Header list of 1wmt.pdb file
Complete list - r 2 2 Bytes
HEADER TOXIN 20-JUL-04 1WMT TITLE SCORPION TOXIN (ISTX) FROM OPISTHACANTHUS MADAGASCARIENSIS COMPND MOL_ID: 1; COMPND 2 MOLECULE: ISTX; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 SYNTHETIC: YES; SOURCE 3 OTHER_DETAILS: THIS PEPTIDE WAS CHEMICALLY SYNTHESIZED. THE SEQUENCE SOURCE 4 OF THIS PEPTIDE NATURALLY OCCURS IN OPISTHACANTHUS MADAGASCARIENSIS. KEYWDS NEUROTOXIN, POTASSIUM CHANNEL BLOCKER, NMR SOLUTION STRUCTURE, ALPHA- KEYWDS 2 K TOXIN FAMILY, SCORPION TOXIN, TOXIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR N.YAMAJI,L.DAI,K.SUGASE,M.ANDRIANTSIFERANA,T.NAKAJIMA,T.IWASHITA REVDAT 3 02-MAR-22 1WMT 1 REMARK REVDAT 2 24-FEB-09 1WMT 1 VERSN REVDAT 1 19-OCT-04 1WMT 0 JRNL AUTH N.YAMAJI,L.DAI,K.SUGASE,M.ANDRIANTSIFERANA,T.NAKAJIMA, JRNL AUTH 2 T.IWASHITA JRNL TITL SOLUTION STRUCTURE OF ISTX: A MALE SCORPION TOXIN FROM JRNL TITL 2 OPISTHACANTHUS MADAGASCARIENSIS (ISCHNURIDAE) JRNL REF EUR.J.BIOCHEM. V. 271 3855 2004 JRNL REFN ISSN 0014-2956 JRNL PMID 15373831 JRNL DOI 10.1111/J.1432-1033.2004.04322.X REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XPLOR-NIH 2.0.5, XPLOR-NIH 2.0.5 REMARK 3 AUTHORS : C.D.SCHWIETERS,J.J.KUSZEWSKI,N.TJANDRA,G.M.CLORE REMARK 3 (XPLOR-NIH), C.D.SCHWIETERS,J.J.KUSZEWSKI, REMARK 3 N.TJANDRA,G.M.CLORE (XPLOR-NIH) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: CONJUGATE GRADIENT MINIMIZATION REMARK 4 REMARK 4 1WMT COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 23-JUL-04. REMARK 100 THE DEPOSITION ID IS D_1000023755. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 3.91 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : ATMOSPHERIC ATM REMARK 210 SAMPLE CONTENTS : 4.7MM ISTX REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; DQF-COSY; REMARK 210 1H13C HSQC REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ; 500 MHZ REMARK 210 SPECTROMETER MODEL : DMX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NULL REMARK 210 METHOD USED : TARSION ANGLE DYNAMICS, REMARK 210 SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST REMARK 210 ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 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 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (RES=RESIDUE NAME; REMARK 470 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 470 MODELS 1-20 REMARK 470 RES CSSEQI ATOMS REMARK 470 VAL A 1 N 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 H1 VAL A 1 O CYS A 35 1.25 REMARK 500 O ASN A 30 HD1 HIS A 32 1.31 REMARK 500 OE1 GLU A 15 HZ1 LYS A 19 1.54 REMARK 500 O THR A 10 H ASP A 12 1.57 REMARK 500 