Header list of 1icy.pdb file
Complete list - 27 20 Bytes
HEADER HORMONE/GROWTH FACTOR 02-APR-01 1ICY
TITLE [ALA31,PRO32]-PNPY BOUND TO DPC MICELLES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NEUROPEPTIDE Y;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: NPY;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SUS SCROFA;
SOURCE 3 ORGANISM_COMMON: PIG;
SOURCE 4 ORGANISM_TAXID: 9823;
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-APNPY-G
KEYWDS Y5 RECEPTOR SELECTIVE NPY MUTANT, HORMONE-GROWTH FACTOR COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 17
AUTHOR R.BADER,G.RYTZ,M.LERCH,A.G.BECK-SICKINGER,O.ZERBE
REVDAT 5 27-OCT-21 1ICY 1 REMARK SEQADV LINK
REVDAT 4 24-FEB-09 1ICY 1 VERSN
REVDAT 3 01-APR-03 1ICY 1 JRNL
REVDAT 2 07-AUG-02 1ICY 1 JRNL
REVDAT 1 08-MAY-02 1ICY 0
JRNL AUTH R.BADER,G.RYTZ,M.LERCH,A.G.BECK-SICKINGER,O.ZERBE
JRNL TITL KEY MOTIF TO GAIN SELECTIVITY AT THE NEUROPEPTIDE
JRNL TITL 2 Y5-RECEPTOR: STRUCTURE AND DYNAMICS OF MICELLE-BOUND [ALA31,
JRNL TITL 3 PRO32]-NPY.
JRNL REF BIOCHEMISTRY V. 41 8031 2002
JRNL REFN ISSN 0006-2960
JRNL PMID 12069594
JRNL DOI 10.1021/BI0201419
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.1, OPAL (AMBER) 1.6
REMARK 3 AUTHORS : BRUKER (XWINNMR), LUNGINBUEHL ET AL. (OPAL
REMARK 3 (AMBER))
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 622 NOE CROSS PEAKS AND 16 HNHA COUPLINGS INDICATIVE OF NON-
REMARK 3 AVERAGED BACKBONE CONFORMATIONS
REMARK 4
REMARK 4 1ICY COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-APR-01.
REMARK 100 THE DEPOSITION ID IS D_1000013168.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 310; 310
REMARK 210 PH : 6.0; 6.0
REMARK 210 IONIC STRENGTH : 0; 0
REMARK 210 PRESSURE : 1 ATM; 1 ATM
REMARK 210 SAMPLE CONTENTS : 2 MM 31ALA,32PRO NPY, 300MM DPC,
REMARK 210 PH=6.0 90%H2O, 10% D2O; 2 MM
REMARK 210 31ALA,32PRO NPY, 300MM DPC, PH=
REMARK 210 6.0 99.9%D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
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 : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 17
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH NMR ENERGIES
REMARK 210 LESS THAN 3 KCAL/MOL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 2D
REMARK 210 HOMONUCLEAR TECHNIQUES
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 2 ARG A 25 NE - CZ - NH2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 4 ARG A 33 NE - CZ - NH2 ANGL. DEV. = -3.4 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 PRO A 2 -163.16 -76.92
REMARK 500 1 SER A 3 -75.60 71.27
REMARK 500 1 LYS A 4 -58.00 163.46
REMARK 500 1 ASP A 6 101.55 177.67
REMARK 500 1 PRO A 8 -169.43 -74.68
REMARK 500 1 ALA A 12 70.68 -170.50
REMARK 500 1 ALA A 14 56.60 -173.47
REMARK 500 1 ARG A 33 75.59 39.16
REMARK 500 1 ARG A 35 38.61 -86.29
REMARK 500 2 GLU A 10 64.79 61.75
REMARK 500 2 ASP A 11 -57.66 -167.17
REMARK 500 2 ALA A 12 73.53 -172.36
REMARK 500 2 ALA A 14 57.99 -171.53
