Header list of 1paa.pdb file
Complete list - 29 20 Bytes
HEADER TRANSCRIPTION REGULATION 15-JUL-94 1PAA
TITLE STRUCTURE OF A HISTIDINE-X4-HISTIDINE ZINC FINGER DOMAIN: INSIGHTS
TITLE 2 INTO ADR1-UAS1 PROTEIN-DNA RECOGNITION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: YEAST TRANSCRIPTION FACTOR ADR1;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 4932
KEYWDS TRANSCRIPTION REGULATION
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR B.E.BERNSTEIN,R.C.HOFFMAN,S.J.HORVATH,J.R.HERRIOTT,R.E.KLEVIT
REVDAT 4 29-NOV-17 1PAA 1 REMARK HELIX
REVDAT 3 24-FEB-09 1PAA 1 VERSN
REVDAT 2 01-APR-03 1PAA 1 JRNL
REVDAT 1 15-OCT-94 1PAA 0
JRNL AUTH B.E.BERNSTEIN,R.C.HOFFMAN,S.HORVATH,J.R.HERRIOTT,R.E.KLEVIT
JRNL TITL STRUCTURE OF A HISTIDINE-X4-HISTIDINE ZINC FINGER DOMAIN:
JRNL TITL 2 INSIGHTS INTO ADR1-UAS1 PROTEIN-DNA RECOGNITION.
JRNL REF BIOCHEMISTRY V. 33 4460 1994
JRNL REFN ISSN 0006-2960
JRNL PMID 8161501
JRNL DOI 10.1021/BI00181A005
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH R.C.HOFFMAN,R.X.XU,R.E.KLEVIT,J.R.HERRIOTT
REMARK 1 TITL A SIMPLE METHOD FOR THE REFINEMENT OF MODELS DERIVED FROM
REMARK 1 TITL 2 NMR DATA DEMONSTRATED ON A ZINC-FINGER DOMAIN FROM YEAST
REMARK 1 TITL 3 ADR1
REMARK 1 REF J.MAGN.RESON.,SER.B V. 102 61 1993
REMARK 1 REFN ISSN 1064-1866
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DIANA, REPENT
REMARK 3 AUTHORS : GUNTERT,BRAUN,WUTHRICH (DIANA),
REMARK 3 HOFFMAN,XU,KLEVIT,HERRIOTT (REPENT)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1PAA 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_1000175559.
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 : 10
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: 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
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 TYR A 132 90.88 -38.26
REMARK 500 1 LEU A 136 -61.54 -91.90
REMARK 500 1 ASN A 138 -11.55 87.42
REMARK 500 1 ILE A 148 -70.14 -66.12
REMARK 500 1 ILE A 154 -72.05 -71.98
REMARK 500 1 SER A 156 82.39 -11.69
REMARK 500 2 LEU A 136 -63.87 -94.02
REMARK 500 2 ASN A 138 -18.45 91.54
REMARK 500 2 ILE A 148 -71.14 -68.05
REMARK 500 2 ARG A 149 -36.32 -38.07
REMARK 500 2 LYS A 153 -67.16 -104.67
REMARK 500 2 ILE A 154 -71.31 -68.77
REMARK 500 2 SER A 156 80.07 -9.32
REMARK 500 3 ALA A 131 165.89 -44.86
REMARK 500 3 LEU A 136 -63.90 -92.31
REMARK 500 3 ASN A 138 -17.51 91.23
REMARK 500 3 LYS A 153 -66.30 -99.93
REMARK 500 3 ILE A 154 -71.22 -70.34
REMARK 500 3 SER A 156 71.36 -9.32
REMARK 500 4 TYR A 132 88.66 -36.03
REMARK 500 4 LEU A 136 -63.47 -92.01
REMARK 500 4 ASN A 138 -13.16 87.06
REMARK 500 4 ILE A 148 -73.10 -72.66
REMARK 500 4 ARG A 149 -36.51 -38.08
REMARK 500 4 LYS A 153 -71.99 -107.37
REMARK 500 4 SER A 156 -174.77 -47.46
REMARK 500 5 TYR A 132 87.77 -44.93
REMARK 500 5 LEU A 136 -63.64 -93.86
REMARK 500 5 ASN A 138 -14.12 90.61
REMARK 500 5 LYS A 153 -68.61 -103.46
REMARK 500 5 SER A 156 88.58 -20.61
REMARK 500 6 TYR A 132 87.41 -37.49
REMARK 500 6 LEU A 136 -63.48 -94.44
REMARK 500 6 ASN A 138 -17.15 89.20
REMARK 500 6 LYS A 153 -66.69 -101.03
REMARK 500 6 ILE A 154 -73.52 -69.47
REMARK 500 6 SER A 156 80.41 -8.66
