Header list of 1auu.pdb file
Complete list - b 16 2 Bytes
HEADER TRANSCRIPTION REGULATION 02-SEP-97 1AUU
TITLE SOLUTION STRUCTURE OF THE RNA-BINDING DOMAIN OF THE ANTITERMINATOR
TITLE 2 PROTEIN SACY, NMR, 10 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SACY;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RNA BINDING DOMAIN, RESIDUES 1 - 55;
COMPND 5 ENGINEERED: YES;
COMPND 6 OTHER_DETAILS: N TERMINAL REGION OF THE SACY PROTEIN. THE STRUCTURE
COMPND 7 IS A SYMMETRIC DIMER IN SOLUTION
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;
SOURCE 3 ORGANISM_TAXID: 1423;
SOURCE 4 CELL_LINE: BL21;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PGEX-2T
KEYWDS ANTITERMINATION, RNA BINDING DOMAIN, TRANSCRIPTION REGULATION
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR M.KOCHOYAN
REVDAT 3 16-FEB-22 1AUU 1 REMARK
REVDAT 2 24-FEB-09 1AUU 1 VERSN
REVDAT 1 12-NOV-97 1AUU 0
JRNL AUTH X.MANIVAL,Y.YANG,M.P.STRUB,M.KOCHOYAN,M.STEINMETZ,S.AYMERICH
JRNL TITL FROM GENETIC TO STRUCTURAL CHARACTERIZATION OF A NEW CLASS
JRNL TITL 2 OF RNA-BINDING DOMAIN WITHIN THE SACY/BGLG FAMILY OF
JRNL TITL 3 ANTITERMINATOR PROTEINS.
JRNL REF EMBO J. V. 16 5019 1997
JRNL REFN ISSN 0261-4189
JRNL PMID 9305643
JRNL DOI 10.1093/EMBOJ/16.16.5019
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE MONOMERIC UNIT WAS MODELLED FIRST
REMARK 3 USING SAFE NOE WITH THE DG-SA PROTOCOL PROVIDED WITH X-PLOR. THE
REMARK 3 DIMER WAS THEN GENERATED BY ADDING EXTRA INTERMOLECULAR
REMARK 3 CONSTRAINTS PLUS A LIST OF AMBIGUOUS (INTER OR INTRA MOLECULAR)
REMARK 3 RESTRAINTS USING THE PROTOCOL DESCRIBED IN NILGES (1993),
REMARK 3 PROTEINS 17, 297-309.
REMARK 4
REMARK 4 1AUU COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000171286.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 297
REMARK 210 PH : 6
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; TOCSY; COSY; HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : AMX600
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR 3.1
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 40
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : RESTRAINT ENERGY VIOLATION
REMARK 210 WITHIN 30% OF THE CONFORMER OF
REMARK 210 LOWER ENERGY VIOLATION. 28
REMARK 210 CONFORMERS SATISFIED THE
REMARK 210 CRITERIA, ONLY 10 ARE SHOWN.
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: 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 1 ASN A 8 -152.61 -162.24
REMARK 500 1 ASN A 10 -41.55 -134.09
REMARK 500 1 GLU A 19 -157.09 179.20
REMARK 500 1 ALA A 26 105.53 -53.71
REMARK 500 1 ASN A 35 -10.52 83.54
REMARK 500 1 ASN B 8 -152.91 -162.17
REMARK 500 1 ASN B 10 -41.71 -134.17
REMARK 500 1 GLU B 19 -157.10 179.12
REMARK 500 1 ALA B 26 105.56 -53.74
REMARK 500 1 ASN B 35 -10.60 83.55
REMARK 500 2 ASN A 8 -157.05 -166.54
REMARK 500 2 GLU A 19 -170.75 179.80
REMARK 500 2 ALA A 26 104.12 -55.46
REMARK 500 2 ASN A 31 39.10 71.68
REMARK 500 2 ILE A 37 153.73 67.20
REMARK 500 2 ILE A 43 108.73 -59.75
REMARK 500 2 PRO A 53 -97.29 -78.30
REMARK 500 2 ASP A 54 -2.75 67.85
REMARK 500 2 ASN B 8 -157.36 -166.61
REMARK 500 2 GLU B 19 -171.23 179.52
REMARK 500 2 ALA B 26 104.00 -55.43
REMARK 500 2 ASN B 31 38.52 71.54
REMARK 500 2 ILE B 37 153.83 67.16
REMARK 500 2 ILE B 43 108.82 -59.72
REMARK 500 2 PRO B 53 -97.32 -78.50
REMARK 500 2 ASP B 54 -2.78 67.82
REMARK 500 3 ASN A 8 -167.13 -167.89
REMARK 500 3 GLU A 19 -75.47 176.85
