Header list of 1uuc.pdb file
Complete list - g 9 2 Bytes
HEADER SERINE PROTEINASE INHIBITOR 18-DEC-03 1UUC TITLE SOLUTION STRUCTURE OF A CHIMERIC LEKTI-DOMAIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: SERINE PROTEASE INHIBITOR KAZAL-TYPE 5; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: CHIMERIC PROTEIN OF LEKTI DOMAIN ONE, RESIDUES 23-77; COMPND 5 SYNONYM: SERINE PROTEINASE INHIBITOR LEKTI, LEKTI, LYMPHO-EPITHELIAL COMPND 6 KAZAL-TYPE RELATED INHIBITOR, CONTAINS HEMOFILTRATE PEPTIDE HF6478, COMPND 7 HEMOFILTRATE PEPTIDE HF7665; COMPND 8 ENGINEERED: YES; COMPND 9 MUTATION: YES; COMPND 10 OTHER_DETAILS: DISULFIDE BONDS BETWEEN CYS 8 AND CYS 44, BETWEEN CYS COMPND 11 22 AND CYS 41 SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 TISSUE: I.E. VAGINAL EPITHELIUM; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: ORIGAMI; SOURCE 9 EXPRESSION_SYSTEM_VARIANT: DE3; SOURCE 10 EXPRESSION_SYSTEM_VECTOR: T7-EXPRESSION VECTOR; SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PET32A KEYWDS PROTEASE, SERINE PROTEINASE INHIBITOR, CHAMELEON SEQUENCE EXPDTA SOLUTION NMR NUMMDL 30 AUTHOR H.TIDOW,T.LAUBER,P.ROESCH,U.C.MARX REVDAT 4 14-JUN-23 1UUC 1 REMARK REVDAT 3 15-JAN-20 1UUC 1 REMARK REVDAT 2 24-FEB-09 1UUC 1 VERSN REVDAT 1 24-SEP-04 1UUC 0 JRNL AUTH H.TIDOW,T.LAUBER,K.VITZITHUM,C.SOMMERHOFF,P.ROESCH,U.C.MARX JRNL TITL THE SOLUTION STRUCTURE OF A CHIMERIC LEKTI DOMAIN REVEALS A JRNL TITL 2 CHAMELEON SEQUENCE JRNL REF BIOCHEMISTRY V. 43 11238 2004 JRNL REFN ISSN 0006-2960 JRNL PMID 15366933 JRNL DOI 10.1021/BI0492399 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.8.5.1 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: SIMULATED ANNEALING REMARK 4 REMARK 4 1UUC COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 18-DEC-03. REMARK 100 THE DEPOSITION ID IS D_1290014201. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 5.0 REMARK 210 IONIC STRENGTH : 10 REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D-TOCSY; 2D-COSY; 2D-NOESY; 1H; REMARK 210 15N-HSQC; HNHA; 3D-1H; 15N-TOCSY- REMARK 210 HSQC; 15N-NOESY-HSQC; 15N-HMQC- REMARK 210 NOESY-HSQC REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ REMARK 210 SPECTROMETER MODEL : DRX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NDEE; NMRVIEW 5.1.4 REMARK 210 METHOD USED : SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 160 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 30 REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST ENERGY; LEAST RESTRAINT REMARK 210 VIOLATION REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD NMR REMARK 210 -TECHNIQUES ON 15N-LABELED AND UNLABELED PROTEIN 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 ENGINEERED MUTATION IN CHAIN A PRO 28 FROM PHE REMARK 400 ENGINEERED MUTATION IN CHAIN A ILE 29 FROM PHE 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 PHE A 37 -59.34 66.15 REMARK 500 2 CYS A 22 72.67 -104.30 REMARK 500 2 PHE A 37 -58.47 66.51 REMARK 500 3 ASN A 17 29.14 47.59 REMARK 500 3 PRO A 23 -163.95 -70.40 REMARK 500 3 MET A 36 31.11 -97.80 REMARK 500 3 ILE A 38 103.76 -46.69 REMARK 500 4 ASN A 17 29.92 49.20 REMARK 500 4 CYS A 22 72.05 -104.09 REMARK 500 4 PHE A 37 -56.37 67.26 REMARK 500 4 ILE A 38 -27.95 -39.93 REMARK 500 5 CYS A 22 67.32 -108.92 REMARK 500 5 PHE A 37 -57.26 66.63 REMARK 500 6 ASN A 17 27.84 47.93 REMARK 500 6 PRO A 23 -161.66 -70.32 REMARK 500 6 ILE A 38 102.95 -46.14 REMARK 500 7 ASN A 17 29.08 