Header list of 1suy.pdb file
Complete list - 25 20 Bytes
HEADER CIRCADIAN CLOCK PROTEIN 26-MAR-04 1SUY TITLE NMR STRUCTURE OF THE THKAIA180C-CIIABD COMPLEX (AVERAGE MINIMIZED TITLE 2 STRUCTURE) COMPND MOL_ID: 1; COMPND 2 MOLECULE: CIRCADIAN CLOCK PROTEIN KAIA; COMPND 3 CHAIN: A, B; COMPND 4 FRAGMENT: C-TERMINAL RESIDUES 180-283; COMPND 5 SYNONYM: THKAIA180C; COMPND 6 ENGINEERED: YES; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: CIRCADIAN CLOCK PROTEIN KAIC; COMPND 9 CHAIN: C, D; COMPND 10 FRAGMENT: C-TERMINAL RESIDUES 488-518; COMPND 11 SYNONYM: CIIABD; COMPND 12 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: PET32A+; SOURCE 11 MOL_ID: 2; SOURCE 12 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS; SOURCE 13 ORGANISM_TAXID: 197221; SOURCE 14 STRAIN: BP-1; SOURCE 15 GENE: KAIC; 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: PET32A+ KEYWDS X-CLASS FOUR HELIX BUNDLE, PROTEIN-PEPTIDE COMPLEX, CIRCADIAN CLOCK KEYWDS 2 PROTEIN EXPDTA SOLUTION NMR MDLTYP MINIMIZED AVERAGE AUTHOR I.VAKONAKIS,A.C.LIWANG REVDAT 3 13-JUL-11 1SUY 1 VERSN REVDAT 2 24-FEB-09 1SUY 1 VERSN REVDAT 1 03-AUG-04 1SUY 0 JRNL AUTH I.VAKONAKIS,A.C.LIWANG JRNL TITL STRUCTURE OF THE C-TERMINAL DOMAIN OF THE CLOCK PROTEIN KAIA JRNL TITL 2 IN COMPLEX WITH A KAIC-DERIVED PEPTIDE: IMPLICATIONS FOR JRNL TITL 3 KAIC REGULATION. JRNL REF PROC.NATL.ACAD.SCI.USA V. 101 10925 2004 JRNL REFN ISSN 0027-8424 JRNL PMID 15256595 JRNL DOI 10.1073/PNAS.0403037101 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XPLOR-NIH 2.9.1 REMARK 3 AUTHORS : C.D.SCHWIETERS,J.J.KUSZEWSKI,N.TJANDRA,G.M.CLORE REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURE IS BASED ON A TOTAL OF REMARK 3 2420 RESTRAINTS: 1858 ARE NOE-DERIVED, 58 ARE FROM HYDROGEN REMARK 3 BONDS, 244 ARE DIHEDRAL ANGLES AND 260 ARE 13C CHEMICAL SHIFTS. REMARK 4 REMARK 4 1SUY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-MAR-04. REMARK 100 THE RCSB ID CODE IS RCSB022012. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 323 REMARK 210 PH : 7 REMARK 210 IONIC STRENGTH : 20 MM NACL, 20 MM NAPI REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1.1 MM THKAIA180C U-15N, 1.1 MM REMARK 210 CIIABD, 20 MM NACL, 20 MM NA2HPO4 REMARK 210 PH 7.07 AT 296K; 1.1 MM REMARK 210 THKAIA180C U-15N,13C, 1.1 MM REMARK 210 CIIABD, 20 MM NACL, 20 MM NA2HPO4 REMARK 210 PH 7.07 AT 296K; 1.2 MM REMARK 210 THKAIA180C, 1.2 MM CIIABD U-15N, REMARK 210 13C, 20 MM NACL, 20 MM NA2HPO4 PH REMARK 210 7.07 AT 296K; 0.8 MM THKAIA180C U REMARK 210 -15N,13C, 0.8 MM THKAIA180C, 1.6 REMARK 210 MM CIIABD U-15N,13C, 20 MM NACL, REMARK 210 20 MM NA2HPO4 PH 7.07 AT 296K REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 4D_13C- REMARK 210 SEPARATED_NOESY; 13C-EDITED/12C- REMARK 210 FILTERED 3D NOESY; 3D_13C- REMARK 210 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 : VNMR 6.1 REV. C, NMRPIPE 2.1 REMARK 210 REV. 2002.044.17.08, PIPP 4.2.6, REMARK 210 XPLOR-NIH 2.9.1 REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED REMARK 