Header list of 1arf.pdb file
Complete list - 29 20 Bytes
HEADER TRANSCRIPTION REGULATION 01-OCT-93 1ARF
TITLE STRUCTURES OF DNA-BINDING MUTANT ZINC FINGER DOMAINS: IMPLICATIONS FOR
TITLE 2 DNA BINDING
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 R.C.HOFFMAN,R.X.XU,S.J.HORVATH,J.R.HERRIOTT,R.E.KLEVIT
REVDAT 3 29-NOV-17 1ARF 1 REMARK HELIX
REVDAT 2 24-FEB-09 1ARF 1 VERSN
REVDAT 1 31-JAN-94 1ARF 0
JRNL AUTH R.C.HOFFMAN,S.J.HORVATH,R.E.KLEVIT
JRNL TITL STRUCTURES OF DNA-BINDING MUTANT ZINC FINGER DOMAINS:
JRNL TITL 2 IMPLICATIONS FOR DNA BINDING.
JRNL REF PROTEIN SCI. V. 2 951 1993
JRNL REFN ISSN 0961-8368
JRNL PMID 8318900
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. V. 102 61 1993
REMARK 1 REFN ISSN 0022-2364
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NULL
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1ARF 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_1000171165.
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 H CYS A 106 O ARG A 111 1.51
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 SER A 103 -172.48 -57.63
REMARK 500 1 THR A 110 23.48 41.39
REMARK 500 2 SER A 103 -146.82 -61.49
REMARK 500 2 CYS A 109 -61.71 -92.54
REMARK 500 2 THR A 110 -17.27 138.01
REMARK 500 2 ASN A 128 83.18 -175.21
REMARK 500 2 GLU A 129 96.02 -25.68
REMARK 500 3 THR A 110 39.42 99.67
REMARK 500 3 PHE A 113 -87.59 -120.23
REMARK 500 3 ALA A 114 -54.27 175.18
REMARK 500 3 ASN A 128 98.69 177.64
REMARK 500 4 SER A 103 174.08 -46.85
REMARK 500 4 VAL A 108 -63.22 -96.44
REMARK 500 4 THR A 110 4.23 123.61
REMARK 500 4 PHE A 113 -95.26 -132.54
REMARK 500 4 ALA A 114 -60.62 -175.94
REMARK 500 4 THR A 127 -76.58 -107.73
REMARK 500 4 ASN A 128 -61.62 -26.16
REMARK 500 4 GLU A 129 115.80 -13.21
REMARK 500 5 GLU A 107 -14.85 -49.39
REMARK 500 5 VAL A 108 -73.77 -78.02
REMARK 500 5 THR A 127 -73.20 -92.11
REMARK 500 5 ASN A 128 116.92 -174.83
REMARK 500 6 VAL A 108 -64.70 -99.64
REMARK 500 6 THR A 110 -5.85 136.98
REMARK 500 6 PHE A 113 -85.13 -122.05
REMARK 500 6 ALA A 114 -54.21 172.04
REMARK 500 6 ASN A 128 91.44 177.07
REMARK 500 6 GLU A 129 114.95 -9.37
REMARK 500 7 SER A 103 173.89 -48.06
REMARK 500 7 THR A 110 -3.21 132.62
REMARK 500 7 PHE A 113 -96.27 -132.42
REMARK 500 7 ALA A 114 -58.15 -177.80
REMARK 500 7 THR A 127 112.50 173.98
REMARK 500 7 ASN A 128 -142.07 -134.90
REMARK 500 8 THR A 110 30.16 90.06
REMARK 500 8 PHE A 113 -88.27 -122.99
REMARK 500 8 ALA A 114 -53.65 174.34
REMARK 500 8 ASN A 128 121.17 172.54
REMARK 500 9 PHE A 104 118.65 -4.66
REMARK 500 9 GLU A 107 20.18 -77.86
REMARK 500 9 PHE A 113 -96.69 -132.69
REMARK 500 9 ALA A 114 -56.73 -175.77
REMARK 500 9 ASN A 128 -83.81 170.43
