Header list of 2afj.pdb file
Complete list - r 9 2 Bytes
HEADER GENE REGULATION 26-JUL-05 2AFJ TITLE SPRY DOMAIN-CONTAINING SOCS BOX PROTEIN 2 (SSB-2) COMPND MOL_ID: 1; COMPND 2 MOLECULE: GENE RICH CLUSTER, C9 GENE; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: N-TERMINAL DOMAIN PLUS THE SPRY DOMAIN; COMPND 5 SYNONYM: SPRY DOMAIN-CONTAINING SOCS BOX PROTEIN SSB-2; 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: SSB-2; 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: PGEX-2T KEYWDS BETA SANDWICH, GENE REGULATION EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR S.L.MASTERS,S.YAO,T.A.WILLSON,J.G.ZHANG,K.R.PALMER,B.J.SMITH, AUTHOR 2 J.J.BABON,N.A.NICOLA,R.S.NORTON,S.E.NICHOLSON REVDAT 4 09-MAR-22 2AFJ 1 REMARK SEQADV REVDAT 3 24-FEB-09 2AFJ 1 VERSN REVDAT 2 24-JAN-06 2AFJ 1 JRNL REVDAT 1 03-JAN-06 2AFJ 0 JRNL AUTH S.L.MASTERS,S.YAO,T.A.WILLSON,J.G.ZHANG,K.R.PALMER, JRNL AUTH 2 B.J.SMITH,J.J.BABON,N.A.NICOLA,R.S.NORTON,S.E.NICHOLSON JRNL TITL THE SPRY DOMAIN OF SSB-2 ADOPTS A NOVEL FOLD THAT PRESENTS JRNL TITL 2 CONSERVED PAR-4-BINDING RESIDUES JRNL REF NAT.STRUCT.MOL.BIOL. V. 13 77 2006 JRNL REFN ISSN 1545-9993 JRNL PMID 16369487 JRNL DOI 10.1038/NSMB1034 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XWINNMR 3.5, X-PLOR 2.9.3 REMARK 3 AUTHORS : BRUKER, BIOSPIN (XWINNMR), SCHWIETERS (X-PLOR) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF REMARK 3 2074, 1738 ARE NON-REDUNDANT NOE-DERIVED DISTANCE CONSTRAINTS, REMARK 3 260 DIHEDRAL ANGLE RESTRAINTS, 76 DISTANTCE RESTRAINTS FROM REMARK 3 HYDROGEN BONDS. REMARK 4 REMARK 4 2AFJ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 27-JUL-05. REMARK 100 THE DEPOSITION ID IS D_1000033832. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 295 REMARK 210 PH : 7.0 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 0.4MM U-15N; 0.6MM U-15N, 13C; REMARK 210 1.0MM U-15N, 13C, 50% RANDOM 2H; REMARK 210 0.4MM U-15N REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C REMARK 210 -SEPARATED_NOESY; HNHA; 2D NOESY; REMARK 210 1H-15N HSQC REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 800 MHZ REMARK 210 SPECTROMETER MODEL : AVANCE; DRX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : XWINNMR 3.5, XEASY 1.3, CYANA REMARK 210 1.0.6, X-PLOR 2.9.3 REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS, REMARK 210 SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 194 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH ACCEPTABLE REMARK 210 COVALENT GEOMETRY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR REMARK 210 SPECTROSCOPY. CONSTRANTS FOR BACKBONE PHI AND PSI WERE ALSO REMARK 210 OBTAINED FROM PROGRAM TALOS USING BACKBONE CHEMICAL SHIFTS. 