168.07 43.83
REMARK 500 2 ASN A 19 -50.32 -130.46
REMARK 500 2 SER A 30 78.05 -118.51
REMARK 500 2 SER A 31 102.16 60.91
REMARK 500 3 MET A 5 92.60 -49.96
REMARK 500 3 GLU A 6 -156.39 -82.98
REMARK 500 3 MET A 10 44.45 -94.89
REMARK 500 3 ARG A 13 -47.45 81.34
REMARK 500 3 ASN A 19 -47.50 -130.34
REMARK 500 3 TYR A 28 -114.16 -149.49
REMARK 500 3 SER A 30 109.11 60.70
REMARK 500 3 SER A 31 75.54 61.11
REMARK 500 4 MET A 5 102.68 -45.23
REMARK 500 4 GLU A 6 -46.76 -158.66
REMARK 500 4 HIS A 9 120.59 176.93
REMARK 500 4 MET A 10 61.70 32.34
REMARK 500 4 ARG A 13 -60.02 -155.85
REMARK 500 4 ASN A 19 -50.94 -131.10
REMARK 500 4 LYS A 26 62.14 -152.58
REMARK 500 4 TYR A 28 82.04 -174.35
REMARK 500 4 SER A 31 168.72 60.62
REMARK 500 5 ASN A 4 22.98 -154.97
REMARK 500 5 MET A 5 174.74 -48.77
REMARK 500 5 GLU A 6 87.01 -54.06
REMARK 500 5 HIS A 9 -62.49 -103.74
REMARK 500 5 ARG A 13 46.22 -163.83
REMARK 500 5 TYR A 28 38.45 176.08
REMARK 500 5 ASN A 29 99.56 51.08
REMARK 500 5 SER A 30 -134.99 -107.36
REMARK 500 5 SER A 31 -56.48 -156.06
REMARK 500 6 MET A 5 90.93 -50.65
REMARK 500 6 GLU A 6 37.85 179.81
REMARK 500 6 PRO A 8 85.35 -61.29
REMARK 500 6 HIS A 9 -65.58 -109.03
REMARK 500 6 ARG A 13 -73.29 -60.75
REMARK 500
REMARK 500 THIS ENTRY HAS 174 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1UJL A 1 42 UNP Q12809 KCH2_HUMAN 570 611
SEQRES 1 A 42 ALA ILE GLY ASN MET GLU GLN PRO HIS MET ASP SER ARG
SEQRES 2 A 42 ILE GLY TRP LEU HIS ASN LEU GLY ASP GLN ILE GLY LYS
SEQRES 3 A 42 PRO TYR ASN SER SER GLY LEU GLY GLY PRO SER ILE LYS
SEQRES 4 A 42 ASP LYS TYR
HELIX 1 1 TRP A 16 GLY A 25 1 10
HELIX 2 2 GLY A 35 TYR A 42 1 8
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