Header list of 1uvg.pdb file
Complete list - t 30 2 Bytes
HEADER SERINE PROTEINASE INHIBITOR 20-JAN-04 1UVG TITLE SOLUTION STRUCTURE OF THE 15TH DOMAIN OF LEKTI COMPND MOL_ID: 1; COMPND 2 MOLECULE: SERINE PROTEINASE INHIBITOR KAZAL TYPE 5; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: LEKTI-DOMAIN15, RESIDUES 989-1064; COMPND 5 SYNONYM: LYMPHO-EPITHELIAL, KAZAL-TYPE RELATED INHIBITOR, LEKTI; COMPND 6 ENGINEERED: YES; COMPND 7 OTHER_DETAILS: DISULPHIDE BONDS BETWEEN CYS5 AND CYS40, BETWEEN CYS18 COMPND 8 AND CYS37, BETWEEN CYS26 AND CYS58 SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 TISSUE: VAGINAL EPITHEL; 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: PET32-A KEYWDS SERINE PROTEINASE INHIBITOR, TRYPSIN INHIBITOR, KAZAL, PROTEASE EXPDTA SOLUTION NMR NUMMDL 31 AUTHOR K.VITZITHUM,P.ROESCH,U.C.MARX REVDAT 4 30-OCT-19 1UVG 1 REMARK REVDAT 3 24-FEB-09 1UVG 1 VERSN REVDAT 2 13-JUN-05 1UVG 1 COMPND REVDAT 1 14-APR-05 1UVG 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 3.8.51 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: SIMULATED ANNEALING REMARK 4 REMARK 4 1UVG COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 20-JAN-04. REMARK 100 THE DEPOSITION ID IS D_1290014419. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298; NULL REMARK 210 PH : 6.4; 4.0 REMARK 210 IONIC STRENGTH : 20; 100 REMARK 210 PRESSURE : 1 ATM; NULL REMARK 210 SAMPLE CONTENTS : 90% H2O/10% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D-NOESY; 2D-TOCSY; 2D-COESY; REMARK 210 1H; 15N-HSQC; HNHA; 3D-1H; 15N- REMARK 210 NOESY-HSQC; 15N-TOCSY-HSQC; 15N- REMARK 210 HMQC-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 5.01.4 REMARK 210 METHOD USED : SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 200 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 31 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 FUNCTION: SERINE PROTEASE INHIBITOR, PROBABLY IMPORTANT FOR THE REMARK 400 ANTI-INFLAMMATORY AND/OR ANTIMICROBIAL PROTECTION OF MUCOUS REMARK 400 EPITHELIA. 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 1-31 REMARK 465 RES C SSSEQI REMARK 465 GLY A -2 REMARK 465 PRO A -1 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 CYS A 26 H ARG A 53 1.57 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 ASP A 7 63.69 -150.56 REMARK 500 1 ASN A 34 -79.95 -47.84 REMARK 500 1 CYS A 58 172.62 -53.51 REMARK 500 2 ASP A 7 63.06 -153.56 REMARK 500 2 ASN A 34 -76.73 -53.95 REMARK 500 3 ASP A 7 59.63 -150.42 REMARK 500 3 ASN A 34 -80.84 -43.88 REMARK 500 4 ASN A 34 -78.82 -43.50 REMARK 500 5 ASN A 34 -80.23 -48.76 REMARK 500 5 ASN A 49 63.60 -102.30 REMARK 500 6 TYR A 16 154.80 -44.88 REMARK 500 6 ASN A 34 -79.55 -46.32 REMARK 500 7 ASN A 34 -75.94 -49.77 REMARK 500 7 THR A 63 70.65 62.16 REMARK 500 7 MET A 71 70.70 47.56 REMARK 500 8 ASN A 34 -80.44 -46.31 REMARK 500 8 ASN A 49 64.84 -102.70 REMARK 500 8 ALA A 69 -151.37 44.17 REMARK 500 9 ASP A 7 64.45 -152.69 REMARK 500 9 ASN A 34 -79.38 -53.21 REMARK 500 9 LYS A 57 152.62 -49.64 REMARK 500 10 ASN A 34 -75.37 -53.57 REMARK 500 11 ASN A 34 -77.57 -55.30 REMARK 500 12 ASN A 34 -78.94 -55.07 REMARK 500 13 ASN A 34 -78.86 -48.30 REMARK 500 14 ASP A 7 10.50 -145.79 REMARK 500 14 ASN A 34 -78.95 -51.09 REMARK 500 15 ASN A 34 -79.09 -51.65 REMARK 500 15 CYS A 58 -179.71 -57.07 REMARK 500 16 ASP A 7 32.66 -159.03 REMARK 500 16 ASN A 34 -78.06 -54.16 REMARK 500 17 ASN A 34 -78.17 -51.66 REMARK 500 17 ALA A 68 53.88 163.30 REMARK 500 18 ASN A 34 -78.98 -49.01 REMARK 500 19 ASN A 34 -79.76 -48.56 REMARK 500 19 ASN A 49 60.89 -107.99 REMARK 500 20 ASP A 7 64.46 -150.10 REMARK 500 20 ASN A 34 -78.40 -55.70 REMARK 500 20 ASN A 49 59.49 -91.49 REMARK 500 21 ASN A 34 -78.77 -51.75 REMARK 500 22 ASN A 34 -76.29 -52.47 REMARK 500 23 TYR A 8 -169.75 -115.07 REMARK 500 23 ASN A 34 -77.22 -49.79 REMARK 500 23 ASN A 49 58.62 -104.58 REMARK 500 24 ASP A 7 63.04 -154.27 REMARK 500 24 ASN A 34 -72.44 -63.92 REMARK 500 24 ASN A 49 54.03 -102.91 REMARK 500 25 ASN A 34 -79.78 -52.55 REMARK 500 25 ASN A 49 59.71 -96.51 REMARK 500 26 ASN A 34 -78.93 -54.80 REMARK 500 REMARK 500 THIS ENTRY HAS 56 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 9 0.30 SIDE CHAIN REMARK 500 1 ARG A 13 0.29 SIDE CHAIN REMARK 500 1 ARG A 46 0.17 SIDE CHAIN REMARK 500 1 ARG A 53 0.18 SIDE CHAIN REMARK 500 2 ARG A 9 0.30 SIDE CHAIN REMARK 500 2 ARG A 13 0.32 SIDE CHAIN REMARK 500 2 ARG A 46 0.21 SIDE CHAIN REMARK 500 2 ARG A 53 0.30 SIDE CHAIN REMARK 500 3 ARG A 9 0.24 SIDE CHAIN REMARK 500 3 ARG A 13 0.31 SIDE CHAIN REMARK 500 3 ARG A 46 0.31 SIDE CHAIN REMARK 500 3 ARG A 53 0.32 SIDE CHAIN REMARK 500 4 ARG A 9 0.10 SIDE CHAIN REMARK 500 4 ARG A 13 0.25 SIDE CHAIN REMARK 500 4 ARG A 46 0.24 SIDE CHAIN REMARK 500 4 ARG A 53 0.30 SIDE CHAIN REMARK 500 5 ARG A 9 0.27 SIDE CHAIN REMARK 500 5 ARG A 13 0.11 SIDE CHAIN REMARK 500 5 ARG A 46 0.09 SIDE CHAIN REMARK 500 5 ARG A 53 0.31 SIDE CHAIN REMARK 500 6 ARG A 9 0.32 SIDE CHAIN REMARK 500 6 ARG A 13 0.21 SIDE CHAIN REMARK 500 6 ARG A 46 