Header list of 1xpw.pdb file
Complete list - r 2 2 Bytes
HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 09-OCT-04 1XPW TITLE SOLUTION NMR STRUCTURE OF HUMAN PROTEIN HSPCO34. NORTHEAST STRUCTURAL TITLE 2 GENOMICS TARGET HR1958 COMPND MOL_ID: 1; COMPND 2 MOLECULE: LOC51668 PROTEIN; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: HSPC034; COMPND 5 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: PP25; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 (LAMDA DE3) PMGK; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET14 KEYWDS GENE PP25, LOCUS LOC51668, C1ORF41, HOMO SAPIENS, NESGC CLUSTER ID KEYWDS 2 3237, TARGET HR1958, STRUCTURAL GENOMICS, APC10-RELATED PROTEIN, KEYWDS 3 NORTHEAST STRUCTURAL GENOMICS CONSORTIUM, PROTEIN STRUCTURE KEYWDS 4 INITIATIVE, PSI, JELLYROLL, BETA-SANDWICH, UNKNOWN FUNCTION EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR T.A.RAMELOT,R.XIAO,L.C.MA,T.B.ACTON,G.T.MONTELIONE,M.A.KENNEDY, AUTHOR 2 NORTHEAST STRUCTURAL GENOMICS CONSORTIUM (NESG) REVDAT 6 02-MAR-22 1XPW 1 REMARK SEQADV REVDAT 5 09-JUN-09 1XPW 1 JRNL REVDAT 4 24-FEB-09 1XPW 1 VERSN REVDAT 3 12-JUL-05 1XPW 1 REMARK MASTER REVDAT 2 25-JAN-05 1XPW 1 AUTHOR REMARK REVDAT 1 09-NOV-04 1XPW 0 JRNL AUTH T.A.RAMELOT,S.RAMAN,A.P.KUZIN,R.XIAO,L.C.MA,T.B.ACTON, JRNL AUTH 2 J.F.HUNT,G.T.MONTELIONE,D.BAKER,M.A.KENNEDY JRNL TITL IMPROVING NMR PROTEIN STRUCTURE QUALITY BY ROSETTA JRNL TITL 2 REFINEMENT: A MOLECULAR REPLACEMENT STUDY. JRNL REF PROTEINS V. 75 147 2009 JRNL REFN ISSN 0887-3585 JRNL PMID 18816799 JRNL DOI 10.1002/PROT.22229 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : NMRPIPE NMRPIPE.LINUX, CNS 1.1 REMARK 3 AUTHORS : DELAGLIO (NMRPIPE), BRUNGER (CNS) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: THE UNSTRUCTURED 10 RESIDUE N-TERMINAL REMARK 3 HIS TAG (MGHHHHHHSH) WAS NOT INCLUDED IN THE STRUCTURE REMARK 3 CALCULATION. REMARK 4 REMARK 4 1XPW COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-OCT-04. REMARK 100 THE DEPOSITION ID IS D_1000030626. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 6.5 REMARK 210 IONIC STRENGTH : 100 MM NACL REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1 MM U-15N,13C PROTEIN, 20 MM REMARK 210 MES, 100 MM NACL, 10 MM DTT, 5 REMARK 210 MM CACL2, 0.02% NAN3, 95% H2O, 5% REMARK 210 D2O; 1 MM U-15N,13C PROTEIN, 20 REMARK 210 MM MES, 100 MM NACL, 10 MM DTT, REMARK 210 5 MM CACL2, 0.02% NAN3, 100% D2O; REMARK 210 1 MM U-15N,5%-13C PROTEIN, 20 REMARK 210 MM MES, 100 MM NACL, 10 MM DTT, REMARK 210 5 MM CACL2, 0.02% NAN3, 95% H2O, REMARK 210 5% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C REMARK 210 -SEPARATED_NOESY; HNHA; 13C_HSQC; REMARK 210 4D_13C-SEPARATED_NOESY; H/D REMARK 210 EXCHANGE REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 750 MHZ; 600 MHZ REMARK 210 SPECTROMETER MODEL : INOVA; UNITY REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : FELIX 98, AUTOSTRUCTURE 2.1.0, X REMARK 210 -PLOR