Header list of 1r21.pdb file
Complete list - r 2 2 Bytes
HEADER CELL CYCLE 25-SEP-03 1R21 TITLE SOLUTION STRUCTURE OF HUMAN KI67 FHA DOMAIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: ANTIGEN KI-67; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: FHA DOMAIN; COMPND 5 SYNONYM: CELL PROLIFERATION ANTIGEN KI-67, LONG FORM; ANTIGEN COMPND 6 IDENTIFIED BY MONOCLONAL ANTIBODY KI-67; PROLIFERATION-RELATED KI-67 COMPND 7 ANTIGEN; COMPND 8 ENGINEERED: YES; COMPND 9 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 CELLULAR_LOCATION: NUCLEUS; SOURCE 6 GENE: MKI67; SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3); SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PEG KEYWDS BETA SANDWICH, CELL CYCLE EXPDTA SOLUTION NMR NUMMDL 23 MDLTYP MINIMIZED AVERAGE AUTHOR I.J.BYEON,H.LI,M.D.TSAI REVDAT 3 02-MAR-22 1R21 1 REMARK SEQADV REVDAT 2 24-FEB-09 1R21 1 VERSN REVDAT 1 30-DEC-03 1R21 0 JRNL AUTH H.LI,I.J.BYEON,Y.JU,M.D.TSAI JRNL TITL STRUCTURE OF HUMAN KI67 FHA DOMAIN AND ITS BINDING TO A JRNL TITL 2 PHOSPHOPROTEIN FRAGMENT FROM HNIFK REVEAL UNIQUE RECOGNITION JRNL TITL 3 SITES AND NEW VIEWS TO THE STRUCTURAL BASIS OF FHA DOMAIN JRNL TITL 4 FUNCTIONS JRNL REF J.MOL.BIOL. V. 335 371 2004 JRNL REFN ISSN 0022-2836 JRNL PMID 14659764 JRNL DOI 10.1016/J.JMB.2003.10.032 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XWINNMR 2.6, X-PLOR NIH VERSION REMARK 3 AUTHORS : BRUKER (XWINNMR), BRUNGER,SCHWIETERS, KUSZEWSKI, REMARK 3 TJANDRA, CLORE (X-PLOR) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: REMARK 3 THE STRUCTURES ARE BASED ON A TOTAL OF 1921 CONSTRAINTS: 1694 FROM REMARK 3 NOE, REMARK 3 62 FROM H-BONDING, 165 FROM DIHEDRAL ANGLE CONSTRAINTS REMARK 4 REMARK 4 1R21 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-OCT-03. REMARK 100 THE DEPOSITION ID IS D_1000020341. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 290; 290 REMARK 210 PH : 8.4; 7.5 REMARK 210 IONIC STRENGTH : 0; 150 MM NACL REMARK 210 PRESSURE : AMBIENT; AMBIENT REMARK 210 SAMPLE CONTENTS : 0.5 MM U-13C,15N-PROTEIN; 10 MM REMARK 210 TRISHCL BUFFER (PH 8.4); 2MM DTT; REMARK 210 1 MM EDTA; 0.5 MM U-13C,15N- REMARK 210 PROTEIN; 5 MM HEPES BUFFER (PH REMARK 210 7.5); 2MM DTT; 1 MM EDTA; 150 MM REMARK 210 NACL; 0.5 MM UNLABELED-PROTEIN; REMARK 210 10 MM TRISHCL BUFFER (PH 8.4); REMARK 210 2MM DTT; 1 MM EDTA; 0.5 MM REMARK 210 UNLABELED-PROTEIN; 10 MM TRISHCL REMARK 210 BUFFER (PH 8.4); 2MM DTT; 1 MM REMARK 210 EDTA REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N