Header list of 1ysf.pdb file
Complete list - r 2 2 Bytes
HEADER TRANSCRIPTION 08-FEB-05 1YSF
TITLE THE SOLUTION STRUCTURE OF THE N-DOMAIN OF THE TRANSCRIPTION FACTOR
TITLE 2 ABRB
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRANSITION STATE REGULATORY PROTEIN ABRB;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: N-TERMINAL DOMAIN;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;
SOURCE 3 ORGANISM_TAXID: 1423;
SOURCE 4 GENE: ABRB;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET30B
KEYWDS NMR; HOMODIMER; BIOINFORMATICS; SWAPPED-HAIRPIN BARREL, TRANSCRIPTION
EXPDTA SOLUTION NMR
NUMMDL 22
AUTHOR V.TRUFFAULT,S.DJURANOVIC,M.COLES
REVDAT 4 02-MAR-22 1YSF 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1YSF 1 VERSN
REVDAT 2 21-JUN-05 1YSF 1 JRNL
REVDAT 1 12-APR-05 1YSF 0
JRNL AUTH M.COLES,S.DJURANOVIC,J.SODING,T.FRICKEY,K.KORETKE,
JRNL AUTH 2 V.TRUFFAULT,J.MARTIN,A.N.LUPAS
JRNL TITL ABRB-LIKE TRANSCRIPTION FACTORS ASSUME A SWAPPED HAIRPIN
JRNL TITL 2 FOLD THAT IS EVOLUTIONARILY RELATED TO DOUBLE-PSI BETA
JRNL TITL 3 BARRELS.
JRNL REF STRUCTURE V. 13 919 2005
JRNL REFN ISSN 0969-2126
JRNL PMID 15939023
JRNL DOI 10.1016/J.STR.2005.03.017
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR NIH-2.9.7, X-PLOR NIH-2.9.7
REMARK 3 AUTHORS : BRUNGER, A.T. (X-PLOR), BRUNGER, A.T. (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1YSF COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-FEB-05.
REMARK 100 THE DEPOSITION ID IS D_1000031877.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 305
REMARK 210 PH : 5.8
REMARK 210 IONIC STRENGTH : 80MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.5MM ABRB-N; 20MM PHOSPHATE
REMARK 210 BUFFER; 80MM KCL; 0.5MM ABRB-N U-
REMARK 210 15N; 20MM PHOSPHATE BUFFER; 80MM
REMARK 210 KCL; 0.25MM ABRB-N U-15N, 0.25MM
REMARK 210 ABRB-N U-13C; 20MM PHOSPHATE
REMARK 210 BUFFER; 80MM KCL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 2D
REMARK 210 NOESY; HNHA; 13C-FILTERED/EDITED
REMARK 210 NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 750 MHZ; 900 MHZ
REMARK 210 SPECTROMETER MODEL : DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR 3.5, NMRVIEW 5.0.15
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 22
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST RESTRAINT VIOLATIONS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: INTERMOLECULAR CONTACTS IDENTIFIED USING A DIFFERENTIALLY
REMARK 210 15N/13C LABELLED DIMER SAMPLE
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-22
REMARK 465 RES C SSSEQI
REMARK 465 MET A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 HIS A -2
REMARK 465 HIS A -1
REMARK 465 HIS A 0
REMARK 465 HIS A 1
REMARK 465 MET B -5
REMARK 465 HIS B -4
REMARK 465 HIS B -3
REMARK 465 HIS B -2
REMARK 465 HIS B -1
REMARK 465 HIS B 0
REMARK 465 HIS B 1
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 LYS A 33 -4.57 74.81
REMARK 500 1 GLU A 43 14.05 58.55
REMARK 500 1 LYS B 33 -4.77 74.84
REMARK 500 1 GLU B 43 14.01 58.41
REMARK 500 2 LYS A 33 -4.35 74.35
REMARK 500 2 SER B 5 -93.64 -71.92
REMARK 500 2 LYS B 33 -4.64 74.42
REMARK 500 3 LYS A 33 -4.92 74.65
REMARK 500 3 GLU A 43 15.71 57.40
REMARK 500 3 LYS B 33 -5.01 74.69
REMARK 500 3 GLU B 43 15.61 57.23
REMARK 500 4 LYS A 33 -4.62 74.83
REMARK 500 4 GLU A 43 16.91 56.99
REMARK 500 4 LYS B 33 -4.91 74.88