47.20 REMARK 500 7 PHE A 37 -92.70 179.59 REMARK 500 7 ASN A 39 -28.43 175.66 REMARK 500 8 PRO A 28 73.42 -69.62 REMARK 500 8 PHE A 37 -75.83 58.11 REMARK 500 9 MET A 36 42.27 -101.05 REMARK 500 9 ILE A 38 97.84 -57.38 REMARK 500 10 ASN A 17 27.66 47.76 REMARK 500 10 PRO A 23 -167.38 -72.40 REMARK 500 10 SER A 31 -167.32 -79.88 REMARK 500 10 PHE A 37 -56.48 68.05 REMARK 500 10 ILE A 38 -29.31 -39.96 REMARK 500 11 ASN A 17 25.09 45.41 REMARK 500 11 PHE A 21 33.13 -93.78 REMARK 500 11 ILE A 38 98.66 -50.38 REMARK 500 12 ASN A 17 26.00 48.54 REMARK 500 12 LYS A 27 75.82 65.47 REMARK 500 12 PHE A 37 -54.81 165.05 REMARK 500 12 ILE A 38 -28.14 -39.96 REMARK 500 13 CYS A 22 76.56 -103.22 REMARK 500 13 ILE A 38 84.35 -64.36 REMARK 500 13 THR A 43 -52.61 -120.35 REMARK 500 14 CYS A 22 70.90 -103.72 REMARK 500 14 PHE A 37 -58.23 65.90 REMARK 500 15 CYS A 22 67.40 -105.64 REMARK 500 15 GLN A 24 99.56 77.03 REMARK 500 15 PHE A 37 -58.77 62.80 REMARK 500 15 ILE A 38 -27.67 -39.92 REMARK 500 16 ASN A 17 27.95 49.78 REMARK 500 16 CYS A 22 64.57 -108.04 REMARK 500 16 PHE A 37 -59.32 66.41 REMARK 500 17 PRO A 28 68.59 -69.44 REMARK 500 17 SER A 31 -166.36 -79.70 REMARK 500 17 PHE A 37 -58.00 66.51 REMARK 500 REMARK 500 THIS ENTRY HAS 86 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 650 REMARK 650 HELIX REMARK 650 DETERMINATION METHOD: AUTHOR PROVIDED. REMARK 700 REMARK 700 SHEET REMARK 700 DETERMINATION METHOD: AUTHOR PROVIDED. REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1HDL RELATED DB: PDB REMARK 900 LEKTI DOMAIN ONE REMARK 900 RELATED ID: 1H0Z RELATED DB: PDB REMARK 900 LEKTI DOMAIN SIX (HF7665) REMARK 900 RELATED ID: 6110 RELATED DB: BMRB REMARK 999 REMARK 999 SEQUENCE REMARK 999 THE LEKTI SEQUENCE PROVIDED BY SWISSPROT DIFFERS FROM THAT REMARK 999 GIVEN IN THE ORIGINAL PAPER BY MAEGERT ET AL., 1999. IN THIS REMARK 999 ENTRY THE SEQUENCE REFERS TO THE ORIGINAL PAPER AND IS ALSO REMARK 999 IDENTICAL (EXCEPT FOR THE TWO MUTATIONS AT POSITIONS 28 AND REMARK 999 29) TO THAT OF LEKTI DOMAIN ONE (HF6478, PDB-CODE 1HDL) AS REMARK 999 ISOLATED FROM HUMAN BLOOD FILTRATE (REFERENCES: REMARK 999 MAGERT ET AL., 1999, J. BIOL. CHEM. 274, 21499-21502. REMARK 999 LAUBER ET AL.,2001, PROTEIN EXPR. PURIF. 22, 108-112; REMARK 999 LAUBER ET AL., 2003, J. MOL. BIOL., 328, 205-219.) REMARK 999 THUS, THE SEQUENCE IN THIS ENTRY REFERS TO RESIDUES 23 TO 77 REMARK 999 OF FULL-LENGTH LEKTI. DBREF 1UUC A 1 55 UNP Q9NQ38 ISK5_HUMAN 23 77 SEQADV 1UUC ASN A 2 UNP Q9NQ38 ASP 24 CONFLICT SEQADV 1UUC GLU A 3 UNP Q9NQ38 SER 25 CONFLICT SEQADV 1UUC ASP A 4 UNP Q9NQ38 LEU 26 CONFLICT SEQADV 1UUC GLN A 5 UNP Q9NQ38 SER 27 CONFLICT SEQADV 1UUC PRO A 28 UNP Q9NQ38 PHE 50 ENGINEERED MUTATION SEQADV 1UUC ILE A 29 UNP Q9NQ38 PHE 51 ENGINEERED MUTATION SEQRES 1 A 55 LYS ASN GLU ASP GLN GLU MET CYS HIS GLU PHE GLN ALA SEQRES 2 A 55 PHE MET LYS ASN GLY LYS LEU PHE CYS PRO GLN ASP LYS SEQRES 3 A 55 LYS PRO ILE GLN SER LEU ASP GLY ILE MET PHE ILE ASN SEQRES 4 A 55 LYS CYS ALA THR CYS LYS MET ILE LEU GLU LYS GLU ALA SEQRES 5 A 55 LYS SER GLN HELIX 1 1 GLU A 3 ALA A 13 1 11 HELIX 2 2 ASN A 39 ALA A 52 1 14 SHEET 1 AA 2 MET A 15 LYS A 16 0 SHEET 2 AA 2 LYS A 19 LEU A 20 -1 O LYS A 19 N LYS A 16 SHEET 1 AB 2 GLN A 30 SER A 31 0 SHEET 2 AB 2 ILE A 35 MET A 36 -1 O ILE A 35 N SER A 31 SSBOND 1 CYS A 8 CYS A 44 1555 1555 2.02 SSBOND 2 CYS A 22 CYS A 41 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 - g 9 2 Bytes