REMARK 500 2 ASP A 16 -78.74 -54.12
REMARK 500 2 LEU A 30 32.23 -153.05
REMARK 500 2 PRO A 32 78.54 -68.24
REMARK 500 2 ARG A 33 -88.99 59.05
REMARK 500 3 ASP A 6 140.86 77.30
REMARK 500 3 PRO A 8 -160.57 -74.44
REMARK 500 3 GLU A 10 140.08 -177.84
REMARK 500 3 ASP A 11 84.29 60.95
REMARK 500 3 ALA A 12 82.51 58.30
REMARK 500 3 LEU A 30 20.62 -153.96
REMARK 500 3 ARG A 33 87.53 -177.55
REMARK 500 3 GLN A 34 66.98 64.21
REMARK 500 4 SER A 3 162.23 70.66
REMARK 500 4 LYS A 4 85.10 -177.34
REMARK 500 4 GLU A 10 51.74 -171.18
REMARK 500 4 ASP A 11 -89.82 172.41
REMARK 500 4 ALA A 14 61.90 -157.51
REMARK 500 4 PRO A 32 91.89 -69.77
REMARK 500 4 ARG A 33 70.79 42.59
REMARK 500 4 GLN A 34 26.95 45.37
REMARK 500 5 SER A 3 156.82 -47.97
REMARK 500 5 LYS A 4 -65.45 176.98
REMARK 500 5 ASP A 6 145.28 178.53
REMARK 500 5 ALA A 12 67.24 -170.77
REMARK 500 5 ALA A 14 61.23 -173.00
REMARK 500 5 GLN A 34 77.01 -169.55
REMARK 500 6 LYS A 4 73.14 -151.37
REMARK 500 6 ASN A 7 82.79 53.47
REMARK 500 6 GLU A 10 51.91 -171.05
REMARK 500 6 ASP A 11 85.98 55.91
REMARK 500 6 ARG A 35 63.56 -118.23
REMARK 500 7 LYS A 4 88.37 171.99
REMARK 500 7 ASN A 7 -56.38 164.15
REMARK 500 7 GLU A 10 72.15 59.64
REMARK 500 7 ASP A 11 98.10 -175.33
REMARK 500 7 ALA A 12 61.85 37.47
REMARK 500 7 ALA A 14 63.68 -176.52
REMARK 500
REMARK 500 THIS ENTRY HAS 130 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 1 0.10 SIDE CHAIN
REMARK 500 1 TYR A 27 0.07 SIDE CHAIN
REMARK 500 1 TYR A 36 0.13 SIDE CHAIN
REMARK 500 2 TYR A 1 0.09 SIDE CHAIN
REMARK 500 4 TYR A 20 0.07 SIDE CHAIN
REMARK 500 5 TYR A 27 0.09 SIDE CHAIN
REMARK 500 6 TYR A 27 0.12 SIDE CHAIN
REMARK 500 6 TYR A 36 0.10 SIDE CHAIN
REMARK 500 7 TYR A 1 0.06 SIDE CHAIN
REMARK 500 8 TYR A 20 0.09 SIDE CHAIN
REMARK 500 8 TYR A 21 0.07 SIDE CHAIN
REMARK 500 9 TYR A 1 0.12 SIDE CHAIN
REMARK 500 9 TYR A 20 0.07 SIDE CHAIN
REMARK 500 9 TYR A 21 0.09 SIDE CHAIN
REMARK 500 9 TYR A 36 0.08 SIDE CHAIN
REMARK 500 10 TYR A 21 0.11 SIDE CHAIN
REMARK 500 11 TYR A 1 0.10 SIDE CHAIN
REMARK 500 12 TYR A 21 0.10 SIDE CHAIN
REMARK 500 13 TYR A 20 0.08 SIDE CHAIN
REMARK 500 14 TYR A 20 0.07 SIDE CHAIN
REMARK 500 14 TYR A 27 0.09 SIDE CHAIN
REMARK 500 14 TYR A 36 0.08 SIDE CHAIN
REMARK 500 16 TYR A 1 0.10 SIDE CHAIN
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: 1F8P RELATED DB: PDB
REMARK 900 WILD-TYPE PORCINE NPY
DBREF 1ICY A 1 36 UNP P01304 NEUY_PIG 1 36
SEQADV 1ICY ALA A 31 UNP P01304 ILE 31 ENGINEERED MUTATION
SEQADV 1ICY PRO A 32 UNP P01304 THR 32 ENGINEERED MUTATION
SEQRES 1 A 37 TYR PRO SER LYS PRO ASP ASN PRO GLY GLU ASP ALA PRO
SEQRES 2 A 37 ALA GLU ASP LEU ALA ARG TYR TYR SER ALA LEU ARG HIS
SEQRES 3 A 37 TYR ILE ASN LEU ALA PRO ARG GLN ARG TYR NH2
HET NH2 A 37 3
HETNAM NH2 AMINO GROUP
FORMUL 1 NH2 H2 N
HELIX 1 1 GLU A 15 ASN A 29 1 15
LINK C TYR A 36 N NH2 A 37 1555 1555 1.33
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 - 27 20 Bytes