Header list of 2a05.pdb file
Complete list - r 9 2 Bytes
HEADER SIGNALING PROTEIN 15-JUN-05 2A05 TITLE THE CYSTEINE-RICH SECRETORY PROTEIN DOMAIN OF TPX-1 IS RELATED TO ION TITLE 2 CHANNEL TOXINS AND REGULATES RYANODINE RECEPTOR CA2+ SIGNALING COMPND MOL_ID: 1; COMPND 2 MOLECULE: CYSTEINE-RICH SECRETORY PROTEIN-2; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: RESIDUES 189-243; COMPND 5 SYNONYM: TPX-1 CRISP, CRISP-2, TESTIS-SPECIFIC PROTEIN TPX-1; COMPND 6 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE; SOURCE 4 ORGANISM_TAXID: 10090; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: ORIGAMI B(DE3) PLACI; SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PTRIEX4 KEYWDS 3 ALPHA HELICES, 5 DISULPHIDE BONDS, 2 DOMAINS, SIGNALING PROTEIN EXPDTA SOLUTION NMR NUMMDL 23 AUTHOR G.M.GIBBS,M.J.SCANLON,J.SWARBRICK,S.CURTIS,A.F.DULHUNTY,M.K.O'BRYAN REVDAT 4 09-MAR-22 2A05 1 REMARK SEQADV REVDAT 3 24-FEB-09 2A05 1 VERSN REVDAT 2 24-JAN-06 2A05 1 JRNL REVDAT 1 17-JAN-06 2A05 0 JRNL AUTH G.M.GIBBS,M.J.SCANLON,J.SWARBRICK,S.CURTIS,E.GALLANT, JRNL AUTH 2 A.F.DULHUNTY,M.K.O'BRYAN JRNL TITL THE CYSTEINE-RICH SECRETORY PROTEIN DOMAIN OF TPX-1 IS JRNL TITL 2 RELATED TO ION CHANNEL TOXINS AND REGULATES RYANODINE JRNL TITL 3 RECEPTOR CA2+ SIGNALING. JRNL REF J.BIOL.CHEM. V. 281 4156 2006 JRNL REFN ISSN 0021-9258 JRNL PMID 16339766 JRNL DOI 10.1074/JBC.M506849200 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XWINNMR 1, CYANA 1.06, XPLOR-NIH 2.9.9 REMARK 3 AUTHORS : BRUKER (XWINNMR), GUNTERT (CYANA), CLORE REMARK 3 SCHWIETERS KUSZEWSKI TJANDRA (XPLOR-NIH) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NOES: 187 INTRA 251 SHORT 253 MED 188 REMARK 3 LONG. 78 CHEM SHIFTS REMARK 4 REMARK 4 2A05 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 20-JUN-05. REMARK 100 THE DEPOSITION ID IS D_1000033326. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 5.8 REMARK 210 IONIC STRENGTH : 1MM REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1MM TPX-1 U-15N 90% H2O 10% D2O; REMARK 210 1MM TPX-1 90% H2O 10% D2O; 1MM REMARK 210 TPX-1 100% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_15N REMARK 210 -SEPARATED TOCSY; 2D NOESY; 2D REMARK 210 TOCSY; DQF-COSY REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ REMARK 210 SPECTROMETER MODEL : DRX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : XWINNMR 1, SPARKY 3.101 REMARK 210 METHOD USED : AUTOMATED RESONANCE ASSIGNMENT REMARK 210 USING TORSION ANGLE DYNAMICS REMARK 210 (CANDID), FURTHER REFINEMENT REMARK 210 WITH CA AND CB CHEM SHIFTS AND REMARK 210 DATABASE POTENTIALS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 49 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 23 REMARK 210 CONFORMERS, SELECTION CRITERIA : VIOLATIONS <0.2A NOE, TOTAL REMARK 210 ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: STANDARD 2D/3D METHODS 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 