Header list of 1cou.pdb file
Complete list - b 16 2 Bytes
HEADER BLOOD CLOTTING 28-MAY-99 1COU
TITLE ANTICOAGULANT PROTEIN FROM THE NEMATODE ANCYLOSTOMA CANINUM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (NEMATODE ANTICOAGULANT PROTEIN C2);
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: NAPC2;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ANCYLOSTOMA CANINUM;
SOURCE 3 ORGANISM_COMMON: DOG HOOKWORM;
SOURCE 4 ORGANISM_TAXID: 29170;
SOURCE 5 EXPRESSION_SYSTEM: PICHIA PASTORIS;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 4922;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: GS115;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR: PYAM7SP8
KEYWDS ANTICOAGULANT, PROTEASE INHIBITOR, BLOOD CLOTTING
EXPDTA SOLUTION NMR
NUMMDL 18
AUTHOR B.M.DUGGAN,H.J.DYSON,P.E.WRIGHT
REVDAT 4 16-FEB-22 1COU 1 REMARK
REVDAT 3 24-FEB-09 1COU 1 VERSN
REVDAT 2 01-APR-03 1COU 1 JRNL
REVDAT 1 20-OCT-99 1COU 0
JRNL AUTH B.M.DUGGAN,H.J.DYSON,P.E.WRIGHT
JRNL TITL INHERENT FLEXIBILITY IN A POTENT INHIBITOR OF BLOOD
JRNL TITL 2 COAGULATION, RECOMBINANT NEMATODE ANTICOAGULANT PROTEIN C2.
JRNL REF EUR.J.BIOCHEM. V. 265 539 1999
JRNL REFN ISSN 0014-2956
JRNL PMID 10504384
JRNL DOI 10.1046/J.1432-1327.1999.00781.X
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH P.STANSSENS,P.W.BERGUM,Y.GANSEMANS,L.JESPERS,Y.LAROCHE,
REMARK 1 AUTH 2 S.HUANG,S.MAKI,J.MESSENS,M.LAUWEREYS,M.CAPPELLO,P.J.HOTEZ,
REMARK 1 AUTH 3 I.LASTERS,G.P.VLASUK
REMARK 1 TITL ANTICOAGULANT REPERTOIRE OF THE HOOKWORM ANCYLOSTOMA CANINUM
REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 93 2149 1996
REMARK 1 REFN ISSN 0027-8424
REMARK 1 DOI 10.1073/PNAS.93.5.2149
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : AMBER 5.1
REMARK 3 AUTHORS : CASE, PEARLMAN, CALDWELL, CHEATHAM, ROSS,
REMARK 3 SIMMERLING, DARDEN, MERZ, SEIBEL, STANTON, CHENG,
REMARK 3 VINCENT, CROWLEY, FERGUSON, RADMER, SINGH, WEINER,
REMARK 3 KOLLMAN
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1COU COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-JUN-99.
REMARK 100 THE DEPOSITION ID IS D_1000001128.
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 : 0.05 M
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 0.050 M NACL, 0.000020 M DSS AND
REMARK 210 EITHER 95% H2O/5% D2O OR 99.99%
REMARK 210 D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; DQ-COSY; 15N HSQC; 15N
REMARK 210 NOESY-HSQC; 15N TOCSY-HSQC; 15N
REMARK 210 HSQC-NOESY-HSQC; HNHA; 13C HSQC;
REMARK 210 15N {1H} NOE
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 750 MHZ
REMARK 210 SPECTROMETER MODEL : AMX500; AMX600; DMX750
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : FELIX 95, FELIX 97, DYANA, AMBER
