Header list of 1adz.pdb file
Complete list - v 3 2 Bytes
HEADER HYDROLASE 19-FEB-97 1ADZ
TITLE THE SOLUTION STRUCTURE OF THE SECOND KUNITZ DOMAIN OF TISSUE FACTOR
TITLE 2 PATHWAY INHIBITOR, NMR, 30 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TISSUE FACTOR PATHWAY INHIBITOR;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: FACTOR XA-BINDING DOMAIN (DOMAIN II);
COMPND 5 SYNONYM: TFPI, EPI, LACI;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 ORGAN: BLOOD;
SOURCE 6 TISSUE: BLOOD;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: JE5505;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PFLAG
KEYWDS HYDROLASE, INHIBITOR, COAGULATION
EXPDTA SOLUTION NMR
NUMMDL 30
AUTHOR M.J.M.BURGERING,L.P.M.ORBONS
REVDAT 4 03-NOV-21 1ADZ 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1ADZ 1 VERSN
REVDAT 2 01-APR-03 1ADZ 1 JRNL
REVDAT 1 25-FEB-98 1ADZ 0
JRNL AUTH M.J.BURGERING,L.P.ORBONS,A.VAN DER DOELEN,J.MULDERS,
JRNL AUTH 2 H.J.THEUNISSEN,P.D.GROOTENHUIS,W.BODE,R.HUBER,M.T.STUBBS
JRNL TITL THE SECOND KUNITZ DOMAIN OF HUMAN TISSUE FACTOR PATHWAY
JRNL TITL 2 INHIBITOR: CLONING, STRUCTURE DETERMINATION AND INTERACTION
JRNL TITL 3 WITH FACTOR XA.
JRNL REF J.MOL.BIOL. V. 269 395 1997
JRNL REFN ISSN 0022-2836
JRNL PMID 9199408
JRNL DOI 10.1006/JMBI.1997.1029
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.T.STUBBS II
REMARK 1 TITL STRUCTURAL ASPECTS OF FACTOR XA INHIBITION
REMARK 1 REF CURR.PHARM.DES. V. 2 543 1996
REMARK 1 REFN ISSN 1381-6128
REMARK 1 REFERENCE 2
REMARK 1 AUTH H.BRANDSTETTER,A.KUHNE,W.BODE,R.HUBER,W.VON DER SAAL,
REMARK 1 AUTH 2 K.WIRTHENSOHN,R.A.ENGH
REMARK 1 TITL X-RAY STRUCTURE OF ACTIVE SITE-INHIBITED CLOTTING FACTOR XA.
REMARK 1 TITL 2 IMPLICATIONS FOR DRUG DESIGN AND SUBSTRATE RECOGNITION
REMARK 1 REF J.BIOL.CHEM. V. 271 29988 1996
REMARK 1 REFN ISSN 0021-9258
REMARK 1 REFERENCE 3
REMARK 1 AUTH A.VAN DE LOCHT,M.T.STUBBS,W.BODE,T.FRIEDRICH,
REMARK 1 AUTH 2 C.BOLLSCHWEILER,W.HOFFKEN,R.HUBER
REMARK 1 TITL THE ORNITHODORIN-THROMBIN CRYSTAL STRUCTURE, A KEY TO THE
REMARK 1 TITL 2 TAP ENIGMA?
