Header list of 1sv1.pdb file
Complete list - r 25 2 Bytes
HEADER CIRCADIAN CLOCK PROTEIN 26-MAR-04 1SV1 TITLE NMR STRUCTURE OF THE THKAIA180C-CIIABD COMPLEX (25-STRUCTURE ENSEMBLE) 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 NUMMDL 25 AUTHOR I.VAKONAKIS,A.C.LIWANG REVDAT 3 13-JUL-11 1SV1 1 VERSN REVDAT 2 24-FEB-09 1SV1 1 VERSN REVDAT 1 03-AUG-04 1SV1 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 2420 TOTAL REMARK 3 RESTRAINTS: 1858 ARE NOE DERIVED, 58 ARE FROM HYDROGEN BONDS, 244 REMARK 3 ARE DIHEDRAL ANGLES AND 260 ARE 13C CHEMICAL SHIFTS. REMARK 4 REMARK 4 1SV1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-MAR-04. REMARK 100 THE RCSB ID CODE IS RCSB022015. 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 : 1.1 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 : 50 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 25 REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST ENERGY STRUCTURES THAT REMARK 210 SATISFY ALL EXPERIMENTAL REMARK 210 RESTRAINTS REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 11 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 REMARK 210 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 ALA C 422 H ILE C 424 1.24 REMARK 500 O ALA D 522 H ILE D 524 1.24 REMARK 500 O LYS B 234 H GLU B 237 1.40 REMARK 500 O LYS A 34 H GLU A 37 1.40 REMARK 500 O SER B 254 H GLU B 258 1.43 REMARK 500 O SER A 54 H GLU A 58 1.43 REMARK 500 O GLN A 70 H GLU A 74 1.48 REMARK 500 O GLN B 270 H GLU B 274 1.48 REMARK 500 O GLU A 16 H ILE A 20 1.50 REMARK 500 O GLU B 216 H ILE B 220 1.50 REMARK 500 O ASN B 236 H ASP B 240 1.54 REMARK 500 O ASN A 36 H ASP A 40 1.54 REMARK 500 O GLN A 55 H ILE A 59 1.55 REMARK 500 O GLN B 255 H ILE B 259 1.55 REMARK 500 OD1 ASP D 516 H GLU D 517 1.56 REMARK 500 OD1 ASP C 416 H GLU C 417 1.56 REMARK 500 O ARG B 211 H ASP B 215 1.59 REMARK 500 O ARG A 11 H ASP A 15 1.59 REMARK 500 O ALA C 422 N ILE C 424 2.19 REMARK 500 O ALA D 522 N ILE D 524 2.19 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 ARG A 4 117.79 -30.29 REMARK 500 1 ASP A 32 -16.84 -145.42 REMARK 500 1 VAL A 35 -32.06 -39.43 REMARK 500 1 ARG B 204 117.91 -30.30 REMARK 500 1 ASP B 232 -16.84 -145.39 REMARK 500 1 VAL B 235 -31.90 -39.62 REMARK 500 1 MET C 402 -75.13 -87.82 REMARK 500 1 ALA C 403 85.81 -166.49 REMARK 500 1 SER C 407 -56.22 -131.50 REMARK 500 1 PRO C 410 168.22 -37.85 REMARK 500 1 THR C 411 95.50 31.70 REMARK 500 1 ARG C 412 -38.87 -162.68 REMARK 500 1 THR C 419 155.20 50.09 REMARK 500 1 GLU C 420 72.25 -64.84 REMARK 500 1 ALA C 422 -88.09 36.56 REMARK 500 1 ARG C 423 -39.12 54.15 REMARK 500 1 ALA C 425 -8.12 52.90 REMARK 500 1 LYS C 426 -7.17 54.09 REMARK 500 1 MET D 