Header list of 2aff.pdb file
Complete list - ar 9 Bytes
HEADER CELL CYCLE 25-JUL-05 2AFF TITLE THE SOLUTION STRUCTURE OF THE KI67FHA/HNIFK(226-269)3P COMPLEX COMPND MOL_ID: 1; COMPND 2 MOLECULE: ANTIGEN KI-67; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: FHA DOMAIN; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: MKI67 FHA DOMAIN INTERACTING NUCLEOLAR PHOSPHOPROTEIN; COMPND 8 CHAIN: B; COMPND 9 FRAGMENT: RESIDUES 226-269; COMPND 10 SYNONYM: NUCLEOLAR PROTEIN INTERACTING WITH THE FHA DOMAIN OF PKI-67; COMPND 11 HNIFK; NUCLEOLAR PHOSPHOPROTEIN NOPP34; COMPND 12 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: MKI67; 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: PEG; SOURCE 11 MOL_ID: 2; SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 13 ORGANISM_COMMON: HUMAN; SOURCE 14 ORGANISM_TAXID: 9606; SOURCE 15 GENE: MKI67IP; SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 17 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PEG KEYWDS KI67; FHA; NIFK; NMR; PHOSPHOPROTEIN, CELL CYCLE EXPDTA SOLUTION NMR NUMMDL 100 AUTHOR I.-J.L.BYEON,H.LI,H.SONG,A.M.GRONENBORN,M.D.TSAI REVDAT 5 09-MAR-22 2AFF 1 REMARK LINK REVDAT 4 26-MAY-10 2AFF 1 SEQADV SOURCE REVDAT 3 24-FEB-09 2AFF 1 VERSN REVDAT 2 28-MAR-06 2AFF 1 JRNL REVDAT 1 25-OCT-05 2AFF 0 JRNL AUTH I.J.BYEON,H.LI,H.SONG,A.M.GRONENBORN,M.D.TSAI JRNL TITL SEQUENTIAL PHOSPHORYLATION AND MULTISITE INTERACTIONS JRNL TITL 2 CHARACTERIZE SPECIFIC TARGET RECOGNITION BY THE FHA DOMAIN JRNL TITL 3 OF KI67. JRNL REF NAT.STRUCT.MOL.BIOL. V. 12 987 2005 JRNL REFN ISSN 1545-9993 JRNL PMID 16244663 JRNL DOI 10.1038/NSMB1008 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH H.LI,I.-J.L.BYEON,Y.JU,M.-D.TSAI REMARK 1 TITL STRUCTURE OF HUMAN KI67 FHA DOMAIN AND ITS BINDING TO A REMARK 1 TITL 2 PHOSPHOPROTEIN FRAGMENT FROM HNIFK REVEAL UNIQUE RECOGNITION REMARK 1 TITL 3 SITES AND NEW VIEWS TO THE STRUCTURAL BASIS OF FHA DOMAIN REMARK 1 TITL 4 FUNCTIONS. REMARK 1 REF J.MOL.BIOL. V. 335 371 2004 REMARK 1 REFN ISSN 0022-2836 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR NIH VERSION, X-PLOR NIH VERSION 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 3476 CONSTRAINTS, 3141 ARE DISTANCE, 215 DIHEDRAL ANGLE, AND 120 REMARK 3 N-H RESIDUAL DIPOLAR COUPLING CONSTRAINTS REMARK 4 REMARK 4 2AFF COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-AUG-05. REMARK 100 THE DEPOSITION ID IS D_1000033829. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 293 REMARK 210 PH : 7.4 REMARK 210 IONIC STRENGTH : 150 MM NACL REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 0.9 MM KI67 FHA U-15N,13C; 1 MM REMARK 210 HNIFK(226-269)3P UNLABELED 5 MM REMARK 210 HEPES, 5 MM DTT, 1 MM EDTA, 150 REMARK 210 MM NACL, PH 7.4; 0.9 MM KI67 FHA REMARK 210 U-15N,13C; 1 MM HNIFK(226-269)3P REMARK 210 UNLABELED 5 MM HEPES, 5 MM DTT, REMARK 210 1 MM EDTA, 150 MM NACL, PH 