Header list of 1aoy.pdb file
Complete list - r 25 2 Bytes
HEADER DNA-BINDING PROTEIN 14-JUL-97 1AOY
TITLE N-TERMINAL DOMAIN OF ESCHERICHIA COLI ARGININE REPRESSOR NMR, 23
TITLE 2 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ARGININE REPRESSOR;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: N-TERMINAL;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 83333;
SOURCE 4 STRAIN: K12;
SOURCE 5 CELL_LINE: BL21;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: X90 (DE3) AND BL21 (DE3) ARG;
SOURCE 9 EXPRESSION_SYSTEM_VARIANT: T7;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PET;
SOURCE 11 EXPRESSION_SYSTEM_VECTOR: PET3A;
SOURCE 12 EXPRESSION_SYSTEM_PLASMID: BL21
KEYWDS DNA-BINDING PROTEIN, EXPRESSION REGULATION, DNA ORGANIZATION, WINGED
KEYWDS 2 HELIX
EXPDTA SOLUTION NMR
NUMMDL 23
AUTHOR M.SUNNERHAGEN,M.NILGES,G.OTTING
REVDAT 3 13-JUL-11 1AOY 1 VERSN
REVDAT 2 24-FEB-09 1AOY 1 VERSN
REVDAT 1 17-SEP-97 1AOY 0
JRNL AUTH M.SUNNERHAGEN,M.NILGES,G.OTTING,J.CAREY
JRNL TITL SOLUTION STRUCTURE OF THE DNA-BINDING DOMAIN AND MODEL FOR
JRNL TITL 2 THE COMPLEX OF MULTIFUNCTIONAL HEXAMERIC ARGININE REPRESSOR
JRNL TITL 3 WITH DNA.
JRNL REF NAT.STRUCT.BIOL. V. 4 819 1997
JRNL REFN ISSN 1072-8368
JRNL PMID 9334747
JRNL DOI 10.1038/NSB1097-819
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR (MODIFIED) (MODIFIED)
REMARK 3 AUTHORS : BRUNGER (MODIFICATIONS: NILGES)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: STRUCTURES WERE CALCULATED WITH A
REMARK 3 MODIFIED VERSION OF X-PLOR WITH A SIMULATED ANNEALING PROTOCOL.
REMARK 3 AN AUTOMATED PROCEDURE (ARIA) WAS USED TO AUTOMATICALLY
REMARK 3 CALIBRATE, SELECT AND ASSIGN PEAK LISTS FROM HOMONUCLEAR H2O AND
REMARK 3 D2O AND N15-EDITED 3D NOESY SPECTRA. 20 STRUCTURES WERE
REMARK 3 ITERATIVELY REFINED, AND THE NOE DATA RE-ASSIGNED ON THE BASIS OF
REMARK 3 THE 7 LOWEST ENERGY STRUCTURES IN EACH ITERATION. THE
REMARK 3 AUTOMATICALLY GENERATED ASSIGNMENTS WERE CHECKED MANUALLY AND
REMARK 3 CORRECTED IF NECESSARY. THE FINAL LIST OF RESTRAINTS CONTAINED
REMARK 3 2008 UNAMBIGUOUS RESTRAINTS AND 280 AMBIGUOUS RESTRAINTS WITH
REMARK 3 MAXIMALLY 5 ASSIGNMENT POSSIBILITIES. WITH THE FINAL RESTRAINT
REMARK 3 LIST, A TOTAL OF 75 STRUCTURES WERE CALCULATED. THE 23 STRUCTURES
REMARK 3 WITH THE LOWEST TOTAL ENERGY WERE REFINED IN AN EXPLICIT SHELL OF
REMARK 3 WATER. THE STRUCTURAL STATISTICS GIVEN BELOW ARE FOR THE
REMARK 3 STRUCTURES AFTER THE REFINEMENT IN WATER. REFINEMENT DETAILS CAN
REMARK 3 BE FOUND IN THE JRNL REFERENCE ABOVE. THE 23 DEPOSITED STRUCTURES
REMARK 3 ARE IN ORDER OF RISING RESTRAINT ENERGY AFTER WATER REFINEMENT.
REMARK 3 NOES TO ALL PROCHIRAL GROUPS WERE TREATED WITH A FLOATING
REMARK 3 CHIRALITY APPROACH THAT ALLOWS EXPLICIT SWAPPING OF PROTONS AND
REMARK 3 METHYL GROUPS; THE ATOM NAMES IN THE COORDINATE ENTRY HAVE BEEN
REMARK 3 RENAMED TO BE CONSISTENT WITH STANDARD IUB/IUPAC CONVENTION.
