Header list of 2adr.pdb file
Complete list - v 3 2 Bytes
HEADER TRANSCRIPTION REGULATION 20-MAR-98 2ADR TITLE ADR1 DNA-BINDING DOMAIN FROM SACCHAROMYCES CEREVISIAE, NMR, 25 TITLE 2 STRUCTURES COMPND MOL_ID: 1; COMPND 2 MOLECULE: ADR1; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: DNA-BINDING DOMAIN; COMPND 5 ENGINEERED: YES; COMPND 6 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE; SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST; SOURCE 4 ORGANISM_TAXID: 4932; SOURCE 5 CELL_LINE: BL21; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3); SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET11A KEYWDS TRANSCRIPTION REGULATION, ADR1, ZINC FINGER EXPDTA SOLUTION NMR NUMMDL 25 AUTHOR P.M.BOWERS,R.E.KLEIVT REVDAT 3 03-NOV-21 2ADR 1 REMARK SEQADV LINK REVDAT 2 24-FEB-09 2ADR 1 VERSN REVDAT 1 17-JUN-98 2ADR 0 JRNL AUTH P.M.BOWERS,L.E.SCHAUFLER,R.E.KLEVIT JRNL TITL A FOLDING TRANSITION AND NOVEL ZINC FINGER ACCESSORY DOMAIN JRNL TITL 2 IN THE TRANSCRIPTION FACTOR ADR1. JRNL REF NAT.STRUCT.BIOL. V. 6 478 1999 JRNL REFN ISSN 1072-8368 JRNL PMID 10331877 JRNL DOI 10.1038/8283 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH D.E.HYRE,R.E.KLEVIT REMARK 1 TITL A DISORDER-TO-ORDER TRANSITION COULED TO DNA BINDING IN THE REMARK 1 TITL 2 ESSENTIAL ZINC-FINGER DNA-BINDING OF YEAST ADR1 ELUCIDATED REMARK 1 TITL 3 BY BACKBONE DYNAMICS AND PROTON EXCHANGE REMARK 1 REF TO BE PUBLISHED REMARK 1 REFN REMARK 1 REFERENCE 2 REMARK 1 AUTH M.SCHMIEDESKAMP,P.RAJAGOPAL,R.E.KLEVIT REMARK 1 TITL NMR CHEMICAL SHIFT PERTURBATION MAPPING OF DNA BINDING BY A REMARK 1 TITL 2 ZINC-FINGER DOMAIN FROM THE YEAST TRANSCRIPTION FACTOR ADR1 REMARK 1 REF PROTEIN SCI. V. 6 1835 1997 REMARK 1 REFN ISSN 0961-8368 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: REFINEMENT DETAILS HAVE BEEN SUBMITTED REMARK 3 FOR PUBLICATION. REMARK 4 REMARK 4 2ADR 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_1000177746. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 303 REMARK 210 PH : 5.5 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : NULL REMARK 210 SAMPLE CONTENTS : NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 13C EDITED NOESY; 15N EDITED REMARK 210 NOESY; HNHB REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ REMARK 210 SPECTROMETER MODEL : DMX750 REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRPIPES, X-PLOR REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED REMARK 210 ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 50 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 25 REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST ENERGY TERM 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 ALA A 114 23.10 -143.64 REMARK 500 1 SER A 125 33.80 -97.41 REMARK 500 1 THR A 127 -43.82 -139.41 REMARK 500 1 ASN A 138 53.08 72.65 REMARK 500 1 ILE A 154 -53.13 -123.82 REMARK 500 1 HIS A 155 -79.57 -76.29 REMARK 500 1 SER A 