Header list of 1v1c.pdb file
Complete list - r 25 2 Bytes
HEADER SH3-DOMAIN 14-APR-04 1V1C TITLE SOLUTION STRUCTURE OF THE SH3 DOMAIN OF OBSCURIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: OBSCURIN; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: SH3 DOMAIN RESIDUES 5601-5668; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 ORGAN: HEART; SOURCE 6 TISSUE: MUSCLE; SOURCE 7 CELL: MYOCYTE; SOURCE 8 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 9 EXPRESSION_SYSTEM_TAXID: 511693; SOURCE 10 EXPRESSION_SYSTEM_STRAIN: BL21; SOURCE 11 EXPRESSION_SYSTEM_VECTOR: PET BASED; SOURCE 12 EXPRESSION_SYSTEM_PLASMID: PET8C KEYWDS MUSCLE, SARCOMERE, ADAPTER, MYOGENESIS, SH3-DOMAIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR M.PFUHL,M.GAUTEL REVDAT 2 24-FEB-09 1V1C 1 VERSN REVDAT 1 14-APR-05 1V1C 0 JRNL AUTH M.PFUHL,M.GAUTEL JRNL TITL SOLUTION STRUCTURE OF THE SH3 DOMAIN OF OBSCURIN JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS 1.1 REMARK 3 AUTHORS : BRUNGER ET.AL. REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: STANDARD ARIA SIMULATED ANNEALING REMARK 3 PROTOCOL ACCORDING TO NILGES. ALL DEFAULT PARAMETERS COMING REMARK 3 WITH VERSION 1.2 WERE USED APART FROM A NUMBER OF 200 REMARK 3 STRUCTURES CALCULATED IN ITERATION 8 OF WHICH 20 WHERE REMARK 3 SELECTED. NO WATER REFINEMENT WAS USED. REMARK 4 REMARK 4 1V1C COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 14-APR-04. REMARK 100 THE PDBE ID CODE IS EBI-14993. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 5.76 REMARK 210 IONIC STRENGTH : 200 MM REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D 15N-RESOLVED NOESY-HSQC, REMARK 210 3D 13C RESOLVED NOESY-HSQC REMARK 210 SPECTROMETER FIELD STRENGTH : 600 REMARK 210 SPECTROMETER MODEL : AVANCE REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : CNS/ARIA REMARK 210 METHOD USED : SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 200 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE REMARK 210 NMR SPECTROSCOPY ON 13C, 15N-LABELED OBSH3 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 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 GLY A -2 REMARK 465 SER A -1 REMARK 465 SER A 0 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 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 ALA A 9 12.27 -141.89 REMARK 500 1 ASP A 10 152.91 63.78 REMARK 500 1 ALA A 35 -77.91 -92.19 REMARK 500 1 LYS A 48 -81.12 65.04 REMARK 500 1 SER A 49 12.46 -147.94 REMARK 500 2 ASP A 10 90.34 57.14 REMARK 500 2 LEU A 32 -70.44 -106.08 REMARK 500 2 ALA A 35 -87.11 59.76 REMARK 500 2 LYS A 48 -79.91 65.38 REMARK 500 2 SER A 49 24.45 -154.95 REMARK 500 2 LYS A 67 -178.01 60.25 REMARK 500 3 PHE A 2 -166.65 57.00 REMARK 500 3 ASP A 10 111.86 61.58 REMARK 500 3 LEU A 32 -71.42 -104.98 REMARK 500 3 ASP A 33 -77.97 -60.72 REMARK 500 3 ALA A 34 87.34 62.52 REMARK 500 3 ALA A 35 -73.86 -143.04 REMARK 500 3 THR A 47 -46.83 -139.08 REMARK 500 3 LYS A 48 -6.43 179.20 REMARK 500 3 SER A 49 -8.74 -154.01 REMARK 500 3 LYS A 67 -9.59 -147.12 REMARK 500 4 ASP A 10 -70.59 68.74 REMARK 500 4 TYR A 11 84.75 65.55 REMARK 500 4 ALA A 35 -18.47 -157.34 REMARK 500 4 THR A 47 36.42 -93.81 REMARK 500 4 SER A 49 -34.66 -162.34 REMARK 500 5 ASP A 10 -80.13 64.01 REMARK 500 5 TYR A 11 83.60 61.76 REMARK 500 5 LEU A 32 -69.29 -96.39 REMARK 500 5 ALA A 35 -87.03 59.58 REMARK 500 5 THR A 47 36.39 -94.81 REMARK 500 5 SER A 49 -17.83 -149.63 REMARK 500 6 ASP A 10 101.95 60.31 REMARK 500 6 LEU A 32 -73.00 -94.11 REMARK 500 6 ALA A 34 11.76 -144.31 REMARK 500 6 HIS A 36 98.31 59.68 REMARK 500 7 ASP A 10 162.27 62.75 REMARK 500 7 TYR A 11 93.38 -161.73 REMARK 500 7 ALA A 34 -69.24 -124.73 REMARK 500 7 ALA A 35 -85.37 60.65 REMARK 500 7 THR A 47 -159.26 -102.89 REMARK 500 7 SER A 49 -30.81 -154.88 REMARK 500 8 PHE A 2 101.86 60.53 REMARK 500 8 ALA A 9 10.11 -144.12 REMARK 500 8 ASP A 10 93.69 55.88 REMARK 500 8 ASP A 19 18.60 59.83 REMARK 500 8 LEU A 32 -77.22 -87.98 REMARK 500 8 HIS A 36 109.69 63.78 REMARK 500 8 SER A 49 3.14 -159.99 REMARK 500 9 PHE A 2 169.85 62.13 REMARK 500 9 ASP A 10 109.32 61.81 REMARK 500 9 LEU A 32 -68.61 -102.94 REMARK 500 9 HIS A 36 101.30 60.92 REMARK 500 9 THR A 47 -162.81 -112.53 REMARK 500 10 ASP A 10 158.88 63.65 REMARK 500 10 TYR A 11 88.50 -157.91 REMARK 500 10 ASP A 19 18.25 58.96 REMARK 500 10 LEU A 32 -71.24 -112.76 REMARK 500 10 ASP A 33 -75.14 -57.27 REMARK 500 10 ALA A 34 91.16 61.94 REMARK 500 10 ALA A 35 -70.63 -140.40 REMARK 500 10 LYS A 48 -80.82 64.52 REMARK 500 10 SER A 49 19.00 -150.24 REMARK 500 10 LYS A 67 147.67 63.90 REMARK 500 11 PHE A 2 99.30 59.06 REMARK 500 11 ASP A 10 -63.88 72.17 REMARK 500 11 TYR A 11 78.11 63.74 REMARK 500 11 LEU A 32 -79.35 -92.17 REMARK 500 11 ASP A 33 -75.53 -80.64 REMARK 500 11 ALA A 34 111.01 68.27 REMARK 500 11 ALA A 35 -64.58 -159.37 REMARK 500 11 SER A 49 -2.61 -163.22 REMARK 500 12 ASP A 10 -73.92 66.80 REMARK 500 12 TYR A 11 87.33 63.72 REMARK 500 12 ASP A 19 18.40 58.24 REMARK 500 12 LEU A 32 -76.65 -100.26 REMARK 500 12 ALA A 34 -84.22 -85.48 REMARK 500 12 ALA A 35 103.24 58.14 REMARK 500 12 HIS A 36 114.66 64.36 REMARK 500 12 THR A 47 -160.56 -127.29 REMARK 500 12 SER A 49 13.35 -158.59 REMARK 500 13 ASP A 10 -78.47 64.94 REMARK 500 13 TYR A 11 86.21 62.32 REMARK 500 13 ASP A 19 18.52 56.20 REMARK 500 13 LEU A 32 -81.98 -105.05 REMARK 500 13 ASP A 33 -79.43 -70.84 REMARK 500 13 LEU A 38 -88.87 -80.22 REMARK 500 13 SER A 49 71.58 52.50 REMARK 500 13 LYS A 67 -177.92 60.26 REMARK 500 14 PHE A 2 -174.43 -69.84 REMARK 500 14 ASP A 10 97.73 60.82 