Header list of 1k19.pdb file
Complete list - b 23 2 Bytes
HEADER LIPID TRANSPORT 24-SEP-01 1K19
TITLE NMR SOLUTION STRUCTURE OF THE CHEMOSENSORY PROTEIN CSP2 FROM MOTH
TITLE 2 MAMESTRA BRASSICAE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CHEMOSENSORY PROTEIN CSP2;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MAMESTRA BRASSICAE;
SOURCE 3 ORGANISM_COMMON: CABBAGE MOTH;
SOURCE 4 ORGANISM_TAXID: 55057;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS CHEMOSENSORY, PHEROMONE, LIPID TRANSPORT
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR A.MOSBAH,V.CAMPANACCI,A.LARTIGUE,M.TEGONI,C.CAMBILLAU,H.DARBON
REVDAT 4 23-FEB-22 1K19 1 REMARK
REVDAT 3 24-FEB-09 1K19 1 VERSN
REVDAT 2 18-MAR-03 1K19 1 JRNL REMARK
REVDAT 1 04-DEC-02 1K19 0
JRNL AUTH A.MOSBAH,V.CAMPANACCI,A.LARTIGUE,M.TEGONI,C.CAMBILLAU,
JRNL AUTH 2 H.DARBON
JRNL TITL SOLUTION STRUCTURE OF A CHEMOSENSORY PROTEIN FROM THE MOTH
JRNL TITL 2 MAMESTRA BRASSICAE
JRNL REF BIOCHEM.J. V. 369 39 2003
JRNL REFN ISSN 0264-6021
JRNL PMID 12217077
JRNL DOI 10.1042/BJ20021217
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH V.CAMPANACCI,A.MOSBAH,O.BORNET,R.WECHSELBERGER,
REMARK 1 AUTH 2 E.JACQUIN-JOLY,C.CAMBILLAU,H.DARBON,M.TEGONI
REMARK 1 TITL CHEMOSENSORY PROTEIN FROM THE MOTH MAMESTRA BRASSICAE.
REMARK 1 TITL 2 EXPRESSION AND SECONDARY STRUCTURE FROM 1H AND 15N NMR
REMARK 1 REF EUR.J.BIOCHEM. V. 268 4731 2001
REMARK 1 REFN ISSN 0014-2956
REMARK 1 DOI 10.1046/J.1432-1327.2001.02398.X
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE
REMARK 3 -KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,READ,RICE,
REMARK 3 SIMONSON,WARREN
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1K19 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-SEP-01.
REMARK 100 THE DEPOSITION ID IS D_1000014433.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 296
REMARK 210 PH : 6.9
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 2 MM OF UNLABELED PROTEIN, IN
REMARK 210 90% H2O AND 10% D2O CONTAINING
REMARK 210 10MM OF SODIUM PHOSPHATE BUFFER,
REMARK 210 25 MM NACL AT PH 6.9; 1 MM OF
REMARK 210 UNIFORMLY LABELED PROTEIN, IN 90%
REMARK 210 H2O AND 10% D2O CONTAINING 10MM
REMARK 210 OF SODIUM PHOSPHATE BUFFER, 25
REMARK 210 MM NACL AT PH 6.9
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; DQF-COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 750 MHZ
REMARK 210 SPECTROMETER MODEL : DRX; INOVA
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR 2.1, XEASY 1.3.13,
REMARK 210 NMRPIPE 1.8, DIANA 2.8, DYANA
REMARK 210 1.5, MOLMOL 2.6, TURBO-FRODO
REMARK 210 MARCH 2001 RELEASE A
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH ACCEPTABLE
REMARK 210 COVALENT GEOMETRY, STRUCTURES
REMARK 210 WITH FAVORABLE NON-BOND ENERGY,
REMARK 210 STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS, STRUCTURES
REMARK 210 WITH THE LOWEST ENERGY, TARGET
REMARK 210 FUNCTION
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 COMBINED WITH 3D HETERONUCLEAR 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: 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 LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 3 TYR A 8 CB TYR A 8 CG -0.097
REMARK 500 5 TYR A 8 CZ TYR A 8 CE2 -0.089
REMARK 500 5 TYR A 26 CG TYR A 26 CD2 -0.080
REMARK 500 5 TYR A 26 CE1 TYR A 26 CZ -0.078
REMARK 500 5 GLU A 111 CD GLU A 111 OE2 -0.079
REMARK 500 7 TYR A 8 CZ TYR A 8 CE2 -0.093
REMARK 500 7 GLU A 32 CD GLU A 32 OE1 -0.078
REMARK 500 9 GLU A 111 CD GLU A 111 OE1 -0.086
