Header list of 1c20.pdb file
Complete list - b 16 2 Bytes
HEADER DNA BINDING PROTEIN 22-JUL-99 1C20
TITLE SOLUTION STRUCTURE OF THE DNA-BINDING DOMAIN FROM THE DEAD RINGER
TITLE 2 PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DEAD RINGER PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: DNA-BINDING DOMAIN;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;
SOURCE 3 ORGANISM_COMMON: FRUIT FLY;
SOURCE 4 ORGANISM_TAXID: 7227;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PGEX-4T-1;
SOURCE 8 OTHER_DETAILS: THIS SEQUENCE OCCURS NATURALLY IN DROSOPHILA
SOURCE 9 MELANOGASTER
KEYWDS DNA-BINDING DOMAIN, ARID, AT-RICH INTERACTION DOMAIN, DNA-BINDING
KEYWDS 2 PROTEIN, DNA BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 21
MDLTYP MINIMIZED AVERAGE
AUTHOR J.IWAHARA,R.T.CLUBB
REVDAT 3 16-FEB-22 1C20 1 KEYWDS REMARK
REVDAT 2 24-FEB-09 1C20 1 VERSN
REVDAT 1 10-NOV-99 1C20 0
JRNL AUTH J.IWAHARA,R.T.CLUBB
JRNL TITL SOLUTION STRUCTURE OF THE DNA BINDING DOMAIN FROM DEAD
JRNL TITL 2 RINGER, A SEQUENCE-SPECIFIC AT-RICH INTERACTION DOMAIN
JRNL TITL 3 (ARID).
JRNL REF EMBO J. V. 18 6084 1999
JRNL REFN ISSN 0261-4189
JRNL PMID 10545119
JRNL DOI 10.1093/EMBOJ/18.21.6084
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE 1999, X-PLOR 3.8
REMARK 3 AUTHORS : DELAGLIO, F. (NMRPIPE), BRUNGER, A. (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1C20 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-JUL-99.
REMARK 100 THE DEPOSITION ID IS D_1000009381.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 6.7
REMARK 210 IONIC STRENGTH : 0.10
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.5MM DEAD RINGER U-15N; 20MM
REMARK 210 TRIS-HCL (PH 6.7); 100MM NACL;
REMARK 210 1.5MM ZNCL2; 2MM DTT; 0.01% NAN3;
REMARK 210 1.5MM DEAD RINGER U-15N,13C;
REMARK 210 20MM TRIS-HCL (PH 6.7); 100MM
REMARK 210 NACL; 1.5MM ZNCL2; 2MM DTT; 0.01%
REMARK 210 NAN3
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : SEE PRIMARY REFERENCE
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRVIEW 4.0.3, X-PLOR 3.8
REMARK 210 METHOD USED : SEE PRIMARY REFERENCE
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 21
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH ACCEPTABLE
REMARK 210 COVALENT GEOMETRY, WITH
REMARK 210 FAVORABLE NON-BOND ENERGY, AND
REMARK 210 WITH THE LEAST RESTRAINT
REMARK 210 VIOLATIONS.
