Header list of 2afd.pdb file
Complete list - t 20 2 Bytes
HEADER LIGAND BINDING PROTEIN 25-JUL-05 2AFD
TITLE SOLUTION STRUCTURE OF ASL1650, AN ACYL CARRIER PROTEIN FROM ANABAENA
TITLE 2 SP. PCC 7120 WITH A VARIANT PHOSPHOPANTETHEINYLATION-SITE SEQUENCE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN ASL1650;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: NOSTOC SP.;
SOURCE 3 ORGANISM_TAXID: 103690;
SOURCE 4 STRAIN: PCC 7120;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)-RIL (STRATAGENE);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET28B;
SOURCE 10 OTHER_DETAILS: SYNONYM NOSTOC SP. PCC 7120
KEYWDS TWISTED ANTIPARALLEL HELICAL BUNDLE; ACYL CARRIER PROTEIN FAMILY,
KEYWDS 2 STRUCTURAL GENOMICS, PSI, PROTEIN STRUCTURE INITIATIVE, JOINT CENTER
KEYWDS 3 FOR STRUCTURAL GENOMICS, JCSG, LIGAND BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR M.A.JOHNSON,W.PETI,T.HERRMANN,I.A.WILSON,K.WUTHRICH,JOINT CENTER FOR
AUTHOR 2 STRUCTURAL GENOMICS (JCSG)
REVDAT 5 20-OCT-21 2AFD 1 REMARK SEQADV
REVDAT 4 13-JUL-11 2AFD 1 VERSN
REVDAT 3 24-FEB-09 2AFD 1 VERSN
REVDAT 2 09-MAY-06 2AFD 1 JRNL
REVDAT 1 16-AUG-05 2AFD 0
JRNL AUTH M.A.JOHNSON,W.PETI,T.HERRMANN,I.A.WILSON,K.WUTHRICH
JRNL TITL SOLUTION STRUCTURE OF ASL1650, AN ACYL CARRIER PROTEIN FROM
JRNL TITL 2 ANABAENA SP. PCC 7120 WITH A VARIANT
JRNL TITL 3 PHOSPHOPANTETHEINYLATION-SITE SEQUENCE
JRNL REF PROTEIN SCI. V. 15 1030 2006
JRNL REFN ISSN 0961-8368
JRNL PMID 16597827
JRNL DOI 10.1110/PS.051964606
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : ATNOS 1, OPALP 1
REMARK 3 AUTHORS : HERRMANN T, GUNTERT P, WUTHRICH K (ATNOS),
REMARK 3 LUGINBUHL P, GUNTERT P, BILLETER M, WUTHRICH K
REMARK 3 (OPALP)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: AUTOMATED NOESY PEAK PICKING, AUTOMATED
REMARK 3 NOE ASSIGNMENT
REMARK 4
REMARK 4 2AFD COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-AUG-05.
REMARK 100 THE DEPOSITION ID IS D_1000033827.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303; 303; 303
REMARK 210 PH : 6.0; 6.0; 6.0
REMARK 210 IONIC STRENGTH : 250 MM NACL; 250 MM NACL; 250 MM
REMARK 210 NACL
REMARK 210 PRESSURE : AMBIENT; AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 2MM ASL1650 U-15N,13C; 20MM
REMARK 210 PHOSPHATE BUFFER, PH 6.0, 250MM
REMARK 210 NACL, 2MM NAN3; 2MM ASL1650 U-
REMARK 210 15N; 20MM PHOSPHATE BUFFER, PH
REMARK 210 6.0, 250MM NACL, 2MM NAN3, 90%
REMARK 210 H2O, 10% D2O; 2MM ASL1650; 20MM
REMARK 210 PHOSPHATE BUFFER, PH 6.0, 250MM
REMARK 210 NACL, 2MM NAN3
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 900 MHZ; 600 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : CANDID 1, DYANA 6.01
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 5
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: 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 4 ARG A 56 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 10 TYR A 43 CB - CG - CD2 ANGL. DEV. = -3.7 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 SER A 2 82.82 -156.01
REMARK 500 1 MET A 4 41.03 178.89
REMARK 500 1 LYS A 5 48.04 -165.31
REMARK 500 1 THR A 6 146.28 59.25
REMARK 500 1 ILE A 7 -122.48 -133.62
REMARK 500 1 ASN A 46 -98.51 -155.64
REMARK 500 1 SER A 47 -69.35 -134.68
REMARK 500 1 LYS A 63 -153.98 -131.68
REMARK 500 1 ASN A 72 -37.29 -131.96
REMARK 500 1 PRO A 74 43.11 -83.11
REMARK 500 1 TYR A 87 -57.69 -127.06
REMARK 500 2 MET A 4 42.27 -101.94
REMARK 500 2 LYS A 5 28.84 -153.21