REMARK 500 7 TYR A 132 87.29 -50.18
REMARK 500 7 LEU A 136 -63.21 -93.72
REMARK 500 7 ASN A 138 -10.25 87.12
REMARK 500 7 ILE A 148 -71.68 -67.50
REMARK 500 7 LYS A 153 -66.87 -107.94
REMARK 500 7 ILE A 154 -73.47 -65.11
REMARK 500 7 SER A 156 82.30 -8.04
REMARK 500 7 ASN A 158 105.70 -39.45
REMARK 500 8 ALA A 131 154.46 -47.45
REMARK 500 8 TYR A 132 86.27 -66.77
REMARK 500 8 LEU A 136 -62.01 -92.31
REMARK 500 8 ASN A 138 -9.30 85.17
REMARK 500 8 ILE A 148 -70.30 -66.24
REMARK 500
REMARK 500 THIS ENTRY HAS 70 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 139 0.15 SIDE CHAIN
REMARK 500 1 ARG A 143 0.26 SIDE CHAIN
REMARK 500 1 ARG A 144 0.30 SIDE CHAIN
REMARK 500 1 ARG A 149 0.28 SIDE CHAIN
REMARK 500 2 ARG A 139 0.16 SIDE CHAIN
REMARK 500 2 ARG A 143 0.25 SIDE CHAIN
REMARK 500 2 ARG A 144 0.28 SIDE CHAIN
REMARK 500 2 ARG A 149 0.30 SIDE CHAIN
REMARK 500 3 ARG A 139 0.16 SIDE CHAIN
REMARK 500 3 ARG A 143 0.08 SIDE CHAIN
REMARK 500 3 ARG A 144 0.28 SIDE CHAIN
REMARK 500 3 ARG A 149 0.30 SIDE CHAIN
REMARK 500 4 ARG A 139 0.18 SIDE CHAIN
REMARK 500 4 ARG A 144 0.19 SIDE CHAIN
REMARK 500 4 ARG A 149 0.30 SIDE CHAIN
REMARK 500 5 ARG A 139 0.30 SIDE CHAIN
REMARK 500 5 ARG A 143 0.30 SIDE CHAIN
REMARK 500 5 ARG A 144 0.15 SIDE CHAIN
REMARK 500 5 ARG A 149 0.10 SIDE CHAIN
REMARK 500 6 ARG A 139 0.27 SIDE CHAIN
REMARK 500 6 ARG A 143 0.29 SIDE CHAIN
REMARK 500 6 ARG A 144 0.20 SIDE CHAIN
REMARK 500 6 ARG A 149 0.10 SIDE CHAIN
REMARK 500 7 ARG A 139 0.12 SIDE CHAIN
REMARK 500 7 ARG A 143 0.29 SIDE CHAIN
REMARK 500 7 ARG A 144 0.24 SIDE CHAIN
REMARK 500 7 ARG A 149 0.20 SIDE CHAIN
REMARK 500 8 ARG A 143 0.29 SIDE CHAIN
REMARK 500 8 ARG A 144 0.29 SIDE CHAIN
REMARK 500 8 ARG A 149 0.29 SIDE CHAIN
REMARK 500 9 ARG A 139 0.11 SIDE CHAIN
REMARK 500 9 ARG A 143 0.30 SIDE CHAIN
REMARK 500 9 ARG A 144 0.30 SIDE CHAIN
REMARK 500 9 ARG A 149 0.30 SIDE CHAIN
REMARK 500 10 ARG A 143 0.28 SIDE CHAIN
REMARK 500 10 ARG A 144 0.30 SIDE CHAIN
REMARK 500 10 ARG A 149 0.21 SIDE CHAIN
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 160 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 155 NE2
REMARK 620 2 CYS A 134 SG 111.4
REMARK 620 3 CYS A 137 SG 131.9 116.3
REMARK 620 4 HIS A 150 NE2 96.9 98.8 81.2
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 160
DBREF 1PAA A 130 159 UNP P07248 ADR1_YEAST 130 159
SEQADV 1PAA ALA A 131 UNP P07248 PRO 131 CONFLICT
SEQADV 1PAA ALA A 133 UNP P07248 PRO 133 CONFLICT
SEQADV 1PAA ALA A 140 UNP P07248 CYS 140 CONFLICT
SEQRES 1 A 30 LYS ALA TYR ALA CYS GLY LEU CYS ASN ARG ALA PHE THR
SEQRES 2 A 30 ARG ARG ASP LEU LEU ILE ARG HIS ALA GLN LYS ILE HIS
SEQRES 3 A 30 SER GLY ASN LEU
HET ZN A 160 1
HETNAM ZN ZINC ION
FORMUL 2 ZN ZN 2+
HELIX 1 AAA ARG A 144 ALA A 151 1ALPHA & 3/10 HELICAL H-BONDS 8
SHEET 1 BBB 2 ALA A 131 CYS A 134 0
SHEET 2 BBB 2 ARG A 139 PHE A 141 -1
LINK ZN ZN A 160 NE2 HIS A 155 1555 1555 2.04
LINK ZN ZN A 160 SG CYS A 134 1555 1555 2.27
LINK ZN ZN A 160 SG CYS A 137 1555 1555 2.27
LINK ZN ZN A 160 NE2 HIS A 150 1555 1555 1.92
SITE 1 AC1 5 CYS A 134 LEU A 136 CYS A 137 HIS A 150
SITE 2 AC1 5 HIS A 155
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 - 29 20 Bytes