Header list of 1zfo.pdb file
Complete list - 2 20 Bytes
HEADER METAL BINDING PROTEIN 06-MAY-96 1ZFO
TITLE AMINO-TERMINAL LIM-DOMAIN PEPTIDE OF LASP-1, NMR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LASP-1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: ZF-1 AMINO-TERMINAL LIM-DOMAIN PEPTIDE;
COMPND 5 ENGINEERED: YES;
COMPND 6 OTHER_DETAILS: IDENTICAL TO 30 N-TERMINAL RESIDUES OF HUMAN LASP-1
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SUS SCROFA;
SOURCE 3 ORGANISM_COMMON: PIG;
SOURCE 4 ORGANISM_TAXID: 9823;
SOURCE 5 ORGAN: INTESTINE
KEYWDS LIM DOMAIN, ZINC-FINGER, METAL-BINDING PROTEIN, METAL BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR A.HAMMARSTROM,K.D.BERNDT,R.SILLARD,K.ADERMANN,G.OTTING
REVDAT 3 02-MAR-22 1ZFO 1 KEYWDS REMARK LINK
REVDAT 2 24-FEB-09 1ZFO 1 VERSN
REVDAT 1 08-NOV-96 1ZFO 0
JRNL AUTH A.HAMMARSTROM,K.D.BERNDT,R.SILLARD,K.ADERMANN,G.OTTING
JRNL TITL SOLUTION STRUCTURE OF A NATURALLY-OCCURRING ZINC-PEPTIDE
JRNL TITL 2 COMPLEX DEMONSTRATES THAT THE N-TERMINAL ZINC-BINDING MODULE
JRNL TITL 3 OF THE LASP-1 LIM DOMAIN IS AN INDEPENDENT FOLDING UNIT.
JRNL REF BIOCHEMISTRY V. 35 12723 1996
JRNL REFN ISSN 0006-2960
JRNL PMID 8841116
JRNL DOI 10.1021/BI961149J
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : OPAL
REMARK 3 AUTHORS : LUGINBUHL,GUNTERT,BILLETER,WUTHRICH
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1ZFO 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_1000177473.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
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 : 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 : 20
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: 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 ARG A 7 -57.49 -122.55
REMARK 500 1 LYS A 17 79.96 -68.40
REMARK 500 1 ASP A 22 -1.17 -154.84
REMARK 500 2 ARG A 7 -54.96 -126.56
REMARK 500 2 LYS A 17 97.96 -20.89
REMARK 500 2 CYS A 20 -155.33 -144.48
REMARK 500 2 LEU A 21 -72.27 -46.25
REMARK 500 2 ASP A 22 16.18 -151.68
REMARK 500 3 ALA A 6 6.76 -69.49
REMARK 500 3 ARG A 7 -70.60 -94.27
REMARK 500 3 GLU A 16 50.01 -141.83
REMARK 500 3 LEU A 21 179.10 165.58
REMARK 500 4 GLU A 16 45.21 -144.33
REMARK 500 4 CYS A 20 25.90 -141.65
REMARK 500 4 LEU A 21 -95.19 -150.95
REMARK 500 4 ASP A 22 4.71 -151.56
REMARK 500 5 ARG A 7 -67.80 -95.33
REMARK 500 5 GLU A 16 -73.51 -105.94
REMARK 500 5 LYS A 17 74.53 23.90
REMARK 500 5 LEU A 21 -152.98 -151.59
REMARK 500 6 ARG A 7 -69.63 -93.83
REMARK 500 6 LYS A 17 95.87 -47.49
REMARK 500 6 CYS A 20 -143.79 -150.30
REMARK 500 6 LEU A 21 -73.92 -44.84
REMARK 500 6 ASP A 22 22.18 -155.91
REMARK 500 7 ARG A 7 -69.24 -95.12
REMARK 500 8 THR A 15 -72.96 -144.96
REMARK 500 8 LYS A 17 97.55 -52.33
REMARK 500 8 CYS A 20 24.21 -154.42
REMARK 500 8 LEU A 21 174.82 158.57
REMARK 500 9 THR A 15 -23.27 173.93
REMARK 500 9 TRP A 25 -158.00 -136.54
REMARK 500 10 PRO A 3 173.32 -59.79
REMARK 500 10 ARG A 7 -66.98 -94.62
REMARK 500 10 LYS A 17 93.25 -53.43
REMARK 500 10 LEU A 21 -95.85 -152.54
REMARK 500 10 LYS A 27 -71.06 -34.05
REMARK 500 11 THR A 15 -65.36 173.79
REMARK 500 11 LYS A 17 64.44 -42.33
REMARK 500 11 VAL A 18 107.18 -53.59
REMARK 500 11 LEU A 21 -91.39 -149.61
REMARK 500 12 ALA A 6 6.17 -63.80
REMARK 500 13 LYS A 17 106.00 -51.77
REMARK 500 13 LEU A 21 -156.67 -165.22
REMARK 500 13 ASP A 22 43.94 -83.71
REMARK 500 13 LYS A 27 -70.28 -37.62
REMARK 500 14 LYS A 17 110.97 -35.65
REMARK 500 14 CYS A 20 -158.76 -145.70
REMARK 500 14 LEU A 21 -72.25 -34.39
REMARK 500 15 ARG A 7 -68.55 -94.16
REMARK 500
REMARK 500 THIS ENTRY HAS 74 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 6 ARG A 7 0.11 SIDE CHAIN
REMARK 500 19 ARG A 7 0.11 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 31 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 5 SG
REMARK 620 2 CYS A 8 SG 97.5
REMARK 620 3 HIS A 26 ND1 110.0 104.6
REMARK 620 4 CYS A 29 SG 110.0 113.6 119.0
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 31
DBREF 1ZFO A 1 30 UNP P80171 LASP1_PIG 1 30
SEQRES 1 A 31 ACE MET ASN PRO ASN CYS ALA ARG CYS GLY LYS ILE VAL
SEQRES 2 A 31 TYR PRO THR GLU LYS VAL ASN CYS LEU ASP LYS PHE TRP
SEQRES 3 A 31 HIS LYS ALA CYS PHE
HET ACE A 0 6
HET ZN A 31 1
HETNAM ACE ACETYL GROUP
HETNAM ZN ZINC ION
FORMUL 1 ACE C2 H4 O
FORMUL 2 ZN ZN 2+
HELIX 1 1 TYR A 13 LYS A 17 5 5
HELIX 2 2 HIS A 26 PHE A 30 5 5
SHEET 1 S1 2 LYS A 10 VAL A 12 0
SHEET 2 S1 2 PRO A 3 ALA A 6 -1 N CYS A 5 O LYS A 10
SHEET 1 S2 2 PHE A 24 HIS A 26 0
SHEET 2 S2 2 LYS A 17 VAL A 18 1 N VAL A 18 O TRP A 25
LINK C ACE A 0 N MET A 1 1555 1555 1.34
LINK SG CYS A 5 ZN ZN A 31 1555 1555 2.30
LINK SG CYS A 8 ZN ZN A 31 1555 1555 2.28
LINK ND1 HIS A 26 ZN ZN A 31 1555 1555 1.98
LINK SG CYS A 29 ZN ZN A 31 1555 1555 2.32
SITE 1 AC1 4 CYS A 5 CYS A 8 HIS A 26 CYS A 29
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 - 2 20 Bytes