REMARK 500 14 LEU A 32 -60.27 -98.57 REMARK 500 14 ASP A 33 -75.17 -71.65 REMARK 500 14 ALA A 34 91.05 61.34 REMARK 500 14 ALA A 35 -64.05 -160.67 REMARK 500 14 THR A 47 -154.48 -96.89 REMARK 500 14 SER A 49 -10.74 -155.78 REMARK 500 14 LYS A 67 179.18 59.72 REMARK 500 15 PHE A 2 -169.21 58.90 REMARK 500 15 LEU A 32 -72.92 -105.20 REMARK 500 15 ASP A 33 -79.57 -83.47 REMARK 500 15 ALA A 34 102.35 62.30 REMARK 500 15 ALA A 35 -62.60 -125.25 REMARK 500 15 THR A 47 99.16 -68.66 REMARK 500 15 LYS A 48 -78.66 64.41 REMARK 500 16 ASP A 10 90.44 56.33 REMARK 500 16 LEU A 32 -78.75 -102.12 REMARK 500 16 ALA A 35 -60.09 -153.40 REMARK 500 16 SER A 49 -4.76 -145.21 REMARK 500 17 LEU A 32 -67.36 -91.38 REMARK 500 17 HIS A 36 104.60 61.23 REMARK 500 17 SER A 49 -22.16 -148.67 REMARK 500 18 PHE A 2 93.21 56.38 REMARK 500 18 ALA A 9 -71.83 -127.93 REMARK 500 18 ASP A 10 -64.50 165.74 REMARK 500 18 TYR A 11 79.21 59.92 REMARK 500 18 ASP A 19 -35.22 170.18 REMARK 500 18 LEU A 32 -68.23 -104.86 REMARK 500 18 ASP A 33 -74.42 -57.90 REMARK 500 18 ALA A 34 78.92 58.75 REMARK 500 18 ALA A 35 -36.75 -169.70 REMARK 500 18 LEU A 38 -72.17 -67.76 REMARK 500 19 ASP A 10 92.28 58.17 REMARK 500 19 LEU A 32 -81.40 -102.20 REMARK 500 19 HIS A 36 108.96 64.90 REMARK 500 19 LEU A 38 -71.14 -54.24 REMARK 500 19 PRO A 46 -168.61 -75.39 REMARK 500 19 THR A 47 -75.37 -107.67 REMARK 500 19 LYS A 48 -11.48 -170.15 REMARK 500 19 SER A 49 -7.09 -143.29 REMARK 500 20 ASP A 10 90.24 56.38 REMARK 500 20 LEU A 32 -79.25 -108.55 REMARK 500 20 ASP A 33 -72.54 -64.38 REMARK 500 20 ALA A 34 92.74 63.19 REMARK 500 20 ALA A 35 -73.13 -150.65 REMARK 500 20 LYS A 48 -81.60 62.63 REMARK 500 20 SER A 49 26.81 -156.38 REMARK 500 20 LYS A 67 78.50 -101.25 REMARK 500 REMARK 500 REMARK: NULL REMARK 999 REMARK 999 SEQUENCE REMARK 999 THE FIRST THREE RESIDUES IN THE SEQRES RECORDS BELOW ARE REMARK 999 THE REMANENTS OF A TEV CLEAVED HIS TAG AND DO NOT FORM PART REMARK 999 OF THE OBSCURIN SH3 DOMAIN DBREF 1V1C A -2 0 PDB 1V1C 1V1C -2 0 DBREF 1V1C A 1 68 UNP Q96AA2 Q96AA2 5601 5668 SEQRES 1 A 71 GLY SER SER ILE PHE ASP ILE TYR VAL VAL THR ALA ASP SEQRES 2 A 71 TYR LEU PRO LEU GLY ALA GLU GLN ASP ALA ILE THR LEU SEQRES 3 A 71 ARG GLU GLY GLN TYR VAL GLU VAL LEU ASP ALA ALA HIS SEQRES 4 A 71 PRO LEU ARG TRP LEU VAL ARG THR LYS PRO THR LYS SER SEQRES 5 A 71 SER PRO SER ARG GLN GLY TRP VAL SER PRO ALA TYR LEU SEQRES 6 A 71 ASP ARG ARG LEU LYS LEU HELIX 1 1 SER A 58 ALA A 60 5 3 SHEET 1 AA 5 GLN A 54 VAL A 57 0 SHEET 2 AA 5 ARG A 39 THR A 44 -1 O TRP A 40 N VAL A 57 SHEET 3 AA 5 TYR A 28 HIS A 36 -1 O GLU A 30 N ARG A 43 SHEET 4 AA 5 ILE A 4 VAL A 7 -1 O TYR A 5 N VAL A 29 SHEET 5 AA 5 LEU A 62 ARG A 65 -1 O ASP A 63 N VAL A 6 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 25 2 Bytes