Header list of 2pta.pdb file
Complete list - 29 20 Bytes
HEADER NEUROTOXIN 26-NOV-96 2PTA TITLE PANDINUS TOXIN K-A (PITX-KA) FROM PANDINUS IMPERATOR, NMR, 20 TITLE 2 STRUCTURES COMPND MOL_ID: 1; COMPND 2 MOLECULE: PANDINUS TOXIN K-ALPHA; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: COMPLETE PEPTIDE; COMPND 5 SYNONYM: PITX-KA, A-KTX5.1; COMPND 6 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: PANDINUS IMPERATOR; SOURCE 3 ORGANISM_COMMON: EMPEROR SCORPION; SOURCE 4 ORGANISM_TAXID: 55084; SOURCE 5 CELL_LINE: BL21; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3); SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PSR9 KEYWDS NEUROTOXIN, POTASSIUM CHANNEL BLOCKERS, NMR SOLUTION STRUCTURE, KEYWDS 2 ALPHA-K TOXIN FAMILY, SCORPION TOXIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR T.C.TENENHOLZ,R.S.ROGOWSKI,J.H.COLLINS,M.P.BLAUSTEIN,D.J.WEBER REVDAT 3 29-NOV-17 2PTA 1 REMARK HELIX REVDAT 2 24-FEB-09 2PTA 1 VERSN REVDAT 1 10-DEC-97 2PTA 0 JRNL AUTH T.C.TENENHOLZ,R.S.ROGOWSKI,J.H.COLLINS,M.P.BLAUSTEIN, JRNL AUTH 2 D.J.WEBER JRNL TITL SOLUTION STRUCTURE FOR PANDINUS TOXIN K-ALPHA (PITX-K JRNL TITL 2 ALPHA), A SELECTIVE BLOCKER OF A-TYPE POTASSIUM CHANNELS. JRNL REF BIOCHEMISTRY V. 36 2763 1997 JRNL REFN ISSN 0006-2960 JRNL PMID 9062103 JRNL DOI 10.1021/BI9628432 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH R.S.ROGOWSKI,J.H.COLLINS,T.J.O'NEILL,T.A.GUSTAFSON, REMARK 1 AUTH 2 T.R.WERKMAN,M.A.ROGAWSKI,T.C.TENENHOLZ,D.J.WEBER, REMARK 1 AUTH 3 M.P.BLAUSTEIN REMARK 1 TITL THREE NEW TOXINS FROM THE SCORPION PANDINUS IMPERATOR REMARK 1 TITL 2 SELECTIVELY BLOCK CERTAIN VOLTAGE-GATED K+ CHANNELS REMARK 1 REF MOL.PHARMACOL. V. 50 1167 1996 REMARK 1 REFN ISSN 0026-895X REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.1 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: 295 NOE DISTANCE CONSTRAINTS, 9 H REMARK 3 -BONDS, 9 CHI ANGLE CONSTRAINTS. REMARK 4 REMARK 4 2PTA COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL. REMARK 100 THE DEPOSITION ID IS D_1000178507. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 310 REMARK 210 PH : 3.45 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : NULL REMARK 210 SAMPLE CONTENTS : NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; ROESY; TOCSY; DQF-COSY; REMARK 210 AND P.E.COSY REMARK 210 SPECTROMETER FIELD STRENGTH : 600.13 MHZ REMARK 210 SPECTROMETER MODEL : DMX-600 REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : X-PLOR REMARK 210 METHOD USED : DISTANCE GEOMETRY SIMULATED REMARK 210 ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 500 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : NO DISTANCE VIOLATIONS GREATER REMARK 210 THAN 0.30 ANGSTROMS, NO ANGULAR REMARK 210 VIOLATIONS > 5 DEG, TOTAL ENERGY REMARK 210 < 120 KCAL/MOL 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 1 ASN A 25 89.93 -62.11 REMARK 500 1 ASN A 30 90.92 -50.32 REMARK 500 1 PHE A 36 43.70 -96.41 REMARK 500 2 ASN A 30 89.94 -52.33 REMARK 500 3 CYS A 7 100.84 175.95 REMARK 500 3 ASN A 30 52.28 39.40 REMARK 500 3 PHE A 36 79.52 -152.97 REMARK 500 4 ILE A 5 171.09 -56.97 REMARK 500 4 ALA A 26 161.64 174.62 REMARK 500 4 PHE A 36 55.56 -105.60 REMARK 500 5 CYS A 35 150.22 -47.14 REMARK 500 5 PHE A 36 43.00 -96.69 REMARK 500 6 GLU A 20 -64.81 -128.93 REMARK 500 6 ASN A 30 55.45 38.18 REMARK 