Header list of 2esy.pdb file
Complete list - 9 20 Bytes
HEADER LIPID BINDING PROTEIN 27-OCT-05 2ESY TITLE STRUCTURE AND INFLUENCE ON STABILITY AND ACTIVITY OF THE N-TERMINAL TITLE 2 PROPETIDE PART OF LUNG SURFACTANT PROTEIN C COMPND MOL_ID: 1; COMPND 2 MOLECULE: LUNG SURFACTANT PROTEIN C; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 SYNTHETIC: YES; SOURCE 3 OTHER_DETAILS: PEPTIDE SYNTHESIS USING F-MOC CHEMISTRY. THE SEQUENCE SOURCE 4 OF THE PEPTIDE IS NATURALLY FOUND IN HUMAN. KEYWDS N-TERMINAL PART OF LUNG SURFACTANT PROTEIN C, LIPID BINDING PROTEIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR J.LI,E.LIEPINSH,A.ALMLEN,J.THYBERG,T.CURSTEDT,H.JORNVALL,J.JOHANSSON REVDAT 4 09-MAR-22 2ESY 1 REMARK LINK REVDAT 3 24-FEB-09 2ESY 1 VERSN REVDAT 2 28-FEB-06 2ESY 1 JRNL REVDAT 1 15-NOV-05 2ESY 0 JRNL AUTH J.LI,E.LIEPINSH,A.ALMLEN,J.THYBERG,T.CURSTEDT,H.JORNVALL, JRNL AUTH 2 J.JOHANSSON JRNL TITL STRUCTURE AND INFLUENCE ON STABILITY AND ACTIVITY OF THE JRNL TITL 2 N-TERMINAL PROPEPTIDE PART OF LUNG SURFACTANT PROTEIN C JRNL REF FEBS J. V. 273 926 2006 JRNL REFN ISSN 1742-464X JRNL PMID 16478467 JRNL DOI 10.1111/J.1742-4658.2006.05124.X REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : VNMR 1.1.D, OPAL 3.0 REMARK 3 AUTHORS : VARIAN (VNMR), P.LUGINBUL (OPAL) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: REMARK 3 THE STRUCTURES ARE BASED ON A TOTAL OF 344 RESTRAINTS, 263 ARE NOE- REMARK 3 DERIVED REMARK 3 DISTANCE CONSTRAINTS, 81 DIHEDRAL ANGLE RESTRAINTS REMARK 4 REMARK 4 2ESY COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 31-OCT-05. REMARK 100 THE DEPOSITION ID IS D_1000035053. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 297; 287 REMARK 210 PH : 7.5; 7 REMARK 210 IONIC STRENGTH : 0.1; 0 REMARK 210 PRESSURE : AMBIENT; AMBIENT REMARK 210 SAMPLE CONTENTS : 0.5MM SP-CI(1-31) IN 35MM REMARK 210 [2H38]DODECYLPHOSPHOCHOLINE (DPC) REMARK 210 , 50MM SODIUM PHOSPHATE BUFFER; REMARK 210 0.5MM SP-CI(1-31) REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; DQF-COSY REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 600 MHZ REMARK 210 SPECTROMETER MODEL : INOVA; DMX REMARK 210 SPECTROMETER MANUFACTURER : VARIAN; BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : PROSA 3.2, XEASY 3.0, DYANA 2.6 REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 50 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH FAVORABLE NON REMARK 210 -BOND ENERGY,STRUCTURES WITH THE REMARK 210 LEAST RESTRAINT VIOLATIONS, REMARK 210 STRUCTURES WITH THE LOWEST REMARK 210 ENERGY,TARGET FUNCTION 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 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 OD2 ASP A 4 HG SER A 6 1.58 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 6 5.24 -65.09 REMARK 500 1 ALA A 7 83.77 -68.84 REMARK 500 1 ARG A 12 114.55 -160.20 REMARK 500 1 PHE A 13 76.03 26.40 REMARK 500 1 PRO A 16 -168.53 -76.91 REMARK 500 1 PHE A 17 18.64 -64.28 REMARK 500 2 TYR A 5 15.68 -55.44 REMARK 500 2 SER A 6 25.79 -60.31 REMARK 500 2 PHE A 13 76.22 23.71 REMARK 500 2 PRO A 16 -167.39 -72.27 REMARK 500 2 PHE A 17 15.40 -60.30 REMARK 500 3 TYR A 5 100.70 -43.80 REMARK 500 3 ARG A 12 90.68 -161.03 REMARK 500 3 PRO A 16 -168.47 -75.24 REMARK 500 3 PHE A 17 14.65 -61.92 REMARK 500 4 SER A 6 4.54 -59.06 REMARK 500 4 PHE A 13 76.44 23.61 REMARK 500 4 PRO A 16 -169.07 -75.73 REMARK 500 4 PHE A 17 18.14 -62.44 REMARK 500 5 PRO A 2 171.36 -59.54 REMARK 500 5 PHE A 13 76.06 31.54 REMARK 500 5 PRO A 16 -168.43 -76.01 REMARK 500 5 PHE A 17 20.28 -63.08 REMARK 500 6 PRO A 2 175.89 -52.36 REMARK 500 6 PRO A 3 46.93 -72.59 REMARK 500 6 ALA A 7 37.11 -72.88 REMARK 500 6 PHE A 13 76.20 23.87 REMARK 500 6 PRO A 16 -166.21 -73.63 REMARK 500 6 PHE A 17 14.26 -61.94 REMARK 500 7 ASP A 4 -156.63 -120.61 REMARK 500 7 SER A 6 48.16 -76.37 REMARK 500 7 ALA A 7 -166.01 -73.36 REMARK 500 7 PHE A 13 9.94 49.79 REMARK 500 7 PRO A 16 -154.22 -76.17 REMARK 500 7 PHE A 17 14.08 -60.87 REMARK 500 8 PRO A 2 172.57 -53.07 REMARK 500 8 PRO A 3 44.08 -72.99 REMARK 500 8 ASP A 4 25.69 -72.46 REMARK 500 8 PHE A 13 66.70 39.63 REMARK 500 8 PHE A 17 18.79 -62.52 REMARK 500 9 ALA A 8 160.82 -49.94 REMARK 500 9 PHE A 13 76.35 24.09 REMARK 500 9 PRO A 16 -168.73 -77.52 REMARK 500 9 PHE A 17 18.80 -63.64 REMARK 500 10 ASP A 4 54.47 -92.39 REMARK 500 10 TYR A 5 17.40 -68.74 REMARK 500 10 SER A 6 -93.43 -136.97 REMARK 500 10 PHE A 13 76.03 23.74 REMARK 500 10 PRO A 16 -169.37 -73.76 REMARK 500 10 PHE A 17 16.71 -62.29 REMARK 500 REMARK 500 THIS ENTRY HAS 100 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 SER A 1 PRO A 2 1 147.19 REMARK 500 SER A 1 PRO A 2 2 148.08 REMARK 500 SER A 1 PRO A 2 4 147.80 REMARK 500 SER A 1 PRO A 2 5 148.25 REMARK 500 SER A 1 PRO A 2 6 148.12 REMARK 500 SER A 1 PRO A 2 7 148.55 REMARK 500 SER A 1 PRO A 2 8 148.37 REMARK 500 SER A 1 PRO A 2 9 146.79 REMARK 500 SER A 1 PRO A 2 11 148.77 REMARK 500 SER A 1 PRO A 2 12 147.86 REMARK 500 SER A 1 PRO A 2 15 147.79 REMARK 500 SER A 1 PRO A 2 16 147.21 REMARK 500 SER A 1 PRO A 2 19 147.76 REMARK 500 SER A 1 PRO A 2 20 149.00 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 3 ARG A 24 0.15 SIDE CHAIN REMARK 500 11 ARG A 12 0.07 SIDE CHAIN REMARK 500 18 ARG A 24 0.08 SIDE CHAIN REMARK 500 19 ARG A 10 0.08 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NH2 A 32 DBREF 2ESY A 1 32 PDB 2ESY 2ESY 1 32 SEQRES 1 A 32 SER PRO PRO ASP TYR SER ALA ALA PRO ARG GLY ARG PHE SEQRES 2 A 32 GLY ILE PRO PHE PHE PRO VAL HIS LEU LYS ARG LEU LEU SEQRES 3 A 32 ILE LEU LEU LEU LEU NH2 HET NH2 A 32 3 HETNAM NH2 AMINO GROUP FORMUL 1 NH2 H2 N HELIX 1 1 PHE A 18 LEU A 31 1 14 LINK C LEU A 31 N NH2 A 32 1555 1555 1.33 SITE 1 AC1 4 LEU A 28 LEU A 29 LEU A 30 LEU A 31 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 - 9 20 Bytes