Header list of 1erg.pdb file
Complete list - 16 20 Bytes
HEADER COMPLEMENT FACTOR 13-DEC-93 1ERG
TITLE THREE-DIMENSIONAL SOLUTION STRUCTURE OF THE EXTRACELLULAR REGION OF
TITLE 2 THE COMPLEMENT REGULATORY PROTEIN, CD59, A NEW CELL SURFACE PROTEIN
TITLE 3 DOMAIN RELATED TO NEUROTOXINS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CD59;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606
KEYWDS COMPLEMENT FACTOR
EXPDTA SOLUTION NMR
AUTHOR B.KIEFFER,P.C.DRISCOLL,I.D.CAMPBELL,A.C.WILLIS,P.A.VAN DER MERWE,
AUTHOR 2 S.J.DAVIS
REVDAT 3 16-FEB-22 1ERG 1 REMARK
REVDAT 2 24-FEB-09 1ERG 1 VERSN
REVDAT 1 30-APR-94 1ERG 0
JRNL AUTH B.KIEFFER,P.C.DRISCOLL,I.D.CAMPBELL,A.C.WILLIS,
JRNL AUTH 2 P.A.VAN DER MERWE,S.J.DAVIS
JRNL TITL THREE-DIMENSIONAL SOLUTION STRUCTURE OF THE EXTRACELLULAR
JRNL TITL 2 REGION OF THE COMPLEMENT REGULATORY PROTEIN CD59, A NEW
JRNL TITL 3 CELL-SURFACE PROTEIN DOMAIN RELATED TO SNAKE VENOM
JRNL TITL 4 NEUROTOXINS.
JRNL REF BIOCHEMISTRY V. 33 4471 1994
JRNL REFN ISSN 0006-2960
JRNL PMID 7512825
JRNL DOI 10.1021/BI00181A006
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1ERG 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_1000173133.
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 : 1
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 PRO A 9 86.80 -56.88
REMARK 500 LYS A 14 32.02 -152.86
REMARK 500 THR A 15 149.04 -32.58
REMARK 500 SER A 20 -99.38 -118.28
REMARK 500 SER A 21 -75.60 73.61
REMARK 500 PHE A 42 -52.18 -17.63
REMARK 500 GLU A 43 39.44 -78.66
REMARK 500 CYS A 45 53.27 -90.77
REMARK 500 ASN A 46 -84.97 -77.34
REMARK 500 PHE A 47 -94.44 -122.59
REMARK 500 ARG A 55 108.39 77.79
REMARK 500 ASN A 57 -96.81 160.25
REMARK 500 LEU A 59 -152.57 -73.76
REMARK 500 THR A 60 72.03 -161.22
REMARK 500 LYS A 65 58.00 -150.84
REMARK 500 LYS A 66 -44.04 -143.95
REMARK 500 ASP A 67 -163.49 -174.65
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: PYB
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1ERH RELATED DB: PDB
DBREF 1ERG A 1 70 UNP P13987 CD59_HUMAN 26 95
SEQRES 1 A 70 LEU GLN CYS TYR ASN CYS PRO ASN PRO THR ALA ASP CYS
SEQRES 2 A 70 LYS THR ALA VAL ASN CYS SER SER ASP PHE ASP ALA CYS
SEQRES 3 A 70 LEU ILE THR LYS ALA GLY LEU GLN VAL TYR ASN LYS CYS
SEQRES 4 A 70 TRP LYS PHE GLU HIS CYS ASN PHE ASN ASP VAL THR THR
SEQRES 5 A 70 ARG LEU ARG GLU ASN GLU LEU THR TYR TYR CYS CYS LYS
SEQRES 6 A 70 LYS ASP LEU CYS ASN
HELIX 1 H1 PHE A 47 LEU A 54 11/5 NOT WELL-DEFINED BY NMR 8
SHEET 1 B1 2 CYS A 3 ASN A 5 0
SHEET 2 B1 2 THR A 15 VAL A 17 -1 O VAL A 17 N CYS A 3
SHEET 1 B2 3 TYR A 36 TRP A 40 0
SHEET 2 B2 3 ALA A 25 LYS A 30 -1 N ALA A 25 O TRP A 40
SHEET 3 B2 3 TYR A 62 CYS A 64 -1 O CYS A 64 N CYS A 26
SSBOND 1 CYS A 3 CYS A 26 1555 1555 2.02
SSBOND 2 CYS A 6 CYS A 13 1555 1555 2.03
SSBOND 3 CYS A 19 CYS A 39 1555 1555 2.02
SSBOND 4 CYS A 45 CYS A 63 1555 1555 2.02
SSBOND 5 CYS A 64 CYS A 69 1555 1555 2.02
SITE 1 PYB 3 THR A 29 PHE A 47 CYS A 69
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 - 16 20 Bytes