REMARK 500 2 THR A 6 167.43 61.48
REMARK 500 2 ILE A 7 -124.15 -134.29
REMARK 500 2 TYR A 43 -159.01 -84.69
REMARK 500 2 ASN A 46 -79.79 -158.02
REMARK 500 2 SER A 47 -68.96 -152.89
REMARK 500 2 LYS A 63 -160.29 -128.26
REMARK 500 2 PRO A 74 42.69 -80.11
REMARK 500 2 TYR A 87 -66.52 -122.79
REMARK 500 3 HIS A 3 -44.22 -155.76
REMARK 500 3 THR A 6 153.69 -43.36
REMARK 500 3 ILE A 7 -111.73 -136.79
REMARK 500 3 VAL A 29 -169.23 -119.53
REMARK 500 3 TYR A 43 -166.60 -79.28
REMARK 500 3 ASN A 46 -95.07 -116.31
REMARK 500 3 SER A 47 -61.15 -139.46
REMARK 500 3 LYS A 63 -152.06 -130.34
REMARK 500 3 ASN A 72 -35.89 -134.70
REMARK 500 3 PRO A 74 44.03 -79.29
REMARK 500 3 TYR A 87 -62.31 -130.26
REMARK 500 4 HIS A 3 175.45 66.44
REMARK 500 4 ILE A 7 -123.15 -119.59
REMARK 500 4 ASN A 46 -104.67 -134.92
REMARK 500 4 SER A 47 -75.53 -115.26
REMARK 500 4 ASN A 72 -45.48 -148.65
REMARK 500 5 MET A 4 95.27 154.05
REMARK 500 5 LYS A 5 141.27 159.49
REMARK 500 5 ILE A 7 -124.97 -132.53
REMARK 500 5 PRO A 9 93.29 -67.37
REMARK 500 5 MET A 36 -4.08 -59.47
REMARK 500 5 LEU A 45 32.11 -73.13
REMARK 500 5 ASN A 46 -63.82 -24.79
REMARK 500 5 SER A 47 -61.19 -153.52
REMARK 500 5 LYS A 63 -153.09 -132.05
REMARK 500 5 ASN A 72 -32.10 -142.87
REMARK 500 5 PRO A 74 42.66 -84.30
REMARK 500 6 MET A 4 39.33 -161.40
REMARK 500 6 ILE A 7 -115.41 -118.26
REMARK 500
REMARK 500 THIS ENTRY HAS 193 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 GLY A 1 SER A 2 10 -147.42
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 43 0.07 SIDE CHAIN
REMARK 500 1 TYR A 73 0.07 SIDE CHAIN
REMARK 500 2 TYR A 73 0.08 SIDE CHAIN
REMARK 500 3 ARG A 82 0.10 SIDE CHAIN
REMARK 500 4 TYR A 73 0.08 SIDE CHAIN
REMARK 500 5 TYR A 73 0.08 SIDE CHAIN
REMARK 500 5 ARG A 82 0.12 SIDE CHAIN
REMARK 500 7 TYR A 73 0.08 SIDE CHAIN
REMARK 500 7 TYR A 87 0.08 SIDE CHAIN
REMARK 500 9 TYR A 73 0.09 SIDE CHAIN
REMARK 500 11 ARG A 56 0.08 SIDE CHAIN
REMARK 500 12 TYR A 73 0.08 SIDE CHAIN
REMARK 500 13 TYR A 73 0.08 SIDE CHAIN
REMARK 500 14 ARG A 82 0.09 SIDE CHAIN
REMARK 500 15 TYR A 73 0.10 SIDE CHAIN
REMARK 500 16 TYR A 73 0.09 SIDE CHAIN
REMARK 500 18 ARG A 56 0.11 SIDE CHAIN
REMARK 500 18 TYR A 73 0.09 SIDE CHAIN
REMARK 500 18 ARG A 82 0.15 SIDE CHAIN
REMARK 500 19 TYR A 73 0.09 SIDE CHAIN
REMARK 500 20 TYR A 73 0.10 SIDE CHAIN
REMARK 500 20 ARG A 82 0.08 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2AFE RELATED DB: PDB
REMARK 900 REPRESENTATIVE CONFORMER
REMARK 900 RELATED ID: 354432 RELATED DB: TARGETDB
DBREF 2AFD A 4 88 UNP Q8YWG3 Q8YWG3_ANASP 1 85
SEQADV 2AFD GLY A 1 UNP Q8YWG3 CLONING ARTIFACT
SEQADV 2AFD SER A 2 UNP Q8YWG3 CLONING ARTIFACT
SEQADV 2AFD HIS A 3 UNP Q8YWG3 CLONING ARTIFACT
SEQADV 2AFD ALA A 10 UNP Q8YWG3 CYS 7 ENGINEERED MUTATION
SEQRES 1 A 88 GLY SER HIS MET LYS THR ILE GLN PRO ALA SER VAL GLU
SEQRES 2 A 88 ASP ILE GLN SER TRP LEU ILE ASP GLN PHE ALA GLN GLN
SEQRES 3 A 88 LEU ASP VAL ASP PRO ASP ASP ILE ASP MET GLU GLU SER
SEQRES 4 A 88 PHE ASP ASN TYR ASP LEU ASN SER SER LYS ALA LEU ILE
SEQRES 5 A 88 LEU LEU GLY ARG LEU GLU LYS TRP LEU GLY LYS GLU LEU
SEQRES 6 A 88 ASN PRO VAL LEU ILE PHE ASN TYR PRO THR ILE ALA GLN
SEQRES 7 A 88 LEU ALA LYS ARG LEU GLY GLU LEU TYR LEU
HELIX 1 1 SER A 11 ASP A 28 1 18
HELIX 2 2 ASP A 30 ILE A 34 5 5
HELIX 3 3 SER A 39 TYR A 43 5 5
HELIX 4 4 SER A 48 LEU A 61 1 14
HELIX 5 5 ASN A 66 ILE A 70 5 5
HELIX 6 6 THR A 75 TYR A 87 1 13
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 - t 20 2 Bytes