Header list of 1cop.pdb file
Complete list - b 16 2 Bytes
HEADER GENE REGULATING PROTEIN 23-JUN-95 1COP
TITLE THREE-DIMENSIONAL DIMER STRUCTURE OF THE LAMBDA-CRO REPRESSOR IN
TITLE 2 SOLUTION AS DETERMINED BY HETERONUCLEAR MULTIDIMENSIONAL NMR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CRO REPRESSOR;
COMPND 3 CHAIN: D, E;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ENTEROBACTERIA PHAGE LAMBDA;
SOURCE 3 ORGANISM_TAXID: 10710;
SOURCE 4 GENE: CRO;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: TG1;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PKH1500;
SOURCE 9 EXPRESSION_SYSTEM_GENE: CRO
KEYWDS GENE REGULATING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR H.MATSUO,M.SHIRAKAWA,Y.KYOGOKU
REVDAT 3 16-FEB-22 1COP 1 REMARK
REVDAT 2 24-FEB-09 1COP 1 VERSN
REVDAT 1 15-OCT-95 1COP 0
JRNL AUTH H.MATSUO,M.SHIRAKAWA,Y.KYOGOKU
JRNL TITL THREE-DIMENSIONAL DIMER STRUCTURE OF THE LAMBDA-CRO
JRNL TITL 2 REPRESSOR IN SOLUTION AS DETERMINED BY HETERONUCLEAR
JRNL TITL 3 MULTIDIMENSIONAL NMR.
JRNL REF J.MOL.BIOL. V. 254 668 1995
JRNL REFN ISSN 0022-2836
JRNL PMID 7500341
JRNL DOI 10.1006/JMBI.1995.0646
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: NULL
REMARK 4
REMARK 4 1COP 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_1000172437.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : NULL
REMARK 210 PH : NULL
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : NULL
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : NULL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
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: D, E
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 GLU D 2 124.91 -179.03
REMARK 500 1 ALA D 46 -18.72 -48.35
REMARK 500 1 ASP D 47 30.89 -82.98
REMARK 500 1 ASN D 61 -156.27 -87.86
REMARK 500 1 LYS D 62 -176.74 67.28
REMARK 500 1 LYS E 39 71.74 37.44
REMARK 500 1 ASP E 47 31.77 -83.69
REMARK 500 1 TYR E 51 81.55 -157.42
REMARK 500 1 PRO E 59 -70.68 -80.15
REMARK 500 1 SER E 60 -80.48 -83.24
REMARK 500 2 ARG D 38 178.51 -51.37
REMARK 500 2 ASP D 47 32.19 -86.27
REMARK 500 2 TYR D 51 73.55 -150.09
REMARK 500 2 PRO D 59 -160.01 -79.91
REMARK 500 2 VAL E 25 -169.98 -104.85
REMARK 500 2 ASP E 47 31.01 -84.33
REMARK 500 2 TYR E 51 78.02 -151.21
REMARK 500 2 LYS E 62 150.81 173.09
REMARK 500 3 VAL D 25 -176.28 -66.99
REMARK 500 3 ALA D 46 -26.53 -39.74
REMARK 500 3 ASP D 47 34.48 -85.66
REMARK 500 3 PRO D 59 -157.39 -81.92
REMARK 500 3 SER D 60 -164.17 -60.51
REMARK 500 3 THR D 65 26.81 -151.47
REMARK 500 3 SER E 60 -149.44 -66.72
REMARK 500 3 LYS E 63 -146.89 -91.54
REMARK 500 3 THR E 65 88.77 -154.33
REMARK 500 4 ASP D 47 32.93 -86.00
REMARK 500 4 LYS D 62 68.70 -164.17
REMARK 500 4 GLU E 2 105.50 173.06
REMARK 500 4 ARG E 38 -156.78 -73.19
