Header list of 1duj.pdb file
Complete list - 21 20 Bytes
HEADER CELL CYCLE 17-JAN-00 1DUJ TITLE SOLUTION STRUCTURE OF THE SPINDLE ASSEMBLY CHECKPOINT PROTEIN HUMAN TITLE 2 MAD2 COMPND MOL_ID: 1; COMPND 2 MOLECULE: SPINDLE ASSEMBLY CHECKPOINT PROTEIN; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: FULL PROTEIN WITHOUT BOTH N- AND C-TERMINAL 10 RESIDUES; 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_VECTOR_TYPE: PLASMID; SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PQE-30 KEYWDS MAD2, SPINDLE ASSEMBLY CHECKPOINT, CELL CYCLE EXPDTA SOLUTION NMR AUTHOR X.LUO,G.FANG,M.COLDIRON,Y.LIN,H.YU REVDAT 5 21-DEC-22 1DUJ 1 SEQADV REVDAT 4 16-FEB-22 1DUJ 1 REMARK REVDAT 3 24-FEB-09 1DUJ 1 VERSN REVDAT 2 01-APR-03 1DUJ 1 JRNL REVDAT 1 08-MAR-00 1DUJ 0 JRNL AUTH X.LUO,G.FANG,M.COLDIRON,Y.LIN,H.YU,M.W.KIRSCHNER,G.WAGNER JRNL TITL STRUCTURE OF THE MAD2 SPINDLE ASSEMBLY CHECKPOINT PROTEIN JRNL TITL 2 AND ITS INTERACTION WITH CDC20. JRNL REF NAT.STRUCT.BIOL. V. 7 224 2000 JRNL REFN ISSN 1072-8368 JRNL PMID 10700282 JRNL DOI 10.1038/73338 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.1, X-PLOR 3.1 REMARK 3 AUTHORS : BRUNGER (X-PLOR), BRUNGER (X-PLOR) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF REMARK 3 3111 RESTRAINTS, 2807 ARE NOE-DERIVED DISTANCE CONSTRAINTS, 214 REMARK 3 DIHEDRAL ANGLE RESTRAINTS,90 DISTANCE RESTRAINTS FROM HYDROGEN REMARK 3 BONDS. REMARK 4 REMARK 4 1DUJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-FEB-00. REMARK 100 THE DEPOSITION ID IS D_1000010381. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 303; 303; 303; 303; 303 REMARK 210 PH : 6.8; 6.8; 6.8; 6.8; 6.8 REMARK 210 IONIC STRENGTH : 300MM KCL; 300MM KCL; 300MM KCL; REMARK 210 300MM KCL; 300MM KCL REMARK 210 PRESSURE : AMBIENT; AMBIENT; AMBIENT; REMARK 210 AMBIENT; AMBIENT REMARK 210 SAMPLE CONTENTS : 1.2MM MAD2 PROTEIN U-15N,13C,2H; REMARK 210 50MM SODIUM PHOSPHATE (PH 6.8), REMARK 210 300MM KCL, 5MM DTT, 0.04% NAN3; REMARK 210 90% H2O, 10% D2O; 1.4MM MAD2 REMARK 210 PROTEIN U-15N,13C; U-60% 2H; REMARK 210 50MM SODIUM PHOSPHATE (PH 6.8), REMARK 210 300MM KCL, 5MM DTT, 0.04% NAN3; REMARK 210 90% H2O, 10% D2O; 1.5MM MAD2 REMARK 210 PROTEIN U-15N; 50MM SODIUM REMARK 210 PHOSPHATE (PH 6.8), 300MM KCL, REMARK 210 5MM DTT, 0.04% NAN3; 90% H2O, 10% REMARK 210 D2O; 1.6MM MAD2 PROTEIN U-10% REMARK 210 13C; 50MM SODIUM PHOSPHATE (PH REMARK 210 6.8), 300MM KCL, 5MM DTT, 0.04% REMARK 210 NAN3; 100% D2O; 1.7MM MAD2 REMARK 210 PROTEIN U-15N,13C; 