Header list of 1bu9.pdb file
Complete list - b 16 2 Bytes
HEADER HORMONE/GROWTH FACTOR 15-SEP-98 1BU9 TITLE SOLUTION STRUCTURE OF P18-INK4C, 21 STRUCTURES COMPND MOL_ID: 1; COMPND 2 MOLECULE: PROTEIN (CYCLIN-DEPENDENT KINASE 6 INHIBITOR); COMPND 3 CHAIN: A; COMPND 4 SYNONYM: P18-INK4C; COMPND 5 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; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: DL21(DE3); SOURCE 8 EXPRESSION_SYSTEM_PLASMID: DL21(DE3) KEYWDS CELL CYCLE INHIBITOR, P18INK4C, TUMOR, SUPPRESSOR, CYCLIN-DEPENDENT KEYWDS 2 KINASE, HORMONE-GROWTH FACTOR COMPLEX EXPDTA SOLUTION NMR NUMMDL 21 AUTHOR I.-J.L.BYEON,J.LI,M.-D.TSAI REVDAT 4 16-FEB-22 1BU9 1 REMARK REVDAT 3 24-FEB-09 1BU9 1 VERSN REVDAT 2 01-APR-03 1BU9 1 JRNL REVDAT 1 13-SEP-99 1BU9 0 JRNL AUTH J.LI,I.J.BYEON,K.ERICSON,M.J.POI,P.O'MAILLE,T.SELBY,M.D.TSAI JRNL TITL TUMOR SUPPRESSOR INK4: DETERMINATION OF THE SOLUTION JRNL TITL 2 STRUCTURE OF P18INK4C AND DEMONSTRATION OF THE FUNCTIONAL JRNL TITL 3 SIGNIFICANCE OF LOOPS IN P18INK4C AND P16INK4A. JRNL REF BIOCHEMISTRY V. 38 2930 1999 JRNL REFN ISSN 0006-2960 JRNL PMID 10074345 JRNL DOI 10.1021/BI982286E REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1BU9 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-JUL-99. REMARK 100 THE DEPOSITION ID IS D_1000007107. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 293 REMARK 210 PH : 7.5 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : NULL REMARK 210 SAMPLE CONTENTS : NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : HNCACB; CBCA(CO)HN; HN(CO)HCCH REMARK 210 -TOCSY; HNHB; 3D 15N-EDITED REMARK 210 NOESY AND TOCSY; 2D NOESY AND REMARK 210 TOCSY; 3D 13C-EDITED NOESY; 3D REMARK 210 15N/13C SA EDITED NOESY; 4D 15N/ REMARK 210 13C-EDITED NOESY; 4D 13C/13C- REMARK 210 EDITED NOES REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ REMARK 210 SPECTROMETER MODEL : DMX600; DRX800 REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : X-PLOR REMARK 210 METHOD USED : SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 50 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 21 REMARK 210 CONFORMERS, SELECTION CRITERIA : CLOSEST TO MEAN STRUCTURE WHICH REMARK 210 SHOWS GOOD AGREEMENT WITH THE REMARK 210 CONSTRAINTS REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL REMARK 210 REMARK 210 REMARK: REMARK 210 THE SOLUTION STRUCTURE OF P18-INK4C HAS BEEN DETERMINED BY MULTI- REMARK 210 DIMENSIONAL REMARK 210 HETERONUCLEAR NMR. THE STRUCTURES WERE CALCULATED USING THE REMARK 210 SIMULATED REMARK 210 ANNEALING PROTOCOL OF NILGES ET AL. (1988) FEBS LETT. 229, 129-136 REMARK 210 USING THE REMARK 210 PROGRAM X-PLOR 3.1 (BRUNGER). THE CALCULATION IS BASED ON 3175 REMARK 210 EXPERIMENTAL REMARK 210 NMR RESTRAINTS (3062 DISTANCE AND 113 TORSION ANGLE RESTRAINTS). 