Header list of 1s2h.pdb file
Complete list - 27 20 Bytes
HEADER CELL CYCLE 08-JAN-04 1S2H TITLE THE MAD2 SPINDLE CHECKPOINT PROTEIN POSSESSES TWO DISTINCT NATIVELY TITLE 2 FOLDED STATES COMPND MOL_ID: 1; COMPND 2 MOLECULE: MITOTIC SPINDLE ASSEMBLY CHECKPOINT PROTEIN MAD2A; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: MAD2-LIKE 1, HSMAD2; COMPND 5 ENGINEERED: YES; COMPND 6 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: MAD2L1, MAD2; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: M15[PREP4]; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PQE-30 KEYWDS MAD2, SPINDLE CHECKPOINT PROTEIN, CELL CYCLE EXPDTA SOLUTION NMR AUTHOR X.LUO,Z.TANG,G.XIA,K.WASSMANN,T.MATSUMOTO,J.RIZO,H.YU REVDAT 3 27-OCT-21 1S2H 1 REMARK SEQADV REVDAT 2 24-FEB-09 1S2H 1 VERSN REVDAT 1 30-MAR-04 1S2H 0 JRNL AUTH X.LUO,Z.TANG,G.XIA,K.WASSMANN,T.MATSUMOTO,J.RIZO,H.YU JRNL TITL THE MAD2 SPINDLE CHECKPOINT PROTEIN HAS TWO DISTINCT JRNL TITL 2 NATIVELY FOLDED STATES. JRNL REF NAT.STRUCT.MOL.BIOL. V. 11 338 2004 JRNL REFN ISSN 1545-9993 JRNL PMID 15024386 JRNL DOI 10.1038/NSMB748 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH X.LUO,G.FANG,M.COLDIRON,Y.LIN,H.YU,M.W.KIRSCHNER,G.WAGNER REMARK 1 TITL STRUCTURE OF THE MAD2 SPINDLE ASSEMBLY CHECKPOINT PROTEIN REMARK 1 TITL 2 AND ITS INTERACTION WITH CDC20 REMARK 1 REF NAT.STRUCT.BIOL. V. 7 224 2000 REMARK 1 REFN ISSN 1072-8368 REMARK 1 DOI 10.1038/73338 REMARK 1 REFERENCE 2 REMARK 1 AUTH X.LUO,Z.TANG,J.RIZO,H.YU REMARK 1 TITL THE MAD2 SPINDLE CHECKPOINT PROTEIN UNDERGOES SIMILAR MAJOR REMARK 1 TITL 2 CONFORMATIONAL CHANGES UPON BINDING TO EITHER MAD1 OR CDC20 REMARK 1 REF MOL.CELL V. 9 59 2002 REMARK 1 REFN ISSN 1097-2765 REMARK 1 DOI 10.1016/S1097-2765(01)00435-X REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS 1.0 REMARK 3 AUTHORS : BRUNGER, A.T. REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: REMARK 3 THE STRUCTURES ARE BASED ON A TOTAL OF 2866 RESTRAINTS, 2323 ARE REMARK 3 NOE-DERIVED REMARK 3 DISTANCE CONSTRAINTS, 339 DIHEDRAL ANGLE RESTRAINTS,204 DISTANCE REMARK 3 RESTRAINTS REMARK 3 FROM HYDROGEN BONDS. REMARK 4 REMARK 4 1S2H COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-JAN-04. REMARK 100 THE DEPOSITION ID IS D_1000021283. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 303 REMARK 210 PH : 6.8 REMARK 210 IONIC STRENGTH : 0.3M KCL REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 0.8MM MAD2 PROTEIN U-15N,13C,2H; REMARK 210 0.8MM MAD2 PROTEIN U-15N; 0.8MM REMARK 210 MAD2 PROTEIN U-15N,13C REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : HNCA, HN(CO)CA, HN(CA)CB, REMARK 210 HN(COCA)CB; 3D_15N-SEPARATED_ REMARK 210 NOESY; 3D_13C-SEPARATED_NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 500 MHZ REMARK 210 SPECTROMETER MODEL : INOVA REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRPIPE 1.8, VNMR 6.1, NMRVIEW REMARK 210 4.1.2 REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 500 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST REMARK 210 ENERGY 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. 