Header list of 1urk.pdb file
Complete list - l 29 2 Bytes
HEADER PLASMINOGEN ACTIVATION 10-JAN-94 1URK TITLE SOLUTION STRUCTURE OF THE AMINO TERMINAL FRAGMENT OF UROKINASE-TYPE TITLE 2 PLASMINOGEN ACTIVATOR COMPND MOL_ID: 1; COMPND 2 MOLECULE: PLASMINOGEN ACTIVATOR; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606 KEYWDS PLASMINOGEN ACTIVATION EXPDTA SOLUTION NMR NUMMDL 15 AUTHOR A.P.HANSEN,A.M.PETROS,R.P.MEADOWS,D.G.NETTESHEIM,A.P.MAZAR, AUTHOR 2 E.T.OLEJNICZAK,R.X.XU,T.M.PEDERSON,J.HENKIN,S.W.FESIK REVDAT 4 29-JUL-20 1URK 1 COMPND REMARK HETNAM LINK REVDAT 4 2 1 SITE REVDAT 3 29-NOV-17 1URK 1 REMARK HELIX REVDAT 2 24-FEB-09 1URK 1 VERSN REVDAT 1 08-MAY-95 1URK 0 JRNL AUTH A.P.HANSEN,A.M.PETROS,R.P.MEADOWS,D.G.NETTESHEIM,A.P.MAZAR, JRNL AUTH 2 E.T.OLEJNICZAK,R.X.XU,T.M.PEDERSON,J.HENKIN,S.W.FESIK JRNL TITL SOLUTION STRUCTURE OF THE AMINO-TERMINAL FRAGMENT OF JRNL TITL 2 UROKINASE-TYPE PLASMINOGEN ACTIVATOR. JRNL REF BIOCHEMISTRY V. 33 4847 1994 JRNL REFN ISSN 0006-2960 JRNL PMID 8161544 JRNL DOI 10.1021/BI00182A013 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.0 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1URK COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL. REMARK 100 THE DEPOSITION ID IS D_1000176978. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : NULL REMARK 210 PH : NULL REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : NULL REMARK 210 SAMPLE CONTENTS : NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL REMARK 210 SPECTROMETER FIELD STRENGTH : NULL REMARK 210 SPECTROMETER MODEL : NULL REMARK 210 SPECTROMETER MANUFACTURER : NULL REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NULL REMARK 210 METHOD USED : NULL REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL REMARK 210 CONFORMERS, NUMBER SUBMITTED : 15 REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL 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 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 PRO A 8 90.91 -50.55 REMARK 500 1 CYS A 11 169.51 158.24 REMARK 500 1 ASP A 12 95.80 -178.56 REMARK 500 1 CYS A 13 -164.13 -118.16 REMARK 500 1 PHE A 25 23.29 -145.25 REMARK 500 1 SER A 26 -42.33 82.85 REMARK 500 1 ASN A 27 98.11 -174.41 REMARK 500 1 TRP A 30 131.78 178.68 REMARK 500 1 PRO A 34 151.13 -49.04 REMARK 500 1 GLN A 40 -89.33 43.07 REMARK 500 1 HIS A 41 45.71 -101.74 REMARK 500 1 LYS A 46 -150.07 -65.40 REMARK 500 1 SER A 47 56.73 -175.32 REMARK 500 1 THR A 49 69.83 178.12 REMARK 500 1 TYR