Header list of 1ma2.pdb file
Complete list - 23 20 Bytes
HEADER ANTIMICROBIAL PROTEIN 31-JUL-02 1MA2
TITLE TACHYPLESIN I WILD TYPE PEPTIDE NMR STRUCTURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TACHYPLESIN I;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THE PEPTIDE WAS CHEMICALLY SYNTHESIZED USING FMOC
SOURCE 4 SOLID STATE SYNTHESIS. THE SEQUENCE OF THE PEPTIDE IS NATURALLY
SOURCE 5 FOUND IN TACHYPLEUS TRIDENTATUS (JAPANESE HORESHOE CRAB).
KEYWDS TACHYPLESIN, BETA HAIRPIN, DISULFIDE BRIDGE, ANTI-MICROBIAL PEPTIDE,
KEYWDS 2 ANTIMICROBIAL PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 31
MDLTYP MINIMIZED AVERAGE
AUTHOR A.LAEDERACH,A.H.ANDREOTTI,D.B.FULTON
REVDAT 4 23-FEB-22 1MA2 1 REMARK
REVDAT 3 03-NOV-09 1MA2 1 ATOM
REVDAT 2 24-FEB-09 1MA2 1 VERSN
REVDAT 1 16-OCT-02 1MA2 0
JRNL AUTH A.LAEDERACH,A.H.ANDREOTTI,D.B.FULTON
JRNL TITL SOLUTION AND MICELLE-BOUND STRUCTURES OF TACHYPLESIN I AND
JRNL TITL 2 ITS ACTIVE AROMATIC LINEAR DERIVATIVES
JRNL REF BIOCHEMISTRY V. 41 12359 2002
JRNL REFN ISSN 0006-2960
JRNL PMID 12369825
JRNL DOI 10.1021/BI026185Z
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0, CNS 1.0
REMARK 3 AUTHORS : BRUNGER, ADAMS, CLORE, DELANO, GROS, GROSSE
REMARK 3 -KUNSTLEVE, JIANG, KUSZEWSKI, NILGES, PANNU, READ,
REMARK 3 RICE, SIMONSON, WARREN (CNS), BRUNGER, ADAMS,
REMARK 3 CLORE, DELANO, GROS, GROSSE-KUNSTLEVE, JIANG,
REMARK 3 KUSZEWSKI, NILGES, PANNU, READ, RICE, SIMONSON,
REMARK 3 WARREN (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1MA2 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-AUG-02.
REMARK 100 THE DEPOSITION ID IS D_1000016784.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298; 277
REMARK 210 PH : 3.0; 3.0
REMARK 210 IONIC STRENGTH : 0.15%; 0.15%
REMARK 210 PRESSURE : 1 ATM; 1 ATM
REMARK 210 SAMPLE CONTENTS : TACHYPLESIN I PEPTIDE AT 0.5 MM
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR 6.1
REMARK 210 METHOD USED : SIMULATED ANNEALING WITH
REMARK 210 COMPLETE CROSS VALIDATION
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 300
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 31
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:
REMARK 210 2D EXPERIMENTS WERE COLLECTED BOTH IN PURE D2O AND 9:1 H2O:D2O.
REMARK 210 TO RESOLVE OVERLAP, TWO TEMPERATURES WERE USED, 277K AND 298K, AND
REMARK 210 NOE RESTRAINTS FROM BOTH TEMPERATURES WERE USED IN THE REFINEMENT
REMARK 210 PROCESS.
