Header list of 1kdu.pdb file
Complete list - 1 20 Bytes
HEADER PLASMINOGEN ACTIVATION 15-JUL-93 1KDU
TITLE SEQUENTIAL 1H NMR ASSIGNMENTS AND SECONDARY STRUCTURE OF THE KRINGLE
TITLE 2 DOMAIN FROM UROKINASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PLASMINOGEN ACTIVATOR;
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
KEYWDS PLASMINOGEN ACTIVATION
EXPDTA SOLUTION NMR
AUTHOR X.LI,A.M.BOKMAN,M.LLINAS,R.A.G.SMITH,C.M.DOBSON
REVDAT 4 01-AUG-12 1KDU 1 JRNL VERSN
REVDAT 3 24-FEB-09 1KDU 1 VERSN
REVDAT 2 01-APR-03 1KDU 1 JRNL
REVDAT 1 31-OCT-93 1KDU 0
JRNL AUTH X.LI,A.M.BOKMAN,M.LLINAS,R.A.SMITH,C.M.DOBSON
JRNL TITL SOLUTION STRUCTURE OF THE KRINGLE DOMAIN FROM UROKINASE-TYPE
JRNL TITL 2 PLASMINOGEN ACTIVATOR.
JRNL REF J.MOL.BIOL. V. 235 1548 1994
JRNL REFN ISSN 0022-2836
JRNL PMID 8107091
JRNL DOI 10.1006/JMBI.1994.1106
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH X.LI,A.M.BOKMAN,M.LLINAS,R.A.G.SMITH,C.M.DOBSON
REMARK 1 TITL SOLUTION STRUCTURE OF THE KRINGLE DOMAIN FROM THE
REMARK 1 TITL 2 UROKINASE-TYPE PLASMINOGEN ACTIVATOR
REMARK 1 REF TO BE PUBLISHED
REMARK 1 REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1KDU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : NULL
REMARK 210 PH : NULL
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : NULL
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : NULL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
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: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 TRP A 25 CG TRP A 25 CD2 -0.115
REMARK 500 HIS A 40 CG HIS A 40 ND1 -0.111
REMARK 500 HIS A 48A NE2 HIS A 48A CD2 -0.073
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 TRP A 25 CA - CB - CG ANGL. DEV. = -14.0 DEGREES
REMARK 500 TRP A 25 CD1 - NE1 - CE2 ANGL. DEV. = 7.4 DEGREES
REMARK 500 TRP A 25 NE1 - CE2 - CZ2 ANGL. DEV. = 11.0 DEGREES
REMARK 500 TRP A 25 NE1 - CE2 - CD2 ANGL. DEV. = -8.0 DEGREES
REMARK 500 TRP A 25 CG - CD2 - CE3 ANGL. DEV. = -8.2 DEGREES
REMARK 500 HIS A 40 N - CA - CB ANGL. DEV. = -12.5 DEGREES
REMARK 500 TRP A 62 CD1 - CG - CD2 ANGL. DEV. = 4.9 DEGREES
REMARK 500 TRP A 62 CG - CD1 - NE1 ANGL. DEV. = -7.0 DEGREES
REMARK 500 TRP A 62 CD1 - NE1 - CE2 ANGL. DEV. = 6.9 DEGREES
REMARK 500 TRP A 62 NE1 - CE2 - CZ2 ANGL. DEV. = 7.5 DEGREES
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 CYS A 1 -55.14 -120.45
REMARK 500 HIS A 7 -80.43 -78.25
REMARK 500 ARG A 10 86.59 24.01
REMARK 500 LYS A 12 69.60 -106.37
REMARK 500 GLN A 34 -148.73 -61.58
REMARK 500 LYS A 48 27.66 47.71
REMARK 500 HIS A 48A -167.76 -79.72
REMARK 500 ARG A 52 -157.70 -133.70
REMARK 500 ASN A 53 47.02 -104.02
REMARK 500 PRO A 54 -7.27 -55.62
REMARK 500 ASP A 55 -75.12 -128.09
REMARK 500 ASN A 56 47.91 151.08
REMARK 500 MET A 76 34.75 -78.12
REMARK 500 VAL A 77 -158.11 -79.43
REMARK 500 CYS A 80 75.46 62.55
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 ARG A 10 0.13 SIDE CHAIN
REMARK 500 ARG A 20 0.31 SIDE CHAIN
REMARK 500 ARG A 41 0.31 SIDE CHAIN
REMARK 500 ARG A 52 0.16 SIDE CHAIN
REMARK 500 ARG A 57 0.18 SIDE CHAIN
REMARK 500 ARG A 58 0.20 SIDE CHAIN
REMARK 500 ARG A 60 0.29 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: BD1
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: BD2
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
DBREF 1KDU A -1 82 UNP P00749 UROK_HUMAN 69 153
SEQRES 1 A 85 THR CYS TYR GLU GLY ASN GLY HIS PHE TYR ARG GLY LYS
SEQRES 2 A 85 ALA SER THR ASP THR MET GLY ARG PRO CYS LEU PRO TRP
SEQRES 3 A 85 ASN SER ALA THR VAL LEU GLN GLN THR TYR HIS ALA HIS
SEQRES 4 A 85 ARG SER ASP ALA LEU GLN LEU GLY LEU GLY LYS HIS ASN
SEQRES 5 A 85 TYR CYS ARG ASN PRO ASP ASN ARG ARG ARG PRO TRP CYS
SEQRES 6 A 85 TYR VAL GLN VAL GLY LEU LYS PRO LEU VAL GLN GLU CYS
SEQRES 7 A 85 MET VAL HIS ASP CYS ALA ASP
HELIX 1 H1 ALA A 28 GLN A 33 11/5, DISORDERED 5
HELIX 2 H2 SER A 42 LEU A 44C 1DISORDERED 6
SHEET 1 B1 2 THR A 15 ASP A 16 0
SHEET 2 B1 2 ARG A 20 CYS A 22 -1 O ARG A 20 N ASP A 16
SHEET 1 B2 2 PRO A 24 TRP A 25 0
SHEET 2 B2 2 HIS A 48A ASN A 49 -1 O HIS A 48A N TRP A 25
SHEET 1 B3 2 TRP A 62 GLN A 66 0
SHEET 2 B3 2 PRO A 70 GLU A 74 -1 O GLN A 73 N CYS A 63
SSBOND 1 CYS A 1 CYS A 80 1555 1555 2.02
SSBOND 2 CYS A 22 CYS A 63 1555 1555 2.02
SSBOND 3 CYS A 51 CYS A 75 1555 1555 2.02
SITE 1 BD1 3 ARG A 57 ARG A 58 ARG A 60
SITE 1 BD2 2 HIS A 37 HIS A 40
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
Complete list - 1 20 Bytes