Header list of 1ruu.pdb file
Complete list - 2 20 Bytes
HEADER HORMONE/GROWTH FACTOR 12-DEC-03 1RUU
TITLE SOLUTION STRUCTURE OF PORCINE PEPTIDE YY (PPYY) BOUND TO DPC MICELLES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PEPTIDE YY;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PYY, PEPTIDE TYROSINE TYROSINE;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SUS SCROFA;
SOURCE 3 ORGANISM_COMMON: PIG;
SOURCE 4 ORGANISM_TAXID: 9823;
SOURCE 5 GENE: PYY;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PUBK19
KEYWDS ALPHA-HELICAL, MICELLE-BOUND FORM, HORMONE-GROWTH FACTOR COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR M.LERCH,M.MAYRHOFER,O.ZERBE
REVDAT 3 02-MAR-22 1RUU 1 REMARK LINK
REVDAT 2 24-FEB-09 1RUU 1 VERSN
REVDAT 1 08-JUN-04 1RUU 0
JRNL AUTH M.LERCH,M.MAYRHOFER,O.ZERBE
JRNL TITL STRUCTURAL SIMILARITIES OF MICELLE-BOUND PEPTIDE YY (PYY)
JRNL TITL 2 AND NEUROPEPTIDE Y (NPY) ARE RELATED TO THEIR AFFINITY
JRNL TITL 3 PROFILES AT THE Y RECEPTORS.
JRNL REF J.MOL.BIOL. V. 339 1153 2004
JRNL REFN ISSN 0022-2836
JRNL PMID 15178255
JRNL DOI 10.1016/J.JMB.2004.04.032
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 3.0, AMBER 6
REMARK 3 AUTHORS : BRUKER (XWINNMR), KOLLMAN ET AL. (AMBER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1RUU COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-DEC-03.
REMARK 100 THE DEPOSITION ID IS D_1000021053.
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 : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 2MM PPYY, PH=5.5, 300MM D38-DPC;
REMARK 210 2MM PPYY, PH=5.5, 300MM D38-DPC;
REMARK 210 1MM 15N-PPYY, PH=5.5, 300MM D38-
REMARK 210 DPC
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 15N{1H}-NOE
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 700 MHZ
REMARK 210 SPECTROMETER MODEL : DRX; AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XEASY 2.51, DYANA 1.5
REMARK 210 METHOD USED : CALCULATION OF STRUCTURE BY
REMARK 210 TORSION ANGLE DYNAMICS;
REMARK 210 REFINEMENT BY ENERGY
REMARK 210 MINIMIZATION WITH FULL FORCE-
REMARK 210 FIELD IN EXPLICIT WATER
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: BACKBONE DYNAMICS INFORMATION WAS USED TO VERIFY
REMARK 210 STRUCTURES.
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: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
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 4 ARG A 35 NE - CZ - NH1 ANGL. DEV. = 3.7 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 LYS A 4 -57.57 162.04
REMARK 500 1 GLU A 15 102.24 79.84
REMARK 500 1 GLU A 16 -49.50 75.18
REMARK 500 2 GLU A 6 76.68 -107.70
REMARK 500 2 ALA A 7 92.20 -162.19
REMARK 500 2 GLU A 16 -52.46 -157.60
REMARK 500 2 ARG A 35 -56.37 -127.30
REMARK 500 3 LYS A 4 84.25 64.59
REMARK 500 3 ALA A 7 162.49 58.57
REMARK 500 3 GLU A 10 41.20 -69.79
REMARK 500 3 PRO A 14 45.92 -73.87
REMARK 500 3 GLU A 16 -45.37 -134.01
REMARK 500 3 ARG A 33 30.02 -81.68
REMARK 500 4 ALA A 3 97.18 -68.61
REMARK 500 4 ALA A 7 164.26 60.55
REMARK 500 4 GLU A 16 -60.41 -164.70
REMARK 500 4 ARG A 35 -54.50 -146.74
REMARK 500 5 ALA A 7 74.29 -117.42
REMARK 500 5 ALA A 12 78.46 -157.92
REMARK 500 5 GLU A 15 95.12 -171.17
REMARK 500 5 GLU A 16 -44.88 75.47
REMARK 500 6 GLU A 6 104.68 -161.70
REMARK 500 6 GLU A 10 72.09 44.50
REMARK 500 6 PRO A 14 -170.00 -69.53
REMARK 500 6 GLU A 15 89.04 78.78
REMARK 500 7 GLU A 10 76.62 -164.28
REMARK 500 7 ASP A 11 82.98 48.50
REMARK 500 7 GLU A 16 -4.51 67.18
REMARK 500 8 GLU A 6 178.74 60.18
REMARK 500 8 ALA A 7 74.73 55.06
REMARK 500 8 GLU A 10 32.04 -74.19
REMARK 500 8 GLU A 16 -39.50 -154.25
REMARK 500 9 ALA A 3 -93.01 -149.85
REMARK 500 9 GLU A 16 -52.27 -168.36
REMARK 500 9 ARG A 35 67.87 -154.73
REMARK 500 10 PRO A 2 -166.67 -71.89
REMARK 500 10 ALA A 3 119.69 -39.62
REMARK 500 10 GLU A 6 40.84 -151.88
REMARK 500 10 GLU A 10 36.99 -74.31
REMARK 500 10 GLU A 16 -53.11 -167.43
REMARK 500 11 LYS A 4 94.65 -36.95
REMARK 500 11 ALA A 7 82.70 -160.28
REMARK 500 11 GLU A 10 145.63 -170.10
REMARK 500 11 ASP A 11 -151.24 -109.96
REMARK 500 11 ALA A 12 47.33 85.92
REMARK 500 11 GLU A 16 -52.33 -168.05
REMARK 500 12 GLU A 10 134.13 -170.48
REMARK 500 12 GLU A 16 -44.18 -163.40
REMARK 500 13 PRO A 5 49.19 -73.86
REMARK 500 13 GLU A 6 109.43 -165.04
REMARK 500
REMARK 500 THIS ENTRY HAS 85 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: 1RU5 RELATED DB: PDB
REMARK 900 STRUCTURE OF PPYY UNLIGATED IN SOLUTION
DBREF 1RUU A 1 36 UNP P68005 PYY_PIG 1 36
SEQRES 1 A 37 TYR PRO ALA LYS PRO GLU ALA PRO GLY GLU ASP ALA SER
SEQRES 2 A 37 PRO GLU GLU LEU SER ARG TYR TYR ALA SER LEU ARG HIS
SEQRES 3 A 37 TYR LEU ASN LEU VAL THR ARG GLN ARG TYR NH2
HET NH2 A 37 3
HETNAM NH2 AMINO GROUP
FORMUL 1 NH2 H2 N
HELIX 1 1 GLU A 16 GLN A 34 1 19
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 - 2 20 Bytes