Header list of 2bbu.pdb file
Complete list - r 9 2 Bytes
HEADER CYTOKINE REGULATOR 17-OCT-05 2BBU TITLE SOLUTION STRUCTURE OF MOUSE SOCS3 IN COMPLEX WITH A PHOSPHOPEPTIDE TITLE 2 FROM THE GP130 RECEPTOR COMPND MOL_ID: 1; COMPND 2 MOLECULE: SUPPRESSOR OF CYTOKINE SIGNALING 3; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: KIR/ESS/SH2 DOMAIN/PEST MOTIF; COMPND 5 SYNONYM: SOCS-3, CYTOKINE-INDUCIBLE SH2 PROTEIN 3, CIS-3, PROTEIN EF- COMPND 6 10; COMPND 7 ENGINEERED: YES; COMPND 8 MOL_ID: 2; COMPND 9 MOLECULE: GP130 PHOSPHOPEPTIDE; COMPND 10 CHAIN: B; COMPND 11 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: SOCS3; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: JLIC1; SOURCE 11 MOL_ID: 2; SOURCE 12 SYNTHETIC: YES; SOURCE 13 OTHER_DETAILS: SYNTHETIC PHOSPHOPEPTIDE KEYWDS SH2 DOMAIN, EXTENDED SH2 SUBDOMAIN, PEST MOTIF, PROTEIN COMPLEX, KEYWDS 2 PHOSPHOPEPTIDE, CYTOKINE REGULATOR EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR J.J.BABON,S.YAO,R.S.NORTON REVDAT 3 09-MAR-22 2BBU 1 REMARK LINK REVDAT 2 24-FEB-09 2BBU 1 VERSN REVDAT 1 02-MAY-06 2BBU 0 JRNL AUTH J.J.BABON,E.J.MCMANUS,S.YAO,D.P.DESOUZA,L.A.MIELKE, JRNL AUTH 2 N.S.SPRIGG,T.A.WILLSON,D.J.HILTON,N.A.NICOLA,M.BACA, JRNL AUTH 3 S.E.NICHOLSON,R.S.NORTON JRNL TITL THE STRUCTURE OF SOCS3 REVEALS THE BASIS OF THE EXTENDED SH2 JRNL TITL 2 DOMAIN FUNCTION AND IDENTIFIES AN UNSTRUCTURED INSERTION JRNL TITL 3 THAT REGULATES STABILITY JRNL REF MOL.CELL V. 22 205 2006 JRNL REFN ISSN 1097-2765 JRNL PMID 16630890 JRNL DOI 10.1016/J.MOLCEL.2006.03.024 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : NMRPIPE, X-PLOR REMARK 3 AUTHORS : DELAGLIO (NMRPIPE), BRUNGER (X-PLOR) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 2BBU COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 25-OCT-05. REMARK 100 THE DEPOSITION ID IS D_1000034916. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 6.7 REMARK 210 IONIC STRENGTH : 50MM REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : 0.3MM U-15N-13C-SOCS3/0.3MM REMARK 210 PHOPHOPEPTIDE, 20MM NA-PHOSPHATE, REMARK 210 PH 6.7, 2MM DTT, 1MM EDTA, 50MM REMARK 210 GLUTAMATE, 50MM ARGININE, 5% D2O; REMARK 210 0.3MM U-15N-SOCS3/0.3MM REMARK 210 PHOPHOPEPTIDE, 20MM NA-PHOSPHATE, REMARK 210 PH 6.7, 2MM DTT, 1MM EDTA, 50MM REMARK 210 GLUTAMATE, 50MM ARGININE, 5% D2O; REMARK 210 0.3MM U-13C-SOCS3/0.3MM REMARK 210 PHOPHOPEPTIDE, 20MM NA-PHOSPHATE, REMARK 210 PH 6.7, 2MM DTT, 1MM EDTA, 50MM REMARK 210 GLUTAMATE, 50MM ARGININE, 5% D2O; REMARK 210 0.3MM SOCS3/0.3MM PHOPHOPEPTIDE, REMARK 210 20MM