Header list of 1xsw.pdb file
Complete list - 2 20 Bytes
HEADER TOXIN 20-OCT-04 1XSW
TITLE THE SOLID-STATE NMR STRUCTURE OF KALIOTOXIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: KALIOTOXIN 1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: KTX 1, ALPHA-KTX 3.1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ANDROCTONUS MAURETANICUS MAURETANICUS;
SOURCE 3 ORGANISM_TAXID: 6860;
SOURCE 4 STRAIN: MAURETANICUS;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS TOXIN
EXPDTA SOLID-STATE NMR
NUMMDL 10
AUTHOR A.LANGE,S.BECKER,K.SEIDEL,K.GILLER,O.PONGS,M.BALDUS
REVDAT 3 02-MAR-22 1XSW 1 REMARK
REVDAT 2 24-FEB-09 1XSW 1 VERSN
REVDAT 1 05-APR-05 1XSW 0
JRNL AUTH A.LANGE,S.BECKER,K.SEIDEL,K.GILLER,O.PONGS,M.BALDUS
JRNL TITL A CONCEPT FOR RAPID PROTEIN-STRUCTURE DETERMINATION BY
JRNL TITL 2 SOLID-STATE NMR SPECTROSCOPY
JRNL REF ANGEW.CHEM.INT.ED.ENGL. V. 44 2089 2005
JRNL REFN ESSN 0570-0833
JRNL PMID 15744789
JRNL DOI 10.1002/ANIE.200462516
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE
REMARK 3 -KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,READ,RICE,
REMARK 3 SIMONSON,WARREN
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1XSW COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 25-OCT-04.
REMARK 100 THE DEPOSITION ID IS D_1000030729.
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 : 800 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 2
REMARK 210
REMARK 210 REMARK: NULL
REMARK 217
REMARK 217 SOLID STATE NMR STUDY
REMARK 217 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLID
REMARK 217 STATE NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 217 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 217 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: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
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 ASP A 20 -64.90 -133.92
REMARK 500 1 PHE A 25 153.55 77.05
REMARK 500 1 LYS A 27 101.92 61.53
REMARK 500 2 ASP A 20 -71.12 -163.67
REMARK 500 2 ASN A 30 105.52 -46.27
REMARK 500 3 PHE A 25 -77.83 63.16
REMARK 500 3 LYS A 27 138.31 62.05
REMARK 500 3 ASN A 30 -81.66 59.50
REMARK 500 3 ARG A 31 33.19 -158.95
REMARK 500 4 LYS A 19 -167.82 63.60
REMARK 500 4 PHE A 25 -87.18 55.03
REMARK 500 4 ASN A 30 95.41 -42.99
REMARK 500 5 LYS A 19 -163.58 56.21
REMARK 500 5 ASP A 20 57.29 -96.69
REMARK 500 5 PHE A 25 91.34 41.66
REMARK 500 5 ASN A 30 -72.57 67.95
REMARK 500 5 ARG A 31 44.11 176.80
REMARK 500 6 ASP A 20 -51.76 -177.12
REMARK 500 6 MET A 23 -163.25 -71.51
REMARK 500 6 PHE A 25 -106.96 -55.00
REMARK 500 6 LYS A 27 119.42 62.60
REMARK 500 6 ASN A 30 76.81 -56.76
REMARK 500 6 ARG A 31 -66.09 178.97
REMARK 500 7 ASP A 20 -87.92 -144.63
REMARK 500 7 PHE A 25 134.08 83.39
REMARK 500 7 LYS A 27 174.46 -50.79
REMARK 500 7 ASN A 30 73.88 -63.70
REMARK 500 7 ARG A 31 -61.73 171.26
REMARK 500 8 LYS A 19 78.06 -65.45
REMARK 500 8 ASP A 20 -68.63 -152.62
REMARK 500 8 PHE A 25 -72.25 175.26
REMARK 500 8 ASN A 30 -84.76 56.63
REMARK 500 8 ARG A 31 29.05 -146.16
REMARK 500 9 PHE A 25 -80.87 -148.64
REMARK 500 9 LYS A 27 119.90 -177.25
REMARK 500 9 ASN A 30 61.09 -66.70
REMARK 500 9 ARG A 31 -40.31 179.27
REMARK 500 10 LYS A 19 147.57 61.59
REMARK 500 10 MET A 23 -169.40 -104.44
REMARK 500 10 LYS A 27 -178.23 -179.19
REMARK 500 10 ASN A 30 -89.43 42.71
REMARK 500 10 ARG A 31 41.02 -140.48
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2KTX RELATED DB: PDB
REMARK 900 THE SOLUTION-STATE NMR STRUCTURE OF KALIOTOXIN
REMARK 900 RELATED ID: 6351 RELATED DB: BMRB
REMARK 900 13C, 15N SOLID-STATE CHEMICAL SHIFT ASSIGNMENTS FOR KALIOTOXIN
DBREF 1XSW A 1 38 UNP P24662 SCK1_ANDMA 1 38
SEQRES 1 A 38 GLY VAL GLU ILE ASN VAL LYS CYS SER GLY SER PRO GLN
SEQRES 2 A 38 CYS LEU LYS PRO CYS LYS ASP ALA GLY MET ARG PHE GLY
SEQRES 3 A 38 LYS CYS MET ASN ARG LYS CYS HIS CYS THR PRO LYS
HELIX 1 1 GLY A 10 CYS A 14 5 5
SSBOND 1 CYS A 8 CYS A 28 1555 1555 2.03
SSBOND 2 CYS A 14 CYS A 33 1555 1555 2.03
SSBOND 3 CYS A 18 CYS A 35 1555 1555 2.03
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