REMARK 210 5.1
REMARK 210 METHOD USED : MOLECULAR DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 18
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATIONS AND
REMARK 210 LOWEST ENERGIES
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 14
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 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 6 TYR A 57 CB - CG - CD1 ANGL. DEV. = -3.6 DEGREES
REMARK 500 14 TYR A 26 CB - CG - CD2 ANGL. DEV. = -5.0 DEGREES
REMARK 500 16 CYS A 15 CA - CB - SG ANGL. DEV. = 7.2 DEGREES
REMARK 500 16 CYS A 46 CA - CB - SG ANGL. DEV. = 7.1 DEGREES
REMARK 500 17 CYS A 15 CA - CB - SG ANGL. DEV. = 6.6 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 1 THR A 3 64.28 -112.71
REMARK 500 1 GLN A 5 58.25 -144.64
REMARK 500 1 GLU A 8 -67.22 61.43
REMARK 500 1 SER A 14 44.48 -75.88
REMARK 500 1 CYS A 15 80.77 -165.39
REMARK 500 1 LYS A 18 -43.21 -152.10
REMARK 500 1 GLU A 19 -12.61 48.24
REMARK 500 1 ASP A 21 -71.79 -62.90
REMARK 500 1 LYS A 22 59.86 -91.99
REMARK 500 1 CYS A 24 89.41 -59.83
REMARK 500 1 LYS A 25 54.86 -66.52
REMARK 500 1 ASP A 34 -60.27 -105.82
REMARK 500 1 ASN A 38 -69.90 60.11
REMARK 500 1 LEU A 42 76.93 27.73
REMARK 500 1 VAL A 43 97.96 -62.80
REMARK 500 1 CYS A 46 49.76 -81.15
REMARK 500 1 ASP A 49 -155.59 -171.48
REMARK 500 1 GLU A 54 80.49 -62.55
REMARK 500 1 LYS A 60 -91.89 -150.42
REMARK 500 1 ASP A 76 48.32 -103.84
REMARK 500 1 PHE A 77 101.77 8.24
REMARK 500 1 THR A 82 -75.22 -92.68
REMARK 500 1 ARG A 83 59.04 -163.43
REMARK 500 1 ASN A 84 70.98 -113.09
REMARK 500 2 THR A 3 -83.68 -92.89
REMARK 500 2 GLN A 5 49.09 -71.73
REMARK 500 2 GLU A 8 82.22 -69.70
REMARK 500 2 ASN A 9 -42.37 73.26
REMARK 500 2 GLU A 10 77.69 -69.55
REMARK 500 2 CYS A 15 61.81 -162.21
REMARK 500 2 LYS A 18 -60.61 68.10
REMARK 500 2 GLU A 19 43.45 39.22
REMARK 500 2 CYS A 20 41.59 39.22
REMARK 500 2 ASP A 21 -71.71 -71.96
REMARK 500 2 TYR A 26 -4.41 -143.43
REMARK 500 2 ASP A 27 -70.75 -18.74
REMARK 500 2 GLU A 36 78.83 49.97
REMARK 500 2 PRO A 37 106.42 -50.94
REMARK 500 2 VAL A 43 143.67 71.17
REMARK 500 2 GLN A 48 104.35 -26.06
REMARK 500 2 ASP A 49 -145.27 -166.04
REMARK 500 2 VAL A 51 -129.55 -107.15
REMARK 500 2 GLU A 54 76.12 -65.19
REMARK 500 2 ARG A 58 89.41 -68.59
REMARK 500 2 LYS A 60 -105.58 38.46
REMARK 500 2 MET A 75 -50.15 74.45
REMARK 500 2 PHE A 77 39.31 86.90
REMARK 500 2 ILE A 78 -75.31 66.83
REMARK 500 2 ARG A 83 -58.66 67.97
REMARK 500 2 ASN A 84 -57.00 -157.88
REMARK 500
REMARK 500 THIS ENTRY HAS 434 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 TYR A 12 0.09 SIDE CHAIN
REMARK 500 2 TYR A 12 0.14 SIDE CHAIN