XPLOR-NIH-2.0.6, SPARKY REMARK 210 3.106 REMARK 210 METHOD USED : XPLOR SIMULATED ANNEALING, CNS REMARK 210 WATER REFINEMENT REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 25 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST REMARK 210 RESTRAINT VIOLATIONS REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: NULL 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 400 REMARK 400 COMPOUND REMARK 400 THIS PROTEIN HAS STOICHIOMETRIC CALCIUM BOUND. CALCIUM REMARK 400 COORDINATION COULD NOT BE DETERMINED, BUT IS CONSISTENT REMARK 400 WITH PDB ENTRY 1TVG 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 1-20 REMARK 465 RES C SSSEQI REMARK 465 MET A -9 REMARK 465 GLY A -8 REMARK 465 HIS A -7 REMARK 465 HIS A -6 REMARK 465 HIS A -5 REMARK 465 HIS A -4 REMARK 465 HIS A -3 REMARK 465 HIS A -2 REMARK 465 SER A -1 REMARK 465 HIS A 0 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 HZ3 LYS A 3 OE1 GLU A 60 1.59 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 2 -170.91 61.58 REMARK 500 1 LYS A 3 70.82 53.15 REMARK 500 1 HIS A 25 74.61 -111.04 REMARK 500 1 PHE A 68 -23.55 73.38 REMARK 500 1 PRO A 82 46.11 -70.10 REMARK 500 1 ASP A 84 84.48 57.25 REMARK 500 1 TRP A 88 -68.93 -96.16 REMARK 500 1 HIS A 95 106.67 -57.05 REMARK 500 2 ARG A 2 23.48 -167.35 REMARK 500 2 LEU A 17 90.28 70.34 REMARK 500 2 ILE A 31 -87.13 -107.96 REMARK 500 2 ASP A 32 -46.14 69.27 REMARK 500 2 THR A 42 36.36 -89.52 REMARK 500 2 PHE A 68 -96.75 65.48 REMARK 500 2 VAL A 69 -168.28 55.90 REMARK 500 2 GLN A 70 -68.32 177.44 REMARK 500 2 PRO A 82 34.43 -77.99 REMARK 500 2 ASP A 84 98.15 61.55 REMARK 500 2 TRP A 88 -79.46 -130.83 REMARK 500 2 LEU A 141 54.22 -93.58 REMARK 500 3 LEU A 17 131.85 73.97 REMARK 500 3 PHE A 68 -93.25 69.32 REMARK 500 3 VAL A 69 -158.42 52.65 REMARK 500 3 GLN A 70 -72.76 177.53 REMARK 500 3 LYS A 80 -49.29 71.81 REMARK 500 3 TRP A 88 -74.11 -100.75 REMARK 500 3 VAL A 138 -71.89 -89.84 REMARK 500 3 LEU A 141 46.29 -93.85 REMARK 500 4 LYS A 3 89.43 70.46 REMARK 500 4 LEU A 17 80.11 62.14 REMARK 500 4 ASP A 32 -67.82 -101.26 REMARK 500 4 HIS A 54 -2.51 67.59 REMARK 500 4 GLN A 70 -88.17 -113.20 REMARK 500 4 PRO A 82 44.67 -75.39 REMARK 500 4 ASP A 84 87.53 64.91 REMARK 500 4 TRP A 88 -73.43 -75.46 REMARK 500 4 ASN A 140 -164.70 -78.78 REMARK 500 4 SER A 142 -49.95 -154.09 REMARK 500 5 ARG A 2 124.56 68.79 REMARK 500 5 LEU A 17 -89.98 73.20 REMARK 500 5 ALA A 18 92.99 55.45 REMARK 500 5 ILE A 31 -86.57 -118.90 REMARK 500 5 ASP A 32 -51.16 68.70 REMARK 500 5 HIS A 54 -5.62 69.35 REMARK 500 5 PHE A 68 -25.90 77.14 REMARK 500 5 GLN A 70 -63.65 -120.23 REMARK 500 5 PRO A 82 38.01 -78.14 REMARK 500 5 ASP A 84 80.45 64.15 REMARK 500 5 TRP A 88 -72.80 -92.96 REMARK 500 5 SER A 130 142.10 -171.11 REMARK 500 REMARK 500 THIS ENTRY HAS 182 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1TVG RELATED DB: PDB REMARK 900 X-RAY CRYSTAL STRUCTURE OF IDENTICAL PROTEIN REMARK 900 RELATED