Header list of 1xc0.pdb file
Complete list - 2 20 Bytes
HEADER SIGNALING PROTEIN 31-AUG-04 1XC0 TITLE TWENTY LOWEST ENERGY STRUCTURES OF PA4 BY SOLUTION NMR COMPND MOL_ID: 1; COMPND 2 MOLECULE: PARDAXIN P-4; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: PA4; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 SYNTHETIC: YES; SOURCE 3 OTHER_DETAILS: PARDAXINS NATURALLY OCCUR IN SOLE FISH OF GENUS SOURCE 4 PARDACHIRUS. PA4 WAS SYNTHESIZED USING STANDARD 9- SOURCE 5 FLUORENYLMETHOXYCARBONYL-BASED SOLID-PAHSE METHODS WITH AN ABI 431A SOURCE 6 PEPTIDE SYNTHESIZER. CRUDE PEPTIDE WAS PURIFIED BY REVERSED-PHASE SOURCE 7 HPLC KEYWDS BEND-HELIX-BEND-HELIX MOTIF, SIGNALING PROTEIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR F.PORCELLI,B.BUCK,D.-K.LEE,K.J.HALLOCK,A.RAMAMOORTHY,G.VEGLIA REVDAT 4 02-MAR-22 1XC0 1 REMARK REVDAT 3 24-FEB-09 1XC0 1 VERSN REVDAT 2 26-APR-05 1XC0 1 JRNL REVDAT 1 28-SEP-04 1XC0 0 JRNL AUTH F.PORCELLI,B.BUCK,D.-K.LEE,K.J.HALLOCK,A.RAMAMOORTHY, JRNL AUTH 2 G.VEGLIA JRNL TITL STRUCTURE AND ORIENTATION OF PARDAXIN DETERMINED BY NMR JRNL TITL 2 EXPERIMENTS IN MODEL MEMBRANES JRNL REF J.BIOL.CHEM. V. 279 45815 2004 JRNL REFN ISSN 0021-9258 JRNL PMID 15292173 JRNL DOI 10.1074/JBC.M405454200 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : VNMR 6.1, X-PLOR 3.851 REMARK 3 AUTHORS : VARIAN (VNMR), BRUNGER (X-PLOR) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: 335 NOES; 13 H-BONDS REMARK 4 REMARK 4 1XC0 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-SEP-04. REMARK 100 THE DEPOSITION ID IS D_1000030186. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 303 REMARK 210 PH : 4.5 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : NULL REMARK 210 SAMPLE CONTENTS : ~1.5 MG OF LYOPHILIZED PA4 IN 20 REMARK 210 MM PBS (PH 6.5),300 MM D31-DPC REMARK 210 AND 10% D2O. SAMPLE PH WAS REMARK 210 ADJUSTED TO ~4.5 WITH NAOH. REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D TOCSY; 2D NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ REMARK 210 SPECTROMETER MODEL : INOVA REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRPIPE 2006, SPARKY 3.110, X REMARK 210 -PLOR 3.851 REMARK 210 METHOD USED : EXTENDED STRUCTURE; RANDOM REMARK 210 SIMULATED ANNEALING; MOLECULAR REMARK 210 DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 350 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 : 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: 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 HZ3 LYS A 16 OG1 THR A 17 1.37 REMARK 500 O LYS A 16 HG SER A 20 1.45 REMARK 500 O LEU A 19 H GLY A 23 1.46 REMARK 500 O ALA A 25 HG SER A 29 1.47 REMARK 500 O LEU A 5 H LYS A 8 1.48 REMARK 500 O ALA A 4 HZ3 LYS A 8 1.51 REMARK 500 O PHE A 15 H LEU A 19 1.52 REMARK 500 O SER A 20 HG SER A 24 1.59 REMARK 500 O VAL A 22 H LEU A 26 1.60 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 2 -59.48 -160.31 REMARK 500 1 PHE A 3 -38.58 -147.23 REMARK 500 1 ALA A 4 -48.18 -173.13 REMARK 500 1 LEU A 14 -59.17 -158.64 REMARK 500 2 PHE A 2 -61.18 -150.92 REMARK 500 2 PHE A 3 -38.19 -145.71 REMARK 500 2 ALA A 4 -44.59 -173.73 REMARK 500 2 LEU A 14 -60.19 -161.68 REMARK 500 3 PHE A 2 -60.65 -156.47 REMARK 500 3 PHE A 3 -39.05 -146.65 REMARK 500 3 ALA A 4 -55.49 -173.56 REMARK 500 3 PRO A 13 30.38 -82.81 REMARK 500 3 LEU A 14 -60.72 -162.34 REMARK 500 3 SER A 28 -66.62 -109.17 REMARK 500 4 PHE A 2 -59.95 -158.55 REMARK 500 4 PHE A 3 -38.92 -146.76 REMARK 500 4 ALA A 4 -54.75 -173.26 REMARK 500 4 PRO A 13 37.36 -84.31 REMARK 500 4 LEU A 14 -58.84 -168.53 REMARK 500 4 SER A 28 -62.56 -91.69 REMARK 500 4 GLN A 32 140.23 76.71 REMARK 500 5 PHE A 2 -60.12 -157.77 REMARK 500 5 PHE A 3 -38.80 -147.28 REMARK 500 5 ALA A 4 -48.19 -172.75 REMARK 500 5 LEU A 14 -59.71 -158.65 REMARK 500 6 PHE A 2 -59.49 -160.05 REMARK 500 6 PHE A 3 -38.81 -147.02 REMARK 500 6 ALA A 4 -47.67 -172.99 REMARK 500 6 LEU A 14 -58.13 -157.79 REMARK 500 6 SER A 28 40.57 -93.54 REMARK 500 6 SER A 29 -70.81 -102.22 REMARK 500 7 PHE A 2 -59.93 -158.21 REMARK 500 7 PHE A 3 -39.16 -147.41 REMARK 500 7 ALA A 4 -47.66 -172.47 REMARK 500 7 LEU A 14 -61.25 -158.82 REMARK 500 7 SER A 29 -48.39 -139.14 REMARK 500 8 PHE A 2 -59.82 -158.00 REMARK 500 8 PHE A 3 -39.52 -145.98 REMARK 500 8 ALA A 4 -54.25 -172.41 REMARK 500 8 LEU A 14 -59.88 -153.62 REMARK 500 9 PHE A 2 -59.14 -160.74 REMARK 500 9 PHE A 3 -39.04 -146.45 REMARK 500 9 ALA A 4 -54.46 -173.11 REMARK 500 9 LEU A 14 -59.23 -151.46 REMARK 500 9 GLN A 32 -51.59 -166.96 REMARK 500 10 PHE A 2 -59.61 -159.63 REMARK 500 10 PHE A 3 -39.14 -146.89 REMARK 500 10 ALA A 4 -48.08 -172.50 REMARK 500 10 PRO A 13 35.85 -83.64 REMARK 500 10 LEU A 14 -58.95 -167.52 REMARK 500 REMARK 500 THIS ENTRY HAS 100 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL DBREF 1XC0 A 1 33 UNP P81861 PAP4_PARMA 1 33 SEQRES 1 A 33 GLY PHE PHE ALA LEU ILE PRO LYS ILE ILE SER SER PRO SEQRES 2 A 33 LEU PHE LYS THR LEU LEU SER ALA VAL GLY SER ALA LEU SEQRES 3 A 33 SER SER SER GLY GLY GLN GLU HELIX 1 1 LEU A 5 ILE A 10 1 6 HELIX 2 2 LEU A 14 LEU A 26 1 13 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