Header list of 1r48.pdb file
Complete list - r 2 2 Bytes
HEADER TRANSPORT PROTEIN 03-OCT-03 1R48
TITLE SOLUTION STRUCTURE OF THE C-TERMINAL CYTOPLASMIC DOMAIN RESIDUES 468-
TITLE 2 497 OF ESCHERICHIA COLI PROTEIN PROP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROLINE/BETAINE TRANSPORTER;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: C-TERMINAL DOMAIN (RESIDUE 468-497);
COMPND 5 SYNONYM: PROLINE PORTER II, PPII;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: SYNTHETIC PEPTIDE INCLUDING A CGG N-TERMINAL LINKER
SOURCE 4 BLOCKED WITH IODOACETAMIDE, N-TERMINALLY ACETYLATED, C-TERMINALLY
SOURCE 5 AMIDATED. THIS SEQUENCE IS NATURALLY PRESENT IN ESCHERICHIA COLI.
KEYWDS OSMOSENSOR, CYTOPLASMIC, COILED-COIL, ANTIPARALLEL, TWO-STRANDED
KEYWDS 2 HOMODIMER, TRANSPORT PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 51
MDLTYP MINIMIZED AVERAGE
AUTHOR D.L.ZOETEWEY,B.P.TRIPET,T.G.KUTATELADZE,M.J.OVERDUIN,J.M.WOOD,
AUTHOR 2 R.S.HODGES
REVDAT 3 02-MAR-22 1R48 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1R48 1 VERSN
REVDAT 1 23-DEC-03 1R48 0
JRNL AUTH D.L.ZOETEWEY,B.P.TRIPET,T.G.KUTATELADZE,M.J.OVERDUIN,
JRNL AUTH 2 J.M.WOOD,R.S.HODGES
JRNL TITL SOLUTION STRUCTURE OF THE C-TERMINAL ANTIPARALLEL
JRNL TITL 2 COILED-COIL DOMAIN FROM ESCHERICHIA COLI OSMOSENSOR PROP.
JRNL REF J.MOL.BIOL. V. 334 1063 2003
JRNL REFN ISSN 0022-2836
JRNL PMID 14643666
JRNL DOI 10.1016/J.JMB.2003.10.020
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1, CNS 1.1
REMARK 3 AUTHORS : BRUNGER, ADAMS, CLORE, DELANO, GROS, GROSSE
REMARK 3 -KUNSTLEVE, JIANG, KUSZEWSKI, NILGES, PANNU, READ,
REMARK 3 RICE, SIMONSON, WARREN (CNS), BRUNGER, ADAMS,
REMARK 3 CLORE, DELANO, GROS, GROSSE-KUNSTLEVE, JIANG,
REMARK 3 KUSZEWSKI, NILGES, PANNU, READ, RICE, SIMONSON,
REMARK 3 WARREN (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON 676 TOTAL
REMARK 3 RESTRAINTS, 632 NOE-DERIVED DISTANCE CONSTRAINTS AND 44 HYDROGEN-
REMARK 3 BOND DISTANCE RESTRAINTS.
REMARK 4
REMARK 4 1R48 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-NOV-03.