REMARK 500 12 GLU A 45 CD GLU A 45 OE1 -0.105
REMARK 500 12 TYR A 98 CG TYR A 98 CD1 -0.083
REMARK 500 14 GLU A 45 CD GLU A 45 OE1 -0.081
REMARK 500 14 GLU A 60 CD GLU A 60 OE1 -0.072
REMARK 500 16 GLU A 45 CD GLU A 45 OE1 -0.068
REMARK 500 16 GLU A 60 CD GLU A 60 OE2 -0.075
REMARK 500 19 GLU A 45 CD GLU A 45 OE1 -0.067
REMARK 500 19 GLU A 111 CD GLU A 111 OE1 -0.088
REMARK 500 20 TYR A 26 CG TYR A 26 CD2 -0.082
REMARK 500 20 TYR A 26 CE1 TYR A 26 CZ -0.080
REMARK 500 20 GLU A 63 CD GLU A 63 OE1 -0.071
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 9 ASP A 6 CB - CG - OD1 ANGL. DEV. = 5.5 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 ASP A 2 -66.88 69.05
REMARK 500 1 LYS A 3 -168.88 45.52
REMARK 500 1 THR A 5 -166.96 43.72
REMARK 500 1 LYS A 7 -158.26 39.57
REMARK 500 1 TYR A 8 -154.80 -62.72
REMARK 500 1 ASN A 12 26.60 43.25
REMARK 500 1 LEU A 13 -21.95 -35.22
REMARK 500 1 LYS A 35 28.84 49.22
REMARK 500 1 CYS A 36 -55.49 -134.85
REMARK 500 1 ALA A 50 -73.41 -103.95
REMARK 500 1 GLU A 52 -161.49 62.01
REMARK 500 1 ASN A 53 83.39 -62.48
REMARK 500 1 CYS A 55 58.71 -144.16
REMARK 500 1 CYS A 58 164.44 -46.82
REMARK 500 1 THR A 59 -95.01 -49.07
REMARK 500 1 GLU A 60 -34.54 -179.06
REMARK 500 1 GLU A 77 30.75 179.99
REMARK 500 1 ILE A 78 40.29 23.43
REMARK 500 1 THR A 91 -72.56 -58.35
REMARK 500 1 ASN A 93 -47.74 -152.56
REMARK 500 1 ILE A 107 102.41 -59.26
REMARK 500 2 LYS A 3 86.93 60.15
REMARK 500 2 TYR A 4 159.83 71.18
REMARK 500 2 LYS A 7 -114.36 37.90
REMARK 500 2 TYR A 8 -150.91 -62.63
REMARK 500 2 ASP A 9 -161.40 -57.53
REMARK 500 2 ASN A 10 -82.48 -91.48
REMARK 500 2 ILE A 11 -178.67 -64.77
REMARK 500 2 ASP A 14 -55.64 -137.10
REMARK 500 2 LEU A 22 -61.16 -100.41
REMARK 500 2 MET A 31 49.39 -171.13
REMARK 500 2 GLU A 32 -87.18 -105.90
REMARK 500 2 LYS A 35 173.15 55.80
REMARK 500 2 CYS A 36 -46.41 68.90
REMARK 500 2 GLU A 39 -86.97 -59.84
REMARK 500 2 LEU A 47 104.62 165.25
REMARK 500 2 ALA A 50 -35.09 164.78
REMARK 500 2 ILE A 51 -49.49 78.30
REMARK 500 2 GLU A 52 -154.17 -122.33
REMARK 500 2 CYS A 55 51.37 -118.06
REMARK 500 2 CYS A 58 87.60 -55.73
REMARK 500 2 GLU A 60 136.70 61.96
REMARK 500 2 ASN A 61 -74.82 51.72
REMARK 500 2 GLU A 77 28.68 -168.31
REMARK 500 2 ILE A 78 39.16 27.86
REMARK 500 2 TYR A 88 -0.29 75.88
REMARK 500 2 ILE A 107 102.36 -59.93
REMARK 500 2 PRO A 110 70.23 -66.83
REMARK 500 3 TYR A 4 163.01 179.44
REMARK 500 3 THR A 5 -174.72 -68.52
REMARK 500
REMARK 500 THIS ENTRY HAS 453 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1K19 A 1 112 UNP Q9NG96 Q9NG96_MAMBR 1 112
SEQRES 1 A 112 GLU ASP LYS TYR THR ASP LYS TYR ASP ASN ILE ASN LEU
SEQRES 2 A 112 ASP GLU ILE LEU ALA ASN LYS ARG LEU LEU VAL ALA TYR
SEQRES 3 A 112 VAL ASN CYS VAL MET GLU ARG GLY LYS CYS SER PRO GLU
SEQRES 4 A 112 GLY LYS GLU LEU LYS GLU HIS LEU GLN ASP ALA ILE GLU
SEQRES 5 A 112 ASN GLY CYS LYS LYS CYS THR GLU ASN GLN GLU LYS GLY
SEQRES 6 A 112 ALA TYR ARG VAL ILE GLU HIS LEU ILE LYS ASN GLU ILE
SEQRES 7 A 112 GLU ILE TRP ARG GLU LEU THR ALA LYS TYR ASP PRO THR
SEQRES 8 A 112 GLY ASN TRP ARG LYS LYS TYR GLU ASP ARG ALA LYS ALA
SEQRES 9 A 112 ALA GLY ILE VAL ILE PRO GLU GLU
HELIX 1 1 ASN A 12 ALA A 18 1 7
HELIX 2 2 ASN A 19 MET A 31 1 13
HELIX 3 3 CYS A 36 ILE A 51 1 16
HELIX 4 4 GLU A 60 ILE A 78 1 19
HELIX 5 5 GLU A 79 LYS A 87 1 9
HELIX 6 6 TRP A 94 GLY A 106 1 13
SSBOND 1 CYS A 29 CYS A 36 1555 1555 2.03
SSBOND 2 CYS A 55 CYS A 58 1555 1555 2.03
CRYST1 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 23 2 Bytes