REMARK 500 2 TYR A 79 0.08 SIDE CHAIN
REMARK 500 2 ARG A 83 0.10 SIDE CHAIN
REMARK 500 3 TYR A 12 0.13 SIDE CHAIN
REMARK 500 3 TYR A 79 0.14 SIDE CHAIN
REMARK 500 4 TYR A 57 0.07 SIDE CHAIN
REMARK 500 5 TYR A 12 0.08 SIDE CHAIN
REMARK 500 5 TYR A 26 0.09 SIDE CHAIN
REMARK 500 5 ARG A 44 0.09 SIDE CHAIN
REMARK 500 5 TYR A 79 0.10 SIDE CHAIN
REMARK 500 6 TYR A 12 0.07 SIDE CHAIN
REMARK 500 6 TYR A 57 0.20 SIDE CHAIN
REMARK 500 6 ARG A 58 0.10 SIDE CHAIN
REMARK 500 7 TYR A 12 0.07 SIDE CHAIN
REMARK 500 7 TYR A 26 0.09 SIDE CHAIN
REMARK 500 7 TYR A 79 0.09 SIDE CHAIN
REMARK 500 8 TYR A 12 0.07 SIDE CHAIN
REMARK 500 8 TYR A 57 0.24 SIDE CHAIN
REMARK 500 9 TYR A 12 0.08 SIDE CHAIN
REMARK 500 9 TYR A 26 0.17 SIDE CHAIN
REMARK 500 9 TYR A 79 0.08 SIDE CHAIN
REMARK 500 10 TYR A 79 0.11 SIDE CHAIN
REMARK 500 11 TYR A 12 0.09 SIDE CHAIN
REMARK 500 11 TYR A 79 0.08 SIDE CHAIN
REMARK 500 11 ARG A 83 0.09 SIDE CHAIN
REMARK 500 12 TYR A 12 0.08 SIDE CHAIN
REMARK 500 12 TYR A 26 0.08 SIDE CHAIN
REMARK 500 13 ARG A 44 0.08 SIDE CHAIN
REMARK 500 13 ARG A 58 0.14 SIDE CHAIN
REMARK 500 13 TYR A 79 0.10 SIDE CHAIN
REMARK 500 14 TYR A 12 0.08 SIDE CHAIN
REMARK 500 14 TYR A 26 0.12 SIDE CHAIN
REMARK 500 14 PHE A 56 0.09 SIDE CHAIN
REMARK 500 15 TYR A 12 0.14 SIDE CHAIN
REMARK 500 15 TYR A 79 0.16 SIDE CHAIN
REMARK 500 16 TYR A 57 0.07 SIDE CHAIN
REMARK 500 17 TYR A 12 0.15 SIDE CHAIN
REMARK 500 17 HIS A 47 0.13 SIDE CHAIN
REMARK 500 17 TYR A 79 0.10 SIDE CHAIN
REMARK 500 18 TYR A 12 0.12 SIDE CHAIN
REMARK 500 18 TYR A 26 0.08 SIDE CHAIN
REMARK 500 18 TYR A 57 0.09 SIDE CHAIN
REMARK 500 18 TYR A 79 0.08 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1COU A 1 84 UNP Q16938 Q16938_ANCCA 8 91
SEQADV 1COU PRO A 85 UNP Q16938 SEE REMARK 999
SEQRES 1 A 85 LYS ALA THR MET GLN CYS GLY GLU ASN GLU LYS TYR ASP
SEQRES 2 A 85 SER CYS GLY SER LYS GLU CYS ASP LYS LYS CYS LYS TYR
SEQRES 3 A 85 ASP GLY VAL GLU GLU GLU ASP ASP GLU GLU PRO ASN VAL
SEQRES 4 A 85 PRO CYS LEU VAL ARG VAL CYS HIS GLN ASP CYS VAL CYS
SEQRES 5 A 85 GLU GLU GLY PHE TYR ARG ASN LYS ASP ASP LYS CYS VAL
SEQRES 6 A 85 SER ALA GLU ASP CYS GLU LEU ASP ASN MET ASP PHE ILE
SEQRES 7 A 85 TYR PRO GLY THR ARG ASN PRO
HELIX 1 1 ALA A 67 LEU A 72 1 6
SHEET 1 A 2 GLU A 10 ASP A 13 0
SHEET 2 A 2 ASP A 49 CYS A 52 -1 O ASP A 49 N ASP A 13
SHEET 1 B 2 TYR A 57 ARG A 58 0
SHEET 2 B 2 CYS A 64 VAL A 65 -1 N VAL A 65 O TYR A 57
SSBOND 1 CYS A 6 CYS A 50 1555 1555 2.08
SSBOND 2 CYS A 15 CYS A 46 1555 1555 2.09
SSBOND 3 CYS A 20 CYS A 41 1555 1555 2.08
SSBOND 4 CYS A 24 CYS A 70 1555 1555 2.07
SSBOND 5 CYS A 52 CYS A 64 1555 1555 2.07
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 - b 16 2 Bytes