50MM SODIUM REMARK 210 PHOSPHATE (PH 6.8), 300MM KCL, REMARK 210 5MM DTT, 0.04% NAN3; 100% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C REMARK 210 -SEPARATED_NOESY; 3D HCCH-TOCSY; REMARK 210 3D_15N-SEPARATED_TOCSY; 3D_H(CC) REMARK 210 (CO)NH; 3D_(H)C(C)(CO)NH REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 750 MHZ REMARK 210 SPECTROMETER MODEL : INOVA REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NULL REMARK 210 METHOD USED : SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1 REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL REMARK 210 REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR REMARK 210 SPECTROSCOPY. 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 HG SER A 150 O LEU A 185 1.48 REMARK 500 H PHE A 153 O SER A 187 1.48 REMARK 500 O ILE A 64 H ASN A 68 1.49 REMARK 500 O LEU A 155 H THR A 191 1.49 REMARK 500 O SER A 18 H VAL A 22 1.49 REMARK 500 O LEU A 61 H LYS A 65 1.49 REMARK 500 O ALA A 125 H GLU A 129 1.50 REMARK 500 O PHE A 176 H PHE A 188 1.51 REMARK 500 H ASN A 92 O GLU A 97 1.52 REMARK 500 O LYS A 85 H TYR A 158 1.52 REMARK 500 O ILE A 13 H ASP A 105 1.53 REMARK 500 H LEU A 15 O ASP A 105 1.54 REMARK 500 O PHE A 26 H ILE A 30 1.55 REMARK 500 O SER A 180 H GLU A 182 1.55 REMARK 500 O GLN A 84 H ILE A 106 1.58 REMARK 500 OD1 ASP A 60 H LEU A 63 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 ARG A 16 -169.29 -105.30 REMARK 500 TYR A 40 58.53 -177.40 REMARK 500 PRO A 41 -158.52 -85.27 REMARK 500 PHE A 45 179.49 -47.94 REMARK 500 TYR A 51 20.33 49.21 REMARK 500 ASP A 60 102.93 -54.57 REMARK 500 ASP A 76 71.68 -172.25 REMARK 500 LEU A 78 32.23 164.38 REMARK 500 LYS A 80 46.45 173.88 REMARK 500 CYS A 81 -74.06 -161.17 REMARK 500 SER A 82 -126.67 -102.81 REMARK 500 VAL A 83 113.74 59.38 REMARK 500 GLN A 84 53.31 174.49 REMARK 500 GLU A 94 44.56 -155.72 REMARK 500 SER A 95 -69.51 -162.61 REMARK 500 GLU A 97 -136.40 56.45 REMARK 500 VAL A 98 156.92 -37.49 REMARK 500 LEU A 99 -46.13 -154.22 REMARK 500 ALA A 112 175.98 169.07 REMARK 500 LYS A 113 -38.34 -145.72 REMARK 500 SER A 116 -81.90 -64.50 REMARK 500 ALA A 117 140.75 65.71 REMARK 500 GLU A 120 -26.35 174.10 REMARK 500 LYS A 121 110.58 70.78 REMARK 500 LEU A 146 79.42 39.22 REMARK 500 GLU A 148 -57.45 -179.87 REMARK 500 VAL A 149 -173.71 43.39 REMARK 500 ASP A 162 23.19 -154.51 REMARK 500 VAL A 164 51.43 -113.34 REMARK 500 VAL A 165 109.89 -45.08 REMARK 500 PRO A 166 -167.52 -74.50 REMARK 500 LYS A 168 -27.60 -38.26 