Header list of 1dip.pdb file
Complete list - b 16 2 Bytes
HEADER ACETYLATION 09-APR-97 1DIP
TITLE THE SOLUTION STRUCTURE OF PORCINE DELTA-SLEEP-INDUCING PEPTIDE
TITLE 2 IMMUNOREACTIVE PEPTIDE, NMR, 10 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DELTA-SLEEP-INDUCING PEPTIDE IMMUNOREACTIVE PEPTIDE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: DSIP-IMMUNOREACTIVE PEPTIDE;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SUS SCROFA;
SOURCE 3 ORGANISM_COMMON: PIG;
SOURCE 4 ORGANISM_TAXID: 9823
KEYWDS DELTA-SLEEP-INDUCING PEPTIDE IMMUNOREACTIVE PEPTIDE, LEUCINE ZIPPER,
KEYWDS 2 PIG, ACETYLATION
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR P.ROESCH,G.SEIDEL,K.ADERMANN,T.SCHINDLER,A.EJCHART,R.JAENICKE,
AUTHOR 2 W.G.FORSSMANN
REVDAT 4 16-FEB-22 1DIP 1 REMARK LINK
REVDAT 3 24-FEB-09 1DIP 1 VERSN
REVDAT 2 30-SEP-03 1DIP 1 DBREF
REVDAT 1 15-OCT-97 1DIP 0
JRNL AUTH G.SEIDEL,K.ADERMANN,T.SCHINDLER,A.EJCHART,R.JAENICKE,
JRNL AUTH 2 W.G.FORSSMANN,P.ROSCH
JRNL TITL SOLUTION STRUCTURE OF PORCINE DELTA SLEEP-INDUCING PEPTIDE
JRNL TITL 2 IMMUNOREACTIVE PEPTIDE A HOMOLOG OF THE SHORTSIGHTED GENE
JRNL TITL 3 PRODUCT.
JRNL REF J.BIOL.CHEM. V. 272 30918 1997
JRNL REFN ISSN 0021-9258
JRNL PMID 9388238
JRNL DOI 10.1074/JBC.272.49.30918
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH R.SILLARD,P.SCHULZ-KNAPPE,P.VOGEL,M.RAIDA,K.W.BENSCH,
REMARK 1 AUTH 2 W.G.FORSSMANN,V.MUTT
REMARK 1 TITL A NOVEL 77-RESIDUE PEPTIDE FROM PORCINE BRAIN CONTAINS A
REMARK 1 TITL 2 LEUCINE-ZIPPER MOTIF AND IS RECOGNIZED BY AN ANTISERUM TO
REMARK 1 TITL 3 DELTA-SLEEP-INDUCING PEPTIDE
REMARK 1 REF EUR.J.BIOCHEM. V. 216 429 1993
REMARK 1 REFN ISSN 0014-2956
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1DIP 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_1000172804.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 3.5
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 : 600 MHZ
REMARK 210 SPECTROMETER MODEL : AMX600
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NDEE, X-PLOR
REMARK 210 METHOD USED : SIMULATED ANNEALING, RESTRAINED
REMARK 210 MOLECULAR DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : ENERGY, AGREEMENT WITH
REMARK 210 EXPERIMENTAL DATA
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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: 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 5 35.84 -88.26
REMARK 500 1 ASN A 6 -48.59 -137.74
REMARK 500 1 HIS A 7 43.43 -82.60
REMARK 500 1 ALA A 11 -22.67 175.55