REMARK 500 3 ALA A 26 101.76 -54.01
REMARK 500 3 ILE A 37 139.17 69.73
REMARK 500 3 ILE A 43 109.75 -53.83
REMARK 500 3 THR A 52 79.28 43.40
REMARK 500 3 PRO A 53 -71.51 -78.47
REMARK 500 3 ASN B 8 -167.04 -167.90
REMARK 500 3 GLU B 19 -75.43 176.89
REMARK 500 3 ALA B 26 101.77 -53.95
REMARK 500 3 ILE B 37 139.90 69.90
REMARK 500 3 ILE B 43 109.67 -53.80
REMARK 500 3 THR B 52 79.26 43.43
REMARK 500 3 PRO B 53 -71.46 -78.45
REMARK 500 4 ASN A 8 -161.87 -167.55
REMARK 500 4 GLU A 19 -148.03 177.99
REMARK 500 4 ALA A 26 100.49 -53.80
REMARK 500 4 ASN A 31 31.52 72.42
REMARK 500 4 ILE A 43 109.04 -56.70
REMARK 500 4 ARG A 49 108.72 -58.04
REMARK 500 4 ASP A 51 -62.69 -163.68
REMARK 500 4 ASP A 54 -54.07 -125.78
REMARK 500 4 ASN B 8 -162.04 -167.57
REMARK 500 4 GLU B 19 -148.01 177.87
REMARK 500
REMARK 500 THIS ENTRY HAS 123 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 1 ARG A 5 0.32 SIDE CHAIN
REMARK 500 1 ARG A 49 0.32 SIDE CHAIN
REMARK 500 1 ARG B 5 0.32 SIDE CHAIN
REMARK 500 1 ARG B 49 0.32 SIDE CHAIN
REMARK 500 2 ARG A 5 0.32 SIDE CHAIN
REMARK 500 2 ARG A 49 0.26 SIDE CHAIN
REMARK 500 2 ARG B 5 0.32 SIDE CHAIN
REMARK 500 2 ARG B 49 0.32 SIDE CHAIN
REMARK 500 3 ARG A 5 0.32 SIDE CHAIN
REMARK 500 3 ARG A 49 0.31 SIDE CHAIN
REMARK 500 3 ARG B 5 0.32 SIDE CHAIN
REMARK 500 3 ARG B 49 0.31 SIDE CHAIN
REMARK 500 4 ARG A 5 0.27 SIDE CHAIN
REMARK 500 4 ARG A 49 0.32 SIDE CHAIN
REMARK 500 4 ARG B 5 0.27 SIDE CHAIN
REMARK 500 4 ARG B 49 0.32 SIDE CHAIN
REMARK 500 5 ARG A 5 0.31 SIDE CHAIN
REMARK 500 5 ARG A 49 0.31 SIDE CHAIN
REMARK 500 5 ARG B 5 0.31 SIDE CHAIN
REMARK 500 5 ARG B 49 0.31 SIDE CHAIN
REMARK 500 6 ARG A 5 0.27 SIDE CHAIN
REMARK 500 6 ARG A 49 0.31 SIDE CHAIN
REMARK 500 6 ARG B 5 0.26 SIDE CHAIN
REMARK 500 6 ARG B 49 0.31 SIDE CHAIN
REMARK 500 7 ARG A 5 0.28 SIDE CHAIN
REMARK 500 7 ARG A 49 0.31 SIDE CHAIN
REMARK 500 7 ARG B 5 0.28 SIDE CHAIN
REMARK 500 7 ARG B 49 0.31 SIDE CHAIN
REMARK 500 8 ARG A 5 0.32 SIDE CHAIN
REMARK 500 8 ARG A 49 0.29 SIDE CHAIN
REMARK 500 8 ARG B 5 0.32 SIDE CHAIN
REMARK 500 8 ARG B 49 0.29 SIDE CHAIN
REMARK 500 9 ARG A 5 0.31 SIDE CHAIN
REMARK 500 9 ARG A 49 0.27 SIDE CHAIN
REMARK 500 9 ARG B 5 0.31 SIDE CHAIN
REMARK 500 9 ARG B 49 0.27 SIDE CHAIN
REMARK 500 10 ARG A 5 0.32 SIDE CHAIN
REMARK 500 10 ARG A 49 0.32 SIDE CHAIN
REMARK 500 10 ARG B 5 0.32 SIDE CHAIN
REMARK 500 10 ARG B 49 0.32 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1AUU A 1 55 UNP P15401 SACY_BACSU 1 55
DBREF 1AUU B 1 55 UNP P15401 SACY_BACSU 1 55
SEQRES 1 A 55 MET LYS ILE LYS ARG ILE LEU ASN HIS ASN ALA ILE VAL
SEQRES 2 A 55 VAL LYS ASP GLN ASN GLU GLU LYS ILE LEU LEU GLY ALA
SEQRES 3 A 55 GLY ILE ALA PHE ASN LYS LYS LYS ASN ASP ILE VAL ASP
SEQRES 4 A 55 PRO SER LYS ILE GLU LYS THR PHE ILE ARG LYS ASP THR
SEQRES 5 A 55 PRO ASP TYR
SEQRES 1 B 55 MET LYS ILE LYS ARG ILE LEU ASN HIS ASN ALA ILE VAL
SEQRES 2 B 55 VAL LYS ASP GLN ASN GLU GLU LYS ILE LEU LEU GLY ALA
SEQRES 3 B 55 GLY ILE ALA PHE ASN LYS LYS LYS ASN ASP ILE VAL ASP
SEQRES 4 B 55 PRO SER LYS ILE GLU LYS THR PHE ILE ARG LYS ASP THR
SEQRES 5 B 55 PRO ASP TYR
SHEET 1 A 3 ALA A 11 LYS A 15 0
SHEET 2 A 3 GLU A 20 LEU A 24 -1 N LEU A 23 O ILE A 12
SHEET 3 A 3 LYS A 45 ILE A 48 -1 N PHE A 47 O ILE A 22
SHEET 1 B 3 ALA B 11 LYS B 15 0
SHEET 2 B 3 GLU B 20 LEU B 24 -1 N LEU B 23 O ILE B 12
SHEET 3 B 3 LYS B 45 ILE B 48 -1 N PHE B 47 O ILE B 22
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 - b 16 2 Bytes