REMARK 500 4 LYS E 39 72.36 -111.95
REMARK 500 4 ASP E 47 33.95 -84.80
REMARK 500 4 TYR E 51 81.27 -159.63
REMARK 500 4 LYS E 63 58.60 -95.45
REMARK 500 4 THR E 65 62.47 -112.27
REMARK 500 5 GLU D 2 -74.56 -163.90
REMARK 500 5 THR D 6 152.67 -49.40
REMARK 500 5 ARG D 38 -154.17 -77.07
REMARK 500 5 ASP D 47 34.06 -85.76
REMARK 500 5 TYR D 51 79.47 -152.76
REMARK 500 5 PRO D 59 -87.77 -82.12
REMARK 500 5 LYS D 63 173.09 58.51
REMARK 500 5 THR D 65 -164.32 -120.41
REMARK 500 5 GLU E 2 108.38 62.43
REMARK 500 5 ASP E 47 31.61 -84.57
REMARK 500 5 THR E 65 -159.72 -118.04
REMARK 500 6 VAL D 25 -173.01 -52.81
REMARK 500 6 ASP D 47 33.66 -84.82
REMARK 500 6 PRO D 59 -160.31 -76.62
REMARK 500
REMARK 500 THIS ENTRY HAS 183 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 D 4 0.29 SIDE CHAIN
REMARK 500 1 ARG D 13 0.25 SIDE CHAIN
REMARK 500 1 ARG D 38 0.21 SIDE CHAIN
REMARK 500 1 ARG E 4 0.23 SIDE CHAIN
REMARK 500 1 ARG E 13 0.26 SIDE CHAIN
REMARK 500 1 ARG E 38 0.31 SIDE CHAIN
REMARK 500 2 ARG D 4 0.18 SIDE CHAIN
REMARK 500 2 ARG D 13 0.26 SIDE CHAIN
REMARK 500 2 ARG D 38 0.32 SIDE CHAIN
REMARK 500 2 ARG E 4 0.20 SIDE CHAIN
REMARK 500 2 ARG E 38 0.09 SIDE CHAIN
REMARK 500 3 ARG D 4 0.32 SIDE CHAIN
REMARK 500 3 ARG D 13 0.32 SIDE CHAIN
REMARK 500 3 ARG D 38 0.20 SIDE CHAIN
REMARK 500 3 ARG E 4 0.29 SIDE CHAIN
REMARK 500 3 ARG E 13 0.24 SIDE CHAIN
REMARK 500 3 ARG E 38 0.32 SIDE CHAIN
REMARK 500 4 ARG D 4 0.30 SIDE CHAIN
REMARK 500 4 ARG D 13 0.16 SIDE CHAIN
REMARK 500 4 ARG D 38 0.31 SIDE CHAIN
REMARK 500 4 ARG E 4 0.32 SIDE CHAIN
REMARK 500 4 ARG E 13 0.29 SIDE CHAIN
REMARK 500 5 ARG D 4 0.32 SIDE CHAIN
REMARK 500 5 ARG D 13 0.24 SIDE CHAIN
REMARK 500 5 ARG D 38 0.20 SIDE CHAIN
REMARK 500 5 ARG E 4 0.18 SIDE CHAIN
REMARK 500 5 ARG E 13 0.20 SIDE CHAIN
REMARK 500 5 ARG E 38 0.18 SIDE CHAIN
REMARK 500 6 ARG D 4 0.25 SIDE CHAIN
REMARK 500 6 ARG D 13 0.31 SIDE CHAIN
REMARK 500 6 ARG D 38 0.26 SIDE CHAIN
REMARK 500 6 ARG E 4 0.19 SIDE CHAIN
REMARK 500 6 ARG E 13 0.32 SIDE CHAIN
REMARK 500 6 ARG E 38 0.31 SIDE CHAIN
REMARK 500 7 ARG D 4 0.28 SIDE CHAIN
REMARK 500 7 ARG D 13 0.26 SIDE CHAIN
REMARK 500 7 ARG D 38 0.27 SIDE CHAIN
REMARK 500 7 ARG E 4 0.26 SIDE CHAIN
REMARK 500 7 ARG E 13 0.19 SIDE CHAIN
REMARK 500 7 ARG E 38 0.31 SIDE CHAIN
REMARK 500 8 ARG D 4 0.19 SIDE CHAIN
REMARK 500 8 ARG D 13 0.29 SIDE CHAIN
REMARK 500 8 ARG D 38 0.29 SIDE CHAIN
REMARK 500 8 ARG E 4 0.15 SIDE CHAIN
REMARK 500 8 ARG E 13 0.32 SIDE CHAIN
REMARK 500 8 ARG E 38 0.23 SIDE CHAIN
REMARK 500 9 ARG D 4 0.21 SIDE CHAIN
REMARK 500 9 ARG D 13 0.23 SIDE CHAIN
REMARK 500 9 ARG D 38 0.19 SIDE CHAIN
REMARK 500 9 ARG E 4 0.29 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 114 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1COP D 1 66 UNP P03040 RCRO_LAMBD 1 66