210 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: ASSIGNMENTS OF THKAIA180C AND CIIABD WERE PERFORMED REMARK 210 THROUGH CBCA(CO)NH, CBCANH, HBHA(CO)NH AND HC(C)H-COSY EXPERIMENTS 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: TETRAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D 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 O LEU C 431 HG2 GLU C 432 0.24 REMARK 500 O LEU D 531 HG2 GLU D 532 0.24 REMARK 500 NE ARG A 85 HE ARG B 285 0.41 REMARK 500 HE ARG A 85 NE ARG B 285 0.42 REMARK 500 HE ARG A 85 HE ARG B 285 0.57 REMARK 500 HH21 ARG A 85 HH21 ARG B 285 0.72 REMARK 500 HH21 ARG A 85 NH2 ARG B 285 0.76 REMARK 500 NH2 ARG A 85 HH21 ARG B 285 0.76 REMARK 500 O ILE C 424 H LYS C 426 0.77 REMARK 500 O ILE D 524 H LYS D 526 0.77 REMARK 500 CG MET B 202 HB2 MET B 205 0.99 REMARK 500 CG MET A 2 HB2 MET A 5 0.99 REMARK 500 HH12 ARG A 100 HD22 LEU D 531 1.02 REMARK 500 HH12 ARG B 300 HD22 LEU C 431 1.02 REMARK 500 HG2 MET A 2 HB2 MET A 5 1.06 REMARK 500 HG2 MET B 202 HB2 MET B 205 1.06 REMARK 500 O LEU D 531 CG GLU D 532 1.08 REMARK 500 O LEU C 431 CG GLU C 432 1.08 REMARK 500 HG3 MET A 2 HB3 MET A 5 1.12 REMARK 500 HG3 MET B 202 HB3 MET B 205 1.12 REMARK 500 C LEU D 531 HG2 GLU D 532 1.19 REMARK 500 C LEU C 431 HG2 GLU C 432 1.19 REMARK 500 HG2 MET B 202 H MET B 205 1.20 REMARK 500 HG2 MET A 2 H MET A 5 1.20 REMARK 500 HD21 ASN A 30 H ALA A 33 1.22 REMARK 500 HD21 ASN B 230 H ALA B 233 1.23 REMARK 500 HG3 MET A 2 HB2 MET A 5 1.28 REMARK 500 HG3 MET B 202 HB2 MET B 205 1.29 REMARK 500 HG3 MET A 2 CB MET A 5 1.31 REMARK 500 HG3 MET B 202 CB MET B 205 1.31 REMARK 500 HD12 LEU B 263 HD12 ILE C 406 1.33 REMARK 500 HG3 GLU C 420 HE ARG C 423 1.33 REMARK 500 HG3 GLU D 520 HE ARG D 523 1.33 REMARK 500 HB3 LEU C 421 H ALA C 422 1.34 REMARK 500 HB3 LEU D 521 H ALA D 522 1.34 REMARK 500 HD12 LEU A 63 HD12 ILE D 506 1.34 REMARK 500 OD1 ASP B 283 H TYR B 284 1.35 REMARK 500 OD1 ASP A 83 H TYR A 84 1.35 REMARK 500 HD2 ARG A 85 HD2 ARG B 285 1.35 REMARK 500 NE ARG A 85 NE ARG B 285 1.38 REMARK 500 O GLU B 306 HG11 VAL B 307 1.39 REMARK 500 O GLU A 106 HG11 VAL A 107 1.39 REMARK 500 HD12 LEU A 82 OG1 THR D 519 1.39 REMARK 500 HD12 LEU B 282 OG1 THR C 419 1.40 REMARK 500 HG22 ILE A 39 HD1 HIS A 94 1.40 REMARK 500 HG22 ILE B 239 HD1 HIS B 294 1.41 REMARK 500 HH22 ARG A 100 HD21 LEU D 531 1.42 REMARK 500 O MET C 428 H ASP C 430 1.42 REMARK 500 O MET D 528 H ASP D 530 1.42 REMARK 500 HG2 LYS D 526 HE1 MET D 528 1.42 REMARK 500 REMARK 500 THIS ENTRY HAS 137 CLOSE CONTACTS 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 MET A 2 148.38 -37.37 REMARK 500 ALA A 3 86.37 -42.54 REMARK 500 VAL A 35 -30.93 -39.45 REMARK 500 MET B 202 148.30 -37.35 REMARK 500 ALA B 203 86.40 -42.49 REMARK 500 VAL B 235 -30.90 -39.50 REMARK 500 MET C 402 -44.48 135.29 REMARK 500 ALA C 403 -64.61 115.86 REMARK 500 SER C 407 -80.65 -109.15 REMARK 500 THR C 409 32.54 108.69 REMARK 500 PRO C 410 150.61 -37.81 REMARK 500 ARG C 412 -44.49 -133.15 REMARK 500 GLU C 417 -102.31 -35.03 REMARK 500 LYS C 418 2.99 -49.41 REMARK 500 THR C 419 126.38 5.47 REMARK 500 GLU C 420 155.93 -5.92 REMARK 500 LEU C 421 -128.68 -158.24 REMARK 500 ARG C 423 -23.46 -36.38 REMARK 500 ALA C 425 -45.28 36.06 REMARK 500 LYS C 426 0.30 98.56 REMARK 500 GLN C 429 45.94 -60.33 REMARK 500 LEU C 431 77.80 -50.87 REMARK 500 GLU C 432 -85.75 151.28 REMARK 500 SER C 433 149.96 -20.62 REMARK 500 MET D 502 -44.05 135.10 REMARK 500 ALA D 503 -64.54 115.52 REMARK 500 SER D 507 -80.59 -109.20 REMARK 500 THR D 509 32.58 108.63 REMARK 500 PRO D 510 150.60 -37.85 REMARK 500 ARG D 512 -44.48 -133.18 REMARK 500 GLU D 517 -102.30 -34.99 REMARK 500 LYS D 518 3.01 -49.45 REMARK 500 THR D 519 126.41 5.47 REMARK 500 GLU D 520 155.93 -5.97 REMARK 500 LEU D 521 -128.67 -158.21 REMARK 500 ARG D 523 -23.46 -36.37 REMARK 500 ALA D 525 -45.29 36.00 REMARK 500 LYS D 526 0.26 98.59 REMARK 500 GLN D 529 45.80 -60.28 REMARK 500 LEU D 531 77.78 -50.89 REMARK 500 GLU D 532 -85.68 151.29 REMARK 500 SER D 533 149.86 -20.47 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1Q6A RELATED DB: PDB REMARK 900 AVERAGE MINIMIZED STRUCTURE OF FREE THKAIA180C REMARK 900 RELATED ID: 1SV1 RELATED DB: PDB REMARK 900 NMR STRUCTURE OF THE THKAIA180C-CIIABD COMPLEX (25- REMARK 900 STRUCTURE ENSEMBLE) DBREF 1SUY A 4 107 UNP Q79V62 KAIA_SYNEL 180 283 DBREF 1SUY B 204 307 UNP Q79V62 KAIA_SYNEL 180 283 DBREF 1SUY C 404 434 UNP Q8RR33 Q8RR33 488 518 DBREF 1SUY D 504 534 UNP Q8RR33 Q8RR33 488 518 SEQADV 1SUY ALA A 1 UNP Q79V62 CLONING ARTIFACT SEQADV 1SUY MET A 2 UNP Q79V62 CLONING ARTIFACT SEQADV 1SUY ALA A 3 UNP Q79V62 CLONING ARTIFACT SEQADV 1SUY ALA B 201 UNP Q79V62 CLONING ARTIFACT SEQADV 1SUY MET B 202 UNP Q79V62 CLONING ARTIFACT SEQADV 1SUY ALA B 203 UNP Q79V62 CLONING ARTIFACT SEQADV 1SUY ALA C 401 UNP Q8RR33 CLONING ARTIFACT SEQADV 1SUY MET C 402 UNP Q8RR33 CLONING ARTIFACT SEQADV 1SUY ALA C 403 UNP Q8RR33 CLONING ARTIFACT SEQADV 1SUY ALA D 501 UNP Q8RR33 CLONING ARTIFACT SEQADV 1SUY MET D 502 UNP Q8RR33 CLONING ARTIFACT SEQADV 1SUY ALA D 503 UNP Q8RR33 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 SEQRES 1 C 34 ALA MET ALA GLY ILE ILE SER GLY THR PRO THR ARG ILE SEQRES 2 C 34 SER VAL ASP GLU LYS THR GLU LEU ALA ARG ILE ALA LYS SEQRES 3 C 34 GLY MET GLN ASP LEU GLU SER GLU SEQRES 1 D 34 ALA MET ALA GLY ILE ILE SER GLY THR PRO THR ARG ILE SEQRES 2 D 34 SER VAL ASP GLU LYS THR GLU LEU ALA ARG ILE ALA LYS SEQRES 3 D 34 GLY MET GLN ASP LEU GLU SER GLU HELIX 1 1 ALA A 1 MET A 5 5 5 HELIX 2 2 SER A 6 TYR A 28 1 23 HELIX 3 3 LYS A 34 ALA A 49 1 16 HELIX 4 4 SER A 52 GLU A 74 1 23 HELIX 5 5 SER A 77 ILE A 80 5 4 HELIX 6 6 LEU A 81 SER A 102 1 22 HELIX 7 7 ALA B 201 MET B 205 5 5 HELIX 8 8 SER B 206 TYR B 228 1 23 HELIX 9 9 LYS B 234 ALA B 249 1 16 HELIX 10 10 SER B 252 GLU B 274 1 23 HELIX 11 11 SER B 277 ILE B 280 5 4 HELIX 12 12 LEU B 281 SER B 302 1 22 HELIX 13 13 LEU C 421 ALA C 425 5 5 HELIX 14 14 LEU D 521 ALA D 525 5 5 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