Header list of 2eyd.pdb file
Complete list - r 9 2 Bytes
HEADER PLANT PROTEIN 09-NOV-05 2EYD
TITLE WATER REFINED SOLUTION STRUCTURE OF CRAMBIN IN DPC MICELLES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CRAMBIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CRAMBE HISPANICA SUBSP. ABYSSINICA;
SOURCE 3 ORGANISM_TAXID: 3721;
SOURCE 4 STRAIN: SUBSP. ABYSSINICA;
SOURCE 5 GENE: THI2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET3A-SN_CRAMBIN
KEYWDS CRAMBIN, DPC, MICELLES, PLANT PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR H.C.AHN,J.L.MARKLEY
REVDAT 3 09-MAR-22 2EYD 1 REMARK
REVDAT 2 24-FEB-09 2EYD 1 VERSN
REVDAT 1 23-MAY-06 2EYD 0
JRNL AUTH H.C.AHN,N.JURANIC,S.MACURA,J.L.MARKLEY
JRNL TITL THREE-DIMENSIONAL STRUCTURE OF THE WATER-INSOLUBLE PROTEIN
JRNL TITL 2 CRAMBIN IN DODECYLPHOSPHOCHOLINE MICELLES AND ITS MINIMAL
JRNL TITL 3 SOLVENT-EXPOSED SURFACE.
JRNL REF J.AM.CHEM.SOC. V. 128 4398 2006
JRNL REFN ISSN 0002-7863
JRNL PMID 16569017
JRNL DOI 10.1021/JA057773D
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XPLOR-NIH 2.9.3
REMARK 3 AUTHORS : SCHWIETERS
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2EYD COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-NOV-05.
REMARK 100 THE DEPOSITION ID IS D_1000035244.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.0
REMARK 210 IONIC STRENGTH : 0
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.5 MM CRAMBIN U-15N,13C, PH
REMARK 210 6.0, 20 MM PHOSPHATE BUFFER,
REMARK 210 300MM DPC, 90% H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_ 15N
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ; 750 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA; DRX
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN; BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XPLOR-NIH 2.9.3
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 20
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : WATER REFINED STRUCTURES WITH
REMARK 210 THE LOWEST 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: 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 ALA A 38 88.75 65.45
REMARK 500 1 THR A 39 95.80 -63.79
REMARK 500 2 PRO A 5 10.44 -64.37
REMARK 500 3 SER A 6 136.05 -172.49
REMARK 500 4 PRO A 5 23.49 -76.83
REMARK 500 4 ALA A 38 15.27 -144.96
REMARK 500 5 GLU A 23 -36.93 -39.50
REMARK 500 5 THR A 39 42.00 -81.81
REMARK 500 6 PRO A 36 79.43 -68.70
REMARK 500 6 ALA A 38 10.34 -142.98
REMARK 500 7 PRO A 5 38.57 -92.30
REMARK 500 7 PRO A 19 21.59 -71.04
REMARK 500 8 ALA A 38 17.00 59.25
REMARK 500 8 THR A 39 54.24 -108.92
REMARK 500 9 ALA A 38 30.19 -81.94
REMARK 500 9 THR A 39 30.69 -85.13
REMARK 500 10 PRO A 5 35.40 -90.04
REMARK 500 10 PRO A 19 11.93 -68.34
REMARK 500 10 ALA A 38 81.06 62.55
REMARK 500 10 THR A 39 97.24 -68.10
REMARK 500 10 ALA A 45 36.11 -94.53
REMARK 500 11 SER A 6 148.70 -170.59
REMARK 500 12 ALA A 45 40.05 -94.10
REMARK 500 13 ALA A 38 14.75 -153.19
REMARK 500 14 PRO A 5 31.69 -88.03
REMARK 500 14 ALA A 38 -5.80 71.32
REMARK 500 14 CYS A 40 141.98 67.02
REMARK 500 15 PRO A 5 30.92 -88.47
REMARK 500 15 ALA A 38 -85.10 -173.74
REMARK 500 15 THR A 39 -3.69 -141.77
REMARK 500 15 CYS A 40 139.70 66.09
REMARK 500 15 ALA A 45 50.89 -113.14
REMARK 500 16 ALA A 38 -19.47 76.46
REMARK 500 17 PRO A 36 80.13 -69.35
REMARK 500 17 ALA A 38 -37.22 -138.77
REMARK 500 17 ALA A 45 42.29 -90.32
REMARK 500 18 GLU A 23 -39.65 -39.38
REMARK 500 18 ALA A 38 41.01 -94.61
REMARK 500 19 PRO A 36 42.76 -80.00
REMARK 500 19 ALA A 38 30.64 76.41
REMARK 500 19 THR A 39 -95.48 46.91
REMARK 500 20 ALA A 45 37.69 -98.97
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6455 RELATED DB: BMRB
REMARK 900 RELATED ID: 1YV8 RELATED DB: PDB
REMARK 900 RELATED ID: 1YVA RELATED DB: PDB
REMARK 900 RELATED ID: 2EYA RELATED DB: PDB
REMARK 900 RELATED ID: 2EYB RELATED DB: PDB
REMARK 900 RELATED ID: 2EYC RELATED DB: PDB
DBREF 2EYD A 1 46 UNP P01542 CRAM_CRAAB 1 46
SEQRES 1 A 46 THR THR CYS CYS PRO SER ILE VAL ALA ARG SER ASN PHE
SEQRES 2 A 46 ASN VAL CYS ARG LEU PRO GLY THR PRO GLU ALA LEU CYS
SEQRES 3 A 46 ALA THR TYR THR GLY CYS ILE ILE ILE PRO GLY ALA THR
SEQRES 4 A 46 CYS PRO GLY ASP TYR ALA ASN
HELIX 1 1 SER A 6 CYS A 16 1 11
HELIX 2 2 PRO A 22 GLY A 31 1 10
SHEET 1 A 2 THR A 2 CYS A 3 0
SHEET 2 A 2 ILE A 33 ILE A 34 -1 O ILE A 33 N CYS A 3
SSBOND 1 CYS A 3 CYS A 40 1555 1555 2.03
SSBOND 2 CYS A 4 CYS A 32 1555 1555 2.03
SSBOND 3 CYS A 16 CYS A 26 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 - r 9 2 Bytes