DBREF 1COP E 1 66 UNP P03040 RCRO_LAMBD 1 66
SEQRES 1 D 66 MET GLU GLN ARG ILE THR LEU LYS ASP TYR ALA MET ARG
SEQRES 2 D 66 PHE GLY GLN THR LYS THR ALA LYS ASP LEU GLY VAL TYR
SEQRES 3 D 66 GLN SER ALA ILE ASN LYS ALA ILE HIS ALA GLY ARG LYS
SEQRES 4 D 66 ILE PHE LEU THR ILE ASN ALA ASP GLY SER VAL TYR ALA
SEQRES 5 D 66 GLU GLU VAL LYS PRO PHE PRO SER ASN LYS LYS THR THR
SEQRES 6 D 66 ALA
SEQRES 1 E 66 MET GLU GLN ARG ILE THR LEU LYS ASP TYR ALA MET ARG
SEQRES 2 E 66 PHE GLY GLN THR LYS THR ALA LYS ASP LEU GLY VAL TYR
SEQRES 3 E 66 GLN SER ALA ILE ASN LYS ALA ILE HIS ALA GLY ARG LYS
SEQRES 4 E 66 ILE PHE LEU THR ILE ASN ALA ASP GLY SER VAL TYR ALA
SEQRES 5 E 66 GLU GLU VAL LYS PRO PHE PRO SER ASN LYS LYS THR THR
SEQRES 6 E 66 ALA
HELIX 1 1 LEU D 7 ARG D 13 1 7
HELIX 2 2 GLN D 16 LEU D 23 1 8
HELIX 3 3 GLN D 27 ALA D 36 1 10
HELIX 4 4 LEU E 7 ARG E 13 1 7
HELIX 5 5 GLN E 16 LEU E 23 1 8
HELIX 6 6 GLN E 27 ALA E 36 1 10
SHEET 1 A 6 GLN D 3 THR D 6 0
SHEET 2 A 6 ILE D 40 ASN D 45 -1 N ILE D 44 O GLN D 3
SHEET 3 A 6 SER D 49 PRO D 57 -1 N GLU D 53 O PHE D 41
SHEET 4 A 6 SER E 49 PRO E 57 -1 N LYS E 56 O GLU D 54
SHEET 5 A 6 ILE E 40 ASN E 45 -1 N ASN E 45 O SER E 49
SHEET 6 A 6 GLN E 3 THR E 6 -1 N ILE E 5 O LEU E 42
CISPEP 1 PHE D 58 PRO D 59 1 -0.65
CISPEP 2 PHE E 58 PRO E 59 1 -0.60
CISPEP 3 PHE D 58 PRO D 59 2 -0.41
CISPEP 4 PHE E 58 PRO E 59 2 -0.37
CISPEP 5 PHE D 58 PRO D 59 3 -0.81
CISPEP 6 PHE E 58 PRO E 59 3 -0.37
CISPEP 7 PHE D 58 PRO D 59 4 -1.01
CISPEP 8 PHE E 58 PRO E 59 4 0.36
CISPEP 9 PHE D 58 PRO D 59 5 -0.80
CISPEP 10 PHE E 58 PRO E 59 5 -0.01
CISPEP 11 PHE D 58 PRO D 59 6 0.36
CISPEP 12 PHE E 58 PRO E 59 6 0.13
CISPEP 13 PHE D 58 PRO D 59 7 -0.85
CISPEP 14 PHE E 58 PRO E 59 7 0.22
CISPEP 15 PHE D 58 PRO D 59 8 0.09
CISPEP 16 PHE E 58 PRO E 59 8 -0.25
CISPEP 17 PHE D 58 PRO D 59 9 -0.71
CISPEP 18 PHE E 58 PRO E 59 9 -0.65
CISPEP 19 PHE D 58 PRO D 59 10 -0.04
CISPEP 20 PHE E 58 PRO E 59 10 -0.07
CISPEP 21 PHE D 58 PRO D 59 11 0.43
CISPEP 22 PHE E 58 PRO E 59 11 0.24
CISPEP 23 PHE D 58 PRO D 59 12 -0.46
CISPEP 24 PHE E 58 PRO E 59 12 -0.50
CISPEP 25 PHE D 58 PRO D 59 13 -0.69
CISPEP 26 PHE E 58 PRO E 59 13 -0.09
CISPEP 27 PHE D 58 PRO D 59 14 0.29
CISPEP 28 PHE E 58 PRO E 59 14 0.22
CISPEP 29 PHE D 58 PRO D 59 15 -0.14
CISPEP 30 PHE E 58 PRO E 59 15 -0.99
CISPEP 31 PHE D 58 PRO D 59 16 -0.17
CISPEP 32 PHE E 58 PRO E 59 16 -0.18
CISPEP 33 PHE D 58 PRO D 59 17 -0.57
CISPEP 34 PHE E 58 PRO E 59 17 -0.72
CISPEP 35 PHE D 58 PRO D 59 18 -0.60
CISPEP 36 PHE E 58 PRO E 59 18 -0.19
CISPEP 37 PHE D 58 PRO D 59 19 -0.90
CISPEP 38 PHE E 58 PRO E 59 19 0.07
CISPEP 39 PHE D 58 PRO D 59 20 0.01
CISPEP 40 PHE E 58 PRO E 59 20 -0.83
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