Header list of 1znf.pdb file
Complete list - v 29 2 Bytes
HEADER ZINC FINGER DNA BINDING DOMAIN 25-SEP-89 1ZNF
TITLE THREE-DIMENSIONAL SOLUTION STRUCTURE OF A SINGLE ZINC FINGER DNA-
TITLE 2 BINDING DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 31ST ZINC FINGER FROM XFIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: XENOPUS LAEVIS;
SOURCE 3 ORGANISM_COMMON: AFRICAN CLAWED FROG;
SOURCE 4 ORGANISM_TAXID: 8355
KEYWDS ZINC FINGER DNA BINDING DOMAIN
EXPDTA SOLUTION NMR
NUMMDL 37
AUTHOR M.S.LEE,G.P.GIPPERT,K.V.SOMAN,D.A.CASE,P.E.WRIGHT
REVDAT 4 29-NOV-17 1ZNF 1 REMARK HELIX
REVDAT 3 24-FEB-09 1ZNF 1 VERSN
REVDAT 2 15-OCT-91 1ZNF 3 COMPND HETATM
REVDAT 1 15-JUL-91 1ZNF 0
JRNL AUTH M.S.LEE,G.P.GIPPERT,K.V.SOMAN,D.A.CASE,P.E.WRIGHT
JRNL TITL THREE-DIMENSIONAL SOLUTION STRUCTURE OF A SINGLE ZINC FINGER
JRNL TITL 2 DNA-BINDING DOMAIN.
JRNL REF SCIENCE V. 245 635 1989
JRNL REFN ISSN 0036-8075
JRNL PMID 2503871
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.S.LEE,G.P.GIPPERT,K.V.SOMAN,D.A.CASE,P.E.WRIGHT
REMARK 1 TITL PROTON NUCLEAR MAGNETIC RESONANCE ASSIGNMENTS AND SOLUTION
REMARK 1 TITL 2 STRUCTURE OF A SYNTHETIC ZINC FINGER FROM XFIN
REMARK 1 EDIT R.H.SARMA, M.H.SARMA
REMARK 1 REF STRUCTURE AND METHODS. V. 2. 83 1990
REMARK 1 REF 2 DNA PROTEIN COMPLEXES AND
REMARK 1 REF 3 PROTEINS
REMARK 1 PUBL ADENINE PRESS, ALBANY, NEW YORK
REMARK 1 REFN
REMARK 1 REFERENCE 2
REMARK 1 AUTH M.S.LEE,J.CAVANAGH,P.E.WRIGHT
REMARK 1 TITL COMPLETE ASSIGNMENT OF THE 1H NUCLEAR MAGNETIC RESONANCE
REMARK 1 TITL 2 SPECTRUM OF A SYNTHETIC ZINC FINGER FROM XFIN. SEQUENTIAL
REMARK 1 TITL 3 RESONANCE ASSIGNMENTS AND SECONDARY STRUCTURE
REMARK 1 REF FEBS LETT. V. 254 159 1989
REMARK 1 REFN ISSN 0014-5793
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : AMBER
REMARK 3 AUTHORS : HAVEL,WUTHRICH (DISGEO),
REMARK 3 PEARLMAN,CASE,CALDWELL,SIEBEL,SINGH,WEINER,KOLLMAN
REMARK 3 (AMBER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1ZNF 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_1000177494.
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 : 37
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: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 4 CYS A 6 CA - CB - SG ANGL. DEV. = 7.0 DEGREES
REMARK 500 23 CYS A 6 CA - CB - SG ANGL. DEV. = 8.8 DEGREES
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 GLU A 7 25.73 38.59
REMARK 500 1 HIS A 23 -48.57 -133.16
REMARK 500 2 CYS A 6 18.54 -159.41
REMARK 500 2 GLU A 7 34.16 33.46
REMARK 500 3 CYS A 6 19.08 -156.82
REMARK 500 3 GLU A 7 41.54 31.04
REMARK 500 4 CYS A 6 -99.51 -155.01
REMARK 500 4 GLU A 7 -125.25 -164.52
REMARK 500 4 ARG A 8 119.67 60.76
REMARK 500 4 VAL A 11 -32.57 70.60
REMARK 500 5 LYS A 24 52.51 32.51
REMARK 500 6 CYS A 6 105.04 -165.64
REMARK 500 6 GLU A 7 58.01 -67.92
REMARK 500 6 HIS A 23 82.56 -154.24
REMARK 500 7 CYS A 6 15.12 -154.92
REMARK 500 7 GLU A 7 17.25 43.72
REMARK 500 8 GLU A 7 59.27 -70.00