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: 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 HD3 ARG A 82 H GLY A 83 1.27 REMARK 500 O LEU A 29 H LEU A 32 1.42 REMARK 500 OD1 ASP A 52 HE ARG A 82 1.49 REMARK 500 O GLU A 30 H SER A 34 1.54 REMARK 500 O ALA A 109 H TYR A 200 1.58 REMARK 500 H GLU A 92 O ARG A 215 1.59 REMARK 500 O SER A 94 H ARG A 213 1.59 REMARK 500 O VAL A 105 H SER A 204 1.59 REMARK 500 O PRO A 38 N LEU A 40 2.18 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 SER A 7 44.66 -145.16 REMARK 500 1 ARG A 10 -71.93 -89.67 REMARK 500 1 SER A 12 -153.39 -127.79 REMARK 500 1 THR A 15 68.43 -115.48 REMARK 500 1 ALA A 18 101.45 -58.28 REMARK 500 1 LEU A 19 -155.08 179.85 REMARK 500 1 TYR A 20 -102.38 -91.79 REMARK 500 1 ASP A 22 66.91 -167.72 REMARK 500 1 PHE A 23 -104.45 -76.70 REMARK 500 1 GLU A 27 45.11 179.68 REMARK 500 1 ALA A 35 -169.99 -72.58 REMARK 500 1 ASP A 39 61.39 3.30 REMARK 500 1 LEU A 40 -45.47 -149.66 REMARK 500 1 TRP A 48 70.56 -103.52 REMARK 500 1 LYS A 51 -95.73 179.81 REMARK 500 1 ASP A 52 33.97 -68.97 REMARK 500 1 SER A 54 101.73 -50.60 REMARK 500 1 GLU A 61 -121.80 -66.21 REMARK 500 1 LEU A 64 88.76 0.61 REMARK 500 1 PRO A 70 -113.50 -72.16 REMARK 500 1 GLN A 73 -34.33 -36.11 REMARK 500 1 SER A 74 -36.52 -149.54 REMARK 500 1 LYS A 81 -97.55 -126.18 REMARK 500 1 ARG A 82 -87.41 -43.33 REMARK 500 1 GLN A 99 -83.71 -42.61 REMARK 500 1 ARG A 100 -59.75 -167.67 REMARK 500 1 THR A 102 -150.55 -156.21 REMARK 500 1 HIS A 103 113.05 -179.68 REMARK 500 1 ALA A 113 109.99 -36.02 REMARK 500 1 PRO A 114 -156.37 -72.81 REMARK 500 1 LEU A 115 59.21 -171.87 REMARK 500 1 GLN A 116 -70.99 -102.07 REMARK 500 1 ALA A 117 56.61 -114.59 REMARK 500 1 ASP A 118 146.65 -32.06 REMARK 500 1 ALA A 121 -67.88 173.48 REMARK 500 1 ALA A 122 88.44 178.65 REMARK 500 1 LEU A 123 -66.52 -98.88 REMARK 500 1 LEU A 124 -153.73 177.27 REMARK 500 1 SER A 126 -101.04 -123.91 REMARK 500 1 SER A 128 -166.42 -160.49 REMARK 500 1 LYS A 139 -164.87 -54.21 REMARK 500 1 HIS A 142 85.81 -150.18 REMARK 500 1 GLN A 143 -69.85 -142.07 REMARK 500 1 ALA A 149 109.83 -56.31 REMARK 500 1 LEU A 161 22.52 -161.24 REMARK 500 1 VAL A 162 88.81 -161.46 REMARK 500 1 GLU A 165 -81.49 -172.29 REMARK 500 1 THR A 185 -74.55 -84.89 REMARK 500 1 LEU A 187 28.19 -177.84 REMARK 500 1 VAL A 206 -159.68 -91.62 REMARK 500 REMARK 500 THIS ENTRY HAS 1116 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 6311 RELATED DB: BMRB REMARK 900 1H, 13C, 15N CHEMICAL SHIFT ASSIGNMENTS