Header list of 1s6x.pdb file
Complete list - 2 20 Bytes
HEADER TOXIN 28-JAN-04 1S6X TITLE SOLUTION STRUCTURE OF VSTX COMPND MOL_ID: 1; COMPND 2 MOLECULE: KVAP CHANNEL; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: VSTX, GATING MODIFIER TOXIN; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 SYNTHETIC: YES; SOURCE 3 OTHER_DETAILS: THIS PEPTIDE WAS SYNTHESIZED CHEMICALLY. KEYWDS DOUBLE STRANDED ANTIPARALLEL BETA-SHEET, INHIBITORY CYSTINE KNOT, KEYWDS 2 TOXIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR H.J.JUNG,Y.J.EU,J.I.KIM REVDAT 3 02-MAR-22 1S6X 1 REMARK REVDAT 2 24-FEB-09 1S6X 1 VERSN REVDAT 1 22-MAR-05 1S6X 0 JRNL AUTH H.J.JUNG,J.Y.LEE,S.H.KIM,Y.J.EU,S.Y.SHIN,M.MILESCU, JRNL AUTH 2 K.J.SWARTZ,J.I.KIM JRNL TITL SOLUTION STRUCTURE AND LIPID MEMBRANE PARTITIONING OF VSTX1, JRNL TITL 2 AN INHIBITOR OF THE KVAP POTASSIUM CHANNEL. JRNL REF BIOCHEMISTRY V. 44 6015 2005 JRNL REFN ISSN 0006-2960 JRNL PMID 15835890 JRNL DOI 10.1021/BI0477034 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.851, X-PLOR 3.851 REMARK 3 AUTHORS : BRUNGER (X-PLOR), BRUNGER (X-PLOR) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF REMARK 3 756 RESTRAINTS, 721 ARE NOE DERIVED DISTANCE CONSTRAINTS, 18 REMARK 3 DIHEDRAL ANGLE RESTRAINTS, 8 DISTANCE RESTRAINTS FROM HYDROGEN REMARK 3 BONDS, AND 9 DISTANCE RESTRAINTS FROM DISULFIDE BONDS. REMARK 4 REMARK 4 1S6X COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 29-JAN-04. REMARK 100 THE DEPOSITION ID IS D_1000021443. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 283; 300 REMARK 210 PH : 3.5; 3.5 REMARK 210 IONIC STRENGTH : 0; 0 REMARK 210 PRESSURE : NULL; NULL REMARK 210 SAMPLE CONTENTS : 10MM VSTX; 90% H20, 10% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : PE-COSY; DQF-COSY; 2D NOESY; 2D REMARK 210 TOCSY REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ REMARK 210 SPECTROMETER MODEL : DRX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : XWINNMR 3.0 REMARK 210 METHOD USED : DISTANCE GEOMETRY SIMULATED REMARK 210 ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST REMARK 210 RESTRAINT VIOLATIONS, STRUCTURES REMARK 210 WITH THE LOWEST ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 7 REMARK 210 REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 2D REMARK 210 HOMONUCLEAR 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: 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 PHE A 5 151.90 -44.34 REMARK 500 1 ASN A 11 -35.20 -169.47 REMARK 500 1 SER A 12 -21.45 166.82 REMARK 500 1 TRP A 27 -168.53 175.59 REMARK 500 1 ALA A 31 42.27 -92.38 REMARK 500 2 PHE A 5 152.45 -44.30 REMARK 500 2 MET A 6 -2.55 73.18 REMARK 500 2 ASN A 11 -42.11 -159.97 REMARK 500 2 SER A 12 28.97 171.99 REMARK 500 2 LYS A 