Header list of 1pyv.pdb file
Complete list - r 2 2 Bytes
HEADER HYDROLASE 09-JUL-03 1PYV
TITLE NMR SOLUTION STRUCTURE OF THE MITOCHONDRIAL F1B PRESEQUENCE PEPTIDE
TITLE 2 FROM NICOTIANA PLUMBAGINIFOLIA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ATP SYNTHASE BETA CHAIN, MITOCHONDRIAL PRECURSOR;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: F1B PRESEQUENCE PEPTIDE;
COMPND 5 EC: 3.6.3.14;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: NICOTIANA PLUMBAGINIFOLIA;
SOURCE 3 ORGANISM_COMMON: CURLED-LEAVED TOBACCO;
SOURCE 4 ORGANISM_TAXID: 4092;
SOURCE 5 GENE: ATPB OR ATP2-1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET21D
KEYWDS HYDROLASE
EXPDTA SOLUTION NMR
NUMMDL 24
AUTHOR P.MOBERG,S.NILSSON,A.STAHL,A.C.ERIKSSON,E.GLASER,L.MALER
REVDAT 3 02-MAR-22 1PYV 1 REMARK
REVDAT 2 24-FEB-09 1PYV 1 VERSN
REVDAT 1 06-APR-04 1PYV 0
JRNL AUTH P.MOBERG,S.NILSSON,A.STAHL,A.C.ERIKSSON,E.GLASER,L.MALER
JRNL TITL NMR SOLUTION STRUCTURE OF THE MITOCHONDRIAL F1BETA
JRNL TITL 2 PRESEQUENCE FROM NICOTIANA PLUMBAGINIFOLIA
JRNL REF J.MOL.BIOL. V. 336 1129 2004
JRNL REFN ISSN 0022-2836
JRNL PMID 15037074
JRNL DOI 10.1016/J.JMB.2004.01.006
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : FELIX 2000.1, DYANA 1.5
REMARK 3 AUTHORS : ACCELRYS (FELIX), GUNTERT, P. (DYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURE IS BASED ON A TOTAL OF 539 RESTRAINTS:
REMARK 3 518 NOE-DERIVED DISTANCE CONSTRAINTS, AND 21 PHI DIHEDRAL ANGLE
REMARK 3 RESTRAINTS FROM J-COUPLINGS.
REMARK 4
REMARK 4 1PYV COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-JUL-03.
REMARK 100 THE DEPOSITION ID IS D_1000019706.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 318
REMARK 210 PH : 7
REMARK 210 IONIC STRENGTH : 300 MM SDS
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1 MM F1B PRESEQUENCE, 300 MM
REMARK 210 SODIUM DODECYL PHOSPHATE, 30 UL
REMARK 210 D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; DQF-COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA; AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN; BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DYANA 1.5
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 24
REMARK 210 CONFORMERS, SELECTION CRITERIA : COMBINATION OF LOWEST ENERGY AND
REMARK 210 RESTRAINT VIOLATIONS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-24
REMARK 465 RES C SSSEQI
REMARK 465 MET A 0
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 ALA A 7 H ARG A 11 1.52
REMARK 500 O ALA A 14 H GLY A 17 1.59
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 ARG A 3 -62.03 70.49
REMARK 500 1 ILE A 21 -31.43 166.84
REMARK 500 1 SER A 24 -88.48 -44.72
REMARK 500 1 SER A 28 52.55 -150.82
REMARK 500 1 SER A 32 34.12 74.57
REMARK 500 1 ARG A 35 53.86 -92.68
REMARK 500 1 ALA A 36 -95.47 -158.36
REMARK 500 1 SER A 37 -68.63 72.77
REMARK 500 2 SER A 2 -174.71 163.08
REMARK 500 2 ARG A 4 -39.21 -38.95
REMARK 500 2 LEU A 20 41.35 -90.33
REMARK 500 2 ILE A 21 -45.01 -158.03
REMARK 500 2 SER A 24 -92.42 -50.13
REMARK 500 2 SER A 34 -38.50 -39.58
REMARK 500 2 ARG A 35 71.67 -117.08
REMARK 500 2 SER A 38 -56.18 82.15
REMARK 500 3 SER A 28 61.13 -159.77
REMARK 500 3 LYS A 31 -55.87 179.14
REMARK 500 3 ARG A 35 56.97 -155.03
REMARK 500 3 ALA A 36 -74.78 -105.52
REMARK 500 3 SER A 37 80.63 54.10
REMARK 500 3 SER A 38 -56.90 177.38
REMARK 500 3 ARG A 39 30.94 -168.21
REMARK 500 4 ARG A 16 -92.52 -155.77
REMARK 500 4 ARG A 23 -45.80 -141.10
REMARK 500 4 SER A 24 -94.89 -51.55
REMARK 500 4 SER A 28 68.14 -161.24
REMARK 500 4 LYS A 31 -61.47 169.07
REMARK 500 4 ARG A 35 50.05 -158.01
REMARK 500 4 ALA A 36 -100.30 -146.42
REMARK 500 4 SER A 37 -171.71 75.25
REMARK 500 4 SER A 38 -64.88 78.36
REMARK 500 5 SER A 2 114.45 -179.73
REMARK 500 5 ARG A 3 -47.36 -139.19
REMARK 500 5 ARG A 16 85.06 38.83
REMARK 500 5 SER A 22 -85.80 -39.23
REMARK 500 5 ARG A 23 24.30 -142.55
REMARK 500 5 SER A 24 -81.22 -84.70
REMARK 500 5 ALA A 33 29.78 46.53
REMARK 500 5 SER A 37 -41.64 -168.91
REMARK 500 6 SER A 28 68.02 174.69
REMARK 500 6 LYS A 31 -57.40 164.29
REMARK 500 6 ARG A 35 -44.61 -155.15
REMARK 500 6 ALA A 36 -91.83 -47.81
REMARK 500 6 SER A 37 151.90 80.46
REMARK 500 6 SER A 38 -70.67 83.36
REMARK 500 7 ARG A 3 -61.61 75.51
REMARK 500 7 LEU A 5 -75.43 -57.48
REMARK 500 7 ARG A 16 -98.29 -163.77
REMARK 500 7 SER A 24 -78.50 -50.16
REMARK 500
REMARK 500 THIS ENTRY HAS 193 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1PYV A 0 53 UNP P17614 ATPBM_NICPL 1 54
SEQRES 1 A 54 MET ALA SER ARG ARG LEU LEU ALA SER LEU LEU ARG GLN
SEQRES 2 A 54 SER ALA GLN ARG GLY GLY GLY LEU ILE SER ARG SER LEU
SEQRES 3 A 54 GLY ASN SER ILE PRO LYS SER ALA SER ARG ALA SER SER
SEQRES 4 A 54 ARG ALA SER PRO LYS GLY PHE LEU LEU ASN ARG ALA VAL
SEQRES 5 A 54 GLN TYR
HELIX 1 1 ARG A 3 GLN A 15 1 13
HELIX 2 2 SER A 24 ILE A 29 5 6
HELIX 3 3 SER A 41 TYR A 53 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 - r 2 2 Bytes