REMARK 500 4 GLU B 43 16.89 56.85
REMARK 500 5 THR A 6 64.40 -170.24
REMARK 500 5 LYS A 33 -4.34 74.43
REMARK 500 5 THR B 6 64.52 -170.84
REMARK 500 5 LYS B 33 -4.58 74.49
REMARK 500 6 LYS A 33 -4.62 74.57
REMARK 500 6 SER B 5 -94.59 -97.58
REMARK 500 6 LYS B 33 -4.78 74.66
REMARK 500 7 LYS A 33 -4.47 74.39
REMARK 500 7 GLU A 43 14.46 57.84
REMARK 500 7 LYS B 33 -4.76 74.59
REMARK 500 7 GLU B 43 14.53 57.61
REMARK 500 8 LYS A 33 -4.35 74.00
REMARK 500 8 GLU A 43 14.09 58.87
REMARK 500 8 SER B 5 -93.16 -73.87
REMARK 500 8 LYS B 33 -4.49 74.13
REMARK 500 8 GLU B 43 14.03 58.79
REMARK 500 9 LYS A 33 -4.68 74.86
REMARK 500 9 GLU A 43 12.69 59.95
REMARK 500 9 THR B 6 -42.68 -147.68
REMARK 500 9 LYS B 33 -4.90 74.99
REMARK 500 9 GLU B 43 12.73 59.85
REMARK 500 9 LYS B 51 75.67 -119.74
REMARK 500 10 LYS A 33 -4.64 74.46
REMARK 500 10 LYS B 33 -4.76 74.63
REMARK 500 11 LYS A 4 43.15 -101.70
REMARK 500 11 LYS A 33 -4.95 74.96
REMARK 500 11 LYS B 33 -5.16 75.03
REMARK 500 12 LYS A 33 -4.58 74.22
REMARK 500 12 LYS B 33 -4.89 74.40
REMARK 500 13 MET A 3 -89.38 -93.76
REMARK 500 13 LYS A 33 -4.56 74.59
REMARK 500 13 GLU A 43 16.18 56.53
REMARK 500 13 LYS B 33 -4.73 74.67
REMARK 500 13 GLU B 43 16.12 56.32
REMARK 500 14 THR A 6 63.58 -170.80
REMARK 500
REMARK 500 THIS ENTRY HAS 90 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1EKT RELATED DB: PDB
REMARK 900 RELATED ID: 1YFB RELATED DB: PDB
REMARK 900 REGULARIZED AVERAGE STRUCTURE
DBREF 1YSF A 2 53 UNP P08874 ABRB_BACSU 2 53
DBREF 1YSF B 2 53 UNP P08874 ABRB_BACSU 2 53
SEQADV 1YSF MET A -5 UNP P08874 EXPRESSION TAG
SEQADV 1YSF HIS A -4 UNP P08874 EXPRESSION TAG
SEQADV 1YSF HIS A -3 UNP P08874 EXPRESSION TAG
SEQADV 1YSF HIS A -2 UNP P08874 EXPRESSION TAG
SEQADV 1YSF HIS A -1 UNP P08874 EXPRESSION TAG
SEQADV 1YSF HIS A 0 UNP P08874 EXPRESSION TAG
SEQADV 1YSF HIS A 1 UNP P08874 EXPRESSION TAG
SEQADV 1YSF MET B -5 UNP P08874 EXPRESSION TAG
SEQADV 1YSF HIS B -4 UNP P08874 EXPRESSION TAG
SEQADV 1YSF HIS B -3 UNP P08874 EXPRESSION TAG
SEQADV 1YSF HIS B -2 UNP P08874 EXPRESSION TAG
SEQADV 1YSF HIS B -1 UNP P08874 EXPRESSION TAG
SEQADV 1YSF HIS B 0 UNP P08874 EXPRESSION TAG
SEQADV 1YSF HIS B 1 UNP P08874 EXPRESSION TAG
SEQRES 1 A 59 MET HIS HIS HIS HIS HIS HIS PHE MET LYS SER THR GLY
SEQRES 2 A 59 ILE VAL ARG LYS VAL ASP GLU LEU GLY ARG VAL VAL ILE
SEQRES 3 A 59 PRO ILE GLU LEU ARG ARG THR LEU GLY ILE ALA GLU LYS
SEQRES 4 A 59 ASP ALA LEU GLU ILE TYR VAL ASP ASP GLU LYS ILE ILE
SEQRES 5 A 59 LEU LYS LYS TYR LYS PRO ASN
SEQRES 1 B 59 MET HIS HIS HIS HIS HIS HIS PHE MET LYS SER THR GLY
SEQRES 2 B 59 ILE VAL ARG LYS VAL ASP GLU LEU GLY ARG VAL VAL ILE
SEQRES 3 B 59 PRO ILE GLU LEU ARG ARG THR LEU GLY ILE ALA GLU LYS
SEQRES 4 B 59 ASP ALA LEU GLU ILE TYR VAL ASP ASP GLU LYS ILE ILE
SEQRES 5 B 59 LEU LYS LYS TYR LYS PRO ASN
HELIX 1 1 PRO A 21 LEU A 28 1 8
HELIX 2 2 PRO B 21 LEU B 28 1 8
SHEET 1 A 6 ILE A 8 LYS A 11 0
SHEET 2 A 6 ALA B 35 ASP B 41 -1 O ILE B 38 N ILE A 8
SHEET 3 A 6 LYS B 44 LYS B 49 -1 O LYS B 44 N ASP B 41
SHEET 4 A 6 LYS A 44 LYS A 49 -1 N LEU A 47 O ILE B 45
SHEET 5 A 6 ALA A 35 ASP A 41 -1 N ASP A 41 O LYS A 44
SHEET 6 A 6 ILE B 8 LYS B 11 -1 O ILE B 8 N ILE A 38
SHEET 1 B 2 ARG A 17 VAL A 19 0
SHEET 2 B 2 ARG B 17 VAL B 19 -1 O VAL B 18 N VAL A 18
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