502 -74.87 -87.88 REMARK 500 1 ALA D 503 85.74 -166.60 REMARK 500 1 SER D 507 -56.23 -131.52 REMARK 500 1 PRO D 510 168.23 -37.91 REMARK 500 1 THR D 511 95.51 31.66 REMARK 500 1 ARG D 512 -38.73 -162.65 REMARK 500 1 THR D 519 155.25 50.18 REMARK 500 1 GLU D 520 72.28 -64.93 REMARK 500 1 ALA D 522 -87.94 36.63 REMARK 500 1 ARG D 523 -39.10 54.01 REMARK 500 1 ALA D 525 -7.92 52.80 REMARK 500 1 LYS D 526 -7.28 53.99 REMARK 500 2 ARG A 4 100.44 18.24 REMARK 500 2 MET A 5 75.70 -58.85 REMARK 500 2 SER A 77 -123.63 0.56 REMARK 500 2 GLU A 78 -10.53 167.86 REMARK 500 2 ARG B 204 100.60 18.20 REMARK 500 2 MET B 205 75.60 -58.85 REMARK 500 2 SER B 277 -123.57 0.53 REMARK 500 2 GLU B 278 -10.55 167.81 REMARK 500 2 SER C 407 -79.80 -167.46 REMARK 500 2 THR C 409 48.24 -158.51 REMARK 500 2 PRO C 410 149.48 -35.68 REMARK 500 2 ASP C 416 -164.09 -105.47 REMARK 500 2 THR C 419 68.28 23.30 REMARK 500 2 GLU C 420 177.44 44.40 REMARK 500 2 LEU C 421 -139.93 -177.22 REMARK 500 2 ALA C 422 2.43 -68.99 REMARK 500 2 ARG C 423 -1.08 -46.71 REMARK 500 2 ALA C 425 -29.81 59.62 REMARK 500 2 LYS C 426 168.42 54.60 REMARK 500 2 MET C 428 -161.68 -49.59 REMARK 500 REMARK 500 THIS ENTRY HAS 779 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1Q6B RELATED DB: PDB REMARK 900 25-STRUCTURE ENSEMBLE OF FREE THKAIA180C REMARK 900 RELATED ID: 1SUY RELATED DB: PDB REMARK 900 NMR STRUCTURE OF THE THKAIA180C-CIIABD COMPLEX (AVERAGE REMARK 900 MINIMIZED STRUCTURE) DBREF 1SV1 A 4 107 UNP Q79V62 KAIA_SYNEL 180 283 DBREF 1SV1 B 204 307 UNP Q79V62 KAIA_SYNEL 180 283 DBREF 1SV1 C 404 434 UNP Q8RR33 Q8RR33 488 518 DBREF 1SV1 D 504 534 UNP Q8RR33 Q8RR33 488 518 SEQADV 1SV1 ALA A 1 UNP Q79V62 CLONING ARTIFACT SEQADV 1SV1 MET A 2 UNP Q79V62 CLONING ARTIFACT SEQADV 1SV1 ALA A 3 UNP Q79V62 CLONING ARTIFACT SEQADV 1SV1 ALA B 201 UNP Q79V62 CLONING ARTIFACT SEQADV 1SV1 MET B 202 UNP Q79V62 CLONING ARTIFACT SEQADV 1SV1 ALA B 203 UNP Q79V62 CLONING ARTIFACT SEQADV 1SV1 ALA C 401 UNP Q8RR33 CLONING ARTIFACT SEQADV 1SV1 MET C 402 UNP Q8RR33 CLONING ARTIFACT SEQADV 1SV1 ALA C 403 UNP Q8RR33 CLONING ARTIFACT SEQADV 1SV1 ALA D 501 UNP Q8RR33 CLONING ARTIFACT SEQADV 1SV1 MET D 502 UNP Q8RR33 CLONING ARTIFACT SEQADV 1SV1 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 SER A 6 TYR A 28 1 23 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 ILE A 80 5 3 HELIX 5 5 LEU A 81 SER A 102 1 22 HELIX 6 6 SER B 206 TYR B 228 1 23 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 ILE B 280 5 3 HELIX 10 10 LEU B 281 SER B 302 1 22 HELIX 11 11 GLY C 427 GLU C 432 5 6 HELIX 12 12 GLY D 527 GLU D 532 5 6 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 MODEL 1
Complete list - r 25 2 Bytes