A 51 85.13 -172.17 REMARK 500 1 PHE A 57 -62.01 -104.76 REMARK 500 1 TYR A 58 136.42 62.11 REMARK 500 1 ARG A 59 56.37 -146.25 REMARK 500 1 ASP A 65 -150.00 -94.60 REMARK 500 1 CYS A 71 165.52 65.57 REMARK 500 1 ALA A 77 -34.29 -32.53 REMARK 500 1 GLN A 82 -144.95 -63.89 REMARK 500 1 THR A 83 -75.15 -113.56 REMARK 500 1 HIS A 85 -148.53 -130.33 REMARK 500 1 ALA A 86 52.09 -102.16 REMARK 500 1 HIS A 87 57.02 173.31 REMARK 500 1 ARG A 88 -62.82 -123.09 REMARK 500 1 SER A 89 -23.02 156.86 REMARK 500 1 LYS A 98 73.14 40.73 REMARK 500 1 HIS A 99 170.95 166.58 REMARK 500 1 ASN A 100 -92.13 -136.23 REMARK 500 1 TYR A 101 -146.17 41.68 REMARK 500 1 ASN A 104 50.17 -142.00 REMARK 500 1 ASP A 106 -135.87 -96.36 REMARK 500 1 TYR A 114 86.27 -64.46 REMARK 500 1 VAL A 117 50.80 -110.00 REMARK 500 1 PRO A 121 97.89 -51.58 REMARK 500 1 GLU A 125 90.01 -51.46 REMARK 500 1 CYS A 126 98.04 -41.15 REMARK 500 1 ASP A 130 134.50 61.75 REMARK 500 1 CYS A 131 59.41 -160.32 REMARK 500 2 VAL A 7 -68.51 -94.30 REMARK 500 2 ASP A 12 61.75 -174.60 REMARK 500 2 LYS A 23 -45.67 -132.42 REMARK 500 2 PHE A 25 -141.49 -94.60 REMARK 500 2 SER A 26 -44.37 -131.06 REMARK 500 2 TRP A 30 -173.75 -179.80 REMARK 500 2 GLN A 40 -86.81 34.15 REMARK 500 2 HIS A 41 46.38 -94.39 REMARK 500 2 SER A 47 -71.95 -179.72 REMARK 500 REMARK 500 THIS ENTRY HAS 647 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 1 ARG A 59 0.23 SIDE CHAIN REMARK 500 1 ARG A 69 0.30 SIDE CHAIN REMARK 500 1 ARG A 88 0.32 SIDE CHAIN REMARK 500 1 ARG A 103 0.32 SIDE CHAIN REMARK 500 1 ARG A 108 0.26 SIDE CHAIN REMARK 500 1 ARG A 109 0.30 SIDE CHAIN REMARK 500 1 ARG A 110 0.09 SIDE CHAIN REMARK 500 2 ARG A 59 0.28 SIDE CHAIN REMARK 500 2 ARG A 69 0.28 SIDE CHAIN REMARK 500 2 ARG A 88 0.15 SIDE CHAIN REMARK 500 2 ARG A 103 0.29 SIDE CHAIN REMARK 500 2 ARG A 108 0.30 SIDE CHAIN REMARK 500 2 ARG A 109 0.30 SIDE CHAIN REMARK 500 2 ARG A 110 0.32 SIDE CHAIN REMARK 500 3 ARG A 59 0.27 SIDE CHAIN REMARK 500 3 ARG A 69 0.18 SIDE CHAIN REMARK 500 3 ARG A 88 0.19 SIDE CHAIN REMARK 500 3 ARG A 103 0.32 SIDE CHAIN REMARK 500 3 ARG A 108 0.21 SIDE CHAIN REMARK 500 3 ARG A 109 0.25 SIDE CHAIN REMARK 500 3 ARG A 110 0.28 SIDE CHAIN REMARK 500 4 ARG A 59 0.23 SIDE CHAIN REMARK 500 4 ARG A 88 0.30 SIDE CHAIN REMARK 500 4 ARG A 103 0.25 SIDE CHAIN REMARK 500 4 ARG A 108 0.27 SIDE CHAIN REMARK 500 4 ARG A 109 0.32 SIDE CHAIN REMARK 500 4 ARG A 110 0.30 SIDE CHAIN REMARK 500 5 ARG A 59 0.32 SIDE CHAIN REMARK 500 5 ARG A 