Header list of 1q6a.pdb file
Complete list - 25 20 Bytes
HEADER CIRCADIAN CLOCK PROTEIN 13-AUG-03 1Q6A TITLE SOLUTION STRUCTURE OF THE C-TERMINAL DOMAIN OF THERMOSYNECHOCOCCUS TITLE 2 ELONGATUS KAIA (THKAIA180C); AVERAGED MINIMIZED STRUCTURE COMPND MOL_ID: 1; COMPND 2 MOLECULE: CIRCADIAN CLOCK PROTEIN KAIA HOMOLOG; COMPND 3 CHAIN: A, B; COMPND 4 FRAGMENT: C-TERMINAL DOMAIN (THKAIA180C); COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS; SOURCE 3 ORGANISM_TAXID: 197221; SOURCE 4 STRAIN: BP-1; SOURCE 5 GENE: KAIA; 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: PET-32A KEYWDS ALL ALPHA-HELIX PROTEIN, HOMODIMER, CIRCADIAN CLOCK PROTEIN EXPDTA SOLUTION NMR MDLTYP MINIMIZED AVERAGE AUTHOR I.VAKONAKIS,J.SUN,A.HOLZENBURG,S.S.GOLDEN,A.C.LIWANG REVDAT 4 13-JUL-11 1Q6A 1 VERSN REVDAT 3 24-FEB-09 1Q6A 1 VERSN REVDAT 2 17-FEB-04 1Q6A 1 JRNL REVDAT 1 19-AUG-03 1Q6A 0 JRNL AUTH I.VAKONAKIS,J.SUN,T.WU,A.HOLZENBURG,S.S.GOLDEN,A.C.LIWANG JRNL TITL NMR STRUCTURE OF THE KAIC-INTERACTING C-TERMINAL DOMAIN OF JRNL TITL 2 KAIA, A CIRCADIAN CLOCK PROTEIN: IMPLICATIONS FOR KAIA-KAIC JRNL TITL 3 INTERACTION JRNL REF PROC.NATL.ACAD.SCI.USA V. 101 1479 2004 JRNL REFN ISSN 0027-8424 JRNL PMID 14749515 JRNL DOI 10.1073/PNAS.0305516101 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XPLOR-NIH 2.9.1 REMARK 3 AUTHORS : CLORE REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURE IS BASED ON 2207 REMARK 3 RESTRAINTS OF WHICH 1740 ARE NOE RESTRAINTS. REMARK 4 REMARK 4 1Q6A COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-AUG-03. REMARK 100 THE RCSB ID CODE IS RCSB019969. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 323 REMARK 210 PH : 7.0 REMARK 210 IONIC STRENGTH : 20 MM NACL, 20 MM NAPI REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1.3 MM THKAIA180C U-15N, 20 MM REMARK 210 NACL, 20 MM PHOSPHATE BUFFER, 95% REMARK 210 H2O, 5% D2O; 1.3 MM THKAIA180C U- REMARK 210 15N,U-13C, 20 MM NACL, 20 MM REMARK 210 PHOSPHATE BUFFER, 95% H2O, 5% REMARK 210 D2O; 1.3 MM THKAIA180C U-15N,U- REMARK 210 13C, 20 MM NACL, 20 MM PHOSPHATE REMARK 210 BUFFER, 100% D2O; 1 MM THKAIA180C REMARK 210 U-15N,U-13C, 1 MM THKAIA180C NA- REMARK 210 N,NA-C, 20 MM NACL, 20 MM REMARK 210 PHOSPHATE BUFFER, 100% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 4D_13C- REMARK 210 SEPARATED_NOESY; 3D 13C-EDITED, REMARK 210 12C FILTERED NOESY; HACAHB; HNHB; REMARK 210 BRCTCO/CN; CBCA(CO)NH; CBCANH 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 2.1 REV 2002.044.17.08, REMARK 210 PIPP 4.2.6, XPLOR-NIH 2.9.1, VNMR REMARK 210 6.1 REV. C REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED REMARK 210 ANNEALING, RADIUS-OF-GYRATION, REMARK 210 CARBON CHEMICAL SHIFT AND REMARK 210 CONFORMATIONAL DATABASE POTENTIAL REMARK 210 REFINEMENT 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 : 1 REMARK 210 REMARK 210 REMARK: THIS IS THE OXIDIZED FORM OF THE PROTEIN. A DISULFIDE BOND REMARK 210 CONNECTS RESIDUE C96 OF EACH MONOMERIC UNIT. 