7.4; REMARK 210 1 MM KI67 FHA UNLABLED; 0.9 MM REMARK 210 HNIFK(226-269)3P U-15N,13C 5 MM REMARK 210 HEPES, 5 MM DTT, 1 MM EDTA, 150 REMARK 210 MM NACL, PH 7.4; 1 MM KI67 FHA REMARK 210 UNLABLED; 0.9 MM HNIFK(226-269) REMARK 210 3P U-15N,13C 5 MM HEPES, 5 MM REMARK 210 DTT, 1 MM EDTA, 150 MM NACL, PH REMARK 210 7.4 REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N REMARK 210 -SEPARATED_NOESY; 3D_12C/14N-FILTERED_13C_SEPARATED NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 750 MHZ; 600 MHZ; 500 REMARK 210 MHZ REMARK 210 SPECTROMETER MODEL : AVANCE; DMX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NULL REMARK 210 METHOD USED : SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 512 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 100 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST REMARK 210 RESTRAINT VIOLATIONS,STRUCTURES REMARK 210 WITH THE LOWEST 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: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B 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 1-100 REMARK 465 RES C SSSEQI REMARK 465 MET A 1 REMARK 465 TRP A 2 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 465 LYS B 226 REMARK 465 THR B 227 REMARK 465 SER B 268 REMARK 465 CYS B 269 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 ILE A 90 H ARG A 93 1.43 REMARK 500 HE ARG A 31 O VAL A 44 1.46 REMARK 500 H ILE A 90 O ARG A 93 1.46 REMARK 500 O GLN A 70 H THR A 89 1.51 REMARK 500 H VAL A 71 O SER A 74 1.52 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 GLN A 40 38.40 -81.74 REMARK 500 1 HIS A 48 -74.13 34.26 REMARK 500 1 ILE A 76 68.46 -113.89 REMARK 500 1 ILE A 91 -101.56 33.24 REMARK 500 1 SEP B 230 4.93 -66.50 REMARK 500 1 ASP B 254 -14.58 -45.44 REMARK 500 1 LYS B 257 -41.38 -20.19 REMARK 500 1 ASP B 258 62.19 -100.12 REMARK 500 1 ASP B 259 -113.67 -50.61 REMARK 500 1 GLU B 260 22.54 -151.72 REMARK 500 2 GLN A 40 28.22 -78.78 REMARK 500 2 PRO A 42 -8.74 -53.84 REMARK 500 2 HIS A 48 -73.31 35.88 REMARK 500 2 ILE A 91 -105.58 35.34 REMARK 500 2 SEP B 230 -7.58 -56.27 REMARK 500 2 LYS B 257 11.53 -67.82 REMARK 500 2 ASP B 259 54.25 4.92 REMARK 500 2 GLU B 260 4.37 55.46 REMARK 500 3 LEU A 22 47.86 -79.06 REMARK 500 3 GLN A 40 25.48 -77.25 REMARK 500 3 HIS A 48 -76.13 37.75 REMARK 500 3 GLU A 55 -26.08 -39.73 REMARK 500 3 GLU A 57 -158.27 -161.84 REMARK 500 3 ILE A 91 -109.30 38.28 REMARK 500 3 SEP B 230 -18.70 89.57 REMARK 500 3 TPO B 234 79.57 -115.30 REMARK 500 3 LYS B 257 -137.68 -125.29 REMARK 500 3 ASP B 258 74.37 -9.58 REMARK 500 3 GLU B 260 2.75 46.48 REMARK 500 4 GLN A 40 28.31 -73.22 REMARK 500 4 HIS A 48 -74.25 31.08 REMARK 500 4 ILE A 91 -94.12 38.61 REMARK 500 4 ASP B 229 158.04 95.55 REMARK 500 4 GLN B 231 23.88 170.41 REMARK 500 4 ASN B 253 27.40 91.39 REMARK 500 4 ASP B 255 58.05 106.28 REMARK 500 4 LYS B 257 -89.24 20.52 REMARK 500 4 ASP B 