Header list of 1dec.pdb file
Complete list - v 29 2 Bytes
HEADER BLOOD COAGULATION 17-MAY-94 1DEC
TITLE STRUCTURE OF THE RGD PROTEIN DECORSIN: CONSERVED MOTIF AND DISTINCT
TITLE 2 FUNCTION IN LEECH PROTEINS THAT AFFECT BLOOD CLOTTING
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DECORSIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MACROBDELLA DECORA;
SOURCE 3 ORGANISM_COMMON: NORTH AMERICAN LEECH;
SOURCE 4 ORGANISM_TAXID: 6405;
SOURCE 5 ORGAN: BLOOD
KEYWDS BLOOD COAGULATION
EXPDTA SOLUTION NMR
NUMMDL 25
AUTHOR A.M.KREZEL,G.WAGNER,J.SEYMOUR-ULMER,R.A.LAZARUS
REVDAT 3 29-NOV-17 1DEC 1 REMARK HELIX
REVDAT 2 24-FEB-09 1DEC 1 VERSN
REVDAT 1 31-AUG-94 1DEC 0
JRNL AUTH A.M.KREZEL,G.WAGNER,J.SEYMOUR-ULMER,R.A.LAZARUS
JRNL TITL STRUCTURE OF THE RGD PROTEIN DECORSIN: CONSERVED MOTIF AND
JRNL TITL 2 DISTINCT FUNCTION IN LEECH PROTEINS THAT AFFECT BLOOD
JRNL TITL 3 CLOTTING.
JRNL REF SCIENCE V. 264 1944 1994
JRNL REFN ISSN 0036-8075
JRNL PMID 8009227
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NULL
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1DEC 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_1000172752.
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 : 25
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 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 1 ARG A 3 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 1 ARG A 28 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 1 ARG A 31 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 2 ARG A 3 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 2 ARG A 28 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 2 ARG A 31 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 3 ARG A 3 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 3 ARG A 28 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 3 ARG A 31 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 4 ARG A 3 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 4 ARG A 28 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 4 ARG A 31 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 5 ARG A 3 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 5 ARG A 28 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 5 ARG A 31 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 6 ARG A 3 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 6 ARG A 28 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 6 ARG A 31 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 7 ARG A 3 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 7 ARG A 28 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 7 ARG A 31 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 8 ARG A 3 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 8 ARG A 28 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 8 ARG A 31 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 9 ARG A 3 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 9 ARG A 28 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 9 ARG A 31 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 10 ARG A 3 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 10 ARG A 28 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 10 ARG A 31 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 11 ARG A 3 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 11 ARG A 28 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 11 ARG A 31 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 12 ARG A 3 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 12 ARG A 28 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 12 ARG A 31 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 13 ARG A 3 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 13 ARG A 28 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 13 ARG A 31 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 14 ARG A 3 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 14 ARG A 28 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 14 ARG A 31 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 15 ARG A 3 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 15 ARG A 28 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 15 ARG A 31 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 16 ARG A 3 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 16 ARG A 28 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 16 ARG A 31 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 17 ARG A 3 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 17 ARG A 28 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 75 ANGLE DEVIATIONS.