DBREF 2AFJ A 12 224 UNP O88838 O88838_MOUSE 12 224 SEQADV 2AFJ GLY A 6 UNP O88838 CLONING ARTIFACT SEQADV 2AFJ SER A 7 UNP O88838 CLONING ARTIFACT SEQADV 2AFJ SER A 8 UNP O88838 CLONING ARTIFACT SEQADV 2AFJ ALA A 9 UNP O88838 CLONING ARTIFACT SEQADV 2AFJ ARG A 10 UNP O88838 CLONING ARTIFACT SEQADV 2AFJ GLN A 11 UNP O88838 CLONING ARTIFACT SEQADV 2AFJ THR A 225 UNP O88838 CLONING ARTIFACT SEQADV 2AFJ ARG A 226 UNP O88838 CLONING ARTIFACT SEQADV 2AFJ ARG A 227 UNP O88838 CLONING ARTIFACT SEQADV 2AFJ ILE A 228 UNP O88838 CLONING ARTIFACT SEQADV 2AFJ HIS A 229 UNP O88838 CLONING ARTIFACT SEQADV 2AFJ ARG A 230 UNP O88838 CLONING ARTIFACT SEQADV 2AFJ ASP A 231 UNP O88838 CLONING ARTIFACT SEQRES 1 A 226 GLY SER SER ALA ARG GLN SER THR PRO THR SER GLN ALA SEQRES 2 A 226 LEU TYR SER ASP PHE SER PRO PRO GLU GLY LEU GLU GLU SEQRES 3 A 226 LEU LEU SER ALA PRO PRO PRO ASP LEU VAL ALA GLN ARG SEQRES 4 A 226 HIS HIS GLY TRP ASN PRO LYS ASP CYS SER GLU ASN ILE SEQRES 5 A 226 ASP VAL LYS GLU GLY GLY LEU CYS PHE GLU ARG ARG PRO SEQRES 6 A 226 VAL ALA GLN SER THR ASP GLY VAL ARG GLY LYS ARG GLY SEQRES 7 A 226 TYR SER ARG GLY LEU HIS ALA TRP GLU ILE SER TRP PRO SEQRES 8 A 226 LEU GLU GLN ARG GLY THR HIS ALA VAL VAL GLY VAL ALA SEQRES 9 A 226 THR ALA LEU ALA PRO LEU GLN ALA ASP HIS TYR ALA ALA SEQRES 10 A 226 LEU LEU GLY SER ASN SER GLU SER TRP GLY TRP ASP ILE SEQRES 11 A 226 GLY ARG GLY LYS LEU TYR HIS GLN SER LYS GLY LEU GLU SEQRES 12 A 226 ALA PRO GLN TYR PRO ALA GLY PRO GLN GLY GLU GLN LEU SEQRES 13 A 226 VAL VAL PRO GLU ARG LEU LEU VAL VAL LEU ASP MET GLU SEQRES 14 A 226 GLU GLY THR LEU GLY TYR SER ILE GLY GLY THR TYR LEU SEQRES 15 A 226 GLY PRO ALA PHE ARG GLY LEU LYS GLY ARG THR LEU TYR SEQRES 16 A 226 PRO SER VAL SER ALA VAL TRP GLY GLN CYS GLN VAL ARG SEQRES 17 A 226 ILE ARG TYR MET GLY GLU ARG ARG VAL GLU GLU THR ARG SEQRES 18 A 226 ARG ILE HIS ARG ASP HELIX 1 1 LEU A 29 SER A 34 1 6 HELIX 2 2 VAL A 41 GLY A 47 1 7 HELIX 3 3 GLY A 136 GLY A 138 5 3 HELIX 4 4 PRO A 156 LEU A 161 5 6 HELIX 5 5 ALA A 190 THR A 198 1 9 SHEET 1 A 2 ASP A 58 LYS A 60 0 SHEET 2 A 2 CYS A 65 GLU A 67 -1 O GLU A 67 N ASP A 58 SHEET 1 B 4 VAL A 78 GLY A 80 0 SHEET 2 B 4 TYR A 200 ALA A 205 -1 O ALA A 205 N VAL A 78 SHEET 3 B 4 VAL A 105 THR A 110 -1 N ALA A 109 O TYR A 200 SHEET 4 B 4 GLU A 129 ASP A 134 -1 O GLU A 129 N THR A 110 SHEET 1 C 4 THR A 177 SER A 181 0 SHEET 2 C 4 LEU A 167 ASP A 172 -1 N VAL A 170 O GLY A 179 SHEET 3 C 4 LEU A 88 SER A 94 -1 N ILE A 93 O LEU A 167 SHEET 4 C 4 ARG A 213 MET A 217 -1 O ARG A 213 N SER A 94 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