REMARK 500 1 GLU A 14 -32.15 175.18
REMARK 500 1 GLU A 15 -85.17 -103.44
REMARK 500 1 PRO A 46 -91.70 -77.14
REMARK 500 1 GLN A 48 25.90 -165.07
REMARK 500 1 LEU A 49 -151.43 -126.06
REMARK 500 1 LYS A 51 135.88 51.35
REMARK 500 1 PHE A 52 -35.16 -172.27
REMARK 500 1 LEU A 56 -76.94 -88.47
REMARK 500 1 GLU A 59 -165.31 -160.25
REMARK 500 1 ALA A 62 155.24 59.01
REMARK 500 1 PRO A 63 -163.82 -78.61
REMARK 500 1 GLU A 67 54.13 -116.83
REMARK 500 1 ALA A 68 142.22 -170.90
REMARK 500 1 LEU B 8 -29.22 -24.53
REMARK 500 1 TYR B 10 -12.90 -43.97
REMARK 500 1 ALA B 11 -43.80 -168.75
REMARK 500 1 VAL B 12 31.52 90.25
REMARK 500 1 ARG B 13 171.30 -44.26
REMARK 500 1 GLU B 14 -2.49 103.30
REMARK 500 1 GLU B 15 -169.15 -59.59
REMARK 500 1 GLN B 48 59.97 -174.78
REMARK 500 1 LEU B 49 -22.16 167.34
REMARK 500 1 GLU B 50 -30.98 -38.62
REMARK 500 1 LYS B 51 -50.68 -22.18
REMARK 500 1 PHE B 52 -154.52 -122.43
REMARK 500 1 GLN B 53 -90.97 -25.45
REMARK 500 1 SER B 54 56.62 144.68
REMARK 500 1 ARG B 55 26.07 168.83
REMARK 500 1 LEU B 56 -66.93 -130.81
REMARK 500 1 GLU B 59 -101.53 159.27
REMARK 500 1 GLU B 60 96.42 41.63
REMARK 500 1 PRO B 63 -163.24 -78.06
REMARK 500 1 GLU B 64 84.89 -68.14
REMARK 500 1 GLU B 70 -54.31 -167.18
REMARK 500 1 ALA B 71 -53.00 165.16
REMARK 500 1 ALA B 76 -163.00 -179.55
REMARK 500 2 ASP A 2 37.38 91.42
REMARK 500 2 LYS A 5 41.17 -100.59
REMARK 500 2 ASN A 6 -47.79 -141.07
REMARK 500 2 MET A 9 33.47 -84.42
REMARK 500 2 TYR A 10 -41.04 -133.25
REMARK 500 2 ALA A 11 -20.76 -140.05
REMARK 500 2 GLU A 14 25.76 41.55
REMARK 500 2 GLU A 15 119.74 177.59
REMARK 500 2 PRO A 46 34.01 -80.77
REMARK 500 2 GLU A 47 -74.21 -38.60
REMARK 500
REMARK 500 THIS ENTRY HAS 420 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 ARG A 13 0.32 SIDE CHAIN
REMARK 500 1 ARG A 24 0.32 SIDE CHAIN
REMARK 500 1 ARG A 35 0.22 SIDE CHAIN
REMARK 500 1 ARG A 55 0.28 SIDE CHAIN
REMARK 500 1 ARG B 13 0.30 SIDE CHAIN
REMARK 500 1 ARG B 24 0.20 SIDE CHAIN
REMARK 500 1 ARG B 35 0.10 SIDE CHAIN
REMARK 500 1 ARG B 55 0.24 SIDE CHAIN
REMARK 500 2 ARG A 13 0.27 SIDE CHAIN
REMARK 500 2 ARG A 35 0.28 SIDE CHAIN
REMARK 500 2 ARG A 55 0.29 SIDE CHAIN
REMARK 500 2 ARG B 13 0.23 SIDE CHAIN
REMARK 500 2 ARG B 35 0.21 SIDE CHAIN
REMARK 500 2 ARG B 55 0.23 SIDE CHAIN
REMARK 500 3 ARG A 13 0.21 SIDE CHAIN
REMARK 500 3 ARG A 24 0.32 SIDE CHAIN
REMARK 500 3 ARG A 35 0.32 SIDE CHAIN
REMARK 500 3 ARG A 55 0.20 SIDE CHAIN
REMARK 500 3 ARG B 13 0.26 SIDE CHAIN
REMARK 500 3 ARG B 24 0.30 SIDE CHAIN
