Header list of 1xx0.pdb file
Complete list - r 2 2 Bytes
HEADER LIPID BINDING PROTEIN 03-NOV-04 1XX0 TITLE STRUCTURE OF THE C-TERMINAL PH DOMAIN OF HUMAN PLECKSTRIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: PLECKSTRIN; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: C-TERMINAL PH DOMAIN; COMPND 5 SYNONYM: PLATELET P47 PROTEIN; COMPND 6 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: PLEK; 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: PET9D_MOD KEYWDS PLECKSTRIN, PH, C-TERMINAL, PLECKSTRIN HOMOLOGY, LIPID BINDING KEYWDS 2 PROTEIN EXPDTA SOLUTION NMR NUMMDL 10 AUTHOR C.EDLICH,G.STIER,B.SIMON,M.SATTLER,C.MUHLE-GOLL REVDAT 3 02-MAR-22 1XX0 1 REMARK SEQADV REVDAT 2 24-FEB-09 1XX0 1 VERSN REVDAT 1 03-MAY-05 1XX0 0 JRNL AUTH C.EDLICH,G.STIER,B.SIMON,M.SATTLER,C.MUHLE-GOLL JRNL TITL STRUCTURE AND PHOSPHATIDYLINOSITOL-(3,4)-BISPHOSPHATE JRNL TITL 2 BINDING OF THE C-TERMINAL PH DOMAIN OF HUMAN PLECKSTRIN JRNL REF STRUCTURE V. 13 277 2005 JRNL REFN ISSN 0969-2126 JRNL PMID 15698571 JRNL DOI 10.1016/J.STR.2004.11.012 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : ARIA 1.2 REMARK 3 AUTHORS : LINGE, J.P., O'DONOGHUE S.I., NILGES M. REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1XX0 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 09-NOV-04. REMARK 100 THE DEPOSITION ID IS D_1000030864. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 295 REMARK 210 PH : 6.8 REMARK 210 IONIC STRENGTH : 100MM NACL REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 0.5MM C-PH, U-15N,13C; 20MM REMARK 210 SODIUM PHOSPHATE BUFFER PH 6.8, REMARK 210 100MM NACL, 0.02% NAN3 REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ; 900 MHZ REMARK 210 SPECTROMETER MODEL : DRX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : ARIA 1.2 REMARK 210 METHOD USED : NULL REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 80 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST REMARK 210 ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD HETERONUCLEAR REMARK 210 TECHNIQUES. 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 1-10 REMARK 465 RES C SSSEQI REMARK 465 MET A 224 REMARK 465 LYS A 225 REMARK 465 HIS A 226 REMARK 465 HIS A 227 REMARK 465 HIS A 228 REMARK 465 HIS A 229 REMARK 465 HIS A 230 REMARK 465 HIS A 231 REMARK 465 PRO A 232 REMARK 465 MET A 233 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 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 LEU A 237 -164.99 -123.13 REMARK 500 1 ARG A 258 -44.99 -130.99 REMARK 500 1 GLU A 270 -169.95 -101.08 REMARK 500 1 ASP A 271 -70.17 95.64 REMARK 500 1 ALA A 273 93.95 70.13 REMARK 500 1 ALA A 283 73.02 -171.42 REMARK 500 1 ARG A 293 101.71 -52.37 REMARK 500 1 GLU A 301 29.09 -76.78 REMARK 500 1 SER A 302 76.25 56.68 REMARK 500 1 ASN A 303 33.27 -83.97 REMARK 500 1 SER A 309 76.87 -68.47 REMARK 500 1 GLU A 312 -68.42 -108.04 REMARK 500 1 ASN A 313 46.40 -85.63 REMARK 500 2 ARG A 257 -38.99 72.35 REMARK 500 2 LYS A 259 -90.13 67.87 REMARK 500 2 ASN A 260 -42.76 -170.16 REMARK 500 2 