500 7 PHE A 36 47.42 -88.44 REMARK 500 8 ASN A 30 53.17 38.37 REMARK 500 8 ARG A 31 29.84 83.36 REMARK 500 8 PHE A 36 49.07 -94.51 REMARK 500 9 CYS A 7 -44.67 -164.22 REMARK 500 9 THR A 8 17.22 59.00 REMARK 500 9 GLU A 20 -63.53 -121.49 REMARK 500 9 ASN A 30 71.22 38.88 REMARK 500 9 PHE A 36 45.33 -87.50 REMARK 500 11 ASN A 30 90.36 -47.94 REMARK 500 12 CYS A 7 -43.76 -131.33 REMARK 500 12 ASN A 9 165.32 174.82 REMARK 500 12 ASN A 30 80.73 40.77 REMARK 500 12 PHE A 36 62.77 -119.72 REMARK 500 13 ASN A 25 87.95 -63.98 REMARK 500 13 ASN A 30 45.97 37.82 REMARK 500 13 ARG A 31 40.63 78.48 REMARK 500 14 SER A 6 75.15 -117.04 REMARK 500 14 MET A 29 116.50 -176.17 REMARK 500 14 ASN A 30 59.45 38.67 REMARK 500 14 PHE A 36 55.48 -100.07 REMARK 500 15 CYS A 33 155.42 -49.18 REMARK 500 15 PHE A 36 51.38 -96.24 REMARK 500 16 THR A 21 -50.88 -126.70 REMARK 500 16 ALA A 26 143.80 177.86 REMARK 500 16 ASN A 30 70.48 37.21 REMARK 500 16 PHE A 36 48.84 -87.18 REMARK 500 17 ASN A 30 91.61 -51.43 REMARK 500 17 CYS A 33 138.91 -173.58 REMARK 500 17 PHE A 36 55.01 -106.24 REMARK 500 18 THR A 21 12.03 -142.72 REMARK 500 18 ALA A 26 149.09 -170.49 REMARK 500 18 ARG A 31 31.89 78.39 REMARK 500 18 PHE A 36 47.32 -87.61 REMARK 500 20 ILE A 5 168.32 56.09 REMARK 500 20 ASN A 25 99.04 -58.24 REMARK 500 REMARK 500 THIS ENTRY HAS 51 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 31 0.32 SIDE CHAIN REMARK 500 2 ARG A 31 0.27 SIDE CHAIN REMARK 500 2 ARG A 38 0.32 SIDE CHAIN REMARK 500 3 ARG A 31 0.30 SIDE CHAIN REMARK 500 3 ARG A 38 0.31 SIDE CHAIN REMARK 500 4 ARG A 38 0.27 SIDE CHAIN REMARK 500 5 ARG A 38 0.19 SIDE CHAIN REMARK 500 6 ARG A 31 0.19 SIDE CHAIN REMARK 500 6 ARG A 38 0.28 SIDE CHAIN REMARK 500 7 ARG A 31 0.29 SIDE CHAIN REMARK 500 7 ARG A 38 0.26 SIDE CHAIN REMARK 500 8 ARG A 31 0.09 SIDE CHAIN REMARK 500 8 ARG A 38 0.31 SIDE CHAIN REMARK 500 9 ARG A 31 0.30 SIDE CHAIN REMARK 500 9 ARG A 38 0.12 SIDE CHAIN REMARK 500 10 ARG A 31 0.10 SIDE CHAIN REMARK 500 10 ARG A 38 0.32 SIDE CHAIN REMARK 500 11 ARG A 31 0.26 SIDE CHAIN REMARK 500 11 ARG A 38 0.27 SIDE CHAIN REMARK 500 12 ARG A 31 0.28 SIDE CHAIN REMARK 500 12 ARG A 38 0.25 SIDE CHAIN REMARK 500 13 ARG A 31 0.31 SIDE CHAIN REMARK 500 13 ARG A 38 0.23 SIDE CHAIN REMARK 500 14 ARG A 38 0.29 SIDE CHAIN REMARK 500 15 ARG A 31 0.30 SIDE CHAIN REMARK 500 15 ARG A 38 0.31 SIDE CHAIN REMARK 500 16 ARG A 31 0.13 SIDE CHAIN REMARK 500 16 ARG A 38 0.32 SIDE CHAIN REMARK 500 17 ARG A 31 0.32 SIDE CHAIN REMARK 500 17 ARG A 38 0.30 SIDE CHAIN REMARK 500 18 ARG A 31 0.28 SIDE CHAIN REMARK 500 18 ARG A 38 0.20 SIDE CHAIN REMARK 500 19 ARG A 31 0.30 SIDE CHAIN REMARK 500 19 ARG A 38 0.31 SIDE CHAIN REMARK 500 20 ARG A 31 0.27 SIDE CHAIN REMARK 500 20 ARG A 38 0.20 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL DBREF 2PTA A 4 38 UNP P55927 SCKA_PANIM 13 47 SEQRES 1 A 35 THR ILE SER CYS THR ASN PRO LYS GLN CYS TYR PRO HIS SEQRES 2 A 35 CYS LYS LYS GLU THR GLY TYR PRO ASN ALA LYS CYS MET SEQRES 3 A 35 ASN ARG LYS CYS LYS CYS PHE GLY ARG HELIX 1 H1 LYS A 11 THR A 21 1 11 SHEET 1 A 2 ALA A 26 CYS A 28 0 SHEET 2 A 2 CYS A 33 CYS A 35 -1 O LYS A 34 N LYS A 27 SSBOND 1 CYS A 7 CYS A 28 1555 1555 2.02 SSBOND 2 CYS A 13 CYS A 33 1555 1555 2.02 SSBOND 3 CYS A 17 CYS A 35 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 - 29 20 Bytes