NA-PHOSPHATE, PH 6.7, 2MM REMARK 210 DTT, 1MM EDTA, 50MM GLUTAMATE, REMARK 210 50MM ARGININE, 5% D2O; 0.3MM REMARK 210 SOCS3/0.3MM PHOPHOPEPTIDE, 20MM REMARK 210 NA-PHOSPHATE, PH 6.7, 2MM DTT, REMARK 210 1MM EDTA, 50MM GLUTAMATE, 50MM REMARK 210 ARGININE, 5% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C REMARK 210 -SEPARATED_NOESY; 2D NOESY; 2D REMARK 210 TOCSY REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 800 MHZ REMARK 210 SPECTROMETER MODEL : AVANCE; DRX; INOVA REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : XWINNMR, X-PLOR REMARK 210 METHOD USED : SIMULATED ANNEALING DISTANCE REMARK 210 GEOMETRY TORSION ANGLE DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 200 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH FAVORABLE NON REMARK 210 -BOND 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 1-20 REMARK 465 RES C SSSEQI REMARK 465 LEU A -7 REMARK 465 LYS A -6 REMARK 465 THR A -5 REMARK 465 PHE A -4 REMARK 465 SER A -3 REMARK 465 SER A -2 REMARK 465 LYS A -1 REMARK 465 SER A 0 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 OH TYR A 139 H HIS B 169 1.53 REMARK 500 O VAL A 9 H GLN A 13 1.54 REMARK 500 H SER A 140 O GLU A 143 1.54 REMARK 500 O LEU A 64 HH TYR A 98 1.56 REMARK 500 H GLN A 67 O SER A 74 1.57 REMARK 500 O VAL A 91 H VAL A 95 1.59 REMARK 500 O ALA A 8 H LEU A 12 1.59 REMARK 500 O TYR A 136 O LEU A 147 2.15 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 ALA A 21 -4.14 164.98 REMARK 500 1 VAL A 22 -159.84 -108.85 REMARK 500 1 GLU A 34 -79.80 -122.12 REMARK 500 1 SER A 45 -145.49 -64.88 REMARK 500 1 ASP A 46 -138.07 67.27 REMARK 500 1 GLN A 76 -157.34 -145.83 REMARK 500 1 SER A 81 56.02 -144.23 REMARK 500 1 PRO A 84 -162.95 -72.38 REMARK 500 1 PHE A 88 -154.07 -58.66 REMARK 500 1 CYS A 90 -109.63 -37.66 REMARK 500 1 PRO A 102 -157.81 -73.13 REMARK 500 1 THR A 104 159.87 -42.43 REMARK 500 1 PHE A 107 92.82 -161.62 REMARK 500 1 SER A 108 -81.69 57.81 REMARK 500 1 LEU A 109 -56.28 173.49 REMARK 500 1 SER A 116 -145.92 -70.28 REMARK 500 1 GLU A 117 104.53 -55.94 REMARK 500 1 VAL A 118 75.64 -154.25 REMARK 500 1 GLU A 120 71.85 53.30 REMARK 500 1 GLN A 125 -81.09 -91.48 REMARK 500 1 LEU A 127 52.68 -155.97 REMARK 500 1 LYS A 133 120.04 61.99 REMARK 500 1 ALA A 135 140.18 169.98 REMARK 500 1 SER A 150 54.83 -167.60 REMARK 500 1 SER A 154 78.77 -117.79 REMARK 500 1 SER A 155 -166.16 42.65 REMARK 500 1 ALA B 159 -88.16 179.63 REMARK 500 1 THR B 161 -36.46 -133.89 REMARK 500 1 PTR B 164 -162.58 174.83 REMARK 500 1 SER B 165 -105.93 -139.47 REMARK 500 1 VAL B 