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 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 RES C SSSEQI REMARK 465 GLY 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 O GLN A 71 H TRP A 75 1.55 REMARK 500 O VAL A 86 H TRP A 100 1.57 REMARK 500 O ILE A 31 H ARG A 35 1.58 REMARK 500 O ILE A 19 H PHE A 23 1.60 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 GLN A 9 50.89 -163.81 REMARK 500 THR A 12 -87.53 -61.00 REMARK 500 PRO A 39 115.78 -39.06 REMARK 500 GLU A 41 -8.89 -55.48 REMARK 500 THR A 42 35.68 -99.17 REMARK 500 TYR A 49 9.85 58.49 REMARK 500 SER A 80 -17.80 150.52 REMARK 500 VAL A 81 135.20 67.74 REMARK 500 GLN A 82 -78.30 -142.42 REMARK 500 ASP A 112 46.35 -176.88 REMARK 500 ARG A 117 -177.67 59.61 REMARK 500 PRO A 143 -158.60 -73.40 REMARK 500 GLU A 146 -36.88 -159.90 REMARK 500 LEU A 161 -76.07 -164.03 REMARK 500 VAL A 163 136.31 65.90 REMARK 500 LYS A 166 128.69 63.39 REMARK 500 GLU A 169 -56.47 -129.36 REMARK 500 SER A 170 98.84 -66.75 REMARK 500 PHE A 174 -46.84 -149.15 REMARK 500 ILE A 175 -72.32 -132.65 REMARK 500 THR A 176 -52.42 174.91 REMARK 500 ASN A 177 73.53 -167.65 REMARK 500 LEU A 183 -61.09 -95.31 REMARK 500 VAL A 203 80.57 42.51 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1DUJ RELATED DB: PDB REMARK 900 THE SAME PROTEIN WITH DIFFERENT FOLD. REMARK 900 RELATED ID: 1KLQ RELATED DB: PDB REMARK 900 THE SAME PROTEIN COMPLEXED WITH MAD2-BINDING PEPTIDE. DBREF 1S2H A 1 205 UNP Q13257 MD2L1_HUMAN 1 205 SEQADV 1S2H GLY A 0 UNP Q13257 CLONING ARTIFACT SEQADV 1S2H ALA A 133 UNP Q13257 ARG 133 ENGINEERED MUTATION SEQRES 1 A 206 GLY MET ALA LEU GLN LEU SER ARG GLU GLN GLY ILE THR SEQRES 2 A 206 LEU ARG GLY SER ALA GLU ILE VAL ALA GLU PHE PHE SER SEQRES 3 A 206 PHE GLY ILE ASN SER ILE LEU TYR GLN ARG GLY ILE TYR SEQRES 4 A 206 PRO SER GLU THR PHE THR ARG VAL GLN LYS TYR GLY LEU SEQRES 5 A 206 THR LEU LEU VAL THR THR ASP LEU GLU LEU ILE LYS TYR SEQRES 6 A 206 LEU ASN ASN VAL VAL GLU GLN LEU LYS ASP TRP LEU TYR SEQRES 7 A 206 LYS CYS SER VAL GLN LYS LEU VAL VAL VAL ILE SER ASN SEQRES 8 A 206 ILE GLU SER GLY GLU VAL LEU GLU ARG TRP GLN PHE ASP SEQRES 9 A 206 ILE GLU CYS ASP LYS THR ALA LYS ASP ASP SER ALA PRO SEQRES 10 A 206 ARG GLU LYS SER GLN LYS ALA ILE GLN ASP GLU ILE ARG SEQRES 11 A 206 SER VAL ILE ALA GLN ILE THR ALA THR VAL THR PHE LEU SEQRES 12 A 206 PRO LEU LEU GLU VAL SER CYS SER PHE ASP LEU LEU ILE SEQRES 13 A 206 TYR THR ASP LYS ASP LEU VAL VAL PRO GLU LYS TRP GLU SEQRES 14 A 206 GLU SER GLY PRO GLN PHE ILE THR ASN SER GLU GLU VAL SEQRES 15 A 206 ARG LEU ARG SER PHE THR THR THR ILE HIS LYS VAL ASN SEQRES 16 A 206 SER MET VAL ALA TYR LYS ILE PRO VAL ASN ASP HELIX 1 1 THR A 12 GLY A 36 1 25 HELIX 2 2 PRO A 39 GLU A 41 5 3 HELIX 3 3 ASP A 58 TRP A 75 1 18 HELIX 4 4 SER A 120 LEU A 142 1 23 SHEET 1 A 2 PHE A 43 LYS A 48 0 SHEET 2 A 2 LEU A 51 THR A 56 -1 O LEU A 53 N VAL A 46 SHEET 1 B 5 CYS A 149 TYR A 156 0 SHEET 2 B 5 LYS A 83 ASN A 90 -1 N SER A 89 O SER A 150 SHEET 3 B 5 GLU A 95 CYS A 106 -1 O TRP A 100 N VAL A 86 SHEET 4 B 5 HIS A 191 LYS A 200 -1 O LYS A 192 N GLU A 105 SHEET 5 B 5 SER A 178 THR A 187 -1 N PHE A 186 O VAL A 193 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 - 27 20 Bytes