Header list of 1ywi.pdb file
Complete list - 2 20 Bytes
HEADER STRUCTURAL PROTEIN 18-FEB-05 1YWI TITLE STRUCTURE OF THE FBP11WW1 DOMAIN COMPLEXED TO THE PEPTIDE APPTPPPLPP COMPND MOL_ID: 1; COMPND 2 MOLECULE: FORMIN-BINDING PROTEIN 3; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: WW1 DOMAIN; COMPND 5 SYNONYM: FORMIN BINDING PROTEIN 11; COMPND 6 ENGINEERED: YES; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: FORMIN; COMPND 9 CHAIN: B; COMPND 10 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21 DE3; SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PGEX-2TK; SOURCE 10 MOL_ID: 2; SOURCE 11 SYNTHETIC: YES; SOURCE 12 OTHER_DETAILS: AUTOMATED SOLID PHASE SYNTHESIS ON CHLORTRITYL RESIN SOURCE 13 USING FMOC STRATEGY KEYWDS WW DOMAIN, CLASS II, PROLINE-RICH PEPTIDES, PROTEIN-PROTEIN KEYWDS 2 INTERACTIONS, STRUCTURAL PROTEIN EXPDTA SOLUTION NMR NUMMDL 15 AUTHOR J.R.PIRES,C.PARTHIER,R.AIDO-MACHADO,U.WIEDEMANN,L.OTTE,G.BOEHM, AUTHOR 2 R.RUDOLPH,H.OSCHKINAT REVDAT 3 02-MAR-22 1YWI 1 REMARK SEQADV REVDAT 2 24-FEB-09 1YWI 1 VERSN REVDAT 1 12-APR-05 1YWI 0 JRNL AUTH J.R.PIRES,C.PARTHIER,R.AIDO-MACHADO,U.WIEDEMANN,L.OTTE, JRNL AUTH 2 G.BOHM,R.RUDOLPH,H.OSCHKINAT JRNL TITL STRUCTURAL BASIS FOR APPTPPPLPP PEPTIDE RECOGNITION BY THE JRNL TITL 2 FBP11WW1 DOMAIN. JRNL REF J.MOL.BIOL. V. 348 399 2005 JRNL REFN ISSN 0022-2836 JRNL PMID 15811376 JRNL DOI 10.1016/J.JMB.2005.02.056 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS 1.1 REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE REMARK 3 -KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,READ,RICE, REMARK 3 SIMONSON,WARREN REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURE WAS ALSO REFINED WITH REMARK 3 ARIA VER.1.2, AUTHORS: LINGE, J.P., O'DONGUE, S.I., NILGES, M. REMARK 4 REMARK 4 1YWI COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 22-FEB-05. REMARK 100 THE DEPOSITION ID IS D_1000032000. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 6.0 REMARK 210 IONIC STRENGTH : 100MM NACL REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : 1.8MM [U-15N,13C] FBP11WW1, REMARK 210 3.6MM APPTPPPLPP, 10MM PHOSPHATE REMARK 210 BUFFER, 100MM NACL, 0.1MM DTT, REMARK 210 0.1MM EDTA; 1.8MM [U-15N,13C] REMARK 210 FBP11WW1, 3.6MM APPTPPPLPP, 10MM REMARK 210 PHOSPHATE BUFFER, 100MM NACL, REMARK 210 0.1MM DTT, 0.1MM EDTA; 1.8MM [U- REMARK 210 15N] FBP11WW1, 3.6MM APPTPPPLPP, REMARK 210 10MM PHOSPHATE BUFFER, 100MM REMARK 210 NACL, 0.1MM DTT, 0.1MM EDTA; REMARK 210 1.8MM FBP11WW1, 3.6MM APPTPPPLPP, REMARK 210 10MM PHOSPHATE BUFFER, 100MM REMARK 210 NACL, 0.1MM DTT, 0.1MM EDTA REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : TRIPLE-RESONANCE; 3D_13C REMARK 210 -SEPARATED_NOESY; 3D_15N- REMARK 210 SEPARATED_NOESY; 2D NOESY; 2D REMARK 210 TOCSY REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ REMARK 210 SPECTROMETER MODEL : DRX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : XWINNMR 3.2, SPARKY 3.1 REMARK 210 METHOD USED : AUTOMATED ASSIGNMENT OF NOES AND REMARK 210 SIMULATED ANNELING WITH TORSION REMARK 210 ANGLE DINAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 200 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 15 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: 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: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B 