156 -167.08 178.13 REMARK 500 1 LEU A 159 83.89 60.00 REMARK 500 2 SER A 103 114.16 -160.28 REMARK 500 2 ALA A 114 25.98 -161.03 REMARK 500 2 TYR A 123 33.57 -96.40 REMARK 500 2 ASN A 128 120.57 63.93 REMARK 500 2 LYS A 130 148.47 62.63 REMARK 500 2 LEU A 136 -46.13 -135.26 REMARK 500 2 ASN A 138 85.87 72.35 REMARK 500 2 ILE A 154 -53.85 -121.10 REMARK 500 2 HIS A 155 -78.32 -76.59 REMARK 500 2 SER A 156 -174.31 -177.53 REMARK 500 2 LEU A 159 160.03 61.46 REMARK 500 3 ARG A 111 -159.14 -89.55 REMARK 500 3 HIS A 126 -72.32 -68.90 REMARK 500 3 THR A 127 -149.39 -98.00 REMARK 500 3 LEU A 136 -46.46 -135.25 REMARK 500 3 ASN A 138 74.70 72.69 REMARK 500 3 ILE A 154 -54.36 -120.34 REMARK 500 3 HIS A 155 -78.38 -78.37 REMARK 500 3 SER A 156 -176.28 -177.80 REMARK 500 3 ASN A 158 -72.53 -82.59 REMARK 500 3 LEU A 159 -64.12 -171.61 REMARK 500 4 VAL A 108 -46.59 -131.67 REMARK 500 4 HIS A 126 -71.32 -67.16 REMARK 500 4 ASN A 128 94.39 42.13 REMARK 500 4 GLU A 129 161.33 60.95 REMARK 500 4 LEU A 136 -46.79 -135.56 REMARK 500 4 ASN A 138 79.97 71.48 REMARK 500 4 SER A 156 119.11 64.37 REMARK 500 4 ASN A 158 -45.26 -133.29 REMARK 500 4 LEU A 159 -67.49 -140.58 REMARK 500 5 VAL A 108 -50.60 -121.83 REMARK 500 5 ARG A 111 -158.04 -83.02 REMARK 500 5 ALA A 114 23.85 -155.48 REMARK 500 5 THR A 127 79.36 -101.31 REMARK 500 5 GLU A 129 -78.47 -137.52 REMARK 500 5 ASN A 138 49.09 74.03 REMARK 500 5 HIS A 155 -75.19 -63.31 REMARK 500 5 SER A 156 143.55 -174.64 REMARK 500 6 ALA A 112 81.34 -150.21 REMARK 500 6 LEU A 136 -45.90 -135.25 REMARK 500 6 ARG A 139 -173.25 -68.18 REMARK 500 6 SER A 156 155.12 61.49 REMARK 500 REMARK 500 THIS ENTRY HAS 193 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 102 0.22 SIDE CHAIN REMARK 500 1 ARG A 111 0.22 SIDE CHAIN REMARK 500 1 ARG A 115 0.29 SIDE CHAIN REMARK 500 1 ARG A 121 0.30 SIDE CHAIN REMARK 500 1 ARG A 124 0.31 SIDE CHAIN REMARK 500 1 ARG A 139 0.23 SIDE CHAIN REMARK 500 1 ARG A 143 0.24 SIDE CHAIN REMARK 500 1 ARG A 144 0.28 SIDE CHAIN REMARK 500 1 ARG A 149 0.31 SIDE CHAIN REMARK 500 2 ARG A 102 0.28 SIDE CHAIN REMARK 500 2 ARG A 111 0.26 SIDE CHAIN REMARK 500 2 ARG A 115 0.32 SIDE CHAIN REMARK 500 2 ARG A 121 0.25 SIDE CHAIN REMARK 500 2 ARG A 124 0.27 SIDE CHAIN REMARK 500 2 ARG A 139 0.30 SIDE CHAIN REMARK 500 2 ARG A 143 0.26 SIDE CHAIN REMARK 500 2 ARG A 144 0.30 SIDE CHAIN REMARK 500 2 ARG A 149 0.32 SIDE CHAIN REMARK 500 3 ARG A 102 0.25 SIDE CHAIN REMARK 500 3 ARG A 111 0.23 SIDE CHAIN REMARK 500 3 ARG A 115 0.24 SIDE CHAIN REMARK 500 3 ARG A 121 0.23 SIDE CHAIN REMARK 500 3 ARG A 124 0.29 SIDE CHAIN REMARK 500 3 ARG A 139 0.31 SIDE CHAIN REMARK 500 3 ARG A 143 0.29 SIDE CHAIN REMARK 500 3 ARG A 144 0.27 SIDE CHAIN REMARK 500 3 ARG A 149 0.28 SIDE CHAIN REMARK 500 4 ARG A 102 0.26 SIDE CHAIN REMARK 500 4 ARG A 111 0.27 SIDE CHAIN REMARK 500 4 ARG A 115 0.24 SIDE CHAIN REMARK 500 4 ARG A 121 0.25 SIDE CHAIN REMARK 500 