REMARK 500 3 ARG B 35 0.19 SIDE CHAIN
REMARK 500 3 ARG B 55 0.09 SIDE CHAIN
REMARK 500 4 ARG A 13 0.23 SIDE CHAIN
REMARK 500 4 ARG A 24 0.24 SIDE CHAIN
REMARK 500 4 ARG A 35 0.24 SIDE CHAIN
REMARK 500 4 ARG A 55 0.27 SIDE CHAIN
REMARK 500 4 ARG B 13 0.32 SIDE CHAIN
REMARK 500 4 ARG B 24 0.08 SIDE CHAIN
REMARK 500 4 ARG B 35 0.16 SIDE CHAIN
REMARK 500 4 ARG B 55 0.29 SIDE CHAIN
REMARK 500 5 ARG A 13 0.30 SIDE CHAIN
REMARK 500 5 ARG A 24 0.27 SIDE CHAIN
REMARK 500 5 ARG A 35 0.30 SIDE CHAIN
REMARK 500 5 ARG A 55 0.32 SIDE CHAIN
REMARK 500 5 ARG B 13 0.26 SIDE CHAIN
REMARK 500 5 ARG B 24 0.32 SIDE CHAIN
REMARK 500 5 ARG B 35 0.28 SIDE CHAIN
REMARK 500 5 ARG B 55 0.32 SIDE CHAIN
REMARK 500 6 ARG A 13 0.09 SIDE CHAIN
REMARK 500 6 ARG A 24 0.25 SIDE CHAIN
REMARK 500 6 ARG A 35 0.29 SIDE CHAIN
REMARK 500 6 ARG B 13 0.21 SIDE CHAIN
REMARK 500 6 ARG B 24 0.32 SIDE CHAIN
REMARK 500 6 ARG B 35 0.32 SIDE CHAIN
REMARK 500 6 ARG B 55 0.26 SIDE CHAIN
REMARK 500 7 ARG A 13 0.30 SIDE CHAIN
REMARK 500 7 ARG A 24 0.31 SIDE CHAIN
REMARK 500 7 ARG A 35 0.31 SIDE CHAIN
REMARK 500 7 ARG B 13 0.21 SIDE CHAIN
REMARK 500 7 ARG B 24 0.25 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 76 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1DIP A 1 77 UNP P80220 T22D3_PIG 1 77
DBREF 1DIP B 1 77 UNP P80220 T22D3_PIG 1 77
SEQRES 1 A 78 ACE MET ASP LEU VAL LYS ASN HIS LEU MET TYR ALA VAL
SEQRES 2 A 78 ARG GLU GLU VAL GLU ILE LEU LYS GLU GLN ILE ARG GLU
SEQRES 3 A 78 LEU VAL GLU LYS ASN SER GLN LEU GLU ARG GLU ASN THR
SEQRES 4 A 78 LEU LEU LYS THR LEU ALA SER PRO GLU GLN LEU GLU LYS
SEQRES 5 A 78 PHE GLN SER ARG LEU SER PRO GLU GLU PRO ALA PRO GLU
SEQRES 6 A 78 THR PRO GLU ALA PRO GLU ALA PRO GLY GLY SER ALA VAL
SEQRES 1 B 78 ACE MET ASP LEU VAL LYS ASN HIS LEU MET TYR ALA VAL
SEQRES 2 B 78 ARG GLU GLU VAL GLU ILE LEU LYS GLU GLN ILE ARG GLU
SEQRES 3 B 78 LEU VAL GLU LYS ASN SER GLN LEU GLU ARG GLU ASN THR
SEQRES 4 B 78 LEU LEU LYS THR LEU ALA SER PRO GLU GLN LEU GLU LYS
SEQRES 5 B 78 PHE GLN SER ARG LEU SER PRO GLU GLU PRO ALA PRO GLU
SEQRES 6 B 78 THR PRO GLU ALA PRO GLU ALA PRO GLY GLY SER ALA VAL
HET ACE A 0 6
HET ACE B 0 6
HETNAM ACE ACETYL GROUP
FORMUL 1 ACE 2(C2 H4 O)
HELIX 1 1 HIS A 7 TYR A 10 5 4
HELIX 2 2 GLU A 17 LEU A 43 1 27
HELIX 3 3 VAL B 4 TYR B 10 1 7
HELIX 4 4 VAL B 16 ALA B 44 1 29
LINK C ACE A 0 N MET A 1 1555 1555 1.30
LINK C ACE B 0 N MET B 1 1555 1555 1.31
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 - b 16 2 Bytes