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 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 HD13 ILE B 220 HZ1 LYS B 245 0.99 REMARK 500 HD13 ILE A 20 HZ1 LYS A 45 0.99 REMARK 500 O VAL A 35 H ILE A 39 1.33 REMARK 500 O VAL B 235 H ILE B 239 1.33 REMARK 500 NH2 ARG A 100 OD1 ASP B 250 1.37 REMARK 500 HG11 VAL A 43 HA LEU A 95 1.39 REMARK 500 HG11 VAL B 243 HA LEU B 295 1.39 REMARK 500 OD1 ASP A 50 NH2 ARG B 300 1.43 REMARK 500 HH21 ARG A 100 OD1 ASP B 250 1.46 REMARK 500 O ILE B 224 H TYR B 228 1.47 REMARK 500 O ILE A 24 H TYR A 28 1.47 REMARK 500 O SER A 77 H ASP A 79 1.49 REMARK 500 O SER B 277 H ASP B 279 1.49 REMARK 500 O HIS B 260 H MET B 264 1.49 REMARK 500 O HIS A 60 H MET A 64 1.49 REMARK 500 OD1 ASN B 230 H ALA B 233 1.51 REMARK 500 OD1 ASN A 30 H ALA A 33 1.51 REMARK 500 OD1 ASP A 50 HH21 ARG B 300 1.52 REMARK 500 O LEU A 17 H TYR A 21 1.54 REMARK 500 O LEU B 217 H TYR B 221 1.54 REMARK 500 HB2 GLU B 216 HZ3 LYS B 245 1.54 REMARK 500 HB2 GLU A 16 HZ3 LYS A 45 1.54 REMARK 500 O LYS B 245 H ALA B 249 1.55 REMARK 500 O LYS A 45 H ALA A 49 1.55 REMARK 500 O SER B 244 H PHE B 248 1.57 REMARK 500 O SER A 44 H PHE A 48 1.57 REMARK 500 O THR B 287 H VAL B 291 1.58 REMARK 500 O THR A 87 H VAL A 91 1.58 REMARK 500 O ASP B 240 OG SER B 244 1.68 REMARK 500 O ASP A 40 OG SER A 44 1.68 REMARK 500 O SER A 77 N ASP A 79 1.87 REMARK 500 O SER B 277 N ASP B 279 1.87 REMARK 500 OD1 ASN B 230 N ALA B 233 1.98 REMARK 500 OD1 ASN A 30 N ALA A 33 1.98 REMARK 500 NH2 ARG A 100 CG ASP B 250 2.13 REMARK 500 NH1 ARG A 18 OE2 GLU A 62 2.17 REMARK 500 NH1 ARG B 218 OE2 GLU B 262 2.18 REMARK 500 CZ ARG A 100 OD1 ASP B 250 2.18 REMARK 500 CG ASP A 50 NH2 ARG B 300 2.18 REMARK 500 O ILE A 24 N TYR A 28 2.18 REMARK 500 O ILE B 224 N TYR B 228 2.18 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 ALA A 3 99.01 -24.97 REMARK 500 ARG A 4 77.03 -112.72 REMARK 500 MET A 5 -77.07 -78.35 REMARK 500 SER A 6 169.87 46.86 REMARK 500 ASN A 30 -175.85 -62.17 REMARK 500 ALA A 49 33.87 -81.76 REMARK 500 ASP A 50 63.51 25.14 REMARK 500 ARG A 76 -124.45 -93.42 REMARK 500 GLU A 78 -12.30 -26.25 REMARK 500 ARG A 105 99.15 24.14 REMARK 500 ALA B 203 98.99 -25.01 REMARK 500 ARG B 204 77.06 -112.61 