Header list of 2rel.pdb file
Complete list - 29 20 Bytes
HEADER SERINE PROTEASE INHIBITOR 01-APR-97 2REL
TITLE SOLUTION STRUCTURE OF R-ELAFIN, A SPECIFIC INHIBITOR OF ELASTASE, NMR,
TITLE 2 11 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: R-ELAFIN;
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;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 OTHER_DETAILS: THE POLYPEPTIDE MAY BE OBTAINED BY EXPRESSION USING
SOURCE 8 PLASMIDIC EXPRESSION SYSTEMS IN HOSTS SUCH AS ESCHERICHIA COLI AND
SOURCE 9 YEAST, THE POLYPEPTIDE BEING ALSO OBTAINABLE FROM PSORIATIC PLAQUES.
SOURCE 10 PATENT NUMBER 5,464,822 DATE OF PATENT NOV. 7, 1995 BY CHRISTOPHERS
SOURCE 11 E., WIEDOW O., SCHRODER J.M. THE PROTEIN WAS PROVIDED BY ZENECA
SOURCE 12 PHARMACEUTICALS.
KEYWDS SERINE PROTEASE INHIBITOR, R-ELAFIN, ELASTASE INHIBITOR
EXPDTA SOLUTION NMR
NUMMDL 11
AUTHOR C.FRANCART,M.DAUCHEZ,A.J.P.ALIX,G.LIPPENS
REVDAT 3 29-NOV-17 2REL 1 REMARK HELIX
REVDAT 2 24-FEB-09 2REL 1 VERSN
REVDAT 1 07-JUL-97 2REL 0
SPRSDE 07-JUL-97 2REL 1REL
JRNL AUTH C.FRANCART,M.DAUCHEZ,A.J.ALIX,G.LIPPENS
JRNL TITL SOLUTION STRUCTURE OF R-ELAFIN, A SPECIFIC INHIBITOR OF
JRNL TITL 2 ELASTASE.
JRNL REF J.MOL.BIOL. V. 268 666 1997
JRNL REFN ISSN 0022-2836
JRNL PMID 9171290
JRNL DOI 10.1006/JMBI.1997.0983
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.TSUNEMI,H.KATO,Y.NISHIUCHI,S.KUMAGAYE,S.SAKAKIBARA
REMARK 1 TITL SYNTHESIS AND STRUCTURE-ACTIVITY RELATIONSHIPS OF ELAFIN, AN
REMARK 1 TITL 2 ELASTASE-SPECIFIC INHIBITOR
REMARK 1 REF BIOCHEM.BIOPHYS.RES.COMMUN. V. 185 967 1992
REMARK 1 REFN ISSN 0006-291X
REMARK 1 REFERENCE 2
REMARK 1 AUTH O.WIEDOW,J.M.SCHRODER,H.GREGORY,J.A.YOUNG,E.CHRISTOPHERS
REMARK 1 TITL ERRATUM. ELAFIN: AN ELASTASE-SPECIFIC INHIBITOR OF HUMAN
REMARK 1 TITL 2 SKIN. PURIFICATION, CHARACTERIZATION, AND COMPLETE AMINO
REMARK 1 TITL 3 ACID SEQUENCE
REMARK 1 REF J.BIOL.CHEM. V. 266 3356 1991
REMARK 1 REFN ISSN 0021-9258
REMARK 1 REFERENCE 3
REMARK 1 AUTH O.WIEDOW,J.M.SCHRODER,H.GREGORY,J.A.YOUNG,E.CHRISTOPHERS
REMARK 1 TITL ELAFIN: AN ELASTASE-SPECIFIC INHIBITOR OF HUMAN SKIN.