REMARK 4
REMARK 4 1AOY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 301
REMARK 210 PH : 5.8
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2QF-COSY; 3QF-COSY; E-COSY;
REMARK 210 CLEAN TOCSY; NOESY; HNHB; 13C-
REMARK 210 HMBC; TOCSY-15N-HSQC; NOESY-15N-
REMARK 210 HSQC; 3D-HNCO
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : DMX600
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 75
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 23
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST ENERGY
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: 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 3 77.00 -102.32
REMARK 500 1 GLN A 7 37.37 -81.93
REMARK 500 1 GLU A 21 72.75 61.55
REMARK 500 1 LYS A 22 -41.88 -140.27
REMARK 500 1 PRO A 70 -154.38 -73.66
REMARK 500 1 GLU A 72 106.07 -45.80
REMARK 500 1 THR A 77 -37.35 -164.85
REMARK 500 2 ARG A 2 43.14 -100.75
REMARK 500 2 SER A 3 -59.26 72.47
REMARK 500 2 LYS A 6 98.82 -69.57
REMARK 500 2 GLU A 8 36.94 -80.92
REMARK 500 2 GLU A 21 80.01 61.74
REMARK 500 2 LYS A 22 -53.00 -142.15
REMARK 500 2 ASN A 40 54.88 92.77
REMARK 500 2 LYS A 62 32.40 -99.73
REMARK 500 2 PRO A 70 -140.27 -67.68
REMARK 500 2 GLU A 72 109.90 -58.21
REMARK 500 3 ARG A 2 -95.10 -75.52
REMARK 500 3 GLU A 21 63.54 61.59
REMARK 500 3 ASN A 40 66.46 -116.44
REMARK 500 3 GLU A 72 108.40 -31.15
REMARK 500 3 THR A 77 55.82 -161.10
REMARK 500 4 ARG A 2 62.51 61.32
REMARK 500 4 SER A 3 75.81 -118.11
REMARK 500 4 GLU A 21 81.00 63.64
REMARK 500 4 LYS A 22 -55.74 -139.18
REMARK 500 4 ASN A 60 -154.96 -83.38
REMARK 500 4 PRO A 70 -159.13 -66.09
REMARK 500 4 GLU A 72 104.69 -46.70
REMARK 500 4 LEU A 73 47.43 -83.87
REMARK 500 5 SER A 3 88.87 66.34
REMARK 500 5 ALA A 5 59.25 -155.55
REMARK 500 5 GLU A 21 72.63 61.95
REMARK 500 5 LYS A 22 -53.32 -137.76
REMARK 500 5 ASN A 40 50.76 94.95
REMARK 500 5 PRO A 70 -149.46 -70.53
REMARK 500 5 GLU A 72 128.18 -39.87
REMARK 500 5 PRO A 76 27.05 -71.34
REMARK 500 6 ALA A 5 78.11 -159.80
REMARK 500 6 GLU A 21 66.97 64.58
REMARK 500 6 LYS A 22 -53.75 -130.12
REMARK 500 6 ASN A 40 32.25 -99.26
REMARK 500 6 ALA A 71 101.12 -49.67
REMARK 500 6 GLU A 72 75.25 52.33
REMARK 500 6 THR A 77 -158.74 -152.90
REMARK 500 7 GLN A 7 33.62 -76.72
REMARK 500 7 LYS A 22 38.72 -142.00
REMARK 500 7 PRO A 70 -146.04 -66.78
REMARK 500 7 ALA A 71 -152.13 -75.41
REMARK 500 7 THR A 77 21.52 -78.12
REMARK 500
REMARK 500 THIS ENTRY HAS 171 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1AOY A 1 78 UNP P0A6D0 ARGR_ECOLI 1 78
SEQRES 1 A 78 MET ARG SER SER ALA LYS GLN GLU GLU LEU VAL LYS ALA
SEQRES 2 A 78 PHE LYS ALA LEU LEU LYS GLU GLU LYS PHE SER SER GLN
SEQRES 3 A 78 GLY GLU ILE VAL ALA ALA LEU GLN GLU GLN GLY PHE ASP
SEQRES 4 A 78 ASN ILE ASN GLN SER LYS VAL SER ARG MET LEU THR LYS
SEQRES 5 A 78 PHE GLY ALA VAL ARG THR ARG ASN ALA LYS MET GLU MET
SEQRES 6 A 78 VAL TYR CYS LEU PRO ALA GLU LEU GLY VAL PRO THR THR
HELIX 1 1 LEU A 10 LYS A 19 1 10
HELIX 2 2 GLN A 26 GLN A 36 1 11
HELIX 3 3 GLN A 43 PHE A 53 1 11
SHEET 1 A 2 ALA A 55 ARG A 59 0
SHEET 2 A 2 MET A 65 LEU A 69 -1 N CYS A 68 O VAL A 56
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 25 2 Bytes