Header list of 2ggr.pdb file
Complete list - r 9 2 Bytes
HEADER PROTEIN BINDING 24-MAR-06 2GGR TITLE SOLUTION STRUCTURE OF THE C-TERMINAL SH3 DOMAIN OF C-CRKII COMPND MOL_ID: 1; COMPND 2 MOLECULE: PROTO-ONCOGENE C-CRK; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: C-TERMINAL DOMAIN; COMPND 5 SYNONYM: P38, ADAPTER MOLECULE CRK; 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 GENE: CRK, CRKO; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 DE3; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PTRCHISA KEYWDS SOLUTION STRUCTURE, CRK-II, SH3 DOMAIN, PROTEIN BINDING EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR V.MURALIDHARAN,K.DUTTA,T.W.MUIR,D.COWBURN REVDAT 3 09-MAR-22 2GGR 1 REMARK SEQADV REVDAT 2 24-FEB-09 2GGR 1 VERSN REVDAT 1 01-AUG-06 2GGR 0 JRNL AUTH V.MURALIDHARAN,K.DUTTA,J.CHO,M.VILA-PERELLO,D.P.RALEIGH, JRNL AUTH 2 D.COWBURN,T.W.MUIR JRNL TITL SOLUTION STRUCTURE AND FOLDING CHARACTERISTICS OF THE JRNL TITL 2 C-TERMINAL SH3 DOMAIN OF C-CRK-II JRNL REF BIOCHEMISTRY V. 45 8874 2006 JRNL REFN ISSN 0006-2960 JRNL PMID 16846230 JRNL DOI 10.1021/BI060590Z REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS 1.1 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 2GGR COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-MAR-06. REMARK 100 THE DEPOSITION ID IS D_1000037097. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 7.2 REMARK 210 IONIC STRENGTH : 50MM REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 0.4 MM CSH3 DOMAIN U-15N,13C; REMARK 210 10MM PHOSPHATE BUFFER PH7.2; REMARK 210 50MM NACL; 5MM DTT-D10; 0.1% REMARK 210 NAN3; 1MM EDTA; 90% H2O, 10% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N REMARK 210 -SEPARATED_NOESY; 3D_13C_ REMARK 210 AROMATIC_NOESY; HNHA; HNCO_3J REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 700 MHZ; 800 MHZ; 600 REMARK 210 MHZ REMARK 210 SPECTROMETER MODEL : AVANCE; INOVA REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : ARIA 2.2 REMARK 210 METHOD USED : DISTANCE GEOMETRY SIMULATED REMARK 210 ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 500 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST REMARK 210 RESTRAINT VIOLATIONS,STRUCTURES REMARK 210 WITH THE LOWEST 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 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 MODELS 1-20 REMARK 465 RES C SSSEQI REMARK 465 GLY A 229 REMARK 465 LEU A 230 REMARK 465 PRO A 231 REMARK 465 ASN A 232 REMARK 465 LEU A 233 REMARK 465 GLN A 234 REMARK 465 ASN A 235 REMARK 465 PRO A 299 REMARK 465 ASP A 300 REMARK 465 GLU A 301 REMARK 465 ASP A 302 REMARK 465 PHE A 303 REMARK 465 SER A 304 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 HD2 PRO A 248 HA ALA A 257 1.30 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 GLN A 244 95.44 -176.90 REMARK 500 1 VAL A 247 70.87 -110.52 REMARK 500 1 ASP A 252 47.81 -95.38 REMARK 500 1 THR A 254 86.22 63.79 REMARK 500 1 ASN A 280 61.31 24.38 REMARK 500 2 GLN A 244 95.43 -176.35 REMARK 500 2 ASP A 252 56.54 -104.56 REMARK 500 2 THR A 254 75.54 59.26 REMARK 500 2 ASN A 280 56.52 34.40 REMARK 500 3 PRO A 237 147.73 -39.99 REMARK 500 3 GLN A 244 95.39 -176.17 REMARK 500 3 VAL A 247 75.67 -108.39 REMARK 500 3 ASP A 252 51.97 -96.88 REMARK 500 3 THR A 254 88.08 65.61 REMARK 500 3 ASN A 280 56.69 39.45 REMARK 500 4 GLN A 244 93.17 -176.59 REMARK 500 4 ASP A 252 65.45 -105.60 REMARK 500 4 ASN A 280 61.31 28.84 REMARK 500 4 HIS A 290 55.13 -119.98 REMARK 500 5 GLN A 244 94.06 -177.80 REMARK 500 5 VAL A 247 78.83 -104.13 REMARK 500 5 ASP A 252 49.19 -95.60 REMARK 500 5 THR A 254 77.63 59.55 REMARK 500 6 PRO A 237 141.79 -38.72 REMARK 500 6 GLN A 244 94.55 -176.30 REMARK 500 6 VAL A 247 75.33 -108.28 REMARK 500 6 ALA A 250 9.70 -69.46 REMARK 500 6 ASP A 252 67.96 -105.28 REMARK 500 6 THR A 254 73.48 55.66 REMARK 500 6 ASN A 280 57.19 33.65 REMARK 500 7 GLN A 244 102.60 -178.47 REMARK 500 7 VAL A 247 75.94 -100.85 REMARK 500 7 ASP A 252 49.27 -103.85 REMARK 500 7 THR A 254 81.94 61.12 REMARK 500 7 THR A 289 1.78 -68.62 REMARK 500 7 HIS A 290 33.71 -147.25 REMARK 500 7 GLN A 297 -34.95 175.33 REMARK 500 8 GLN A 244 94.08 -172.25 REMARK 500 8 VAL A 247 72.46 -110.48 REMARK 500 8 ASP A 252 63.73 -105.41 REMARK 500 8 ASN A 280 55.13 36.38 REMARK 500 9 GLN A 244 95.58 -178.22 REMARK 500 9 VAL A 247 75.48 -101.72 REMARK 500 9 ASP A 252 55.02 -93.34 REMARK 500 9 THR A 254 83.59 64.65 REMARK 500 9 ASN A 280 60.33 28.69 REMARK 500 9 GLN A 297 20.06 178.76 REMARK 500 10 GLN A 244 99.32 -173.78 REMARK 500 10 VAL A 247 77.45 -105.81 REMARK 500 10 ASP A 252 49.58 -102.73 REMARK 500 REMARK 500 THIS ENTRY HAS 95 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1CKA RELATED DB: PDB REMARK 900 N TERMINAL SH3 DOMAIN OF CRKII REMARK 900 RELATED ID: 1JEG RELATED DB: PDB REMARK 900 SH3 DOMAIN OF CSK DBREF 2GGR A 230 304 UNP Q64010 CRK_MOUSE 230 304 SEQADV 2GGR GLY A 229 UNP Q64010 CLONING ARTIFACT SEQRES 1 A 76 GLY LEU PRO ASN LEU GLN ASN GLY PRO ILE TYR ALA ARG SEQRES 2 A 76 VAL ILE GLN LYS ARG VAL PRO ASN ALA TYR ASP LYS THR SEQRES 3 A 76 ALA LEU ALA LEU GLU VAL GLY GLU LEU VAL LYS VAL THR SEQRES 4 A 76 LYS ILE ASN VAL SER GLY GLN TRP GLU GLY GLU CYS ASN SEQRES 5 A 76 GLY LYS ARG GLY HIS PHE PRO PHE THR HIS VAL ARG LEU SEQRES 6 A 76 LEU ASP GLN GLN ASN PRO ASP GLU ASP PHE SER HELIX 1 1 PRO A 287 THR A 289 5 3 SHEET 1 A 5 LYS A 282 PHE A 286 0 SHEET 2 A 5 TRP A 275 CYS A 279 -1 N CYS A 279 O LYS A 282 SHEET 3 A 5 GLU A 262 LYS A 268 -1 N LYS A 265 O GLU A 278 SHEET 4 A 5 ILE A 238 VAL A 242 -1 N ALA A 240 O VAL A 264 SHEET 5 A 5 VAL A 291 LEU A 294 -1 O LEU A 294 N TYR A 239 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