168 76.30 22.23 REMARK 500 1 HIS B 169 -78.67 -44.72 REMARK 500 1 SER B 170 -76.73 -128.64 REMARK 500 2 PHE A 17 28.17 -145.39 REMARK 500 2 SER A 20 -15.60 178.98 REMARK 500 2 VAL A 22 -154.51 -99.39 REMARK 500 2 GLU A 34 -80.59 -122.90 REMARK 500 2 ASP A 46 -135.42 -102.30 REMARK 500 2 HIS A 49 90.26 46.99 REMARK 500 2 THR A 57 -154.02 -97.70 REMARK 500 2 SER A 59 29.36 -177.02 REMARK 500 2 GLN A 76 -139.83 -109.78 REMARK 500 2 SER A 77 44.83 -164.49 REMARK 500 2 SER A 81 169.25 174.96 REMARK 500 2 THR A 82 71.70 -104.75 REMARK 500 2 PRO A 84 -99.06 -71.40 REMARK 500 2 MET A 99 114.99 -167.16 REMARK 500 2 PRO A 105 -91.46 -72.99 REMARK 500 2 SER A 106 -41.36 -131.21 REMARK 500 2 THR A 112 99.00 53.79 REMARK 500 REMARK 500 THIS ENTRY HAS 676 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL DBREF 2BBU A -7 156 UNP O35718 SOCS3_MOUSE 22 185 DBREF 2BBU B 157 171 PDB 2BBU 2BBU 157 171 SEQRES 1 A 164 LEU LYS THR PHE SER SER LYS SER GLU TYR GLN LEU VAL SEQRES 2 A 164 VAL ASN ALA VAL ARG LYS LEU GLN GLU SER GLY PHE TYR SEQRES 3 A 164 TRP SER ALA VAL THR GLY GLY GLU ALA ASN LEU LEU LEU SEQRES 4 A 164 SER ALA GLU PRO ALA GLY THR PHE LEU ILE ARG ASP SER SEQRES 5 A 164 SER ASP GLN ARG HIS PHE PHE THR LEU SER VAL LYS THR SEQRES 6 A 164 GLN SER GLY THR LYS ASN LEU ARG ILE GLN CYS GLU GLY SEQRES 7 A 164 GLY SER PHE SER LEU GLN SER ASP PRO ARG SER THR GLN SEQRES 8 A 164 PRO VAL PRO ARG PHE ASP CYS VAL LEU LYS LEU VAL HIS SEQRES 9 A 164 HIS TYR MET PRO PRO PRO GLY THR PRO SER PHE SER LEU SEQRES 10 A 164 PRO PRO THR GLU PRO SER SER GLU VAL PRO GLU GLN PRO SEQRES 11 A 164 PRO ALA GLN ALA LEU PRO GLY SER THR PRO LYS ARG ALA SEQRES 12 A 164 TYR TYR ILE TYR SER GLY GLY GLU LYS ILE PRO LEU VAL SEQRES 13 A 164 LEU SER ARG PRO LEU SER SER ASN SEQRES 1 B 15 SER THR ALA SER THR VAL GLU PTR SER THR VAL VAL HIS SEQRES 2 B 15 SER GLY MODRES 2BBU PTR B 164 TYR O-PHOSPHOTYROSINE HET PTR B 164 24 HETNAM PTR O-PHOSPHOTYROSINE HETSYN PTR PHOSPHONOTYROSINE FORMUL 2 PTR C9 H12 N O6 P HELIX 1 1 GLU A 1 SER A 15 1 15 HELIX 2 2 THR A 23 GLU A 34 1 12 HELIX 3 3 ASP A 89 MET A 99 1 11 SHEET 1 A 3 LEU A 40 ASP A 43 0 SHEET 2 A 3 PHE A 51 VAL A 55 -1 O THR A 52 N ARG A 42 SHEET 3 A 3 LYS A 62 ARG A 65 -1 O LEU A 64 N LEU A 53 SHEET 1 B 2 GLN A 67 GLU A 69 0 SHEET 2 B 2 SER A 72 SER A 74 -1 O SER A 74 N GLN A 67 SHEET 1 C 2 ILE A 138 TYR A 139 0 SHEET 2 C 2 LYS A 144 ILE A 145 -1 O ILE A 145 N ILE A 138 LINK C GLU B 163 N PTR B 164 1555 1555 1.31 LINK C PTR B 164 N SER B 165 1555 1555 1.31 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