Header list of 1t50.pdb file
Complete list - r 2 2 Bytes
HEADER ATTRACTIN 30-APR-04 1T50
TITLE NMR SOLUTION STRUCTURE OF APLYSIA ATTRACTIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ATTRACTIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: APLYSIA CALIFORNICA;
SOURCE 3 ORGANISM_COMMON: CALIFORNIA SEA HARE;
SOURCE 4 ORGANISM_TAXID: 6500;
SOURCE 5 GENE: ATT;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: SF9;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 11 EXPRESSION_SYSTEM_VECTOR: PFASTBAC 1;
SOURCE 12 OTHER_DETAILS: SF-900 II SERUM-FREE MEDIUM
KEYWDS MOLLUSK, PHEROMONE, APLYSIA ATTRACTIN, ATTRACTIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR G.RAVINDRANATH,Y.XU,C.H.SCHEIN,K.RAJARATNAM,S.D.PAINTER,G.T.NAGLE,
AUTHOR 2 W.BRAUN
REVDAT 3 02-MAR-22 1T50 1 REMARK
REVDAT 2 24-FEB-09 1T50 1 VERSN
REVDAT 1 11-MAY-04 1T50 0
SPRSDE 11-MAY-04 1T50 1NJ7
JRNL AUTH G.RAVINDRANATH,Y.XU,C.H.SCHEIN,K.RAJARATHNAM,G.T.NAGLE,
JRNL AUTH 2 S.D.PAINTER,W.BRAUN
JRNL TITL NMR SOLUTION STRUCTURE OF ATTRACTIN, A WATER-BORNE PHEROMONE
JRNL TITL 2 FROM THE MOLLUSK APLYSIA ATTRACTIN
JRNL REF BIOCHEMISTRY V. 42 9970 2003
JRNL REFN ISSN 0006-2960
JRNL PMID 12924946
JRNL DOI 10.1021/BI0274322
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH C.H.SCHEIN,G.T.NAGLE,J.S.PAGE,J.V.SWEEDLER,Y.XU,S.D.PAINTER,
REMARK 1 AUTH 2 W.BRAUN
REMARK 1 TITL APLYSIA ATTRACTIN: BIOPHYSICAL CHARACTERIZATION AND MODELING
REMARK 1 TITL 2 OF A WATER-BORNE PHEROMONE
REMARK 1 REF BIOPHYS.J. V. 81 463 2001
REMARK 1 REFN ISSN 0006-3495
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NOAH/DIAMOND, FANTOM
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1T50 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-MAY-04.
REMARK 100 THE DEPOSITION ID IS D_1000022319.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298; 288
REMARK 210 PH : 6.8; 6.8
REMARK 210 IONIC STRENGTH : 1 MM; 1 MM
REMARK 210 PRESSURE : AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.7MM UNLABLED PROTEIN, 10 MM
REMARK 210 SODIUM PHOSPHATE BUFFER, 90% H20,
REMARK 210 10% D20
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; TOCSY; DQF-COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : UNITYPLUS
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : SELF-CORRECTING DG/ VTF
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : VTF VALUES
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: HOMONUCLEAR 1H NMR SPECTROSCOPY
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 GLN A 2 151.76 66.41
REMARK 500 1 ASN A 3 46.08 -92.34
REMARK 500 1 CYS A 4 155.83 61.77
REMARK 500 1 CYS A 20 117.91 67.31