REMARK 500 MET B 205 -77.03 -78.41 REMARK 500 SER B 206 169.85 46.86 REMARK 500 ASN B 230 -175.87 -62.16 REMARK 500 ALA B 249 33.79 -81.76 REMARK 500 ASP B 250 63.54 25.23 REMARK 500 ARG B 276 -124.43 -93.45 REMARK 500 GLU B 278 -12.37 -26.14 REMARK 500 ARG B 305 99.12 24.14 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 5824 RELATED DB: BMRB REMARK 900 1H, 13C AND 15N BACKBONE AND SIDECHAIN CHEMICAL SHIFTS FOR REMARK 900 THE OXIDIZED FORM OF THIS PROTEIN REMARK 900 RELATED ID: 5825 RELATED DB: BMRB REMARK 900 1H, 13C AND 15N BACKBONE AND SIDECHAIN CHEMICAL SHIFTS FOR REMARK 900 THE REDUCED FORM OF THIS PROTEIN DBREF 1Q6A A 4 107 UNP Q8RR35 Q8RR35 180 283 DBREF 1Q6A B 204 307 UNP Q8RR35 Q8RR35 180 283 SEQADV 1Q6A ALA A 1 UNP Q8RR35 CLONING ARTIFACT SEQADV 1Q6A MET A 2 UNP Q8RR35 CLONING ARTIFACT SEQADV 1Q6A ALA A 3 UNP Q8RR35 CLONING ARTIFACT SEQADV 1Q6A ALA B 201 UNP Q8RR35 CLONING ARTIFACT SEQADV 1Q6A MET B 202 UNP Q8RR35 CLONING ARTIFACT SEQADV 1Q6A ALA B 203 UNP Q8RR35 CLONING ARTIFACT SEQRES 1 A 107 ALA MET ALA ARG MET SER PRO ALA ASP LYS ARG LYS LEU SEQRES 2 A 107 LEU ASP GLU LEU ARG SER ILE TYR ARG THR ILE VAL LEU SEQRES 3 A 107 GLU TYR PHE ASN THR ASP ALA LYS VAL ASN GLU ARG ILE SEQRES 4 A 107 ASP GLU PHE VAL SER LYS ALA PHE PHE ALA ASP ILE SER SEQRES 5 A 107 VAL SER GLN VAL LEU GLU ILE HIS VAL GLU LEU MET ASP SEQRES 6 A 107 THR PHE SER LYS GLN LEU LYS LEU GLU GLY ARG SER GLU SEQRES 7 A 107 ASP ILE LEU LEU ASP TYR ARG LEU THR LEU ILE ASP VAL SEQRES 8 A 107 ILE ALA HIS LEU CYS GLU MET TYR ARG ARG SER ILE PRO SEQRES 9 A 107 ARG GLU VAL SEQRES 1 B 107 ALA MET ALA ARG MET SER PRO ALA ASP LYS ARG LYS LEU SEQRES 2 B 107 LEU ASP GLU LEU ARG SER ILE TYR ARG THR ILE VAL LEU SEQRES 3 B 107 GLU TYR PHE ASN THR ASP ALA LYS VAL ASN GLU ARG ILE SEQRES 4 B 107 ASP GLU PHE VAL SER LYS ALA PHE PHE ALA ASP ILE SER SEQRES 5 B 107 VAL SER GLN VAL LEU GLU ILE HIS VAL GLU LEU MET ASP SEQRES 6 B 107 THR PHE SER LYS GLN LEU LYS LEU GLU GLY ARG SER GLU SEQRES 7 B 107 ASP ILE LEU LEU ASP TYR ARG LEU THR LEU ILE ASP VAL SEQRES 8 B 107 ILE ALA HIS LEU CYS GLU MET TYR ARG ARG SER ILE PRO SEQRES 9 B 107 ARG GLU VAL HELIX 1 1 PRO A 7 TYR A 28 1 22 HELIX 2 2 LYS A 34 ALA A 49 1 16 HELIX 3 3 SER A 52 GLY A 75 1 24 HELIX 4 4 GLU A 78 ASP A 83 1 6 HELIX 5 5 ASP A 83 SER A 102 1 20 HELIX 6 6 PRO B 207 TYR B 228 1 22 HELIX 7 7 LYS B 234 ALA B 249 1 16 HELIX 8 8 SER B 252 GLY B 275 1 24 HELIX 9 9 GLU B 278 ASP B 283 1 6 HELIX 10 10 ASP B 283 SER B 302 1 20 SSBOND 1 CYS A 96 CYS B 296 1555 1555 2.02 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 - 25 20 Bytes