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 21
REMARK 210
REMARK 210 REMARK: SEE PRIMARY REFERENCE
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: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O THR A 92 H ALA A 94 1.45
REMARK 500 O SER A 93 H THR A 97 1.54
REMARK 500 O MET A 49 H SER A 52 1.54
REMARK 500 O GLN A 123 H ASP A 127 1.55
REMARK 500
REMARK 500 REMARK: NULL
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 GLN A 37 -9.31 -55.51
REMARK 500 1 PRO A 42 -154.81 -54.38
REMARK 500 1 ILE A 43 -149.87 -70.76
REMARK 500 1 ALA A 50 -97.08 47.63
REMARK 500 1 LEU A 54 97.66 -60.76
REMARK 500 1 HIS A 86 117.37 -35.97
REMARK 500 1 PRO A 88 -72.70 -56.96
REMARK 500 1 SER A 89 20.18 179.55
REMARK 500 1 ILE A 91 60.38 39.96
REMARK 500 1 THR A 92 -148.99 -60.41
REMARK 500 1 SER A 93 52.29 -68.04
REMARK 500 2 GLN A 37 -8.52 -48.52
REMARK 500 2 PRO A 42 -164.74 -52.70
REMARK 500 2 ILE A 43 -145.09 -61.01
REMARK 500 2 ASN A 44 -80.04 -89.97
REMARK 500 2 ALA A 50 -89.97 42.92
REMARK 500 2 LYS A 76 54.88 39.34
REMARK 500 2 LEU A 85 56.65 -99.30
REMARK 500 2 HIS A 86 149.99 -40.00
REMARK 500 2 SER A 89 19.14 173.93
REMARK 500 2 SER A 90 8.26 -153.69
REMARK 500 2 SER A 93 30.01 -145.98
REMARK 500 3 PRO A 42 -152.28 -56.52
REMARK 500 3 ILE A 43 -157.57 -66.99
REMARK 500 3 ALA A 50 -89.96 41.04
REMARK 500 3 LEU A 54 97.08 -61.23
REMARK 500 3 LEU A 85 56.68 -140.79
REMARK 500 3 PRO A 88 -70.49 -61.66
REMARK 500 3 SER A 89 27.44 170.88
REMARK 500 3 SER A 90 -29.11 -163.87
REMARK 500 3 SER A 93 61.16 3.09
REMARK 500 4 PRO A 42 -154.21 -56.86
REMARK 500 4 ILE A 43 -156.13 -70.05
REMARK 500 4 ALA A 50 80.78 36.22
REMARK 500 4 LYS A 51 -20.50 57.68
REMARK 500 4 LEU A 54 95.86 -64.02
REMARK 500 4 LEU A 85 58.63 -149.87
REMARK 500 4 PRO A 88 19.14 -55.67
REMARK 500 4 SER A 90 17.93 -159.36
REMARK 500 4 THR A 92 40.92 -90.02
REMARK 500 4 SER A 93 18.86 -162.43
REMARK 500 5 PRO A 42 -155.68 -54.06
REMARK 500 5 ILE A 43 -152.39 -70.97
REMARK 500 5 ALA A 50 -88.92 39.97
REMARK 500 5 LEU A 54 99.22 -59.92
REMARK 500 5 LEU A 85 58.35 -98.77
REMARK 500 5 HIS A 86 157.37 -36.45
REMARK 500 5 PRO A 88 26.44 -63.06
REMARK 500 5 SER A 90 -32.44 -152.24
REMARK 500 5 SER A 93 44.44 -146.72
REMARK 500
REMARK 500 THIS ENTRY HAS 222 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 14 0.14 SIDE CHAIN
REMARK 500 1 ARG A 25 0.09 SIDE CHAIN
REMARK 500 1 ARG A 39 0.27 SIDE CHAIN
REMARK 500 1 ARG A 45 0.31 SIDE CHAIN
REMARK 500 1 ARG A 66 0.21 SIDE CHAIN
REMARK 500 1 ARG A 99 0.30 SIDE CHAIN
REMARK 500 1 ARG A 130 0.25 SIDE CHAIN
REMARK 500 2 ARG A 25 0.28 SIDE CHAIN
REMARK 500 2 ARG A 39 0.20 SIDE CHAIN
REMARK 500 2 ARG A 45 0.32 SIDE CHAIN
REMARK 500 2 ARG A 66 0.31 SIDE CHAIN
REMARK 500 2 ARG A 99 0.32 SIDE CHAIN