0.30 SIDE CHAIN REMARK 500 6 ARG A 53 0.31 SIDE CHAIN REMARK 500 7 ARG A 9 0.30 SIDE CHAIN REMARK 500 7 ARG A 13 0.24 SIDE CHAIN REMARK 500 7 ARG A 46 0.15 SIDE CHAIN REMARK 500 7 ARG A 53 0.32 SIDE CHAIN REMARK 500 8 ARG A 9 0.27 SIDE CHAIN REMARK 500 8 ARG A 13 0.26 SIDE CHAIN REMARK 500 8 ARG A 46 0.24 SIDE CHAIN REMARK 500 8 ARG A 53 0.31 SIDE CHAIN REMARK 500 9 ARG A 9 0.32 SIDE CHAIN REMARK 500 9 ARG A 13 0.32 SIDE CHAIN REMARK 500 9 ARG A 46 0.32 SIDE CHAIN REMARK 500 9 ARG A 53 0.25 SIDE CHAIN REMARK 500 10 ARG A 9 0.26 SIDE CHAIN REMARK 500 10 ARG A 13 0.30 SIDE CHAIN REMARK 500 10 ARG A 46 0.17 SIDE CHAIN REMARK 500 10 ARG A 53 0.30 SIDE CHAIN REMARK 500 11 ARG A 9 0.26 SIDE CHAIN REMARK 500 11 ARG A 13 0.28 SIDE CHAIN REMARK 500 11 ARG A 46 0.32 SIDE CHAIN REMARK 500 11 ARG A 53 0.31 SIDE CHAIN REMARK 500 12 ARG A 9 0.20 SIDE CHAIN REMARK 500 12 ARG A 13 0.29 SIDE CHAIN REMARK 500 12 ARG A 46 0.31 SIDE CHAIN REMARK 500 12 ARG A 53 0.29 SIDE CHAIN REMARK 500 13 ARG A 9 0.19 SIDE CHAIN REMARK 500 13 ARG A 13 0.26 SIDE CHAIN REMARK 500 REMARK 500 THIS ENTRY HAS 122 PLANE DEVIATIONS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1H0Z RELATED DB: PDB REMARK 900 LEKTI DOMAIN SIX (HF7665) REMARK 900 RELATED ID: 1HDL RELATED DB: PDB REMARK 900 LEKTI DOMAIN ONE REMARK 900 RELATED ID: 1UUC RELATED DB: PDB REMARK 900 SOLUTION STRUCTURE OF A CHIMARIC LEKTI- DOMAIN REMARK 900 RELATED ID: 1UVF RELATED DB: PDB REMARK 900 SOLUTION STRUCTURE OF THE STRUCTURED PART OF THE 15TH DOMAIN OF REMARK 900 LEKTI REMARK 900 RELATED ID: 6180 RELATED DB: BMRB DBREF 1UVG A -2 -1 PDB 1UVG 1UVG -2 -1 DBREF 1UVG A 1 76 UNP Q9NQ38 ISK5_HUMAN 989 1064 SEQRES 1 A 78 GLY PRO ASP SER GLU MET CYS LYS ASP TYR ARG VAL LEU SEQRES 2 A 78 PRO ARG ILE GLY TYR LEU CYS PRO LYS ASP LEU LYS PRO SEQRES 3 A 78 VAL CYS GLY ASP ASP GLY GLN THR TYR ASN ASN PRO CYS SEQRES 4 A 78 MET LEU CYS HIS GLU ASN LEU ILE ARG GLN THR ASN THR SEQRES 5 A 78 HIS ILE ARG SER THR GLY LYS CYS GLU GLU SER SER THR SEQRES 6 A 78 PRO GLY THR THR ALA ALA SER MET PRO PRO SER ASP GLU HELIX 1 1 ASP A 1 LYS A 6 1 6 HELIX 2 2 PRO A 36 GLN A 47 1 12 HELIX 3 3 CYS A 58 SER A 62 5 5 HELIX 4 4 THR A 66 MET A 71 1 6 SHEET 1 AA 3 THR A 32 TYR A 33 0 SHEET 2 AA 3 VAL A 25 GLY A 27 -1 O VAL A 25 N TYR A 33 SHEET 3 AA 3 ILE A 52 THR A 55 -1 N ARG A 53 O CYS A 26 SSBOND 1 CYS A 5 CYS A 40 1555 1555 2.01 SSBOND 2 CYS A 18 CYS A 37 1555 1555 2.02 SSBOND 3 CYS A 26 CYS A 58 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 - t 30 2 Bytes