O ASN A 30 ND1 HIS A 32 2.00 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 11 43.50 -67.71 REMARK 500 1 ASP A 12 -41.88 -163.07 REMARK 500 1 LYS A 20 -70.91 -91.33 REMARK 500 1 CYS A 23 -32.91 -138.25 REMARK 500 1 ALA A 24 -141.22 60.63 REMARK 500 1 ARG A 31 33.14 39.28 REMARK 500 2 CYS A 7 -164.06 -129.72 REMARK 500 2 ARG A 8 -42.60 -140.31 REMARK 500 2 SER A 11 48.86 -65.52 REMARK 500 2 ASP A 12 -41.24 -166.15 REMARK 500 2 LYS A 20 -75.01 -90.36 REMARK 500 2 CYS A 23 -36.69 -135.26 REMARK 500 2 ALA A 24 -148.18 61.31 REMARK 500 2 ARG A 25 36.47 39.90 REMARK 500 2 MET A 29 -148.31 -82.99 REMARK 500 2 ASN A 30 92.62 -52.95 REMARK 500 2 ARG A 31 34.51 35.17 REMARK 500 2 CYS A 35 -161.36 -114.39 REMARK 500 2 TYR A 36 -0.13 -146.96 REMARK 500 2 ASN A 37 10.88 48.06 REMARK 500 2 PRO A 40 -17.29 -42.01 REMARK 500 3 SER A 11 40.29 -64.55 REMARK 500 3 ASP A 12 -34.05 -166.22 REMARK 500 3 LYS A 20 -71.14 -92.70 REMARK 500 3 CYS A 23 -37.58 -136.19 REMARK 500 3 ALA A 24 -143.48 59.09 REMARK 500 4 SER A 11 41.04 -64.52 REMARK 500 4 ASP A 12 -40.02 -165.40 REMARK 500 4 LYS A 20 -72.84 -86.22 REMARK 500 4 ALA A 24 -137.32 -79.39 REMARK 500 4 ARG A 25 71.41 43.30 REMARK 500 4 ALA A 26 -167.09 -107.05 REMARK 500 4 ASN A 30 -139.08 49.39 REMARK 500 4 ARG A 31 36.17 -98.31 REMARK 500 4 TYR A 36 12.49 -143.39 REMARK 500 4 PRO A 40 -19.04 -41.90 REMARK 500 5 SER A 11 38.90 -63.02 REMARK 500 5 ASP A 12 -38.22 -166.52 REMARK 500 5 LYS A 20 -67.25 -90.59 REMARK 500 5 ALA A 24 -129.15 -87.00 REMARK 500 5 CYS A 35 -166.36 -101.82 REMARK 500 5 ASN A 38 56.28 -157.76 REMARK 500 5 PRO A 40 -10.34 -44.44 REMARK 500 6 ARG A 8 -40.77 -135.28 REMARK 500 6 SER A 11 36.66 -62.77 REMARK 500 6 ASP A 12 -40.03 -162.68 REMARK 500 6 LYS A 20 -72.49 -89.01 REMARK 500 6 ALA A 24 -141.43 -82.82 REMARK 500 6 TYR A 36 16.31 -145.94 REMARK 500 7 SER A 11 40.52 -63.81 REMARK 500 REMARK 500 THIS ENTRY HAS 161 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL DBREF 1WMT A 1 41 PDB 1WMT 1WMT 1 41 SEQRES 1 A 41 VAL HIS THR ASN ILE PRO CYS ARG GLY THR SER ASP CYS SEQRES 2 A 41 TYR GLU PRO CYS GLU LYS LYS TYR ASN CYS ALA ARG ALA SEQRES 3 A 41 LYS CYS MET ASN ARG HIS CYS ASN CYS TYR ASN ASN CYS SEQRES 4 A 41 PRO TRP HELIX 1 1 GLY A 9 LYS A 20 1 12 SHEET 1 A 3 HIS A 2 PRO A 6 0 SHEET 2 A 3 HIS A 32 ASN A 34 -1 O CYS A 33 N THR A 3 SHEET 3 A 3 LYS A 27 MET A 29 -1 N MET A 29 O HIS A 32 SSBOND 1 CYS A 7 CYS A 28 1555 1555 2.02 SSBOND 2 CYS A 13 CYS A 33 1555 1555 2.01 SSBOND 3 CYS A 17 CYS A 35 1555 1555 2.04 SSBOND 4 CYS A 23 CYS A 39 1555 1555 2.01 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 - r 2 2 Bytes