Header list of 1ljv.pdb file
Complete list - 23 20 Bytes
HEADER HORMONE/GROWTH FACTOR 22-APR-02 1LJV
TITLE BOVINE PANCREATIC POLYPEPTIDE BOUND TO DPC MICELLES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PANCREATIC HORMONE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PANCREATIC POLYPEPTIDE, PP;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: CATTLE;
SOURCE 4 ORGANISM_TAXID: 9913;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PUBK19
KEYWDS NMR MICELLE PEPTIDE HORMONE, HORMONE-GROWTH FACTOR COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR M.LERCH,V.GAFNER,R.BADER,B.CHRISTEN,O.ZERBE
REVDAT 4 23-FEB-22 1LJV 1 REMARK LINK
REVDAT 3 24-FEB-09 1LJV 1 VERSN
REVDAT 2 01-APR-03 1LJV 1 JRNL
REVDAT 1 09-OCT-02 1LJV 0
JRNL AUTH M.LERCH,V.GAFNER,R.BADER,B.CHRISTEN,G.FOLKERS,O.ZERBE
JRNL TITL BOVINE PANCREATIC POLYPEPTIDE (BPP) UNDERGOES SIGNIFICANT
JRNL TITL 2 CHANGES IN CONFORMATION AND DYNAMICS UPON BINDING TO DPC
JRNL TITL 3 MICELLES.
JRNL REF J.MOL.BIOL. V. 322 1117 2002
JRNL REFN ISSN 0022-2836
JRNL PMID 12367532
JRNL DOI 10.1016/S0022-2836(02)00889-6
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.6, AMBER 6
REMARK 3 AUTHORS : BRUKER (XWINNMR), P. KOLLMAN (AMBER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: 441 NOE-BASED DISTANCE RESTRAINTS, 137
REMARK 3 TORSION ANGLE RESTRAINTS
REMARK 4
REMARK 4 1LJV COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-APR-02.
REMARK 100 THE DEPOSITION ID IS D_1000016008.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 310
REMARK 210 PH : 5.5
REMARK 210 IONIC STRENGTH : 0
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 3MM BPP, 300MM D-38 DPC
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; E-COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XEASY 1.53, DYANA 1.5
REMARK 210 METHOD USED : SIMULATED ANNEALING RESTRAINT
REMARK 210 ENERGY MINIMIZATION WITH
REMARK 210 EXPLICIT WATER
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH ACCEPTABLE
REMARK 210 COVALENT GEOMETRY, STRUCTURES
REMARK 210 WITH FAVORABLE NON-BOND ENERGY,
REMARK 210 STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS, STRUCTURES
REMARK 210 WITH THE LOWEST ENERGY, TARGET
REMARK 210 FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
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: 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 LEU A 3 111.75 -167.12
REMARK 500 1 GLU A 4 75.69 36.41
REMARK 500 1 TYR A 7 94.62 -44.44
REMARK 500 1 ASP A 10 59.26 -153.16
REMARK 500 1 THR A 32 16.36 58.46
REMARK 500 2 LEU A 3 65.61 -166.80
REMARK 500 2 GLU A 4 76.61 54.85
REMARK 500 2 ASN A 11 92.55 -174.97
REMARK 500 3 LEU A 3 80.98 44.68
REMARK 500 3 GLU A 6 112.26 69.12
REMARK 500 3 ASN A 11 87.38 61.72
REMARK 500 3 ALA A 12 159.16 63.76
REMARK 500 4 ASN A 11 82.14 -167.26
REMARK 500 4 ARG A 33 101.48 -43.93
REMARK 500 5 GLU A 4 89.15 53.58
REMARK 500 5 ASN A 11 84.96 53.55
REMARK 500 5 THR A 13 152.54 -47.76
REMARK 500 5 GLU A 15 -104.50 -94.77
REMARK 500 5 ARG A 33 101.08 -47.29
REMARK 500 5 ARG A 35 165.14 64.08
REMARK 500 6 LEU A 3 99.58 -57.15
REMARK 500 6 ASN A 11 89.20 -160.41
REMARK 500 7 GLU A 6 89.05 52.79
REMARK 500 7 TYR A 7 74.28 -116.50
REMARK 500 7 ASN A 11 75.54 -168.00
REMARK 500 7 ARG A 33 100.46 -45.15
REMARK 500 8 GLU A 4 152.52 66.38
REMARK 500 8 ASN A 11 79.33 -169.23
REMARK 500 8 THR A 13 152.66 -48.64
REMARK 500 9 GLU A 4 152.52 66.38
REMARK 500 9 ASN A 11 79.33 -169.23
REMARK 500 9 THR A 13 152.66 -48.64
REMARK 500 10 GLU A 4 151.95 66.73
REMARK 500 10 ASN A 11 75.73 -165.60
REMARK 500 11 PRO A 2 45.76 -74.22
REMARK 500 11 GLU A 4 78.59 -164.60
REMARK 500 11 GLU A 6 169.48 55.74
REMARK 500 11 TYR A 7 87.25 -157.34
REMARK 500 11 ASN A 11 96.99 -168.21
REMARK 500 11 ARG A 33 99.16 -49.58
REMARK 500 12 LEU A 3 178.35 58.03
REMARK 500 12 GLU A 6 -179.25 -55.57
REMARK 500 12 ASN A 11 81.64 -153.79
REMARK 500 12 ARG A 35 86.15 -154.83
REMARK 500 13 PRO A 2 -89.38 -72.88
REMARK 500 13 GLU A 6 89.17 63.99
REMARK 500 13 ASP A 10 80.80 -164.57
REMARK 500 13 ASN A 11 101.19 -168.68
REMARK 500 13 THR A 13 150.49 -42.57
REMARK 500 13 ALA A 22 -70.78 -56.56
REMARK 500
REMARK 500 THIS ENTRY HAS 78 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NH2 A 37
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1BBA RELATED DB: PDB
REMARK 900 THE SAME MOLECULE IN SOLUTION
REMARK 900 RELATED ID: 1F8P RELATED DB: PDB
REMARK 900 PEPTIDE FROM THE SAME FAMILY UNDER SIMILIAR CONDITIONS
REMARK 900 RELATED ID: 1ICY RELATED DB: PDB
REMARK 900 PEPTIDE-MUTANT FROM THE SAME FAMILY UNDER SIMILIAR CONDITIONS
DBREF 1LJV A 1 36 UNP P01302 PAHO_BOVIN 30 65
SEQRES 1 A 37 ALA PRO LEU GLU PRO GLU TYR PRO GLY ASP ASN ALA THR
SEQRES 2 A 37 PRO GLU GLN MET ALA GLN TYR ALA ALA GLU LEU ARG ARG
SEQRES 3 A 37 TYR ILE ASN MET LEU THR ARG PRO ARG TYR NH2
HET NH2 A 37 3
HETNAM NH2 AMINO GROUP
FORMUL 1 NH2 H2 N
HELIX 1 1 THR A 13 THR A 32 1 20
LINK C TYR A 36 N NH2 A 37 1555 1555 1.32
SITE 1 AC1 1 TYR A 36
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 - 23 20 Bytes