REMARK 1 REF EMBO J. V. 15 6011 1996
REMARK 1 REFN ISSN 0261-4189
REMARK 1 REFERENCE 4
REMARK 1 AUTH M.T.STUBBS,R.HUBER,W.BODE
REMARK 1 TITL CRYSTAL STRUCTURES OF FACTOR XA SPECIFIC INHIBITORS IN
REMARK 1 TITL 2 COMPLEX WITH TRYPSIN: STRUCTURAL GROUNDS FOR INHIBITION OF
REMARK 1 TITL 3 FACTOR XA AND SELECTIVITY AGAINST THROMBIN
REMARK 1 REF FEBS LETT. V. 375 103 1995
REMARK 1 REFN ISSN 0014-5793
REMARK 1 REFERENCE 5
REMARK 1 AUTH K.PADMANABHAN,K.P.PADMANABHAN,A.TULINSKY,C.H.PARK,W.BODE,
REMARK 1 AUTH 2 R.HUBER,D.T.BLANKENSHIP,A.D.CARDIN,W.KISIEL
REMARK 1 TITL STRUCTURE OF HUMAN DES(1-45) FACTOR XA AT 2.2 A RESOLUTION
REMARK 1 REF J.MOL.BIOL. V. 232 947 1993
REMARK 1 REFN ISSN 0022-2836
REMARK 1 REFERENCE 6
REMARK 1 AUTH K.D.BERNDT,P.GUNTERT,L.P.ORBONS,K.WUTHRICH
REMARK 1 TITL DETERMINATION OF A HIGH-QUALITY NUCLEAR MAGNETIC RESONANCE
REMARK 1 TITL 2 SOLUTION STRUCTURE OF THE BOVINE PANCREATIC TRYPSIN
REMARK 1 TITL 3 INHIBITOR AND COMPARISON WITH THREE CRYSTAL STRUCTURES
REMARK 1 REF J.MOL.BIOL. V. 227 757 1992
REMARK 1 REFN ISSN 0022-2836
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DIANA
REMARK 3 AUTHORS : GUNTERT,WUTHRICH
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES WERE CALCULATED USING
REMARK 3 THE DIANA PROGRAM BUT WERE NOT FURTHER REFINED USING A FORCE
REMARK 3 FIELD AND ENERGY MINIMIZATION AND/OR MOLECULAR DYNAMICS
REMARK 3 CALCULATIONS
REMARK 4
REMARK 4 1ADZ 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_1000170700.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 310
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 : HOMONUCLEAR NOESY; COSY; TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : DRX600
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : TRIAD NMR FROM TRIPOS TRIPOS
REMARK 210 METHOD USED : DIANA
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 300
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 30
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST VALUE OF VARIABLE TARGET
REMARK 210 FUNCTION
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: 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
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 TYR A 2 -152.08 65.63
REMARK 500 1 ASP A 4 76.23 -69.61
REMARK 500 1 ASP A 6 -58.69 82.12
REMARK 500 1 LYS A 8 45.83 35.27
REMARK 500 1 LEU A 9 80.84 36.59
REMARK 500 1 GLU A 17 158.98 -46.93
REMARK 500 1 CYS A 23 108.29 -59.38
REMARK 500 1 TYR A 26 124.90 64.82
REMARK 500 1 ILE A 27 21.93 -146.41
REMARK 500 1 THR A 28 76.95 46.34
REMARK 500 1 LYS A 37 54.56 32.91
REMARK 500 1 CYS A 47 -97.17 -10.08
REMARK 500 1 LEU A 48 -132.53 -61.28
REMARK 500 1 ASN A 50 -155.07 -151.77
REMARK 500 1 ASN A 52 76.46 -60.13