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 PRO A 5 171.32 -53.81
REMARK 500 1 ASP A 10 83.17 63.50
REMARK 500 1 ASN A 18 -84.55 69.80
REMARK 500 1 LYS A 19 59.20 -146.79
REMARK 500 1 ASP A 33 65.29 -113.25
REMARK 500 2 PRO A 5 176.20 -56.12
REMARK 500 2 ASP A 10 83.56 53.15
REMARK 500 2 ASN A 18 -88.33 74.36
REMARK 500 2 LYS A 19 43.26 -145.15
REMARK 500 2 ASP A 33 66.02 -106.92
REMARK 500 3 PRO A 5 176.90 -55.55
REMARK 500 3 ASP A 10 82.05 59.92
REMARK 500 3 ASN A 18 -83.74 72.23
REMARK 500 3 LYS A 19 50.86 -143.88
REMARK 500 4 PRO A 5 173.15 -55.84
REMARK 500 4 ASP A 10 89.76 65.43
REMARK 500 4 ASN A 18 -89.07 70.27
REMARK 500 4 LYS A 19 57.51 -153.71
REMARK 500 4 ASP A 33 64.06 -110.56
REMARK 500 5 ASP A 10 84.31 62.29
REMARK 500 5 ASN A 18 -89.07 74.58
REMARK 500 5 LYS A 19 43.60 -144.35
REMARK 500 6 PRO A 5 173.25 -54.62
REMARK 500 6 ASP A 10 86.93 59.63
REMARK 500 6 ASN A 18 -91.69 71.76
REMARK 500 6 LYS A 19 51.07 -144.29
REMARK 500 7 ASP A 10 89.32 67.08
REMARK 500 7 ASN A 18 -84.59 70.89
REMARK 500 7 LYS A 19 56.60 -148.00
REMARK 500 7 ASP A 33 64.48 -106.56
REMARK 500 8 ASP A 10 84.88 62.94
REMARK 500 8 ASN A 18 -86.19 72.33
REMARK 500 8 LYS A 19 51.62 -144.95
REMARK 500 9 PRO A 5 175.22 -56.01
REMARK 500 9 ASP A 10 87.65 65.24
REMARK 500 9 ASN A 18 -89.64 74.08
REMARK 500 9 LYS A 19 45.45 -142.98
REMARK 500 9 ASP A 33 64.67 -107.84
REMARK 500 10 PRO A 5 175.36 -55.52
REMARK 500 10 ASP A 10 83.43 58.24
REMARK 500 10 ASN A 18 -81.16 74.03
REMARK 500 11 PRO A 5 174.13 -56.80
REMARK 500 11 ASP A 10 83.34 61.47
REMARK 500 11 ASN A 18 -84.77 71.44
REMARK 500 12 ASP A 10 84.45 62.72
REMARK 500 12 ASN A 18 -83.42 72.25
REMARK 500 12 LYS A 19 49.80 -143.17
REMARK 500 13 PRO A 5 176.75 -55.17
REMARK 500 13 ASP A 10 84.60 58.97
REMARK 500 13 ASN A 18 -84.19 71.53
REMARK 500
REMARK 500 THIS ENTRY HAS 97 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: RGD
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: ARG-GLY-ASP RECOGNITION SITE COMPRISES RESIDUES
REMARK 800 31 - 33
DBREF 1DEC A 1 39 UNP P17350 DECO_MACDE 1 39
SEQRES 1 A 39 ALA PRO ARG LEU PRO GLN CYS GLN GLY ASP ASP GLN GLU
SEQRES 2 A 39 LYS CYS LEU CYS ASN LYS ASP GLU CYS PRO PRO GLY GLN
SEQRES 3 A 39 CYS ARG PHE PRO ARG GLY ASP ALA ASP PRO TYR CYS GLU
SHEET 1 MIX 3 PRO A 5 CYS A 7 0
SHEET 2 MIX 3 CYS A 15 CYS A 17 1 O LEU A 16 N CYS A 7
SHEET 3 MIX 3 ASP A 20 CYS A 22 -1 N CYS A 22 O CYS A 15
SHEET 1 HRP 2 GLN A 26 PHE A 29 0
SHEET 2 HRP 2 PRO A 36 GLU A 39 -1 O TYR A 37 N ARG A 28
SSBOND 1 CYS A 7 CYS A 15 1555 1555 2.00
SSBOND 2 CYS A 17 CYS A 27 1555 1555 2.00
SSBOND 3 CYS A 22 CYS A 38 1555 1555 1.99
SITE 1 RGD 3 ARG A 31 GLY A 32 ASP A 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 29 2 Bytes