HD1 HIS A 225 H LEU A 227 1.14 REMARK 500 O ASN A 213 H LEU A 217 1.52 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 CYS A 196 88.84 -151.86 REMARK 500 1 ASN A 198 39.35 -159.73 REMARK 500 1 ALA A 221 -84.29 -134.73 REMARK 500 1 CYS A 236 -65.34 -99.29 REMARK 500 1 CYS A 238 -159.54 -124.44 REMARK 500 1 GLU A 239 31.64 -175.34 REMARK 500 1 ASP A 240 1.22 53.39 REMARK 500 2 PRO A 193 76.41 -43.63 REMARK 500 2 ASN A 198 43.13 -161.76 REMARK 500 2 ALA A 221 -86.51 -121.98 REMARK 500 2 CYS A 236 -65.51 -103.70 REMARK 500 2 GLU A 239 -154.38 -150.53 REMARK 500 3 PRO A 193 -81.30 -52.55 REMARK 500 3 GLU A 197 -89.93 -86.03 REMARK 500 3 ALA A 221 -85.84 -128.28 REMARK 500 3 HIS A 225 -102.20 -61.32 REMARK 500 3 GLU A 226 -53.74 -173.14 REMARK 500 3 CYS A 236 -62.57 -102.89 REMARK 500 3 CYS A 238 2.21 48.66 REMARK 500 3 LYS A 241 105.82 74.82 REMARK 500 4 ALA A 221 -84.45 -118.64 REMARK 500 4 GLU A 239 45.64 -146.00 REMARK 500 5 CYS A 192 76.07 -152.07 REMARK 500 5 CYS A 196 102.74 -164.88 REMARK 500 5 ASN A 198 32.04 -141.80 REMARK 500 5 ASN A 203 -6.92 -147.47 REMARK 500 5 CYS A 205 96.76 -167.38 REMARK 500 5 ALA A 221 -84.98 -130.63 REMARK 500 5 CYS A 236 -68.33 -106.60 REMARK 500 5 ASP A 240 -12.14 -49.26 REMARK 500 5 LYS A 241 99.85 93.39 REMARK 500 6 PRO A 193 -79.13 -63.69 REMARK 500 6 ASN A 198 44.55 -161.43 REMARK 500 6 ALA A 221 -79.38 -76.21 REMARK 500 6 GLU A 239 93.67 -177.47 REMARK 500 7 CYS A 189 35.76 -69.50 REMARK 500 7 ASN A 195 55.90 -140.88 REMARK 500 7 ASN A 198 -19.01 -43.12 REMARK 500 7 LEU A 200 -153.76 38.80 REMARK 500 7 ALA A 221 -94.30 -115.97 REMARK 500 7 CYS A 236 -67.82 -103.12 REMARK 500 7 GLU A 239 -25.05 -175.96 REMARK 500 8 ASN A 198 42.88 -161.87 REMARK 500 8 ALA A 221 -85.65 -121.43 REMARK 500 8 CYS A 236 -64.10 -100.79 REMARK 500 8 GLU A 239 85.36 179.79 REMARK 500 8 ASP A 240 85.13 57.41 REMARK 500 9 ALA A 190 -67.42 -145.12 REMARK 500 9 ASN A 198 43.82 -159.15 REMARK 500 9 SER A 204 59.97 -146.95 REMARK 500 REMARK 500 THIS ENTRY HAS 142 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL DBREF 2A05 A 189 243 UNP P16563 CRIS2_MOUSE 189 243 SEQADV 2A05 GLY A 187 UNP P16563 CLONING ARTIFACT SEQADV 2A05 SER A 188 UNP P16563 CLONING ARTIFACT SEQRES 1 A 57 GLY SER CYS ALA SER CYS PRO ASN ASN CYS GLU ASN GLY SEQRES 2 A 57 LEU CYS THR ASN SER CYS ASP PHE GLU ASP LEU LEU SER SEQRES 3 A 57 ASN CYS GLU SER LEU LYS THR SER ALA GLY CYS LYS HIS SEQRES 4 A 57 GLU LEU LEU LYS THR LYS CYS GLN ALA THR CYS LEU CYS SEQRES 5 A 57 GLU ASP LYS ILE HIS HELIX 1 1 ASN A 213 ALA A 221 1 9 HELIX 2 2 LEU A 227 CYS A 232 1 6 HELIX 3 3 CYS A 232 LEU A 237 1 6 SSBOND 1 CYS A 189 CYS A 196 1555 1555 2.02 SSBOND 2 CYS A 192 CYS A 201 1555 1555 2.02 SSBOND 3 CYS A 205 CYS A 238 1555 1555 2.02 SSBOND 4 CYS A 214 CYS A 232 1555 1555 2.02 SSBOND 5 CYS A 223 CYS A 236 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 - r 9 2 Bytes