4 ARG A 124 0.28 SIDE CHAIN REMARK 500 4 ARG A 139 0.26 SIDE CHAIN REMARK 500 4 ARG A 143 0.22 SIDE CHAIN REMARK 500 4 ARG A 144 0.25 SIDE CHAIN REMARK 500 4 ARG A 149 0.26 SIDE CHAIN REMARK 500 5 ARG A 102 0.31 SIDE CHAIN REMARK 500 5 ARG A 111 0.27 SIDE CHAIN REMARK 500 5 ARG A 115 0.31 SIDE CHAIN REMARK 500 5 ARG A 121 0.32 SIDE CHAIN REMARK 500 5 ARG A 124 0.31 SIDE CHAIN REMARK 500 5 ARG A 139 0.31 SIDE CHAIN REMARK 500 5 ARG A 143 0.31 SIDE CHAIN REMARK 500 5 ARG A 144 0.31 SIDE CHAIN REMARK 500 5 ARG A 149 0.31 SIDE CHAIN REMARK 500 6 ARG A 102 0.27 SIDE CHAIN REMARK 500 6 ARG A 111 0.22 SIDE CHAIN REMARK 500 6 ARG A 115 0.28 SIDE CHAIN REMARK 500 6 ARG A 121 0.30 SIDE CHAIN REMARK 500 6 ARG A 124 0.30 SIDE CHAIN REMARK 500 REMARK 500 THIS ENTRY HAS 225 PLANE DEVIATIONS. REMARK 500 REMARK 500 REMARK: NULL REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN A 163 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS A 106 SG REMARK 620 2 CYS A 109 SG 114.4 REMARK 620 3 HIS A 122 NE2 116.7 126.2 REMARK 620 4 HIS A 126 NE2 103.1 102.1 82.0 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN A 162 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS A 134 SG REMARK 620 2 CYS A 137 SG 102.4 REMARK 620 3 HIS A 150 NE2 110.4 88.3 REMARK 620 4 HIS A 155 NE2 121.8 124.8 103.6 REMARK 620 N 1 2 3 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: ZNC REMARK 800 EVIDENCE_CODE: UNKNOWN REMARK 800 SITE_DESCRIPTION: ZINC FINGER 2. REMARK 800 REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 162 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 163 DBREF 2ADR A 102 161 UNP P07248 ADR1_YEAST 102 161 SEQADV 2ADR ALA A 140 UNP P07248 CYS 140 ENGINEERED MUTATION SEQRES 1 A 60 ARG SER PHE VAL CYS GLU VAL CYS THR ARG ALA PHE ALA SEQRES 2 A 60 ARG GLN GLU HIS LEU LYS ARG HIS TYR ARG SER HIS THR SEQRES 3 A 60 ASN GLU LYS PRO TYR PRO CYS GLY LEU CYS ASN ARG ALA SEQRES 4 A 60 PHE THR ARG ARG ASP LEU LEU ILE ARG HIS ALA GLN LYS SEQRES 5 A 60 ILE HIS SER GLY ASN LEU GLY GLU HET ZN A 162 1 HET ZN A 163 1 HETNAM ZN ZINC ION FORMUL 2 ZN 2(ZN 2+) HELIX 1 1 GLN A 116 HIS A 126 1 11 HELIX 2 2 ARG A 144 ALA A 151 1 8 SHEET 1 A 2 TYR A 132 PRO A 133 0 SHEET 2 A 2 ALA A 140 PHE A 141 -1 N PHE A 141 O TYR A 132 LINK SG CYS A 106 ZN ZN A 163 1555 1555 2.37 LINK SG CYS A 109 ZN ZN A 163 1555 1555 2.35 LINK NE2 HIS A 122 ZN ZN A 163 1555 1555 2.05 LINK NE2 HIS A 126 ZN ZN A 163 1555 1555 2.06 LINK SG CYS A 134 ZN ZN A 162 1555 1555 2.35 LINK SG CYS A 137 ZN ZN A 162 1555 1555 2.28 LINK NE2 HIS A 150 ZN ZN A 162 1555 1555 2.05 LINK NE2 HIS A 155 ZN ZN A 162 1555 1555 2.03 SITE 1 ZNC 8 CYS A 106 CYS A 109 HIS A 122 HIS A 126 SITE 2 ZNC 8 CYS A 134 CYS A 137 HIS A 150 HIS A 155 SITE 1 AC1 4 CYS A 134 CYS A 137 HIS A 150 HIS A 155 SITE 1 AC2 5 CYS A 106 CYS A 109 ARG A 111 HIS A 122 SITE 2 AC2 5 HIS A 126 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 - v 3 2 Bytes