Header list of 1fvn.pdb file
Complete list - v 3 2 Bytes
HEADER HORMONE/GROWTH FACTOR 20-SEP-00 1FVN
TITLE [ALA31, AIB32]-NEUROPEPTIDE Y
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NEUROPEPTIDE Y;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THE PEPTIDE WAS A DESIGNED SYNTHETIC MOLECULE. THE
SOURCE 4 SEQUENCE OF THE PEPTIDE IS DERIVED FROM NPY NATURALLY FOUND IN SUS
SOURCE 5 SCROFA (PIG).
KEYWDS ALPHA, 310-HELIX, HORMONE-GROWTH FACTOR COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 30
AUTHOR R.BADER,O.ZERBE,A.G.BECK-SICKINGER
REVDAT 4 03-NOV-21 1FVN 1 REMARK SEQADV LINK
REVDAT 3 24-FEB-09 1FVN 1 VERSN
REVDAT 2 20-DEC-00 1FVN 1 JRNL
REVDAT 1 04-OCT-00 1FVN 0
JRNL AUTH C.CABRELE,M.LANGER,R.BADER,H.A.WIELAND,H.N.DOODS,O.ZERBE,
JRNL AUTH 2 A.G.BECK-SICKINGER
JRNL TITL THE FIRST SELECTIVE AGONIST FOR THE NEUROPEPTIDE YY5
JRNL TITL 2 RECEPTOR INCREASES FOOD INTAKE IN RATS.
JRNL REF J.BIOL.CHEM. V. 275 36043 2000
JRNL REFN ISSN 0021-9258
JRNL PMID 10944518
JRNL DOI 10.1074/JBC.M000626200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.1, DYANA 1.5
REMARK 3 AUTHORS : BRUKER (XWINNMR), GUNTERT & WUTHRICH (DYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1FVN COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-SEP-00.
REMARK 100 THE DEPOSITION ID IS D_1000011938.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 310; 310; 310
REMARK 210 PH : 3.1; 3.1; 3.1
REMARK 210 IONIC STRENGTH : 0; 0; 0
REMARK 210 PRESSURE : 1 ATM; 1 ATM; 1 ATM
REMARK 210 SAMPLE CONTENTS : 2MM; 4MM; 2MM
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 : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 30
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: THIS STRUCTURE WAS DETERMINED USING STANDARD 2D
REMARK 210 HOMONUCLEAR TECHNIQUES USING 200MS NOESY MIXING TIME
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 O ILE A 28 H ALA A 31 1.54
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 SER A 3 76.23 63.72
REMARK 500 1 ASP A 6 95.29 50.18
REMARK 500 1 PRO A 8 -168.44 -74.95
REMARK 500 1 ASP A 11 115.76 172.87
REMARK 500 1 ALA A 12 158.07 178.45
REMARK 500 1 ALA A 14 -51.58 83.59
REMARK 500 1 ALA A 31 105.76 -171.20
REMARK 500 1 AIB A 32 -38.13 -154.47
REMARK 500 2 ASP A 6 128.14 173.59
REMARK 500 2 ASP A 11 99.21 53.13
REMARK 500 2 ALA A 14 -51.58 83.49
REMARK 500 2 ARG A 33 -46.15 -146.77
REMARK 500 3 SER A 3 70.11 -67.79
REMARK 500 3 LYS A 4 142.31 62.84
REMARK 500 3 GLU A 10 72.23 68.30
REMARK 500 3 ALA A 31 100.05 -169.95
REMARK 500 3 AIB A 32 -37.41 -149.94
REMARK 500 4 LYS A 4 93.65 56.16
REMARK 500 4 ASN A 7 146.76 169.52
REMARK 500 4 ASP A 11 -54.20 -141.03
REMARK 500 4 PRO A 13 -168.79 -74.97
REMARK 500 4 ALA A 14 26.30 42.62
REMARK 500 4 ALA A 31 99.80 -163.77
REMARK 500 4 AIB A 32 -33.17 -168.67
REMARK 500 5 LYS A 4 93.62 67.80
REMARK 500 5 ASP A 6 125.81 65.32
REMARK 500 5 ASN A 7 150.83 178.25
REMARK 500 5 ALA A 12 69.34 66.75
REMARK 500 5 GLU A 15 -34.65 -135.05
REMARK 500 5 AIB A 32 -39.16 -157.99
REMARK 500 6 SER A 3 174.53 53.51
REMARK 500 6 ASP A 6 170.93 55.20
REMARK 500 6 ASN A 7 100.71 -40.46
REMARK 500 6 GLU A 10 65.91 69.73
REMARK 500 6 ASP A 11 -50.41 -132.24
REMARK 500 6 ALA A 12 67.62 71.22
REMARK 500 6 ALA A 31 37.76 -97.26
REMARK 500 7 SER A 3 151.73 63.58
REMARK 500 7 ASP A 6 118.16 76.66
REMARK 500 7 ALA A 12 75.93 -168.45
REMARK 500 7 AIB A 32 -39.63 -159.70
REMARK 500 8 PRO A 2 -80.89 -75.03
REMARK 500 8 SER A 3 110.46 61.52
REMARK 500 8 ASP A 6 -35.10 163.59
REMARK 500 8 GLU A 10 -44.40 -130.10
REMARK 500 8 ALA A 12 154.33 66.85
REMARK 500 8 ALA A 14 26.28 42.53
REMARK 500 8 ALA A 31 -96.31 -79.49
REMARK 500 8 AIB A 32 -25.83 81.43
REMARK 500 9 ALA A 12 86.78 66.59
REMARK 500
REMARK 500 THIS ENTRY HAS 168 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: 1RON RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF HUMAN NEUROPEPTIDE Y
DBREF 1FVN A 1 36 UNP P01304 NEUY_PIG 1 36
SEQADV 1FVN ALA A 31 UNP P01304 ILE 31 ENGINEERED MUTATION
SEQADV 1FVN AIB 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 AIB ARG GLN ARG TYR NH2
MODRES 1FVN AIB A 32 ALA ALPHA-AMINOISOBUTYRIC ACID
HET AIB A 32 13
HET NH2 A 37 3
HETNAM AIB ALPHA-AMINOISOBUTYRIC ACID
HETNAM NH2 AMINO GROUP
FORMUL 1 AIB C4 H9 N O2
FORMUL 1 NH2 H2 N
HELIX 1 1 ASP A 16 ASN A 29 1 14
LINK C ALA A 31 N AIB A 32 1555 1555 1.35
LINK C AIB A 32 N ARG A 33 1555 1555 1.33
LINK C TYR A 36 N NH2 A 37 1555 1555 1.33
SITE 1 AC1 2 ARG A 33 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 - v 3 2 Bytes