Header list of 2a1c.pdb file
Complete list - 9 20 Bytes
HEADER HORMONE/GROWTH FACTOR 20-JUN-05 2A1C
TITLE SOLUTION STRUCTURE OF CSP1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CSP1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: COMPETENCE STIMULATING PEPTIDE TYPE 1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THE PEPTIDE WAS CHEMICALLY SYNTHESIZED. THIS SEQUENCE
SOURCE 4 OCCURES NATURALLY.
KEYWDS A-HELIX, HORMONE-GROWTH FACTOR COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR O.JOHNSBORG,P.E.KRISTIANSEN
REVDAT 3 09-MAR-22 2A1C 1 REMARK
REVDAT 2 24-FEB-09 2A1C 1 VERSN
REVDAT 1 30-MAY-06 2A1C 0
JRNL AUTH O.JOHNSBORG,P.E.KRISTIANSEN
JRNL TITL A HYDROPHOBIC PATCH IN THE PNEUMOCOCCAL COMPETENCE PHEROMONE
JRNL TITL 2 CSP IS ESSENTIAL FOR SPECIFICITY AND BIOLOGICAL ACTIVITY
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE 2004, CYANA 2004
REMARK 3 AUTHORS : DELAGLIO, F., GRZESIEK, S., VUISTER, G. W., ZHU,
REMARK 3 G., PFEIFER, J., BAX, A. (NMRPIPE), GUNTERT, P.,
REMARK 3 MUMENTHALER, C., WUTHRICH, K. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2A1C COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 23-JUN-05.
REMARK 100 THE DEPOSITION ID IS D_1000033368.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 301
REMARK 210 PH : 5.2
REMARK 210 IONIC STRENGTH : 0
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.9MM CSP1 0.1% TFA, 90% H2O,
REMARK 210 10% D2O, 250MM D38 DPC
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D TOCSY; 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : SPARKY 2004, TALOS 2004
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 : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
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 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 -57.86 -154.95
REMARK 500 1 SER A 5 -54.29 -161.36
REMARK 500 1 LYS A 16 151.13 -40.38
REMARK 500 2 SER A 5 -52.57 -149.81
REMARK 500 3 SER A 5 -51.11 -152.15
REMARK 500 4 SER A 5 -55.73 -163.87
REMARK 500 4 GLN A 14 176.26 51.76
REMARK 500 5 SER A 5 -58.29 -144.39
REMARK 500 6 SER A 5 -58.81 -144.12
REMARK 500 7 SER A 5 -53.59 -160.21
REMARK 500 8 MET A 2 -88.88 64.21
REMARK 500 8 SER A 5 -50.08 -159.81
REMARK 500 9 LEU A 4 109.94 71.61
REMARK 500 9 SER A 5 -53.66 -153.97
REMARK 500 9 LYS A 16 101.43 -40.39
REMARK 500 10 SER A 5 -52.34 -158.89
REMARK 500 11 SER A 5 -54.40 -155.45
REMARK 500 11 LYS A 16 131.43 -39.92
REMARK 500 12 ARG A 3 -58.93 178.39
REMARK 500 12 SER A 5 -52.73 -162.51
REMARK 500 12 LYS A 16 99.66 -40.08
REMARK 500 13 ARG A 3 -59.94 -171.74
REMARK 500 13 SER A 5 -58.37 -145.29
REMARK 500 13 LYS A 16 135.24 -39.93
REMARK 500 14 ARG A 3 -58.24 -134.57
REMARK 500 14 SER A 5 -54.65 -150.53
REMARK 500 14 GLN A 14 170.40 54.09
REMARK 500 15 SER A 5 -56.93 -149.20
REMARK 500 16 SER A 5 -52.72 -162.83
REMARK 500 17 SER A 5 -54.12 -160.57
REMARK 500 17 GLN A 14 159.48 57.61
REMARK 500 18 SER A 5 -53.71 -158.56
REMARK 500 18 GLN A 14 178.56 50.59
REMARK 500 19 SER A 5 -53.97 -148.40
REMARK 500 19 LYS A 16 155.37 -40.41
REMARK 500 20 SER A 5 -57.44 -152.15
REMARK 500 20 LYS A 16 -76.70 -40.48
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2A1C A 1 17 PDB 2A1C 2A1C 1 17
SEQRES 1 A 17 GLU MET ARG LEU SER LYS PHE PHE ARG ASP PHE ILE LEU
SEQRES 2 A 17 GLN ARG LYS LYS
HELIX 1 1 SER A 5 LEU A 13 1 9
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 - 9 20 Bytes