Header list of 1zdd.pdb file
Complete list - 2 202 Bytes
HEADER IGG BINDING DOMAIN 09-JUL-97 1ZDD
TITLE DISULFIDE-STABILIZED MINI PROTEIN A DOMAIN, Z34C, NMR, MINIMIZED MEAN
TITLE 2 STRUCTURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: STABLE MINI PROTEIN A DOMAIN, Z34C;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 OTHER_DETAILS: STABLE, TWO-HELIX, IGG-BINDING VARIANT OF PROTEIN A
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 3 ORGANISM_TAXID: 32630
KEYWDS IGG BINDING DOMAIN, PROTEIN A MIMIC
EXPDTA SOLUTION NMR
AUTHOR M.A.STAROVASNIK
REVDAT 3 02-MAR-22 1ZDD 1 REMARK LINK
REVDAT 2 24-FEB-09 1ZDD 1 VERSN
REVDAT 1 17-SEP-97 1ZDD 0
JRNL AUTH M.A.STAROVASNIK,A.C.BRAISTED,J.A.WELLS
JRNL TITL STRUCTURAL MIMICRY OF A NATIVE PROTEIN BY A MINIMIZED
JRNL TITL 2 BINDING DOMAIN.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 94 10080 1997
JRNL REFN ISSN 0027-8424
JRNL PMID 9294166
JRNL DOI 10.1073/PNAS.94.19.10080
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : AMBER
REMARK 3 AUTHORS : HAVEL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1ZDD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000177462.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 281
REMARK 210 PH : 5.1
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : IN H2O: NOESY; TOCSY; COSY; IN
REMARK 210 D2O: NOESY; COSY-35; 2Q
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : AMX500
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DGII, DISCOVER
REMARK 210 METHOD USED : METRIX MATRIX DISTANCE GEOMETRY
REMARK 210 FOLLOWED BY RESTRAINED MOLECULAR
REMARK 210 DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 48
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST RESTRAINT VIOLATION
REMARK 210 ENERGY
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 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NH2 A 40
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1ZDC RELATED DB: PDB
DBREF 1ZDD A 6 40 PDB 1ZDD 1ZDD 6 40
SEQRES 1 A 35 PHE ASN MET GLN CYS GLN ARG ARG PHE TYR GLU ALA LEU
SEQRES 2 A 35 HIS ASP PRO ASN LEU ASN GLU GLU GLN ARG ASN ALA LYS
SEQRES 3 A 35 ILE LYS SER ILE ARG ASP ASP CYS NH2
HET NH2 A 40 3
HETNAM NH2 AMINO GROUP
FORMUL 1 NH2 H2 N
HELIX 1 H1 MET A 8 LEU A 18 1 11
HELIX 2 H2 GLU A 25 CYS A 39 1 15
SSBOND 1 CYS A 10 CYS A 39 1555 1555 2.05
LINK C CYS A 39 N NH2 A 40 1555 1555 1.33
SITE 1 AC1 2 ARG A 36 CYS A 39
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
Complete list - 2 202 Bytes