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 O ASP A 95 H ILE A 98 1.42 REMARK 500 O ALA A 13 H LYS A 46 1.46 REMARK 500 O ALA A 53 H LEU A 57 1.48 REMARK 500 OD1 ASN A 134 H GLY A 137 1.50 REMARK 500 O THR A 40 H GLN A 43 1.50 REMARK 500 O GLN A 87 H GLU A 91 1.54 REMARK 500 O ASN A 30 H ALA A 33 1.54 REMARK 500 O ASN A 35 H GLY A 38 1.54 REMARK 500 O VAL A 118 H PHE A 121 1.56 REMARK 500 O VAL A 96 HD22 ASN A 129 1.57 REMARK 500 O ALA A 77 H PHE A 82 1.58 REMARK 500 OD1 ASP A 67 H PHE A 71 1.59 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 2 51.72 -110.81 REMARK 500 1 TRP A 5 -152.51 52.39 REMARK 500 1 ASN A 7 -71.84 -53.45 REMARK 500 1 LEU A 9 -78.78 -62.75 REMARK 500 1 SER A 11 -83.00 -67.64 REMARK 500 1 ASP A 17 98.06 -54.93 REMARK 500 1 ASN A 28 139.16 -176.13 REMARK 500 1 ASN A 30 85.84 -62.49 REMARK 500 1 VAL A 31 -27.04 -37.70 REMARK 500 1 ALA A 33 178.37 -49.70 REMARK 500 1 GLN A 34 98.78 -174.91 REMARK 500 1 ASN A 35 170.13 -53.23 REMARK 500 1 MET A 45 112.38 2.60 REMARK 500 1 LYS A 46 93.23 -42.00 REMARK 500 1 LEU A 65 78.06 -63.22 REMARK 500 1 LYS A 66 172.67 -52.41 REMARK 500 1 ASP A 67 -142.06 -127.96 REMARK 500 1 ASP A 95 88.35 -47.43 REMARK 500 1 GLU A 99 -149.30 -128.28 REMARK 500 1 ASP A 100 -155.58 -113.10 REMARK 500 1 ASN A 101 38.38 -89.98 REMARK 500 1 GLU A 102 -54.03 -163.66 REMARK 500 1 ASN A 104 150.10 -48.60 REMARK 500 1 HIS A 115 69.73 -65.48 REMARK 500 1 LEU A 116 -79.24 -52.04 REMARK 500 1 ARG A 117 -30.32 -39.55 REMARK 500 1 HIS A 125 -137.79 -126.01 REMARK 500 1 THR A 126 -161.42 37.42 REMARK 500 1 SER A 128 161.65 52.56 REMARK 500 1 ASN A 129 53.51 -119.39 REMARK 500 1 VAL A 130 -78.93 -50.13 REMARK 500 1 HIS A 132 76.76 -61.14 REMARK 500 1 ASN A 134 -152.53 -55.90 REMARK 500 1 ASP A 138 87.50 -66.43 REMARK 500 1 THR A 139 -166.39 -61.27 REMARK 500 1 LEU A 143 -68.41 -92.91 REMARK 500 1 ARG A 149 100.73 -39.33 REMARK 500 1 ASN A 159 44.80 -81.79 REMARK 500 1 ALA A 164 71.83 41.93 REMARK 500 1 THR A 165 62.62 -101.19 REMARK 500 2 ALA A 2 76.09 -161.40 REMARK 500 2 GLU A 3 61.62 33.93 REMARK 500 2 TRP A 5 89.79 62.71 REMARK 500 2 SER A 11 -75.76 -63.40 REMARK 500 2 THR A 22 -70.04 -62.19 REMARK 500 2 ASN A 28 140.68 -179.77 REMARK 500 2 ASN A 30 75.24 -105.71 REMARK 500 2 ALA A 33 -166.89 -53.55 REMARK 500 2 GLN A 34 113.82 -170.88 REMARK 500 2 MET A 45 118.07 -8.31 REMARK 500 REMARK 500 THIS ENTRY HAS 777 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 1 ARG A 15 0.17 SIDE CHAIN REMARK 500 1 ARG A 39 0.10 SIDE CHAIN REMARK 500 1 ARG A 54 0.32 SIDE CHAIN REMARK 500 1 ARG A 55 0.18 SIDE CHAIN REMARK 500 1 ARG A 68 0.20 SIDE CHAIN REMARK 500 1 ARG A 79 0.31 SIDE CHAIN REMARK 500 1 ARG A 117 0.30 SIDE CHAIN REMARK 500 1 ARG A 133 0.26 SIDE CHAIN REMARK 500 1 ARG A 145 0.18 SIDE CHAIN REMARK 500 1 ARG A 149 0.29 SIDE CHAIN REMARK 500 2 ARG A 15 0.32 SIDE CHAIN REMARK 500 2 ARG A 39 0.28 SIDE CHAIN REMARK 500 2 ARG A 