REMARK 500 2 ARG A 130 0.30 SIDE CHAIN
REMARK 500 3 ARG A 14 0.20 SIDE CHAIN
REMARK 500 3 ARG A 25 0.22 SIDE CHAIN
REMARK 500 3 ARG A 45 0.22 SIDE CHAIN
REMARK 500 3 ARG A 66 0.14 SIDE CHAIN
REMARK 500 3 ARG A 99 0.30 SIDE CHAIN
REMARK 500 3 ARG A 130 0.28 SIDE CHAIN
REMARK 500 4 ARG A 14 0.27 SIDE CHAIN
REMARK 500 4 ARG A 25 0.24 SIDE CHAIN
REMARK 500 4 ARG A 39 0.30 SIDE CHAIN
REMARK 500 4 ARG A 45 0.16 SIDE CHAIN
REMARK 500 4 ARG A 66 0.30 SIDE CHAIN
REMARK 500 4 ARG A 130 0.24 SIDE CHAIN
REMARK 500 5 ARG A 14 0.29 SIDE CHAIN
REMARK 500 5 ARG A 25 0.30 SIDE CHAIN
REMARK 500 5 ARG A 39 0.18 SIDE CHAIN
REMARK 500 5 ARG A 45 0.29 SIDE CHAIN
REMARK 500 5 ARG A 66 0.29 SIDE CHAIN
REMARK 500 5 ARG A 99 0.29 SIDE CHAIN
REMARK 500 5 ARG A 130 0.32 SIDE CHAIN
REMARK 500 6 ARG A 14 0.23 SIDE CHAIN
REMARK 500 6 ARG A 25 0.12 SIDE CHAIN
REMARK 500 6 ARG A 39 0.32 SIDE CHAIN
REMARK 500 6 ARG A 45 0.19 SIDE CHAIN
REMARK 500 6 ARG A 66 0.15 SIDE CHAIN
REMARK 500 6 ARG A 99 0.14 SIDE CHAIN
REMARK 500 6 ARG A 130 0.23 SIDE CHAIN
REMARK 500 7 ARG A 14 0.17 SIDE CHAIN
REMARK 500 7 ARG A 25 0.27 SIDE CHAIN
REMARK 500 7 ARG A 39 0.30 SIDE CHAIN
REMARK 500 7 ARG A 45 0.29 SIDE CHAIN
REMARK 500 7 ARG A 66 0.29 SIDE CHAIN
REMARK 500 7 ARG A 99 0.31 SIDE CHAIN
REMARK 500 7 ARG A 130 0.26 SIDE CHAIN
REMARK 500 8 ARG A 14 0.32 SIDE CHAIN
REMARK 500 8 ARG A 25 0.26 SIDE CHAIN
REMARK 500 8 ARG A 39 0.32 SIDE CHAIN
REMARK 500 8 ARG A 45 0.23 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 134 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4334 RELATED DB: BMRB
REMARK 900 CHEMICAL SHIFT ASSIGNMENTS OF THE DEAD RINGER DNA-BINDING DOMAIN
DBREF 1C20 A 3 130 UNP Q24573 DRI_DROME 262 389
SEQRES 1 A 128 GLY TRP SER PHE GLU GLU GLN PHE LYS GLN VAL ARG GLN
SEQRES 2 A 128 LEU TYR GLU ILE ASN ASP ASP PRO LYS ARG LYS GLU PHE
SEQRES 3 A 128 LEU ASP ASP LEU PHE SER PHE MET GLN LYS ARG GLY THR
SEQRES 4 A 128 PRO ILE ASN ARG LEU PRO ILE MET ALA LYS SER VAL LEU
SEQRES 5 A 128 ASP LEU TYR GLU LEU TYR ASN LEU VAL ILE ALA ARG GLY
SEQRES 6 A 128 GLY LEU VAL ASP VAL ILE ASN LYS LYS LEU TRP GLN GLU
SEQRES 7 A 128 ILE ILE LYS GLY LEU HIS LEU PRO SER SER ILE THR SER
SEQRES 8 A 128 ALA ALA PHE THR LEU ARG THR GLN TYR MET LYS TYR LEU
SEQRES 9 A 128 TYR PRO TYR GLU CYS GLU LYS LYS ASN LEU SER THR PRO
SEQRES 10 A 128 ALA GLU LEU GLN ALA ALA ILE ASP GLY ASN ARG
HELIX 1 1 SER A 5 ILE A 19 1 15
HELIX 2 2 ASP A 22 GLN A 37 1 16
HELIX 3 3 ASP A 55 ARG A 66 1 12
HELIX 4 4 GLY A 68 LYS A 76 1 9
HELIX 5 5 LEU A 77 LEU A 85 1 9
HELIX 6 6 SER A 93 LEU A 106 1 14
HELIX 7 7 LEU A 106 ASN A 115 1 10
HELIX 8 8 THR A 118 ARG A 130 1 13
SHEET 1 1 2 ILE A 48 MET A 49 0
SHEET 2 1 2 SER A 52 VAL A 53 -1
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