ID: HR1958 RELATED DB: TARGETDB DBREF 1XPW A 1 143 UNP Q9Y547 Q9Y547_HUMAN 1 144 SEQADV 1XPW MET A -9 UNP Q9Y547 EXPRESSION TAG SEQADV 1XPW GLY A -8 UNP Q9Y547 EXPRESSION TAG SEQADV 1XPW HIS A -7 UNP Q9Y547 EXPRESSION TAG SEQADV 1XPW HIS A -6 UNP Q9Y547 EXPRESSION TAG SEQADV 1XPW HIS A -5 UNP Q9Y547 EXPRESSION TAG SEQADV 1XPW HIS A -4 UNP Q9Y547 EXPRESSION TAG SEQADV 1XPW HIS A -3 UNP Q9Y547 EXPRESSION TAG SEQADV 1XPW HIS A -2 UNP Q9Y547 EXPRESSION TAG SEQADV 1XPW SER A -1 UNP Q9Y547 EXPRESSION TAG SEQADV 1XPW HIS A 0 UNP Q9Y547 EXPRESSION TAG SEQADV 1XPW A UNP Q9Y547 ASP 109 DELETION SEQRES 1 A 153 MET GLY HIS HIS HIS HIS HIS HIS SER HIS MET ARG LYS SEQRES 2 A 153 ILE ASP LEU CYS LEU SER SER GLU GLY SER GLU VAL ILE SEQRES 3 A 153 LEU ALA THR SER SER ASP GLU LYS HIS PRO PRO GLU ASN SEQRES 4 A 153 ILE ILE ASP GLY ASN PRO GLU THR PHE TRP THR THR THR SEQRES 5 A 153 GLY MET PHE PRO GLN GLU PHE ILE ILE CYS PHE HIS LYS SEQRES 6 A 153 HIS VAL ARG ILE GLU ARG LEU VAL ILE GLN SER TYR PHE SEQRES 7 A 153 VAL GLN THR LEU LYS ILE GLU LYS SER THR SER LYS GLU SEQRES 8 A 153 PRO VAL ASP PHE GLU GLN TRP ILE GLU LYS ASP LEU VAL SEQRES 9 A 153 HIS THR GLU GLY GLN LEU GLN ASN GLU GLU ILE VAL ALA SEQRES 10 A 153 HIS GLY SER ALA THR TYR LEU ARG PHE ILE ILE VAL SER SEQRES 11 A 153 ALA PHE ASP HIS PHE ALA SER VAL HIS SER VAL SER ALA SEQRES 12 A 153 GLU GLY THR VAL VAL SER ASN LEU SER SER HELIX 1 1 LEU A 8 GLY A 12 5 5 HELIX 2 2 PRO A 26 ILE A 30 5 5 SHEET 1 A 4 ILE A 4 ASP A 5 0 SHEET 2 A 4 SER A 127 SER A 139 -1 O GLY A 135 N ILE A 4 SHEET 3 A 4 GLN A 47 TYR A 67 -1 N GLN A 65 O SER A 130 SHEET 4 A 4 GLU A 14 ILE A 16 -1 N ILE A 16 O ILE A 50 SHEET 1 B 4 TRP A 39 THR A 40 0 SHEET 2 B 4 SER A 127 SER A 139 -1 O VAL A 128 N TRP A 39 SHEET 3 B 4 GLN A 47 TYR A 67 -1 N GLN A 65 O SER A 130 SHEET 4 B 4 GLN A 101 ILE A 105 -1 O GLU A 103 N ILE A 64 SHEET 1 C 6 ILE A 4 ASP A 5 0 SHEET 2 C 6 SER A 127 SER A 139 -1 O GLY A 135 N ILE A 4 SHEET 3 C 6 GLN A 47 TYR A 67 -1 N GLN A 65 O SER A 130 SHEET 4 C 6 GLY A 109 ILE A 118 -1 O ILE A 118 N GLN A 47 SHEET 5 C 6 THR A 71 SER A 77 -1 N SER A 77 O THR A 112 SHEET 6 C 6 GLU A 86 ASP A 92 -1 O GLU A 86 N LYS A 76 CISPEP 1 PHE A 45 PRO A 46 1 -1.77 CISPEP 2 PHE A 45 PRO A 46 2 -1.61 CISPEP 3 PHE A 45 PRO A 46 3 -0.22 CISPEP 4 PHE A 45 PRO A 46 4 -1.73 CISPEP 5 PHE A 45 PRO A 46 5 -1.87 CISPEP 6 PHE A 45 PRO A 46 6 -2.13 CISPEP 7 PHE A 45 PRO A 46 7 -3.34 CISPEP 8 PHE A 45 PRO A 46 8 -1.00 CISPEP 9 PHE A 45 PRO A 46 9 -0.59 CISPEP 10 PHE A 45 PRO A 46 10 -1.82 CISPEP 11 PHE A 45 PRO A 46 11 -0.40 CISPEP 12 PHE A 45 PRO A 46 12 -0.17 CISPEP 13 PHE A 45 PRO A 46 13 -0.31 CISPEP 14 PHE A 45 PRO A 46 14 -2.74 CISPEP 15 PHE A 45 PRO A 46 15 -1.41 CISPEP 16 PHE A 45 PRO A 46 16 -0.09 CISPEP 17 PHE A 45 PRO A 46 17 0.86 CISPEP 18 PHE A 45 PRO A 46 18 -0.77 CISPEP 19 PHE A 45 PRO A 46 19 1.20 CISPEP 20 PHE A 45 PRO A 46 20 -1.28 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