REMARK 500 8 HIS A 23 74.54 -158.03
REMARK 500 10 GLU A 7 49.96 -72.06
REMARK 500 11 GLU A 7 59.07 -55.46
REMARK 500 11 ARG A 21 -37.79 -36.02
REMARK 500 12 LYS A 24 71.72 -68.32
REMARK 500 13 CYS A 6 93.25 -165.02
REMARK 500 13 GLU A 7 61.16 -65.84
REMARK 500 13 HIS A 23 -49.10 72.41
REMARK 500 14 CYS A 6 -175.28 -171.47
REMARK 500 14 VAL A 11 -7.71 57.30
REMARK 500 15 GLN A 20 1.71 -64.17
REMARK 500 15 HIS A 23 -61.70 72.24
REMARK 500 16 VAL A 11 -0.90 53.34
REMARK 500 16 GLN A 20 -9.76 -55.84
REMARK 500 17 CYS A 6 -19.65 -163.67
REMARK 500 17 GLU A 7 55.40 38.73
REMARK 500 17 VAL A 11 -23.67 61.87
REMARK 500 17 LYS A 24 112.69 91.03
REMARK 500 18 CYS A 6 21.38 -159.45
REMARK 500 18 GLU A 7 23.51 35.34
REMARK 500 19 CYS A 6 10.56 -151.52
REMARK 500 19 GLU A 7 19.05 45.98
REMARK 500 19 GLN A 20 0.69 -63.08
REMARK 500 19 HIS A 23 -58.64 73.20
REMARK 500 20 CYS A 6 30.54 -152.44
REMARK 500 20 GLU A 7 19.57 21.76
REMARK 500 20 LYS A 24 65.68 -64.61
REMARK 500 21 CYS A 6 18.79 -154.67
REMARK 500 21 GLU A 7 34.21 36.76
REMARK 500 21 VAL A 11 -36.44 72.58
REMARK 500 21 HIS A 23 -55.30 -123.25
REMARK 500 21 LYS A 24 34.74 39.55
REMARK 500 22 CYS A 6 20.86 -152.99
REMARK 500
REMARK 500 THIS ENTRY HAS 102 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 PHE A 10 0.09 SIDE CHAIN
REMARK 500 2 PHE A 10 0.13 SIDE CHAIN
REMARK 500 3 PHE A 10 0.08 SIDE CHAIN
REMARK 500 7 PHE A 10 0.08 SIDE CHAIN
REMARK 500 9 PHE A 10 0.08 SIDE CHAIN
REMARK 500 10 TYR A 1 0.07 SIDE CHAIN
REMARK 500 11 HIS A 19 0.10 SIDE CHAIN
REMARK 500 15 PHE A 10 0.09 SIDE CHAIN
REMARK 500 17 TYR A 1 0.09 SIDE CHAIN
REMARK 500 21 PHE A 10 0.10 SIDE CHAIN
REMARK 500 27 PHE A 10 0.10 SIDE CHAIN
REMARK 500 32 PHE A 10 0.09 SIDE CHAIN
REMARK 500 33 PHE A 10 0.08 SIDE CHAIN
REMARK 500 34 HIS A 19 0.09 SIDE CHAIN
REMARK 500 37 TYR A 1 0.08 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 27 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 6 SG
REMARK 620 2 HIS A 19 NE2 102.1
REMARK 620 3 CYS A 3 SG 113.8 110.9
REMARK 620 4 HIS A 23 NE2 119.7 105.1 104.9
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 27
DBREF 1ZNF A 1 25 UNP P08045 XFIN_XENLA 1044 1068
SEQRES 1 A 27 ACE TYR LYS CYS GLY LEU CYS GLU ARG SER PHE VAL GLU
SEQRES 2 A 27 LYS SER ALA LEU SER ARG HIS GLN ARG VAL HIS LYS ASN
SEQRES 3 A 27 NH2
HET ACE A 0 6
HET NH2 A 26 3
HET ZN A 27 1
HETNAM ACE ACETYL GROUP
HETNAM NH2 AMINO GROUP
HETNAM ZN ZINC ION
FORMUL 1 ACE C2 H4 O
FORMUL 1 NH2 H2 N
FORMUL 2 ZN ZN 2+
HELIX 1 1H GLU A 12 LYS A 24 1 13
SHEET 1 S1 2 TYR A 1 GLY A 4 0
SHEET 2 S1 2 GLU A 7 PHE A 10 -1 N PHE A 10 O TYR A 1
LINK C ACE A 0 N TYR A 1 1555 1555 1.33
LINK C ASN A 25 N NH2 A 26 1555 1555 1.33
LINK ZN ZN A 27 SG CYS A 6 1555 1555 2.31
LINK ZN ZN A 27 NE2 HIS A 19 1555 1555 1.95
LINK ZN ZN A 27 SG CYS A 3 1555 1555 2.29
LINK ZN ZN A 27 NE2 HIS A 23 1555 1555 1.99
SITE 1 AC1 4 CYS A 3 CYS A 6 HIS A 19 HIS A 23
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 29 2 Bytes