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: 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 TRP A 2 -81.09 -126.93
REMARK 500 1 ARG A 9 -79.52 64.00
REMARK 500 2 PHE A 4 28.16 -160.42
REMARK 500 2 ARG A 5 131.18 63.08
REMARK 500 2 VAL A 6 177.59 178.43
REMARK 500 2 ARG A 9 -77.58 64.07
REMARK 500 2 TYR A 13 -103.07 -136.79
REMARK 500 2 ARG A 14 -81.17 -131.34
REMARK 500 2 ARG A 15 162.26 59.36
REMARK 500 3 TRP A 2 86.07 61.45
REMARK 500 3 PHE A 4 -179.65 -49.72
REMARK 500 3 VAL A 6 163.37 86.46
REMARK 500 3 ARG A 9 -71.24 65.04
REMARK 500 3 TYR A 13 -157.80 -154.42
REMARK 500 4 TRP A 2 -154.24 -167.16
REMARK 500 4 CYS A 3 129.82 76.70
REMARK 500 4 PHE A 4 69.90 61.03
REMARK 500 4 VAL A 6 -86.31 46.13
REMARK 500 4 CYS A 7 116.27 -171.34
REMARK 500 4 ARG A 9 -64.76 66.27
REMARK 500 5 CYS A 3 67.70 174.00
REMARK 500 5 ARG A 9 -67.11 68.78
REMARK 500 5 ARG A 15 130.02 178.62
REMARK 500 5 CYS A 16 -162.65 -73.01
REMARK 500 6 TRP A 2 -162.51 179.55
REMARK 500 6 CYS A 3 -164.87 -57.53
REMARK 500 6 ARG A 5 -72.93 -73.53
REMARK 500 6 VAL A 6 132.14 98.84
REMARK 500 6 ARG A 9 -146.10 63.99
REMARK 500 6 ARG A 14 87.12 -174.56
REMARK 500 6 ARG A 15 -142.37 -83.20
REMARK 500 7 TRP A 2 -152.26 -178.43
REMARK 500 7 CYS A 3 130.27 71.93
REMARK 500 7 VAL A 6 146.98 -179.28
REMARK 500 7 ARG A 15 158.14 65.94
REMARK 500 8 CYS A 3 41.08 -99.21
REMARK 500 8 ARG A 5 79.09 61.76
REMARK 500 8 ARG A 9 -86.35 53.85
REMARK 500 9 TRP A 2 130.27 63.06
REMARK 500 9 CYS A 3 -163.21 -107.63
REMARK 500 9 ARG A 5 93.23 -47.23
REMARK 500 9 VAL A 6 152.17 170.31
REMARK 500 9 CYS A 7 -173.55 -173.16
REMARK 500 9 ARG A 9 83.33 -61.85
REMARK 500 9 ILE A 11 154.37 166.86
REMARK 500 9 ARG A 15 83.70 57.31
REMARK 500 9 CYS A 16 173.35 171.56
REMARK 500 10 CYS A 3 83.47 -150.49
REMARK 500 10 PHE A 4 -75.82 -154.21
REMARK 500 10 ARG A 5 -174.88 63.80
REMARK 500
REMARK 500 THIS ENTRY HAS 185 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1MA4 RELATED DB: PDB
REMARK 900 TPY4 SOLUTION STRUCTURE IN WATER
REMARK 900 RELATED ID: 1MA5 RELATED DB: PDB
REMARK 900 TACHYPLESIN I IN THE PRESENCE OF DODECYLPHOSPHOCHOLINE MICELLES
REMARK 900 RELATED ID: 1MA6 RELATED DB: PDB
REMARK 900 TPY4 TACHYPLESIN I TYROSINE MUTANT IN THE PRESENCE OF
REMARK 900 DODECYLPHOSPHOCHOLINE MICELLES
DBREF 1MA2 A 1 17 UNP P14213 TAC1_TACTR 24 40
SEQRES 1 A 17 LYS TRP CYS PHE ARG VAL CYS TYR ARG GLY ILE CYS TYR
SEQRES 2 A 17 ARG ARG CYS ARG
SHEET 1 A 2 VAL A 6 TYR A 8 0
SHEET 2 A 2 ILE A 11 TYR A 13 -1 O ILE A 11 N TYR A 8
SSBOND 1 CYS A 3 CYS A 16 1555 1555 2.03
SSBOND 2 CYS A 7 CYS A 12 1555 1555 2.03
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 - 23 20 Bytes