258 87.76 -27.11 REMARK 500 4 ASP B 259 -93.09 -87.06 REMARK 500 5 GLN A 40 34.24 -73.73 REMARK 500 5 HIS A 48 -78.05 39.22 REMARK 500 5 GLU A 55 -28.85 -39.75 REMARK 500 5 ILE A 91 -98.69 35.99 REMARK 500 5 ASP B 229 -78.70 15.10 REMARK 500 5 SEP B 230 9.28 -152.91 REMARK 500 5 TPO B 234 78.27 -112.55 REMARK 500 5 ASN B 253 12.79 -177.47 REMARK 500 5 ASP B 255 66.30 156.27 REMARK 500 5 LYS B 257 8.29 -66.20 REMARK 500 6 GLN A 40 25.64 -75.88 REMARK 500 REMARK 500 THIS ENTRY HAS 925 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1R21 RELATED DB: PDB REMARK 900 THE SOLUTION STRUCTURE OF KI67FHA IN A FREE FORM DBREF 2AFF A 1 120 UNP P46013 KI67_HUMAN 1 120 DBREF 2AFF B 226 269 UNP Q9BYG3 MK67I_HUMAN 226 269 SEQRES 1 A 120 MET TRP PRO THR ARG ARG LEU VAL THR ILE LYS ARG SER SEQRES 2 A 120 GLY VAL ASP GLY PRO HIS PHE PRO LEU SER LEU SER THR SEQRES 3 A 120 CYS LEU PHE GLY ARG GLY ILE GLU CYS ASP ILE ARG ILE SEQRES 4 A 120 GLN LEU PRO VAL VAL SER LYS GLN HIS CYS LYS ILE GLU SEQRES 5 A 120 ILE HIS GLU GLN GLU ALA ILE LEU HIS ASN PHE SER SER SEQRES 6 A 120 THR ASN PRO THR GLN VAL ASN GLY SER VAL ILE ASP GLU SEQRES 7 A 120 PRO VAL ARG LEU LYS HIS GLY ASP VAL ILE THR ILE ILE SEQRES 8 A 120 ASP ARG SER PHE ARG TYR GLU ASN GLU SER LEU GLN ASN SEQRES 9 A 120 GLY ARG LYS SER THR GLU PHE PRO ARG LYS ILE ARG GLU SEQRES 10 A 120 GLN GLU PRO SEQRES 1 B 44 LYS THR VAL ASP SEP GLN GLY PRO TPO PRO VAL CYS TPO SEQRES 2 B 44 PRO THR PHE LEU GLU ARG ARG LYS SER GLN VAL ALA GLU SEQRES 3 B 44 LEU ASN ASP ASP ASP LYS ASP ASP GLU ILE VAL PHE LYS SEQRES 4 B 44 GLN PRO ILE SER CYS MODRES 2AFF SEP B 230 SER PHOSPHOSERINE MODRES 2AFF TPO B 234 THR PHOSPHOTHREONINE MODRES 2AFF TPO B 238 THR PHOSPHOTHREONINE HET SEP B 230 14 HET TPO B 234 17 HET TPO B 238 17 HETNAM SEP PHOSPHOSERINE HETNAM TPO PHOSPHOTHREONINE HETSYN SEP PHOSPHONOSERINE HETSYN TPO PHOSPHONOTHREONINE FORMUL 2 SEP C3 H8 N O6 P FORMUL 2 TPO 2(C4 H10 N O6 P) HELIX 1 1 TPO B 238 LEU B 252 1 15 HELIX 2 2 ASN B 253 ASP B 258 5 6 SHEET 1 A 6 ASP A 16 PRO A 21 0 SHEET 2 A 6 ARG A 5 ILE A 10 -1 N LEU A 7 O PHE A 20 SHEET 3 A 6 ARG A 93 ASN A 99 -1 O GLU A 98 N ARG A 6 SHEET 4 A 6 VAL A 87 ILE A 90 -1 N ILE A 90 O ARG A 93 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 6 VAL A 80 LEU A 82 0 SHEET 2 B 6 ALA A 58 ASN A 62 -1 N ALA A 58 O LEU A 82 SHEET 3 B 6 CYS A 49 ILE A 53 -1 N LYS A 50 O HIS A 61 SHEET 4 B 6 THR A 26 GLY A 30 -1 N PHE A 29 O CYS A 49 SHEET 5 B 6 ILE A 37 ILE A 39 1 O ILE A 37 N LEU A 28 SHEET 6 B 6 ILE B 261 PHE B 263 -1 O VAL B 262 N ARG A 38 LINK C ASP B 229 N SEP B 230 1555 1555 1.33 LINK C SEP B 230 N GLN B 231 1555 1555 1.33 LINK C PRO B 233 N TPO B 234 1555 1555 1.33 LINK C TPO B 234 N PRO B 235 1555 1555 1.31 LINK C CYS B 237 N TPO B 238 1555 1555 1.34 LINK C TPO B 238 N PRO B 239 1555 1555 1.32 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 - ar 9 Bytes