REMARK 210 -SEPARATED_NOESY; 2D NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 600 MHZ REMARK 210 SPECTROMETER MODEL : DRX; DMX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : XWINNMR 2.6, X-PLOR NIH VERSION REMARK 210 METHOD USED : SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 23 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST REMARK 210 ENERGY,TARGET FUNCTION 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 MODELS 1-23 REMARK 465 RES C SSSEQI REMARK 465 GLY A -7 REMARK 465 SER A -6 REMARK 465 PRO A -5 REMARK 465 GLU A -4 REMARK 465 PHE A -3 REMARK 465 PRO A -2 REMARK 465 GLY A -1 REMARK 465 GLY A 0 REMARK 465 SER A 101 REMARK 465 LEU A 102 REMARK 465 GLN A 103 REMARK 465 ASN A 104 REMARK 465 GLY A 105 REMARK 465 ARG A 106 REMARK 465 LYS A 107 REMARK 465 SER A 108 REMARK 465 THR A 109 REMARK 465 GLU A 110 REMARK 465 PHE A 111 REMARK 465 PRO A 112 REMARK 465 ARG A 113 REMARK 465 LYS A 114 REMARK 465 ILE A 115 REMARK 465 ARG A 116 REMARK 465 GLU A 117 REMARK 465 GLN A 118 REMARK 465 GLU A 119 REMARK 465 PRO A 120 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 HD1 HIS A 84 H ASN A 99 1.32 REMARK 500 H LYS A 83 OD2 ASP A 86 1.40 REMARK 500 H GLU A 52 O ILE A 59 1.47 REMARK 500 H HIS A 54 O GLU A 57 1.54 REMARK 500 O ILE A 88 H PHE A 95 1.55 REMARK 500 O GLN A 70 H THR A 89 1.55 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 TRP A 2 77.68 -119.46 REMARK 500 1 THR A 4 93.22 37.62 REMARK 500 1 GLN A 56 13.27 -145.97 REMARK 500 1 ASN A 72 29.67 46.52 REMARK 500 1 ILE A 90 -146.55 -97.56 REMARK 500 1 ASP A 92 10.17 -142.65 REMARK 500 2 TRP A 2 70.49 -154.93 REMARK 500 2 SER A 13 36.28 35.19 REMARK 500 2 SER A 23 -43.00 -130.40 REMARK 500 2 ASN A 72 26.00 49.51 REMARK 500 2 ILE A 90 -150.46 -97.79 REMARK 500 2 ASP A 92 18.20 -143.47 REMARK 500 3 SER A 13 -127.52 44.39 REMARK 500 3 GLU A 34 -11.01 -48.00 REMARK 500 3 GLN A 56 21.73 -146.07 REMARK 500 3 ASN A 67 78.88 -119.62 REMARK 500 3 ILE A 90 -145.48 -94.34 REMARK 500 3 ASP A 92 17.91 -148.16 REMARK 500 4 TRP A 2 66.47 -167.97 REMARK 500 4 ARG A 12 -98.91 37.21 REMARK 500 4 GLU A 55 -68.27 -21.09 REMARK 500 4 GLN A 56 28.05 -146.17 REMARK 500 4 ASN A 67 79.78 -119.48 REMARK 500 4 ILE A 90 -147.34 -84.56 REMARK 500 4 ASP A 92 14.46 -142.73 REMARK 500 5 ARG A 12 25.04 33.62 REMARK 500 5 SER A 13 9.36 58.55 REMARK 500 5 GLU A 55 -19.09 -42.18 REMARK 500 5 SER A 65 -53.94 -129.76 REMARK 500 5 ILE A 90 -147.46 -87.83 REMARK 500 5 ASP A 92 19.92 -147.80 