REMARK 100 THE DEPOSITION ID IS D_1000020416.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293
REMARK 210 PH : 5
REMARK 210 IONIC STRENGTH : 150 MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 2 MM UNLABLED PEPTIDE PROP 468
REMARK 210 -497, 50 MM POTASSIUM PHOSPHATE,
REMARK 210 100 MM KCL, 90% H2O, 10% D2O, 1
REMARK 210 MM NAN3
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; DQF-COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 63
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 51
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH FAVORABLE NON
REMARK 210 -BOND ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
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 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 13 ASP A 4 -80.80 -158.86
REMARK 500 13 ASN A 5 -43.32 -144.67
REMARK 500 15 ASP A 4 -83.92 -121.49
REMARK 500 15 ASN A 5 -45.18 -146.62
REMARK 500 16 ASP A 4 -83.66 -118.07
REMARK 500 16 ASN A 5 -44.09 -146.63
REMARK 500 18 ASP A 4 -84.26 -127.39
REMARK 500 18 ASN A 5 -44.22 -144.33
REMARK 500 19 ASP B 4 -84.87 -129.47
REMARK 500 19 ASN B 5 -44.26 -140.29
REMARK 500 21 PRO A 32 -167.65 -69.84
REMARK 500 25 ASP A 4 -84.14 -125.88
REMARK 500 25 ASN A 5 -45.61 -144.31
REMARK 500 27 ASP A 4 -84.13 -135.45
REMARK 500 27 ASN A 5 -43.77 -143.25
REMARK 500 27 PRO A 32 -71.74 -57.99
REMARK 500 28 ASP A 4 -84.54 -123.69
REMARK 500 28 ASN A 5 -44.37 -142.94
REMARK 500 30 ASP A 4 -83.58 -138.49
REMARK 500 30 ASN A 5 -44.45 -145.46
REMARK 500 30 ASP B 4 -84.84 -128.83
REMARK 500 30 ASN B 5 -45.01 -141.19
REMARK 500 31 PRO B 32 -168.03 -69.06
REMARK 500 32 ASP A 4 -84.21 -119.47
REMARK 500 32 ASN A 5 -45.05 -144.75
REMARK 500 34 ASP A 4 -83.97 -132.94
REMARK 500 34 ASN A 5 -44.78 -144.13
REMARK 500 34 PRO B 32 -167.74 -77.87
REMARK 500 35 ASP A 4 -83.88 -122.77
REMARK 500 35 ASN A 5 -45.12 -145.68
REMARK 500 36 ASP A 4 -83.71 -141.10
REMARK 500 36 ASN A 5 -43.07 -142.90
REMARK 500 36 ASP B 4 -84.78 -123.07
REMARK 500 36 ASN B 5 -44.80 -141.46
REMARK 500 38 ASP A 4 -79.85 -161.16
REMARK 500 38 ASN A 5 -44.47 -146.95
REMARK 500 38 ASP B 4 -84.43 -130.73
REMARK 500 38 ASN B 5 -44.69 -142.43
REMARK 500 40 ASP B 4 -80.31 -160.31
REMARK 500 40 ASN B 5 -43.48 -144.81
REMARK 500 41 ASP A 4 -80.13 -161.21
REMARK 500 41 ASN A 5 -43.91 -144.09
REMARK 500 42 ASP A 4 -84.15 -126.87
REMARK 500 42 ASN A 5 -43.66 -144.57
REMARK 500 43 ASP B 4 -81.87 -156.71
REMARK 500 43 ASN B 5 -43.37 -139.35
REMARK 500 44 ILE A 6 -48.97 -139.98
REMARK 500 45 ASP A 4 -80.79 -158.54
REMARK 500 45 ASN A 5 -43.69 -145.69
REMARK 500 45 PRO A 32 -168.08 -72.85
REMARK 500
REMARK 500 THIS ENTRY HAS 63 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1R48 A 4 33 UNP P30848 PROP_ECOLI 468 497
DBREF 1R48 B 4 33 UNP P30848 PROP_ECOLI 468 497
SEQADV 1R48 CYS A 1 UNP P30848 INSERTION
SEQADV 1R48 GLY A 2 UNP P30848 INSERTION
SEQADV 1R48 GLY A 3 UNP P30848 INSERTION
SEQADV 1R48 CYS B 1 UNP P30848 INSERTION
SEQADV 1R48 GLY B 2 UNP P30848 INSERTION
SEQADV 1R48 GLY B 3 UNP P30848 INSERTION
SEQRES 1 A 33 CYS GLY GLY ASP ASN ILE GLU GLN LYS ILE ASP ASP ILE
SEQRES 2 A 33 ASP HIS GLU ILE ALA ASP LEU GLN ALA LYS ARG THR ARG
SEQRES 3 A 33 LEU VAL GLN GLN HIS PRO ARG
SEQRES 1 B 33 CYS GLY GLY ASP ASN ILE GLU GLN LYS ILE ASP ASP ILE
SEQRES 2 B 33 ASP HIS GLU ILE ALA ASP LEU GLN ALA LYS ARG THR ARG
SEQRES 3 B 33 LEU VAL GLN GLN HIS PRO ARG
HELIX 1 1 ASP A 4 HIS A 31 1 28
HELIX 2 2 ASP B 4 HIS B 31 1 28
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