REMARK 500 1 THR A 28 -61.56 -159.51
REMARK 500 1 LYS A 34 -70.11 -80.41
REMARK 500 1 SER A 48 -59.52 69.89
REMARK 500 1 ALA A 49 -48.57 -159.27
REMARK 500 1 ALA A 50 -54.69 -134.49
REMARK 500 2 GLN A 2 84.04 -156.53
REMARK 500 2 HIS A 17 43.84 -156.89
REMARK 500 2 CYS A 20 -45.03 -150.62
REMARK 500 2 GLU A 21 35.64 71.52
REMARK 500 2 PHE A 46 79.19 30.70
REMARK 500 2 SER A 48 52.77 -165.40
REMARK 500 2 ALA A 50 -56.21 -162.78
REMARK 500 2 SER A 52 -59.84 81.06
REMARK 500 2 THR A 53 24.22 -140.33
REMARK 500 3 CYS A 4 -83.44 -151.12
REMARK 500 3 ASP A 5 91.28 -164.61
REMARK 500 3 HIS A 17 74.93 -151.02
REMARK 500 3 GLU A 21 44.27 73.73
REMARK 500 3 THR A 28 -63.31 -96.68
REMARK 500 3 PHE A 46 76.35 29.82
REMARK 500 3 THR A 53 -176.24 51.69
REMARK 500 3 THR A 54 46.80 34.69
REMARK 500 4 CYS A 4 -46.43 -176.28
REMARK 500 4 ASP A 5 -47.33 -157.98
REMARK 500 4 ILE A 6 -52.38 -29.59
REMARK 500 4 HIS A 17 64.64 -151.45
REMARK 500 4 LYS A 18 63.55 -172.96
REMARK 500 4 ASN A 24 38.08 -162.63
REMARK 500 4 CYS A 26 45.26 -91.00
REMARK 500 4 THR A 28 -61.46 -107.58
REMARK 500 4 LYS A 34 -70.01 -91.49
REMARK 500 4 SER A 48 85.95 -68.15
REMARK 500 4 ALA A 50 45.27 -156.77
REMARK 500 4 SER A 52 49.64 -158.43
REMARK 500 4 THR A 54 145.68 70.16
REMARK 500 5 ASN A 3 -52.87 -167.71
REMARK 500 5 ASP A 5 94.21 -66.99
REMARK 500 5 CYS A 26 47.81 -106.04
REMARK 500 5 THR A 28 -61.48 -140.17
REMARK 500 5 LYS A 34 -77.78 -81.00
REMARK 500 5 PHE A 46 63.83 -103.22
REMARK 500 5 SER A 48 -79.31 58.26
REMARK 500 6 ASN A 3 -169.94 -167.41
REMARK 500 6 CYS A 4 138.53 -39.89
REMARK 500 6 HIS A 17 58.04 -154.83
REMARK 500 6 LYS A 18 83.32 -156.34
REMARK 500
REMARK 500 THIS ENTRY HAS 196 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 LYS A 18 ASN A 19 3 147.65
REMARK 500 ASP A 5 ILE A 6 4 -98.62
REMARK 500 CYS A 20 GLU A 21 11 149.65
REMARK 500 GLY A 56 PRO A 57 11 141.16
REMARK 500 PRO A 57 GLN A 58 11 -128.19
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1T50 A 1 58 UNP O96910 ATT_APLCA 19 76
SEQRES 1 A 58 ASP GLN ASN CYS ASP ILE GLY ASN ILE THR SER GLN CYS
SEQRES 2 A 58 GLN MET GLN HIS LYS ASN CYS GLU ASP ALA ASN GLY CYS
SEQRES 3 A 58 ASP THR ILE ILE GLU GLU CYS LYS THR SER MET VAL GLU
SEQRES 4 A 58 ARG CYS GLN ASN GLN GLU PHE GLU SER ALA ALA GLY SER
SEQRES 5 A 58 THR THR LEU GLY PRO GLN
HELIX 1 1 ILE A 9 HIS A 17 1 9
HELIX 2 2 ILE A 29 GLU A 39 1 11
HELIX 3 3 CYS A 41 PHE A 46 1 6
SSBOND 1 CYS A 4 CYS A 41 1555 1555 2.05
SSBOND 2 CYS A 13 CYS A 33 1555 1555 2.03
SSBOND 3 CYS A 20 CYS A 26 1555 1555 2.06
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 - r 2 2 Bytes