REMARK 500 10 PHE A 104 99.17 -6.66
REMARK 500 10 THR A 110 78.86 32.89
REMARK 500 10 ASN A 128 98.95 -177.96
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 111 0.28 SIDE CHAIN
REMARK 500 1 ARG A 115 0.10 SIDE CHAIN
REMARK 500 1 ARG A 121 0.20 SIDE CHAIN
REMARK 500 1 ARG A 124 0.24 SIDE CHAIN
REMARK 500 2 ARG A 102 0.30 SIDE CHAIN
REMARK 500 2 ARG A 111 0.13 SIDE CHAIN
REMARK 500 2 ARG A 115 0.14 SIDE CHAIN
REMARK 500 2 ARG A 124 0.14 SIDE CHAIN
REMARK 500 3 ARG A 102 0.12 SIDE CHAIN
REMARK 500 3 ARG A 111 0.29 SIDE CHAIN
REMARK 500 3 ARG A 115 0.30 SIDE CHAIN
REMARK 500 4 ARG A 102 0.17 SIDE CHAIN
REMARK 500 4 ARG A 111 0.27 SIDE CHAIN
REMARK 500 4 ARG A 115 0.28 SIDE CHAIN
REMARK 500 4 ARG A 121 0.29 SIDE CHAIN
REMARK 500 4 ARG A 124 0.24 SIDE CHAIN
REMARK 500 5 ARG A 102 0.26 SIDE CHAIN
REMARK 500 5 ARG A 115 0.29 SIDE CHAIN
REMARK 500 5 ARG A 124 0.29 SIDE CHAIN
REMARK 500 6 ARG A 102 0.24 SIDE CHAIN
REMARK 500 6 ARG A 111 0.30 SIDE CHAIN
REMARK 500 6 ARG A 115 0.29 SIDE CHAIN
REMARK 500 6 ARG A 121 0.23 SIDE CHAIN
REMARK 500 7 ARG A 111 0.30 SIDE CHAIN
REMARK 500 7 ARG A 115 0.27 SIDE CHAIN
REMARK 500 7 ARG A 121 0.24 SIDE CHAIN
REMARK 500 7 ARG A 124 0.26 SIDE CHAIN
REMARK 500 8 ARG A 102 0.19 SIDE CHAIN
REMARK 500 8 ARG A 111 0.30 SIDE CHAIN
REMARK 500 8 ARG A 121 0.27 SIDE CHAIN
REMARK 500 8 ARG A 124 0.26 SIDE CHAIN
REMARK 500 9 ARG A 102 0.08 SIDE CHAIN
REMARK 500 9 ARG A 111 0.18 SIDE CHAIN
REMARK 500 9 ARG A 115 0.26 SIDE CHAIN
REMARK 500 9 ARG A 124 0.20 SIDE CHAIN
REMARK 500 10 ARG A 111 0.29 SIDE CHAIN
REMARK 500 10 ARG A 115 0.16 SIDE CHAIN
REMARK 500 10 ARG A 121 0.25 SIDE CHAIN
REMARK 500 10 ARG A 124 0.29 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 1 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 106 SG
REMARK 620 2 HIS A 122 NE2 102.2
REMARK 620 3 HIS A 126 NE2 103.0 94.3
REMARK 620 4 CYS A 109 SG 117.6 88.4 137.7
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 1
DBREF 1ARF A 102 130 UNP P07248 ADR1_YEAST 102 130
SEQADV 1ARF TYR A 118 UNP P07248 HIS 118 CONFLICT
SEQRES 1 A 29 ARG SER PHE VAL CYS GLU VAL CYS THR ARG ALA PHE ALA
SEQRES 2 A 29 ARG GLN GLU TYR LEU LYS ARG HIS TYR ARG SER HIS THR
SEQRES 3 A 29 ASN GLU LYS
HET ZN A 1 1
HETNAM ZN ZINC ION
FORMUL 2 ZN ZN 2+
HELIX 1 AAA GLN A 116 HIS A 126 1ALPHA AND 3/10 HELICAL H-BONDS 11
SHEET 1 BBB 2 PHE A 104 CYS A 106 0
SHEET 2 BBB 2 THR A 110 PHE A 113 -1
LINK ZN ZN A 1 SG CYS A 106 1555 1555 2.31
LINK ZN ZN A 1 NE2 HIS A 122 1555 1555 1.99
LINK ZN ZN A 1 NE2 HIS A 126 1555 1555 2.00
LINK ZN ZN A 1 SG CYS A 109 1555 1555 2.28
SITE 1 AC1 5 CYS A 106 VAL A 108 CYS A 109 HIS A 122
SITE 2 AC1 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 - 29 20 Bytes