REMARK 500 GLU A 170 34.04 171.85 REMARK 500 GLU A 171 -6.88 75.09 REMARK 500 SER A 172 45.00 161.41 REMARK 500 GLN A 175 86.01 -150.18 REMARK 500 ASN A 179 31.63 -179.26 REMARK 500 GLU A 181 57.13 -67.86 REMARK 500 GLU A 182 -31.99 178.86 REMARK 500 ARG A 184 -134.21 44.73 REMARK 500 LEU A 185 -166.82 44.37 REMARK 500 ARG A 186 -34.74 179.51 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 ARG A 16 0.30 SIDE CHAIN REMARK 500 ARG A 37 0.16 SIDE CHAIN REMARK 500 ARG A 47 0.31 SIDE CHAIN REMARK 500 ARG A 101 0.31 SIDE CHAIN REMARK 500 ARG A 119 0.26 SIDE CHAIN REMARK 500 ARG A 131 0.25 SIDE CHAIN REMARK 500 ARG A 135 0.23 SIDE CHAIN REMARK 500 ARG A 184 0.26 SIDE CHAIN REMARK 500 ARG A 186 0.26 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL DBREF 1DUJ A 13 197 UNP Q13257 MD2L1_HUMAN 11 195 SEQADV 1DUJ GLY A 11 UNP Q13257 CLONING ARTIFACT SEQADV 1DUJ SER A 12 UNP Q13257 CLONING ARTIFACT SEQRES 1 A 187 GLY SER ILE THR LEU ARG GLY SER ALA GLU ILE VAL ALA SEQRES 2 A 187 GLU PHE PHE SER PHE GLY ILE ASN SER ILE LEU TYR GLN SEQRES 3 A 187 ARG GLY ILE TYR PRO SER GLU THR PHE THR ARG VAL GLN SEQRES 4 A 187 LYS TYR GLY LEU THR LEU LEU VAL THR THR ASP LEU GLU SEQRES 5 A 187 LEU ILE LYS TYR LEU ASN ASN VAL VAL GLU GLN LEU LYS SEQRES 6 A 187 ASP TRP LEU TYR LYS CYS SER VAL GLN LYS LEU VAL VAL SEQRES 7 A 187 VAL ILE SER ASN ILE GLU SER GLY GLU VAL LEU GLU ARG SEQRES 8 A 187 TRP GLN PHE ASP ILE GLU CYS ASP LYS THR ALA LYS ASP SEQRES 9 A 187 ASP SER ALA PRO ARG GLU LYS SER GLN LYS ALA ILE GLN SEQRES 10 A 187 ASP GLU ILE ARG SER VAL ILE ARG GLN ILE THR ALA THR SEQRES 11 A 187 VAL THR PHE LEU PRO LEU LEU GLU VAL SER CYS SER PHE SEQRES 12 A 187 ASP LEU LEU ILE TYR THR ASP LYS ASP LEU VAL VAL PRO SEQRES 13 A 187 GLU LYS TRP GLU GLU SER GLY PRO GLN PHE ILE THR ASN SEQRES 14 A 187 SER GLU GLU VAL ARG LEU ARG SER PHE THR THR THR ILE SEQRES 15 A 187 HIS LYS VAL ASN SER HELIX 1 1 SER A 18 ARG A 37 1 20 HELIX 2 2 ASP A 60 ASP A 76 1 17 HELIX 3 3 GLN A 123 LEU A 144 1 22 SHEET 1 A 6 SER A 12 THR A 14 0 SHEET 2 A 6 GLU A 97 ASP A 105 1 O GLN A 103 N ILE A 13 SHEET 3 A 6 LYS A 85 ASN A 92 -1 O LEU A 86 N PHE A 104 SHEET 4 A 6 CYS A 151 ASP A 160 -1 N SER A 152 O SER A 91 SHEET 5 A 6 SER A 187 VAL A 195 1 O SER A 187 N PHE A 153 SHEET 6 A 6 GLN A 175 ILE A 177 -1 O PHE A 176 N PHE A 188 SHEET 1 B 2 THR A 46 LYS A 50 0 SHEET 2 B 2 LEU A 53 VAL A 57 -1 N LEU A 53 O LYS A 50 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
Complete list - 21 20 Bytes