17 152.72 -44.86 REMARK 500 2 TRP A 27 -179.87 179.51 REMARK 500 2 LEU A 30 49.96 -63.30 REMARK 500 2 ALA A 31 46.58 18.74 REMARK 500 3 PHE A 5 148.70 -39.45 REMARK 500 3 MET A 6 -2.62 74.93 REMARK 500 3 ASN A 11 -27.80 175.03 REMARK 500 3 SER A 12 -20.40 168.52 REMARK 500 3 TRP A 27 -178.63 175.64 REMARK 500 3 LEU A 30 97.17 -50.28 REMARK 500 3 SER A 32 94.75 66.47 REMARK 500 4 CYS A 2 -161.80 -66.90 REMARK 500 4 ASN A 11 -33.80 179.58 REMARK 500 4 SER A 12 -36.82 169.98 REMARK 500 4 TRP A 27 178.32 176.67 REMARK 500 4 LEU A 30 80.02 -56.37 REMARK 500 4 ALA A 31 59.80 33.80 REMARK 500 5 MET A 6 -9.52 78.19 REMARK 500 5 ASN A 11 -44.39 -165.78 REMARK 500 5 SER A 12 32.87 168.96 REMARK 500 5 ASP A 18 16.65 58.51 REMARK 500 5 TRP A 27 178.45 177.68 REMARK 500 5 ALA A 31 45.38 -85.18 REMARK 500 6 CYS A 2 -157.12 -74.51 REMARK 500 6 MET A 6 -4.00 76.20 REMARK 500 6 ASN A 11 -41.01 -168.65 REMARK 500 6 SER A 12 32.28 172.22 REMARK 500 6 LYS A 17 152.19 -49.52 REMARK 500 6 ASP A 18 16.68 57.02 REMARK 500 6 TRP A 27 175.37 179.64 REMARK 500 6 CYS A 28 92.17 -64.24 REMARK 500 6 ALA A 31 39.20 -88.96 REMARK 500 6 SER A 32 -178.56 50.99 REMARK 500 7 CYS A 2 -160.84 -103.67 REMARK 500 7 PHE A 5 141.81 -38.67 REMARK 500 7 ASN A 11 -29.05 174.64 REMARK 500 7 SER A 12 -23.48 167.24 REMARK 500 7 TRP A 27 179.44 177.81 REMARK 500 7 LEU A 30 104.64 -58.28 REMARK 500 7 ALA A 31 43.22 -94.00 REMARK 500 7 SER A 32 125.57 -179.88 REMARK 500 REMARK 500 THIS ENTRY HAS 148 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 1 ARG A 24 0.26 SIDE CHAIN REMARK 500 2 ARG A 24 0.31 SIDE CHAIN REMARK 500 3 ARG A 24 0.31 SIDE CHAIN REMARK 500 5 ARG A 24 0.27 SIDE CHAIN REMARK 500 6 ARG A 24 0.20 SIDE CHAIN REMARK 500 7 ARG A 24 0.20 SIDE CHAIN REMARK 500 8 ARG A 24 0.18 SIDE CHAIN REMARK 500 9 ARG A 24 0.13 SIDE CHAIN REMARK 500 10 ARG A 24 0.31 SIDE CHAIN REMARK 500 11 ARG A 24 0.31 SIDE CHAIN REMARK 500 12 ARG A 24 0.19 SIDE CHAIN REMARK 500 13 ARG A 24 0.22 SIDE CHAIN REMARK 500 15 ARG A 24 0.31 SIDE CHAIN REMARK 500 16 ARG A 24 0.28 SIDE CHAIN REMARK 500 17 ARG A 24 0.14 SIDE CHAIN REMARK 500 18 ARG A 24 0.18 SIDE CHAIN REMARK 500 19 ARG A 24 0.24 SIDE CHAIN REMARK 500 20 ARG A 24 0.19 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL DBREF 1S6X A 1 34 PDB 1S6X 1S6X 1 34 SEQRES 1 A 34 GLU CYS GLY LYS PHE MET TRP LYS CYS LYS ASN SER ASN SEQRES 2 A 34 ASP CYS CYS LYS ASP LEU VAL CYS SER SER ARG TRP LYS SEQRES 3 A 34 TRP CYS VAL LEU ALA SER PRO PHE SHEET 1 A 2 LEU A 19 SER A 22 0 SHEET 2 A 2 TRP A 27 LEU A 30 -1 O VAL A 29 N VAL A 20 SSBOND 1 CYS A 2 CYS A 16 1555 1555 2.02 SSBOND 2 CYS A 9 CYS A 21 1555 1555 2.02 SSBOND 3 CYS A 15 CYS A 28 1555 1555 2.02 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