REMARK 500 1 ASN A 53 66.40 -153.79
REMARK 500 1 CYS A 64 -82.40 -79.50
REMARK 500 1 GLU A 65 -29.99 -37.34
REMARK 500 1 ASP A 66 73.64 38.35
REMARK 500 1 ASN A 69 -88.35 42.84
REMARK 500 2 LYS A 3 -43.68 -177.79
REMARK 500 2 ASP A 5 -26.24 92.89
REMARK 500 2 ASP A 6 -72.28 -57.53
REMARK 500 2 LEU A 9 36.76 33.19
REMARK 500 2 GLU A 17 173.27 -52.30
REMARK 500 2 PRO A 20 -86.99 -73.45
REMARK 500 2 CYS A 23 -114.45 -75.81
REMARK 500 2 ARG A 24 -78.64 -167.54
REMARK 500 2 TYR A 26 112.93 82.80
REMARK 500 2 LYS A 43 -166.36 -62.27
REMARK 500 2 TYR A 44 -112.75 -158.70
REMARK 500 2 CYS A 47 -69.04 -9.70
REMARK 500 2 LEU A 48 -163.65 -121.06
REMARK 500 2 ASN A 50 -157.37 -145.87
REMARK 500 2 ASN A 52 64.75 -65.59
REMARK 500 2 CYS A 64 -82.25 -83.38
REMARK 500 2 GLU A 65 -32.89 -35.70
REMARK 500 2 ASP A 66 175.18 94.53
REMARK 500 3 TYR A 2 100.33 -59.56
REMARK 500 3 LEU A 9 -118.38 -141.32
REMARK 500 3 GLU A 17 135.81 -39.97
REMARK 500 3 ILE A 22 -78.68 -31.66
REMARK 500 3 CYS A 23 151.61 -33.93
REMARK 500 3 TYR A 26 153.71 -48.76
REMARK 500 3 ILE A 27 22.79 -153.24
REMARK 500 3 LYS A 37 52.41 32.73
REMARK 500 3 CYS A 47 -176.48 -51.73
REMARK 500 3 ASN A 50 -157.51 -172.09
REMARK 500 3 MET A 51 -84.79 -80.61
REMARK 500 3 ASN A 52 98.51 -30.56
REMARK 500
REMARK 500 THIS ENTRY HAS 562 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1ADZ A 1 71 UNP P10646 TFPI1_HUMAN 107 182
SEQADV 1ADZ TYR A 2 UNP P10646 ASN 108 ENGINEERED MUTATION
SEQADV 1ADZ LYS A 3 UNP P10646 ALA 109 CONFLICT
SEQADV 1ADZ ASP A 4 UNP P10646 ASN 110 ENGINEERED MUTATION
SEQADV 1ADZ ASP A 5 UNP P10646 ARG 111 ENGINEERED MUTATION
SEQADV 1ADZ ASP A 6 UNP P10646 ILE 112 ENGINEERED MUTATION
SEQADV 1ADZ ASP A 7 UNP P10646 ILE 113 ENGINEERED MUTATION
SEQADV 1ADZ A UNP P10646 THR 115 DELETION
SEQADV 1ADZ A UNP P10646 THR 116 DELETION
SEQADV 1ADZ A UNP P10646 GLN 118 DELETION
SEQADV 1ADZ A UNP P10646 GLN 119 DELETION
SEQADV 1ADZ A UNP P10646 GLU 120 DELETION
SEQRES 1 A 71 ASP TYR LYS ASP ASP ASP ASP LYS LEU LYS PRO ASP PHE
SEQRES 2 A 71 CYS PHE LEU GLU GLU ASP PRO GLY ILE CYS ARG GLY TYR
SEQRES 3 A 71 ILE THR ARG TYR PHE TYR ASN ASN GLN THR LYS GLN CYS
SEQRES 4 A 71 GLU ARG PHE LYS TYR GLY GLY CYS LEU GLY ASN MET ASN
SEQRES 5 A 71 ASN PHE GLU THR LEU GLU GLU CYS LYS ASN ILE CYS GLU
SEQRES 6 A 71 ASP GLY PRO ASN GLY PHE
HELIX 1 1 ASP A 12 PHE A 15 5 4
HELIX 2 2 ASN A 34 THR A 36 5 3
HELIX 3 3 LEU A 57 ILE A 63 1 7
SHEET 1 A 2 ARG A 29 ASN A 33 0
SHEET 2 A 2 GLN A 38 PHE A 42 -1 N PHE A 42 O ARG A 29
SSBOND 1 CYS A 14 CYS A 64 1555 1555 2.41
SSBOND 2 CYS A 23 CYS A 47 1555 1555 2.15
SSBOND 3 CYS A 39 CYS A 60 1555 1555 2.33
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 - v 3 2 Bytes