Header list of 1hpk.pdb file
Complete list - 29 20 Bytes
HEADER SERINE PROTEASE 14-AUG-96 1HPK
TITLE SOLUTION NMR STRUCTURE OF THE HUMAN PLASMINOGEN KRINGLE 1 DOMAIN
TITLE 2 COMPLEXED WITH 6-AMINOHEXANOIC ACID AT PH 5.3, 310K, DERIVED FROM
TITLE 3 RANDOMLY GENERATED STRUCTURES USING SIMULATED ANNEALING, MINIMIZED
TITLE 4 AVERAGE STRUCTURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PLASMINOGEN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: KRINGLE 1 DOMAIN;
COMPND 5 EC: 3.4.21.7;
COMPND 6 OTHER_DETAILS: CONTAINS THE 6-AMINOHEXANOIC ACID LIGAND
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 PLASMA
KEYWDS SERINE PROTEASE, FIBRINOLYTIC ENZYME, LYSINE-BINDING DOMAIN
EXPDTA SOLUTION NMR
AUTHOR M.REJANTE,M.LLINAS
REVDAT 3 29-NOV-17 1HPK 1 REMARK HELIX
REVDAT 2 24-FEB-09 1HPK 1 VERSN
REVDAT 1 12-MAR-97 1HPK 0
JRNL AUTH M.R.REJANTE,M.LLINAS
JRNL TITL SOLUTION STRUCTURE OF THE EPSILON-AMINOHEXANOIC ACID COMPLEX
JRNL TITL 2 OF HUMAN PLASMINOGEN KRINGLE 1.
JRNL REF EUR.J.BIOCHEM. V. 221 939 1994
JRNL REFN ISSN 0014-2956
JRNL PMID 8181476
JRNL DOI 10.1111/J.1432-1033.1994.TB18809.X
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.R.REJANTE,M.LLINAS
REMARK 1 TITL 1H-NMR ASSIGNMENTS AND SECONDARY STRUCTURE OF HUMAN
REMARK 1 TITL 2 PLASMINOGEN KRINGLE 1
REMARK 1 REF EUR.J.BIOCHEM. V. 221 927 1994
REMARK 1 REFN ISSN 0014-2956
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 1HPK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000173956.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 310
REMARK 210 PH : 5.3
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 : 500 MHZ
REMARK 210 SPECTROMETER MODEL : AM-500
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
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 : MINIMIZED AVERAGE
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 HIS A 31 CG HIS A 31 ND1 -0.125
REMARK 500 HIS A 40 CG HIS A 40 ND1 -0.115
REMARK 500 TRP A 61 CG TRP A 61 CD2 -0.108
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 CD1 - NE1 - CE2 ANGL. DEV. = 5.7 DEGREES
REMARK 500 TRP A 61 CD1 - CG - CD2 ANGL. DEV. = 5.2 DEGREES
REMARK 500 TRP A 61 NE1 - CE2 - CZ2 ANGL. DEV. = 8.2 DEGREES
REMARK 500 TRP A 61 NE1 - CE2 - CD2 ANGL. DEV. = -6.8 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 LYS A 2 79.69 -102.25
REMARK 500 THR A 3 38.38 -78.66
REMARK 500 LYS A 7 -50.22 -153.80
REMARK 500 ARG A 10 -55.74 -142.87
REMARK 500 MET A 13 -75.27 -44.93
REMARK 500 SER A 14 59.36 178.56
REMARK 500 LYS A 17 -47.08 -20.20
REMARK 500 THR A 21 104.48 -37.67
REMARK 500 CYS A 22 -156.24 -61.24
REMARK 500 GLN A 23 -169.11 -114.42
REMARK 500 SER A 26 -81.88 -79.34
REMARK 500 SER A 27 170.37 172.23
REMARK 500 PRO A 30 -70.49 -67.92
REMARK 500 HIS A 31 116.01 176.96
REMARK 500 ARG A 32 131.85 162.31
REMARK 500 PRO A 33 -162.69 -61.03
REMARK 500 SER A 36 -6.03 156.79
REMARK 500 THR A 39 22.81 -78.70
REMARK 500 SER A 42 -149.35 -141.85
REMARK 500 GLU A 43 49.55 -177.07
REMARK 500 GLU A 47 -75.33 45.94
REMARK 500 ARG A 51 -150.43 -142.58
REMARK 500 ASP A 54 -87.45 -105.46
REMARK 500 ASN A 55 73.40 -177.22
REMARK 500 CYS A 62 135.87 -177.26
REMARK 500 THR A 65 12.38 -52.00
REMARK 500 PRO A 67 -76.88 -57.30
REMARK 500 GLU A 68 -31.02 -33.90
REMARK 500 ASP A 72 -177.55 152.80
REMARK 500 TYR A 73 -160.36 -74.67
REMARK 500 GLU A 78 -168.18 -53.02
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 0.28 SIDE CHAIN
REMARK 500 ARG A 32 0.31 SIDE CHAIN
REMARK 500 ARG A 34 0.24 SIDE CHAIN
REMARK 500 ARG A 51 0.32 SIDE CHAIN
REMARK 500 ARG A 70 0.22 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AHA
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: THESE RESIDUES COMPRISE THE 6-AMINOHEXANOIC ACID
REMARK 800 BINDING SITE AND, QUITE LIKELY, THE PHYSIOLOGICAL LIGAND (FIBRIN)
REMARK 800 BINDING SITE AS WELL.
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACA A 80
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1HPJ RELATED DB: PDB
DBREF 1HPK A 1 79 UNP P00747 PLMN_HUMAN 103 181
SEQRES 1 A 79 CYS LYS THR GLY ASN GLY LYS ASN TYR ARG GLY THR MET
SEQRES 2 A 79 SER LYS THR LYS ASN GLY ILE THR CYS GLN LYS TRP SER
SEQRES 3 A 79 SER THR SER PRO HIS ARG PRO ARG PHE SER PRO ALA THR
SEQRES 4 A 79 HIS PRO SER GLU GLY LEU GLU GLU ASN TYR CYS ARG ASN
SEQRES 5 A 79 PRO ASP ASN ASP PRO GLN GLY PRO TRP CYS TYR THR THR
SEQRES 6 A 79 ASP PRO GLU LYS ARG TYR ASP TYR CYS ASP ILE LEU GLU
SEQRES 7 A 79 CYS
HET ACA A 80 22
HETNAM ACA 6-AMINOHEXANOIC ACID
HETSYN ACA AMINOCAPROIC ACID
FORMUL 2 ACA C6 H13 N O2
HELIX 1 1 GLY A 11 MET A 13 5 3
SHEET 1 N1 2 SER A 14 THR A 16 0
SHEET 2 N1 2 ILE A 20 CYS A 22 -1 O ILE A 20 N THR A 16
SHEET 1 N2 2 PRO A 60 TYR A 63 0
SHEET 2 N2 2 TYR A 71 CYS A 74 -1 O ASP A 72 N CYS A 62
SSBOND 1 CYS A 1 CYS A 79 1555 1555 2.02
SSBOND 2 CYS A 22 CYS A 62 1555 1555 2.02
SSBOND 3 CYS A 50 CYS A 74 1555 1555 2.01
SITE 1 AHA 10 PRO A 33 ARG A 34 PHE A 35 ASP A 54
SITE 2 AHA 10 ASP A 56 TRP A 61 TYR A 63 ARG A 70
SITE 3 AHA 10 TYR A 71 TYR A 73
SITE 1 AC1 5 PRO A 33 ASP A 54 ASP A 56 TRP A 61
SITE 2 AC1 5 TYR A 63
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 - 29 20 Bytes