ASP A 271 -54.45 145.17 REMARK 500 2 ALA A 273 82.91 66.14 REMARK 500 2 ALA A 283 102.88 72.66 REMARK 500 2 ARG A 293 107.50 -54.88 REMARK 500 2 GLU A 301 39.55 -80.45 REMARK 500 2 ASN A 305 -60.76 76.60 REMARK 500 2 THR A 348 124.29 62.18 REMARK 500 3 VAL A 235 82.00 -66.64 REMARK 500 3 HIS A 256 -159.81 58.50 REMARK 500 3 ARG A 258 87.26 68.53 REMARK 500 3 LYS A 259 -68.54 -168.11 REMARK 500 3 ASP A 271 -72.78 93.13 REMARK 500 3 ALA A 273 85.67 64.93 REMARK 500 3 ALA A 283 107.06 -178.04 REMARK 500 3 ARG A 293 91.14 -58.60 REMARK 500 3 GLU A 301 45.83 -84.81 REMARK 500 3 ALA A 320 1.81 -67.60 REMARK 500 4 LEU A 237 109.65 -55.37 REMARK 500 4 ASN A 260 -167.39 -163.09 REMARK 500 4 ASP A 271 -76.11 94.63 REMARK 500 4 ALA A 273 98.32 66.31 REMARK 500 4 ARG A 293 99.93 -48.44 REMARK 500 4 SER A 302 85.27 64.43 REMARK 500 4 ARG A 307 -39.54 -142.84 REMARK 500 4 LYS A 308 23.73 -141.73 REMARK 500 4 GLU A 311 89.86 -58.15 REMARK 500 4 THR A 348 35.18 -87.66 REMARK 500 5 VAL A 235 70.70 -68.90 REMARK 500 5 ARG A 257 -170.48 62.82 REMARK 500 5 ARG A 258 37.37 -84.53 REMARK 500 5 ASN A 260 -100.12 58.94 REMARK 500 5 ASP A 271 -59.98 148.39 REMARK 500 5 ALA A 273 88.78 64.48 REMARK 500 5 ALA A 283 123.59 75.19 REMARK 500 REMARK 500 THIS ENTRY HAS 116 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL DBREF 1XX0 A 234 350 UNP P08567 PLEK_HUMAN 234 350 SEQADV 1XX0 MET A 224 UNP P08567 EXPRESSION TAG SEQADV 1XX0 LYS A 225 UNP P08567 EXPRESSION TAG SEQADV 1XX0 HIS A 226 UNP P08567 EXPRESSION TAG SEQADV 1XX0 HIS A 227 UNP P08567 EXPRESSION TAG SEQADV 1XX0 HIS A 228 UNP P08567 EXPRESSION TAG SEQADV 1XX0 HIS A 229 UNP P08567 EXPRESSION TAG SEQADV 1XX0 HIS A 230 UNP P08567 EXPRESSION TAG SEQADV 1XX0 HIS A 231 UNP P08567 EXPRESSION TAG SEQADV 1XX0 PRO A 232 UNP P08567 EXPRESSION TAG SEQADV 1XX0 MET A 233 UNP P08567 EXPRESSION TAG SEQRES 1 A 127 MET LYS HIS HIS HIS HIS HIS HIS PRO MET ASP VAL ILE SEQRES 2 A 127 LEU LYS GLU GLU PHE ARG GLY VAL ILE ILE LYS GLN GLY SEQRES 3 A 127 CYS LEU LEU LYS GLN GLY HIS ARG ARG LYS ASN TRP LYS SEQRES 4 A 127 VAL ARG LYS PHE ILE LEU ARG GLU ASP PRO ALA TYR LEU SEQRES 5 A 127 HIS TYR TYR ASP PRO ALA GLY ALA GLU ASP PRO LEU GLY SEQRES 6 A 127 ALA ILE HIS LEU ARG GLY CYS VAL VAL THR SER VAL GLU SEQRES 7 A 127 SER ASN SER ASN GLY ARG LYS SER GLU GLU GLU ASN LEU SEQRES 8 A 127 PHE GLU ILE ILE THR ALA ASP GLU VAL HIS TYR PHE LEU SEQRES 9 A 127 GLN ALA ALA THR PRO LYS GLU ARG THR GLU TRP ILE LYS SEQRES 10 A 127 ALA ILE GLN MET ALA SER ARG THR GLY LYS HELIX 1 1 LYS A 238 ARG A 242 5 5 HELIX 2 2 THR A 331 SER A 346 1 16 SHEET 1 A 7 ALA A 283 HIS A 291 0 SHEET 2 A 7 TYR A 274 ASP A 279 -1 N LEU A 275 O ILE A 290 SHEET 3 A 7 TRP A 261 ARG A 269 -1 N ILE A 267 O HIS A 276 SHEET 4 A 7 ILE A 245 GLN A 254 -1 N LEU A 251 O ARG A 264 SHEET 5 A 7 HIS A 324 GLN A 328 -1 O GLN A 328 N LEU A 252 SHEET 6 A 7 LEU A 314 ILE A 318 -1 N ILE A 317 O TYR A 325 SHEET 7 A 7 VAL A 296 SER A 299 -1 N VAL A 296 O ILE A 318 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 2 2 Bytes