Header list of 1ma6.pdb file
Complete list - 27 20 Bytes
HEADER ANTIMICROBIAL PROTEIN 31-JUL-02 1MA6
TITLE TPY4 TACHYPLESIN I TYROSINE MUTANT IN THE PRESENCE OF
TITLE 2 DODECYLPHOSPHOCHOLINE MICELLES (300 MM)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TACHYPLESIN I;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: 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 I, TPY4, DODECYLPHOSPHOCHOLINE, MICELLE, BETA HAIRPIN,
KEYWDS 2 ANTIMICROBIAL PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 31
MDLTYP MINIMIZED AVERAGE
AUTHOR A.LAEDERACH,A.H.ANDREOTTI,D.B.FULTON
REVDAT 3 27-OCT-21 1MA6 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1MA6 1 VERSN
REVDAT 1 16-OCT-02 1MA6 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 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 1MA6 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_1000016788.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 313
REMARK 210 PH : 3.0
REMARK 210 IONIC STRENGTH : 0.15%
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : TPY4 MUTANT OF TACHYPLESIN I 1MM
REMARK 210 300 MM DODECYLPHOSPHOCHOLINE
REMARK 210 (D38)
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: THIS STRUCTURE WAS DETERMINED USING STANDARD 2D
REMARK 210 HOMONUCLEAR TECHNIQUES. A TEMPERATURE OF 313K WAS USED TO REDUCE
REMARK 210 SPECTRAL OVERLAP.
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 -80.10 -57.48
REMARK 500 1 TYR A 3 -142.05 -121.39
REMARK 500 1 PHE A 4 -34.90 -24.83
REMARK 500 1 VAL A 6 70.24 35.14
REMARK 500 1 TYR A 7 14.08 -146.28
REMARK 500 1 TYR A 8 -89.29 -139.54
REMARK 500 1 ARG A 9 116.41 103.54
REMARK 500 2 TRP A 2 -105.66 -82.63
REMARK 500 2 TYR A 3 -111.77 -142.77
REMARK 500 2 PHE A 4 55.23 -66.52
REMARK 500 2 ARG A 5 36.92 175.38
REMARK 500 2 VAL A 6 70.58 -69.98
REMARK 500 2 TYR A 8 -76.75 -135.42
REMARK 500 2 ARG A 9 128.44 96.90
REMARK 500 2 ARG A 14 -83.31 -115.15
REMARK 500 2 ARG A 15 -86.12 24.44
REMARK 500 2 TYR A 16 166.93 57.69
REMARK 500 3 TRP A 2 -97.05 -53.41
REMARK 500 3 TYR A 3 -127.12 -122.55
REMARK 500 3 VAL A 6 66.72 22.87
REMARK 500 3 TYR A 7 23.74 -153.32
REMARK 500 3 TYR A 8 -94.41 -137.62
REMARK 500 3 ARG A 9 -61.91 -160.38
REMARK 500 3 ILE A 11 -76.31 -25.24
REMARK 500 3 TYR A 16 119.28 60.54
REMARK 500 4 TRP A 2 -14.20 69.69
REMARK 500 4 TYR A 3 -79.39 -141.27
REMARK 500 4 PHE A 4 64.11 -65.07
REMARK 500 4 ARG A 5 -46.63 170.76
REMARK 500 4 VAL A 6 69.39 36.65
REMARK 500 4 TYR A 7 13.45 -152.01
REMARK 500 4 ARG A 9 72.46 -176.43
REMARK 500 4 ILE A 11 -74.09 -35.40
REMARK 500 4 TYR A 12 -28.93 168.05
REMARK 500 4 TYR A 16 171.78 -46.93
REMARK 500 5 TYR A 3 -150.70 125.08
REMARK 500 5 PHE A 4 78.97 -12.91
REMARK 500 5 ARG A 5 -51.11 155.60
REMARK 500 5 VAL A 6 66.72 34.73
REMARK 500 5 TYR A 7 11.84 -149.74
REMARK 500 5 ARG A 9 -25.36 -151.66
REMARK 500 5 ARG A 15 -75.03 -45.16
REMARK 500 5 TYR A 16 -66.64 68.11
REMARK 500 6 TRP A 2 -103.26 -68.43
REMARK 500 6 TYR A 3 -37.89 -146.79
REMARK 500 6 VAL A 6 29.52 39.91
REMARK 500 6 TYR A 8 -78.93 -161.74
REMARK 500 6 ARG A 9 -153.33 115.22
REMARK 500 6 TYR A 16 150.15 -45.52
REMARK 500 7 TRP A 2 -102.41 -77.70
REMARK 500
REMARK 500 THIS ENTRY HAS 243 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1MA2 RELATED DB: PDB
REMARK 900 TACHYPLESIN I SOLUTION STRUCTURE IN WATER
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 300 MM DODECYLPHOSPHOCHOLINE
REMARK 900 MICELLES
DBREF 1MA6 A 1 17 UNP P14213 TAC1_TACTR 24 40
SEQADV 1MA6 TYR A 3 UNP P14213 CYS 26 ENGINEERED MUTATION
SEQADV 1MA6 TYR A 7 UNP P14213 CYS 30 ENGINEERED MUTATION
SEQADV 1MA6 TYR A 12 UNP P14213 CYS 35 ENGINEERED MUTATION
SEQADV 1MA6 TYR A 16 UNP P14213 CYS 39 ENGINEERED MUTATION
SEQRES 1 A 17 LYS TRP TYR PHE ARG VAL TYR TYR ARG GLY ILE TYR TYR
SEQRES 2 A 17 ARG ARG TYR ARG
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 - 27 20 Bytes