54 0.29 SIDE CHAIN REMARK 500 2 ARG A 55 0.26 SIDE CHAIN REMARK 500 2 ARG A 59 0.27 SIDE CHAIN REMARK 500 2 ARG A 68 0.31 SIDE CHAIN REMARK 500 2 ARG A 79 0.18 SIDE CHAIN REMARK 500 2 ARG A 117 0.22 SIDE CHAIN REMARK 500 2 ARG A 133 0.25 SIDE CHAIN REMARK 500 2 ARG A 145 0.26 SIDE CHAIN REMARK 500 2 ARG A 149 0.31 SIDE CHAIN REMARK 500 3 ARG A 15 0.31 SIDE CHAIN REMARK 500 3 ARG A 39 0.12 SIDE CHAIN REMARK 500 3 ARG A 54 0.28 SIDE CHAIN REMARK 500 3 ARG A 55 0.11 SIDE CHAIN REMARK 500 3 ARG A 59 0.26 SIDE CHAIN REMARK 500 3 ARG A 68 0.32 SIDE CHAIN REMARK 500 3 ARG A 79 0.24 SIDE CHAIN REMARK 500 3 ARG A 117 0.14 SIDE CHAIN REMARK 500 3 ARG A 133 0.21 SIDE CHAIN REMARK 500 3 ARG A 145 0.19 SIDE CHAIN REMARK 500 3 ARG A 149 0.31 SIDE CHAIN REMARK 500 4 ARG A 15 0.31 SIDE CHAIN REMARK 500 4 ARG A 39 0.16 SIDE CHAIN REMARK 500 4 ARG A 54 0.24 SIDE CHAIN REMARK 500 4 ARG A 55 0.20 SIDE CHAIN REMARK 500 4 ARG A 59 0.20 SIDE CHAIN REMARK 500 4 ARG A 68 0.32 SIDE CHAIN REMARK 500 4 ARG A 79 0.30 SIDE CHAIN REMARK 500 4 ARG A 117 0.32 SIDE CHAIN REMARK 500 4 ARG A 133 0.23 SIDE CHAIN REMARK 500 4 ARG A 145 0.19 SIDE CHAIN REMARK 500 4 ARG A 149 0.27 SIDE CHAIN REMARK 500 5 ARG A 15 0.32 SIDE CHAIN REMARK 500 5 ARG A 39 0.16 SIDE CHAIN REMARK 500 5 ARG A 54 0.31 SIDE CHAIN REMARK 500 5 ARG A 55 0.24 SIDE CHAIN REMARK 500 5 ARG A 59 0.11 SIDE CHAIN REMARK 500 5 ARG A 68 0.32 SIDE CHAIN REMARK 500 5 ARG A 79 0.23 SIDE CHAIN REMARK 500 REMARK 500 THIS ENTRY HAS 214 PLANE DEVIATIONS. REMARK 500 REMARK 500 REMARK: NULL DBREF 1BU9 A 1 168 UNP P42773 CDN2C_HUMAN 1 168 SEQRES 1 A 168 MET ALA GLU PRO TRP GLY ASN GLU LEU ALA SER ALA ALA SEQRES 2 A 168 ALA ARG GLY ASP LEU GLU GLN LEU THR SER LEU LEU GLN SEQRES 3 A 168 ASN ASN VAL ASN VAL ASN ALA GLN ASN GLY PHE GLY ARG SEQRES 4 A 168 THR ALA LEU GLN VAL MET LYS LEU GLY ASN PRO GLU ILE SEQRES 5 A 168 ALA ARG ARG LEU LEU LEU ARG GLY ALA ASN PRO ASP LEU SEQRES 6 A 168 LYS ASP ARG THR GLY PHE ALA VAL ILE HIS ASP ALA ALA SEQRES 7 A 168 ARG ALA GLY PHE LEU ASP THR LEU GLN THR LEU LEU GLU SEQRES 8 A 168 PHE GLN ALA ASP VAL ASN ILE GLU ASP ASN GLU GLY ASN SEQRES 9 A 168 LEU PRO LEU HIS LEU ALA ALA LYS GLU GLY HIS LEU ARG SEQRES 10 A 168 VAL VAL GLU PHE LEU VAL LYS HIS THR ALA SER ASN VAL SEQRES 11 A 168 GLY HIS ARG ASN HIS LYS GLY ASP THR ALA CYS ASP LEU SEQRES 12 A 168 ALA ARG LEU TYR GLY ARG ASN GLU VAL VAL SER LEU MET SEQRES 13 A 168 GLN ALA ASN GLY ALA GLY GLY ALA THR ASN LEU GLN HELIX 1 IA GLU A 8 ARG A 15 1 8 HELIX 2 1B LEU A 18 GLN A 26 1 9 HELIX 3 2A ALA A 41 VAL A 44 1 4 HELIX 4 2B PRO A 50 LEU A 58 1 9 HELIX 5 3A VAL A 73 ARG A 79 1 7 HELIX 6 3B LEU A 83 GLU A 91 1 9 HELIX 7 4A PRO A 106 LYS A 112 1 7 HELIX 8 4B LEU A 116 VAL A 123 1 8 HELIX 9 5A ALA A 140 TYR A 147 1 8 HELIX 10 5B ASN A 150 ALA A 158 1 9 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 - b 16 2 Bytes