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 1-15 REMARK 465 RES C SSSEQI REMARK 465 GLY A 4 REMARK 465 SER A 5 REMARK 465 ARG A 6 REMARK 465 ARG A 7 REMARK 465 ALA A 8 REMARK 465 SER A 9 REMARK 465 VAL A 10 REMARK 465 GLY A 11 REMARK 465 SER A 12 REMARK 465 ALA A 13 REMARK 465 LYS A 14 REMARK 465 ASP A 43 REMARK 465 ASP A 44 REMARK 465 ALA B 1 REMARK 465 PRO B 2 REMARK 465 PRO B 3 REMARK 465 THR B 4 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 MET A 16 85.22 59.28 REMARK 500 1 LYS A 35 62.51 72.03 REMARK 500 1 GLU A 40 147.38 62.83 REMARK 500 2 LYS A 35 66.33 67.94 REMARK 500 2 GLU A 40 137.03 64.16 REMARK 500 3 MET A 16 67.89 62.67 REMARK 500 3 LYS A 35 77.26 69.07 REMARK 500 3 GLU A 40 138.00 65.60 REMARK 500 4 MET A 16 96.40 58.19 REMARK 500 4 LYS A 35 65.98 62.60 REMARK 500 4 GLU A 40 136.97 64.47 REMARK 500 5 GLU A 33 -74.06 -83.12 REMARK 500 5 LYS A 35 65.34 69.46 REMARK 500 5 GLU A 40 136.09 62.99 REMARK 500 6 LYS A 35 65.19 72.71 REMARK 500 6 GLU A 40 133.28 169.39 REMARK 500 7 LYS A 35 67.74 66.28 REMARK 500 7 GLU A 40 138.26 64.50 REMARK 500 8 MET A 16 62.64 69.91 REMARK 500 8 LYS A 35 78.64 71.03 REMARK 500 8 GLU A 40 141.58 64.11 REMARK 500 9 MET A 16 71.93 66.84 REMARK 500 9 LYS A 35 68.68 71.55 REMARK 500 9 GLU A 40 139.82 62.84 REMARK 500 10 MET A 16 56.71 70.26 REMARK 500 10 LYS A 35 67.46 72.27 REMARK 500 10 GLU A 40 142.46 65.91 REMARK 500 11 LYS A 35 60.43 68.05 REMARK 500 11 GLU A 40 137.03 64.18 REMARK 500 12 MET A 16 61.50 71.44 REMARK 500 12 LYS A 35 71.28 61.14 REMARK 500 12 GLU A 40 148.84 63.39 REMARK 500 13 MET A 16 68.48 68.22 REMARK 500 13 LYS A 35 64.17 72.75 REMARK 500 13 GLU A 40 136.92 64.64 REMARK 500 14 MET A 16 60.77 70.03 REMARK 500 14 GLU A 33 -67.99 -91.32 REMARK 500 14 LYS A 35 70.89 73.92 REMARK 500 14 GLU A 40 147.65 62.70 REMARK 500 15 LYS A 35 65.35 70.41 REMARK 500 15 GLU A 40 139.14 63.13 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1F8A RELATED DB: PDB REMARK 900 RELATED ID: 1I5H RELATED DB: PDB REMARK 900 RELATED ID: 1EG4 RELATED DB: PDB REMARK 900 RELATED ID: 1CKA RELATED DB: PDB REMARK 900 RELATED ID: 1O6W RELATED DB: PDB REMARK 900 RELATED ID: 1YWJ RELATED DB: PDB REMARK 900 THE SAME PROTEIN OF THE FBP11WW1 DOMAIN DBREF 1YWI A 13 44 UNP O75400 FNBP3_HUMAN 142 173 DBREF 1YWI B 1 10 PDB 1YWI 1YWI 1 10 SEQADV 1YWI GLY A 4 UNP O75400 CLONING ARTIFACT SEQADV 1YWI SER A 5 UNP O75400 CLONING ARTIFACT SEQADV 1YWI ARG A 6 UNP O75400 CLONING ARTIFACT SEQADV 1YWI ARG A 7 UNP O75400 CLONING ARTIFACT SEQADV 1YWI ALA A 8 UNP O75400 CLONING ARTIFACT SEQADV 1YWI SER A 9 UNP O75400 CLONING ARTIFACT SEQADV 1YWI VAL A 10 UNP O75400 CLONING ARTIFACT SEQADV 1YWI GLY A 11 UNP O75400 CLONING ARTIFACT SEQADV 1YWI SER A 12 UNP O75400 CLONING ARTIFACT SEQRES 1 A 41 GLY SER ARG ARG ALA SER VAL GLY SER ALA LYS SER MET SEQRES 2 A 41 TRP THR GLU HIS LYS SER PRO ASP GLY ARG THR TYR TYR SEQRES 3 A 41 TYR ASN THR GLU THR LYS GLN SER THR TRP GLU LYS PRO SEQRES 4 A 41 ASP ASP SEQRES 1 B 10 ALA PRO PRO THR PRO PRO PRO LEU PRO PRO SHEET 1 A 3 TRP A 17 SER A 22 0 SHEET 2 A 3 ARG A 26 ASN A 31 -1 O TYR A 28 N HIS A 20 SHEET 3 A 3 GLN A 36 TRP A 39 -1 O THR A 38 N TYR A 29 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 - 2 20 Bytes