REMARK 500 6 ARG A 12 91.26 34.18 REMARK 500 6 SER A 13 105.48 -7.11 REMARK 500 6 GLU A 55 -61.04 -29.21 REMARK 500 6 GLN A 56 27.00 -145.09 REMARK 500 6 ASN A 72 18.83 50.68 REMARK 500 6 ILE A 90 -144.66 -91.67 REMARK 500 6 ASP A 92 14.19 -147.58 REMARK 500 7 ARG A 12 -139.65 -143.58 REMARK 500 7 GLN A 47 58.81 -117.16 REMARK 500 7 GLN A 56 22.83 -146.21 REMARK 500 7 ASN A 72 29.07 45.60 REMARK 500 7 GLU A 78 169.10 176.41 REMARK 500 7 ILE A 90 -146.64 -77.57 REMARK 500 7 ASP A 92 13.56 -142.80 REMARK 500 8 TRP A 2 148.54 56.79 REMARK 500 8 ARG A 12 -87.93 -143.93 REMARK 500 8 ASN A 72 14.96 46.14 REMARK 500 8 ILE A 90 -147.06 -80.86 REMARK 500 8 ASP A 92 20.50 -141.65 REMARK 500 REMARK 500 THIS ENTRY HAS 147 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL DBREF 1R21 A 1 120 UNP P46013 KI67_HUMAN 1 120 SEQADV 1R21 GLY A -7 UNP P46013 CLONING ARTIFACT SEQADV 1R21 SER A -6 UNP P46013 CLONING ARTIFACT SEQADV 1R21 PRO A -5 UNP P46013 CLONING ARTIFACT SEQADV 1R21 GLU A -4 UNP P46013 CLONING ARTIFACT SEQADV 1R21 PHE A -3 UNP P46013 CLONING ARTIFACT SEQADV 1R21 PRO A -2 UNP P46013 CLONING ARTIFACT SEQADV 1R21 GLY A -1 UNP P46013 CLONING ARTIFACT SEQADV 1R21 GLY A 0 UNP P46013 CLONING ARTIFACT SEQRES 1 A 128 GLY SER PRO GLU PHE PRO GLY GLY MET TRP PRO THR ARG SEQRES 2 A 128 ARG LEU VAL THR ILE LYS ARG SER GLY VAL ASP GLY PRO SEQRES 3 A 128 HIS PHE PRO LEU SER LEU SER THR CYS LEU PHE GLY ARG SEQRES 4 A 128 GLY ILE GLU CYS ASP ILE ARG ILE GLN LEU PRO VAL VAL SEQRES 5 A 128 SER LYS GLN HIS CYS LYS ILE GLU ILE HIS GLU GLN GLU SEQRES 6 A 128 ALA ILE LEU HIS ASN PHE SER SER THR ASN PRO THR GLN SEQRES 7 A 128 VAL ASN GLY SER VAL ILE ASP GLU PRO VAL ARG LEU LYS SEQRES 8 A 128 HIS GLY ASP VAL ILE THR ILE ILE ASP ARG SER PHE ARG SEQRES 9 A 128 TYR GLU ASN GLU SER LEU GLN ASN GLY ARG LYS SER THR SEQRES 10 A 128 GLU PHE PRO ARG LYS ILE ARG GLU GLN GLU PRO SHEET 1 A 6 VAL A 15 PRO A 21 0 SHEET 2 A 6 ARG A 5 ARG A 12 -1 N LEU A 7 O PHE A 20 SHEET 3 A 6 SER A 94 ASN A 99 -1 O ARG A 96 N VAL A 8 SHEET 4 A 6 ASP A 86 THR A 89 -1 N ILE A 88 O PHE A 95 SHEET 5 A 6 GLN A 70 VAL A 71 -1 N GLN A 70 O THR A 89 SHEET 6 A 6 SER A 74 VAL A 75 -1 O SER A 74 N VAL A 71 SHEET 1 B 5 ILE A 37 ARG A 38 0 SHEET 2 B 5 THR A 26 GLY A 30 1 N GLY A 30 O ILE A 37 SHEET 3 B 5 CYS A 49 ILE A 53 -1 O CYS A 49 N PHE A 29 SHEET 4 B 5 ALA A 58 LEU A 60 -1 O ILE A 59 N GLU A 52 SHEET 5 B 5 VAL A 80 ARG A 81 -1 O VAL A 80 N LEU A 60 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 2 2 Bytes