Header list of 2g57.pdb file
Complete list - 9 20 Bytes
HEADER ONCOPROTEIN 22-FEB-06 2G57 TITLE STRUCTURE OF THE PHOSPHORYLATION MOTIF OF THE ONCOGENIC PROTEIN BETA- TITLE 2 CATENIN RECOGNIZED BY A SELECTIVE MONOCLONAL ANTIBODY COMPND MOL_ID: 1; COMPND 2 MOLECULE: BETA-CATENIN; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: RESIDUES 19-44; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 SYNTHETIC: YES; SOURCE 3 OTHER_DETAILS: THIS SEQUENCE OCCURS NATURALLY IN HUMANS. KEYWDS BETA-CATENIN ONCOGENIC PROTEIN, P-BETA-CATENIN PHOSPHORYLATED KEYWDS 2 PEPTIDE, EPITOPE MAPPING, ANTIBODY, P-BETA-CATENIN-ANTIBODY COMPLEX, KEYWDS 3 STD-NMR, TRNOESY, RESTRAINED MOLECULAR DYNAMICS, BOUND STRUCTURE, KEYWDS 4 BINDING FRAGMENT, ONCOPROTEIN EXPDTA SOLUTION NMR NUMMDL 10 AUTHOR S.MEGY,G.BERTHO,J.GHARBI-BENAROUS,F.BALEUX,R.BENAROUS,J.P.GIRAULT REVDAT 4 09-MAR-22 2G57 1 REMARK SEQADV LINK REVDAT 3 24-FEB-09 2G57 1 VERSN REVDAT 2 10-OCT-06 2G57 1 JRNL REVDAT 1 28-MAR-06 2G57 0 JRNL AUTH S.MEGY,G.BERTHO,J.GHARBI-BENAROUS,F.BALEUX,R.BENAROUS, JRNL AUTH 2 J.P.GIRAULT JRNL TITL STD AND TRNOESY NMR STUDIES FOR THE EPITOPE MAPPING OF THE JRNL TITL 2 PHOSPHORYLATION MOTIF OF THE ONCOGENIC PROTEIN BETA-CATENIN JRNL TITL 3 RECOGNIZED BY A SELECTIVE MONOCLONAL ANTIBODY JRNL REF FEBS LETT. V. 580 5411 2006 JRNL REFN ISSN 0014-5793 JRNL PMID 16996060 JRNL DOI 10.1016/J.FEBSLET.2006.08.084 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XWINNMR, ARIA 1.2 REMARK 3 AUTHORS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 2G57 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 24-FEB-06. REMARK 100 THE DEPOSITION ID IS D_1000036702. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 278 REMARK 210 PH : 7.4 REMARK 210 IONIC STRENGTH : 20MM REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : 1MM P-BETA-CAT PEPTIDE WITH REMARK 210 0.01MM ANTIBODY; 20MM PHOSPHATE REMARK 210 BUFFERED SALINE(PH 7.4); 15MM REMARK 210 SODIUM AZIDE; 90% H2O, 10% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ REMARK 210 SPECTROMETER MODEL : AVANCE REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : FELIX REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED REMARK 210 ANNEALING, TORSION ANGLE DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 20 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST REMARK 210 RESTRAINT VIOLATIONS 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 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 28 -18.65 -142.44 REMARK 500 1 HIS A 36 13.39 58.31 REMARK 500 1 SEP A 37 15.75 58.49 REMARK 500 2 THR A 41 38.51 -156.26 REMARK 500 2 ALA A 43 -51.00 -157.20 REMARK 500 3 GLN A 28 -31.84 -132.69 REMARK 500 3 ASP A 32 -74.30 -73.46 REMARK 500 3 SEP A 33 -80.87 60.99 REMARK 500 3 THR A 41 32.11 -151.07 REMARK 500 3 ALA A 43 77.18 51.83 REMARK 500 4 ILE A 35 74.35 55.75 REMARK 500 4 THR A 41 34.69 -147.80 REMARK 500 4 ALA A 43 88.01 57.00 REMARK 500 5 ILE A 35 -37.77 -130.41 REMARK 500 5 HIS A 36 42.86 -81.38 REMARK 500 5 ALA A 39 -8.52 71.68 REMARK 500 5 THR A 41 29.68 173.90 REMARK 500 5 THR A 42 8.98 59.21 REMARK 500 5 ALA A 43 80.30 50.08 REMARK 500 6 SEP A 37 17.06 56.23 REMARK 500 7 HIS A 36 10.99 58.43 REMARK 500 7 ALA A 43 -50.67 -171.06 REMARK 500 8 SEP A 33 12.79 -145.39 REMARK 500 8 HIS A 36 -2.85 67.57 REMARK 500 8 THR A 40 24.75 -147.30 REMARK 500 8 THR A 42 31.22 -142.56 REMARK 500 9 GLN A 28 -10.61 -143.57 REMARK 500 9 THR A 41 26.95 -169.53 REMARK 500 9 ALA A 43 76.02 46.99 REMARK 500 10 GLN A 28 -1.01 -144.03 REMARK 500 10 ILE A 35 97.07 68.87 REMARK 500 10 HIS A 36 104.03 51.67 REMARK 500 10 SEP A 37 -9.85 -54.79 REMARK 500 REMARK 500 REMARK: NULL REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACE A 18 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NH2 A 45 DBREF 2G57 A 19 44 UNP P35222 CTNB1_HUMAN 19 44 SEQADV 2G57 SEP A 33 UNP P35222 SER 33 MODIFIED RESIDUE SEQADV 2G57 SEP A 37 UNP P35222 SER 37 MODIFIED RESIDUE SEQRES 1 A 28 ACE LYS ALA ALA VAL SER HIS TRP GLN GLN GLN SER TYR SEQRES 2 A 28 LEU ASP SEP GLY ILE HIS SEP GLY ALA THR THR THR ALA SEQRES 3 A 28 PRO NH2 MODRES 2G57 SEP A 33 SER PHOSPHOSERINE MODRES 2G57 SEP A 37 SER PHOSPHOSERINE HET ACE A 18 6 HET SEP A 33 14 HET SEP A 37 14 HET NH2 A 45 3 HETNAM ACE ACETYL GROUP HETNAM SEP PHOSPHOSERINE HETNAM NH2 AMINO GROUP HETSYN SEP PHOSPHONOSERINE FORMUL 1 ACE C2 H4 O FORMUL 1 SEP 2(C3 H8 N O6 P) FORMUL 1 NH2 H2 N LINK C ACE A 18 N LYS A 19 1555 1555 1.33 LINK C ASP A 32 N SEP A 33 1555 1555 1.33 LINK C SEP A 33 N GLY A 34 1555 1555 1.33 LINK C HIS A 36 N SEP A 37 1555 1555 1.33 LINK C SEP A 37 N GLY A 38 1555 1555 1.33 LINK C PRO A 44 N NH2 A 45 1555 1555 1.33 SITE 1 AC1 1 VAL A 22 SITE 1 AC2 1 PRO A 44 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 - 9 20 Bytes