Header list of 1hdl.pdb file
Complete list - g 9 2 Bytes
HEADER PUTATIVE SERINE PROTEINASE INHIBITOR 16-NOV-00 1HDL
TITLE LEKTI DOMAIN ONE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SERINE PROTEINASE INHIBITOR LEKTI;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: LEKTI DOMAIN ONE;
COMPND 5 SYNONYM: HF6478;
COMPND 6 ENGINEERED: YES;
COMPND 7 OTHER_DETAILS: DISULFIDE BRIDGES BETWEEN CYS 8 AND CYS 44, AND
COMPND 8 BETWEEN CYS 21 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 (DE3);
SOURCE 9 EXPRESSION_SYSTEM_CELLULAR_LOCATION: CYTOPLASM;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET32A
KEYWDS PUTATIVE SERINE PROTEINASE INHIBITOR
EXPDTA SOLUTION NMR
NUMMDL 21
AUTHOR T.LAUBER,P.ROESCH,U.C.MARX
REVDAT 6 14-JUN-23 1HDL 1 REMARK
REVDAT 5 15-JAN-20 1HDL 1 REMARK
REVDAT 4 24-FEB-09 1HDL 1 VERSN
REVDAT 3 26-JUN-03 1HDL 1 AUTHOR
REVDAT 2 17-APR-03 1HDL 1 JRNL REMARK DBREF SEQADV
REVDAT 1 15-NOV-01 1HDL 0
JRNL AUTH T.LAUBER,A.SCHULZ,K.SCHWEIMER,K.ADERMANN,U.C.MARX
JRNL TITL HOMOLOGOUS PROTEINS WITH DIFFERENT FOLDS: THE
JRNL TITL 2 THREE-DIMENSIONAL STRUCTURES OF DOMAINS 1 AND 6 OF THE
JRNL TITL 3 MULTIPLE KAZAL-TYPE INHIBITOR LEKTI
JRNL REF J.MOL.BIOL. V. 328 205 2003
JRNL REFN ISSN 0022-2836
JRNL PMID 12684009
JRNL DOI 10.1016/S0022-2836(03)00245-6
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1HDL COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 16-NOV-00.
REMARK 100 THE DEPOSITION ID IS D_1290005546.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 4.5
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D-TOCSY; 2D-NOESY; 2D-COSY; 1H;
REMARK 210 15N-HSQC; HNHA; 3D-1H; 15N-TOCSY-
REMARK 210 HSQC; 15N-NOESY-HSQC; 15N/1H;
REMARK 210 15N-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 4.1.0, X-PLOR
REMARK 210 3.851
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 60
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 21
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 3
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING STANDARD NMR TECHNIQUES
REMARK 210 ON 15N-LABELED AND UNLABELED HF6478
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: 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 H LYS A 16 O LYS A 19 1.54
REMARK 500 O PHE A 11 H PHE A 14 1.55
REMARK 500 O LYS A 40 H CYS A 44 1.56
REMARK 500 O LYS A 26 H PHE A 29 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 PRO A 23 84.45 -63.82
REMARK 500 1 GLN A 24 -83.94 -121.70
REMARK 500 1 CYS A 41 -71.61 -65.26
REMARK 500 2 MET A 7 165.40 -41.60
REMARK 500 2 PRO A 23 79.09 -65.30
REMARK 500 2 GLN A 24 -112.96 -122.19
REMARK 500 3 GLN A 5 -71.64 69.86
REMARK 500 3 GLU A 6 59.73 -69.04
REMARK 500 3 PRO A 23 83.12 -61.99
REMARK 500 3 GLN A 24 -77.11 -126.56
REMARK 500 3 CYS A 41 -71.80 -54.33
REMARK 500 4 MET A 7 -142.99 58.81
REMARK 500 4 PRO A 23 73.86 -62.35
REMARK 500 4 ASP A 25 64.67 -165.03
REMARK 500 4 CYS A 41 -72.44 -54.66
REMARK 500 5 ASP A 4 84.90 -152.61
REMARK 500 5 PRO A 23 82.69 -62.43
REMARK 500 5 GLN A 24 -76.48 -125.63
REMARK 500 5 CYS A 41 -73.48 -60.61
REMARK 500 6 ASP A 4 24.78 46.20
REMARK 500 6 GLU A 6 25.62 -144.19
REMARK 500 6 PRO A 23 83.11 -62.05
REMARK 500 6 GLN A 24 -79.61 -112.38
REMARK 500 7 HIS A 9 -39.39 -135.80
REMARK 500 7 PHE A 21 73.58 -103.48
REMARK 500 7 PRO A 23 82.54 -61.56
REMARK 500 7 GLN A 24 -78.35 -126.02
REMARK 500 7 CYS A 41 -75.61 -53.86
REMARK 500 8 PHE A 21 64.16 -101.73
REMARK 500 8 PRO A 23 84.27 -65.19
REMARK 500 8 ASP A 25 55.04 -179.97
REMARK 500 9 GLN A 5 -85.01 57.84
REMARK 500 9 GLU A 6 60.70 -68.53
REMARK 500 9 MET A 7 -30.55 -39.56
REMARK 500 9 HIS A 9 -44.86 -132.14
REMARK 500 9 PRO A 23 82.74 -61.58
REMARK 500 9 GLN A 24 -86.13 -120.77
REMARK 500 10 GLN A 5 -47.58 75.44
REMARK 500 10 GLU A 6 -30.05 -38.79
REMARK 500 10 CYS A 8 -78.73 -45.29
REMARK 500 10 HIS A 9 24.67 47.93
REMARK 500 10 LYS A 16 77.64 -105.31
REMARK 500 10 PRO A 23 82.06 -61.12
REMARK 500 10 GLN A 24 -78.31 -113.45
REMARK 500 10 CYS A 41 -73.46 -42.61
REMARK 500 11 GLU A 6 44.67 -141.72
REMARK 500 11 PRO A 23 73.79 -62.01
REMARK 500 11 ASP A 25 61.00 -171.81
REMARK 500 11 CYS A 41 -72.25 -47.04
REMARK 500 12 ASP A 4 55.97 -110.02
REMARK 500
REMARK 500 THIS ENTRY HAS 90 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: 1H0Z RELATED DB: PDB
REMARK 900 LEKTI DOMAIN SIX (HF7665)
REMARK 900 RELATED ID: 4910 RELATED DB: BMRB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE SEQUENCE FOR RESIDUES A 2 TO A 5 ARE IN CONFLICT
REMARK 999 WITH THE SWISS-PROT SEQUENCE DATABASE AND HAVE BEEN
REMARK 999 DESCRIBED BY MAEGERT H.-J.,J.BIOL.CHEM. (1999)
DBREF 1HDL A 1 55 UNP Q9NQ38 ISK5_HUMAN 23 77
SEQADV 1HDL ASN A 2 UNP Q9NQ38 ASP 24 VARIANT
SEQADV 1HDL GLU A 3 UNP Q9NQ38 SER 25 VARIANT
SEQADV 1HDL ASP A 4 UNP Q9NQ38 LEU 26 VARIANT
SEQADV 1HDL GLN A 5 UNP Q9NQ38 SER 27 VARIANT
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 PHE PHE 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 GLN A 12 PHE A 14 1 3
HELIX 2 2 LYS A 26 GLN A 30 1 5
HELIX 3 3 LEU A 32 ALA A 52 1 21
SHEET 1 S1 2 MET A 15 LYS A 16 0
SHEET 2 S1 2 LYS A 19 LEU A 20 -1 O LYS A 19 N LYS A 16
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