Header list of 1orl.pdb file
Complete list - 25 20 Bytes
HEADER TOXIN 14-MAR-03 1ORL TITLE 1H NMR STRUCTURE DETERMINATION OF VISCOTOXIN C1 COMPND MOL_ID: 1; COMPND 2 MOLECULE: VISCOTOXIN C1; COMPND 3 CHAIN: A SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: VISCUM ALBUM; SOURCE 3 ORGANISM_COMMON: EUROPEAN MISTLETOE; SOURCE 4 ORGANISM_TAXID: 3972; SOURCE 5 OTHER_DETAILS: VISCOTOXIN C1 HAS BEEN ISOLATED FROM EUROPEAN SOURCE 6 MISTLETOE LEAVES KEYWDS HELIX-TURN-HELIX, BETA-SHEET, CONCENTRIC MOTIF OF DISULPHIDE BRIDGES, KEYWDS 2 TOXIN EXPDTA SOLUTION NMR NUMMDL 10 AUTHOR H.MOLINARI,S.ROMAGNOLI,F.FOGOLARI,M.CATALANO,K.URECH,M.GIANNATTASIO, AUTHOR 2 L.RAGONA REVDAT 4 20-OCT-10 1ORL 1 REMARK REVDAT 3 24-FEB-09 1ORL 1 VERSN REVDAT 2 21-SEP-04 1ORL 1 JRNL REVDAT 1 01-APR-03 1ORL 0 JRNL AUTH S.ROMAGNOLI,F.FOGOLARI,M.CATALANO,L.ZETTA,G.SCHALLER, JRNL AUTH 2 K.URECH,M.GIANNATTASIO,L.RAGONA,H.MOLINARI JRNL TITL NMR SOLUTION STRUCTURE OF VISCOTOXIN C1 FROM VISCUM ALBUM JRNL TITL 2 SPECIES COLORATUM OHWI: TOWARD A STRUCTURE-FUNCTION ANALYSIS JRNL TITL 3 OF VISCOTOXINS. JRNL REF BIOCHEMISTRY V. 42 12503 2003 JRNL REFN ISSN 0006-2960 JRNL PMID 14580196 JRNL DOI 10.1021/BI034762T REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH H.MOLINARI,S.ROMAGNOLI,F.FOGOLARI,M.CATALANO,K.URECH, REMARK 1 AUTH 2 M.GIANNATTASIO,L.RAGONA REMARK 1 TITL NMR STRUCTURAL DETERMINATION OF VISCOTOXIN A3 FROM VISCUM REMARK 1 TITL 2 ALBUM L. REMARK 1 REF BIOCHEM.J. V. 350 569 2000 REMARK 1 REFN ISSN 0264-6021 REMARK 1 DOI 10.1042/0264-6021:3500569 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : DISCOVER 1997 VERSION REMARK 3 AUTHORS : MOLECULAR SIMULATIONS, SAN DIEGO, CA, USA REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF REMARK 3 691 RESTRAINTS. 631 ARE NOE-DERIVED DISTANCE RESTRAINTS, REMARK 3 (224INTRARESIDUES,159 SHORT RANGE, 125 MEDIUM RANGE AND 123 LONG REMARK 3 RANGE), 18 DIHEDRAL ANGLE RESTRAINTS, 24 FOR BACKBONE H-BONDS AND REMARK 3 18 FOR DISULPHIDE BRIDGES. BOND LENGTHS CD-OE2 IN GLUTAMIC ACID REMARK 3 RESIDUES AND CG-OD2 IN ASPARTIC ACID RESIDUES ARE LARGER THAN REMARK 3 TYPICAL VALUES (AS SEEN IN REMARK 500) BECAUSE PROTONATED FORMS REMARK 3 WERE CONSIDERED DUE TO THE LOW EXPERIMENTAL PH. REMARK 4 REMARK 4 1ORL COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-MAR-03. REMARK 100 THE RCSB ID CODE IS RCSB018597. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 285; 295; 285 REMARK 210 PH : 3.6; 3.6; 3.6 REMARK 210 IONIC STRENGTH : 50MM PHOSPHATE BUFFER; 50MM REMARK 210 PHOSPHATE BUFFER; 50MM DEUTERATED REMARK 210 PHOSPHATE BUFFER REMARK 210 PRESSURE : AMBIENT; AMBIENT; AMBIENT REMARK 210 SAMPLE CONTENTS : 0.7 MM VISCOTOXIN B; PHOSPHATE REMARK 210 BUFFER PH 3.6 50MM; 90%H20, 10% REMARK 210 D2O; 0.7 MM VISCOTOXIN B; REMARK 210 PHOSPHATE BUFFER PH 3.6 50MM; D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D TOCSY; 2D NOESY; DQF-COSY REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ REMARK 210 SPECTROMETER MODEL : DRX; DMX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : DYANA 1.4, DISCOVER 1997 REMARK 210 VERSION, XWINNMR 2.6, XEASY 1.3 REMARK 210 METHOD USED : DYANA WAS EMPLOYED FOR STRUCTURE REMARK 210 DETERMINATION DISCOVER WAS REMARK 210 EMPLOYED FOR ENERGY MINIMISATION REMARK 210 OF DYANA STRUCTURES REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 600 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 1H 2D NMR REMARK 210 TECHNIQUES 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 LENGTHS 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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) 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 RES CSSEQI ATM2 DEVIATION REMARK 500 1 GLU A 24 CD GLU A 24 OE2 0.111 REMARK 500 2 GLU A 24 CD GLU A 24 OE2 0.110 REMARK 500 3 GLU A 24 CD GLU A 24 OE2 0.113 REMARK 500 4 GLU A 24 CD GLU A 24 OE2 0.110 REMARK 500 5 GLU A 24 CD GLU A 24 OE2 0.111 REMARK 500 6 GLU A 24 CD GLU A 24 OE2 0.113 REMARK 500 7 GLU A 24 CD GLU A 24 OE2 0.111 REMARK 500 8 GLU A 24 CD GLU A 24 OE2 0.113 REMARK 500 9 GLU A 24 CD GLU A 24 OE2 0.112 REMARK 500 10 GLU A 24 CD GLU A 24 OE2 0.112 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 38 -35.28 74.59 REMARK 500 1 ASP A 43 -34.69 -155.40 REMARK 500 1 TYR A 44 74.47 -116.91 REMARK 500 2 SER A 2 98.04 60.49 REMARK 500 2 SER A 36 30.55 -93.02 REMARK 500 2 ASP A 43 19.12 -146.83 REMARK 500 2 PRO A 45 40.52 -89.06 REMARK 500 4 SER A 2 128.23 70.03 REMARK 500 4 SER A 36 30.10 -99.42 REMARK 500 4 ASP A 43 -42.19 -171.02 REMARK 500 4 TYR A 44 78.24 -114.94 REMARK 500 5 SER A 2 119.43 64.70 REMARK 500 5 SER A 36 33.12 -96.37 REMARK 500 5 ASP A 43 -39.72 -149.10 REMARK 500 6 ASP A 43 -38.26 -143.73 REMARK 500 7 ASP A 43 -37.31 -145.87 REMARK 500 8 SER A 2 102.24 67.35 REMARK 500 8 SER A 36 35.21 -97.31 REMARK 500 8 ASP A 43 -29.67 -149.69 REMARK 500 9 SER A 36 34.26 -93.07 REMARK 500 9 ASP A 43 -36.15 -152.63 REMARK 500 10 SER A 36 43.09 -91.85 REMARK 500 10 SER A 42 -64.99 -22.93 REMARK 500 10 ASP A 43 83.98 -150.16 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1ED0 RELATED DB: PDB REMARK 900 STRUCTURE OF VISCOTOXIN A3 ISOFORM, FROM VISCUM ALBUM REMARK 999 REMARK 999 SEQUENCE REMARK 999 THE AUTHOR INDICATED THAT THE REMARK 999 PRIMARY SEQUENCE FOR THIS REMARK 999 PROTEIN HAS NOT YET BEEN REMARK 999 DEPOSITED IN ANY SEQUENCE REMARK 999 DATABASE. DBREF 1ORL A 1 46 UNP P08943 THNB_VISAL 7 52 SEQRES 1 A 46 LYS SER CYS CYS PRO ASN THR THR GLY ARG ASN ILE TYR SEQRES 2 A 46 ASN THR CYS ARG PHE ALA GLY GLY SER ARG GLU ARG CYS SEQRES 3 A 46 ALA LYS LEU SER GLY CYS LYS ILE ILE SER ALA SER THR SEQRES 4 A 46 CYS PRO SER ASP TYR PRO LYS HELIX 1 1 ASN A 6 GLY A 20 1 15 HELIX 2 2 SER A 22 GLY A 31 1 10 SHEET 1 A 2 SER A 2 CYS A 3 0 SHEET 2 A 2 LYS A 33 ILE A 34 -1 O LYS A 33 N CYS A 3 SSBOND 1 CYS A 3 CYS A 40 1555 1555 2.03 SSBOND 2 CYS A 4 CYS A 32 1555 1555 2.04 SSBOND 3 CYS A 16 CYS A 26 1555 1555 2.04 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 - 25 20 Bytes