69 0.31 SIDE CHAIN REMARK 500 5 ARG A 88 0.31 SIDE CHAIN REMARK 500 5 ARG A 103 0.25 SIDE CHAIN REMARK 500 5 ARG A 108 0.31 SIDE CHAIN REMARK 500 5 ARG A 109 0.29 SIDE CHAIN REMARK 500 5 ARG A 110 0.32 SIDE CHAIN REMARK 500 6 ARG A 59 0.29 SIDE CHAIN REMARK 500 6 ARG A 69 0.29 SIDE CHAIN REMARK 500 6 ARG A 88 0.17 SIDE CHAIN REMARK 500 6 ARG A 103 0.25 SIDE CHAIN REMARK 500 6 ARG A 108 0.32 SIDE CHAIN REMARK 500 6 ARG A 109 0.21 SIDE CHAIN REMARK 500 6 ARG A 110 0.26 SIDE CHAIN REMARK 500 7 ARG A 59 0.13 SIDE CHAIN REMARK 500 7 ARG A 69 0.24 SIDE CHAIN REMARK 500 7 ARG A 88 0.30 SIDE CHAIN REMARK 500 7 ARG A 103 0.17 SIDE CHAIN REMARK 500 7 ARG A 108 0.31 SIDE CHAIN REMARK 500 7 ARG A 109 0.21 SIDE CHAIN REMARK 500 7 ARG A 110 0.28 SIDE CHAIN REMARK 500 8 ARG A 59 0.32 SIDE CHAIN REMARK 500 8 ARG A 69 0.20 SIDE CHAIN REMARK 500 REMARK 500 THIS ENTRY HAS 102 PLANE DEVIATIONS. REMARK 500 REMARK 500 REMARK: NULL DBREF 1URK A 6 135 UNP P00749 UROK_HUMAN 26 155 SEQRES 1 A 130 GLN VAL PRO SER ASN CYS ASP CYS LEU ASN GLY GLY THR SEQRES 2 A 130 CYS VAL SER ASN LYS TYR PHE SER ASN ILE HIS TRP CYS SEQRES 3 A 130 ASN CYS PRO LYS LYS PHE GLY GLY GLN HIS CYS GLU ILE SEQRES 4 A 130 ASP LYS SER LYS THR CYS TYR GLU GLY ASN GLY HIS PHE SEQRES 5 A 130 TYR ARG GLY LYS ALA SER THR ASP THR MET GLY ARG PRO SEQRES 6 A 130 CYS LEU PRO TRP ASN SER ALA THR VAL LEU GLN GLN THR SEQRES 7 A 130 TYR HIS ALA HIS ARG SER ASP ALA LEU GLN LEU GLY LEU SEQRES 8 A 130 GLY LYS HIS ASN TYR CYS ARG ASN PRO ASP ASN ARG ARG SEQRES 9 A 130 ARG PRO TRP CYS TYR VAL GLN VAL GLY LEU LYS PRO LEU SEQRES 10 A 130 VAL GLN GLU CYS MET VAL HIS ASP CYS ALA ASP GLY LYS MODRES 1URK THR A 18 THR GLYCOSYLATION SITE HET FUC A 136 10 HETNAM FUC ALPHA-L-FUCOPYRANOSE FORMUL 2 FUC C6 H12 O5 HELIX 1 H1 ALA A 77 GLN A 82 1 6 HELIX 2 H2 ASP A 90 LEU A 94 1IRREGULAR 5 SHEET 1 B1 2 THR A 18 SER A 21 0 SHEET 2 B1 2 HIS A 29 ASN A 32 -1 N ASN A 32 O THR A 18 SHEET 1 B2 2 PHE A 37 GLY A 38 0 SHEET 2 B2 2 ILE A 44 ASP A 45 -1 O ILE A 44 N GLY A 38 SHEET 1 B3 2 PRO A 111 VAL A 117 0 SHEET 2 B3 2 LYS A 120 CYS A 126 -1 N CYS A 126 O PRO A 111 SSBOND 1 CYS A 11 CYS A 19 1555 1555 2.02 SSBOND 2 CYS A 13 CYS A 31 1555 1555 2.02 SSBOND 3 CYS A 33 CYS A 42 1555 1555 2.02 SSBOND 4 CYS A 50 CYS A 131 1555 1555 2.02 SSBOND 5 CYS A 71 CYS A 113 1555 1555 2.02 SSBOND 6 CYS A 102 CYS A 126 1555 1555 2.02 LINK OG1 THR A 18 C1 FUC A 136 1555 1555 1.43 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 - l 29 2 Bytes