REMARK 1 TITL 2 PURIFICATION, CHARACTERIZATION, AND COMPLETE AMINO ACID
REMARK 1 TITL 3 SEQUENCE
REMARK 1 REF J.BIOL.CHEM. V. 265 14791 1990
REMARK 1 REFN ISSN 0021-9258
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2REL 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_1000178555.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : TOCSY; NOESY; DQFCOSY; 1H-13C
REMARK 210 HSQC; 1H-13C HSQC-TOCSY; 1H-13C
REMARK 210 HSQC-NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : DMX 600
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR 3.1
REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 11
REMARK 210 CONFORMERS, SELECTION CRITERIA : NOE AND DIHEDRAL ANGLE
REMARK 210 VIOLATIONS, ENERGY
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 VAL A 5 -88.80 51.88
REMARK 500 1 PRO A 8 -153.19 -77.93
REMARK 500 1 VAL A 9 42.07 -83.46
REMARK 500 1 SER A 10 108.60 59.99
REMARK 500 1 PRO A 13 -93.16 -77.46
REMARK 500 1 ILE A 18 123.81 62.62
REMARK 500 1 LEU A 20 -87.42 37.11
REMARK 500 1 ILE A 21 -85.27 -150.15
REMARK 500 1 ARG A 22 35.18 -173.87
REMARK 500 1 CYS A 23 91.36 5.13
REMARK 500 1 ALA A 24 61.49 -101.86
REMARK 500 1 MET A 25 -100.12 -96.07
REMARK 500 1 LEU A 26 -134.23 -117.68
REMARK 500 1 LEU A 33 -60.54 -158.04
REMARK 500 1 ILE A 41 58.13 -117.95
REMARK 500 1 CYS A 45 -159.64 -124.78
REMARK 500 1 SER A 48 85.46 44.52
REMARK 500 1 CYS A 49 104.25 87.40
REMARK 500 1 ALA A 52 -170.40 -170.90
REMARK 500 2 GLN A 2 71.34 -163.25
REMARK 500 2 VAL A 5 168.42 -43.89
REMARK 500 2 LYS A 6 -148.13 -106.51
REMARK 500 2 SER A 15 73.58 -109.14
REMARK 500 2 PRO A 17 -157.49 -81.84
REMARK 500 2 ILE A 21 92.79 117.95
REMARK 500 2 ARG A 22 39.30 27.32
REMARK 500 2 CYS A 23 21.68 38.06
REMARK 500 2 ALA A 24 -87.41 45.78
REMARK 500 2 MET A 25 102.78 -5.22
REMARK 500 2 ASN A 27 80.47 58.74
REMARK 500 2 LEU A 33 -41.35 -152.39
REMARK 500 2 LYS A 34 -32.67 174.44
REMARK 500 2 ASP A 35 -77.14 -41.32
REMARK 500 2 THR A 36 -36.15 172.45
REMARK 500 2 ASP A 37 94.51 -42.33
REMARK 500 2 CYS A 38 65.77 -170.63
REMARK 500 2 ILE A 41 -118.90 -84.24
REMARK 500 2 LYS A 42 -34.58 -142.37
REMARK 500 2 CYS A 49 91.71 78.92
REMARK 500 3 GLN A 2 -68.28 -91.04
REMARK 500 3 GLU A 3 99.73 61.11
REMARK 500 3 PRO A 4 -159.29 -78.66
REMARK 500 3 VAL A 5 -82.80 -68.43
REMARK 500 3 LYS A 6 179.30 170.19
REMARK 500 3 VAL A 9 -94.98 65.67
REMARK 500 3 SER A 10 75.68 -168.62
REMARK 500 3 CYS A 16 166.25 -47.80
REMARK 500 3 ILE A 18 131.14 61.03
REMARK 500 3 ILE A 19 -138.00 -132.76
REMARK 500 3 LEU A 20 -41.30 -161.70
REMARK 500
REMARK 500 THIS ENTRY HAS 228 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 22 0.26 SIDE CHAIN
REMARK 500 1 ARG A 31 0.19 SIDE CHAIN
REMARK 500 2 ARG A 22 0.25 SIDE CHAIN
REMARK 500 2 ARG A 31 0.31 SIDE CHAIN
REMARK 500 3 ARG A 22 0.19 SIDE CHAIN
REMARK 500 3 ARG A 31 0.31 SIDE CHAIN
REMARK 500 4 ARG A 22 0.11 SIDE CHAIN
REMARK 500 4 ARG A 31 0.28 SIDE CHAIN
REMARK 500 5 ARG A 22 0.31 SIDE CHAIN
REMARK 500 5 ARG A 31 0.12 SIDE CHAIN
REMARK 500 6 ARG A 31 0.32 SIDE CHAIN
REMARK 500 7 ARG A 22 0.27 SIDE CHAIN
REMARK 500 7 ARG A 31 0.32 SIDE CHAIN
REMARK 500 8 ARG A 22 0.32 SIDE CHAIN
REMARK 500 8 ARG A 31 0.24 SIDE CHAIN
REMARK 500 9 ARG A 22 0.30 SIDE CHAIN
REMARK 500 9 ARG A 31 0.20 SIDE CHAIN
REMARK 500 10 ARG A 22 0.23 SIDE CHAIN
REMARK 500 11 ARG A 22 0.29 SIDE CHAIN
REMARK 500 11 ARG A 31 0.17 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2REL A 1 57 UNP P19957 ELAF_HUMAN 61 117
SEQRES 1 A 57 ALA GLN GLU PRO VAL LYS GLY PRO VAL SER THR LYS PRO
SEQRES 2 A 57 GLY SER CYS PRO ILE ILE LEU ILE ARG CYS ALA MET LEU
SEQRES 3 A 57 ASN PRO PRO ASN ARG CYS LEU LYS ASP THR ASP CYS PRO
SEQRES 4 A 57 GLY ILE LYS LYS CYS CYS GLU GLY SER CYS GLY MET ALA
SEQRES 5 A 57 CYS PHE VAL PRO GLN
SHEET 1 A 2 LYS A 42 GLU A 46 0
SHEET 2 A 2 MET A 51 VAL A 55 -1 N PHE A 54 O LYS A 43
SSBOND 1 CYS A 16 CYS A 45 1555 1555 2.02
SSBOND 2 CYS A 23 CYS A 49 1555 1555 2.01
SSBOND 3 CYS A 32 CYS A 44 1555 1555 2.02
SSBOND 4 CYS A 38 CYS A 53 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 - 29 20 Bytes