Header list of 1eww.pdb file
Complete list - b 16 2 Bytes
HEADER ANTIFREEZE PROTEIN 27-APR-00 1EWW
TITLE SOLUTION STRUCTURE OF SPRUCE BUDWORM ANTIFREEZE PROTEIN AT 30 DEGREES
TITLE 2 CELSIUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ANTIFREEZE PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CHORISTONEURA FUMIFERANA;
SOURCE 3 ORGANISM_COMMON: SPRUCE BUDWORM;
SOURCE 4 ORGANISM_TAXID: 7141;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET21
KEYWDS BETA-HELIX, ANTIFREEZE PROTEIN, ICE, INSECT
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR S.P.GRAETHER,M.J.KUIPER,S.M.GAGNE,V.K.WALKER,Z.JIA,B.D.SYKES,
AUTHOR 2 P.L.DAVIES
REVDAT 3 16-FEB-22 1EWW 1 REMARK
REVDAT 2 24-FEB-09 1EWW 1 VERSN
REVDAT 1 27-JUL-00 1EWW 0
JRNL AUTH S.P.GRAETHER,M.J.KUIPER,S.M.GAGNE,V.K.WALKER,Z.JIA,
JRNL AUTH 2 B.D.SYKES,P.L.DAVIES
JRNL TITL BETA-HELIX STRUCTURE AND ICE-BINDING PROPERTIES OF A
JRNL TITL 2 HYPERACTIVE ANTIFREEZE PROTEIN FROM AN INSECT.
JRNL REF NATURE V. 406 325 2000
JRNL REFN ISSN 0028-0836
JRNL PMID 10917537
JRNL DOI 10.1038/35018610
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.G.TYSHENKO,D.DOUCET,P.L.DAVIES,V.K.WALKER
REMARK 1 TITL THE ANTIFREEZE POTENTIAL OF THE SPRUCE BUDWORM THERMAL
REMARK 1 TITL 2 HYSTERESIS PROTEIN.
REMARK 1 REF NAT.BIOTECHNOL. V. 15 887 1997
REMARK 1 REFN ISSN 1087-0156
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851, X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER (X-PLOR), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: 1014 NOE-DERIVED DISTANCE CONSTRAINTS,
REMARK 3 88 DIHEDRAL ANGLE RESTRAINTS,
REMARK 3 59 CARBON CHEMICAL SHIFT RESTRAINTS
REMARK 4
REMARK 4 1EWW COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-MAY-00.
REMARK 100 THE DEPOSITION ID IS D_1000010977.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 5.5
REMARK 210 IONIC STRENGTH : 0
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1: U-15N/U-13C SPRUCE BUDWORM
REMARK 210 ANTIFREEZE PROTEIN, 18 MG/ML, 2:
REMARK 210 U-15N SPRUCE BUDWORM ANTIFREEZE
REMARK 210 PROTEIN, 18 MG/ML
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C/15N-SEPARATED_NOESY;
REMARK 210 3D_15N-SEPARATED_NOESY; HNHA;
REMARK 210 HNCACB; CBCA(CO)NNH; HCCH-TOCSY;
REMARK 210 2D NOESY; 3D_15N-SEPARATED_TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA; UNITY
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 1.7, PIPP 4.2
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
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 : 10
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY.
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 HG SER A 52 O ILE A 68 1.41
REMARK 500 O SER A 77 H CYS A 80 1.48
REMARK 500 HG SER A 12 OG SER A 15 1.51
REMARK 500 O ASP A 28 H GLY A 44 1.54
REMARK 500 OG1 THR A 66 H CYS A 67 1.57
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 SER A 3 78.75 49.14
REMARK 500 1 CYS A 4 -75.06 68.65
REMARK 500 1 THR A 5 13.59 -145.46
REMARK 500 1 ASN A 8 -32.10 -177.33
REMARK 500 1 SER A 9 -151.29 -108.73
REMARK 500 1 LEU A 11 36.22 -94.15
REMARK 500 1 ALA A 13 23.48 46.56
REMARK 500 1 ASN A 14 12.12 -159.91
REMARK 500 1 SER A 15 -144.30 -98.65
REMARK 500 1 CYS A 17 64.47 -65.55
REMARK 500 1 LYS A 19 133.01 -171.33
REMARK 500 1 SER A 20 -163.70 -58.71
REMARK 500 1 LEU A 22 -83.58 -95.29
REMARK 500 1 THR A 23 24.55 -165.03
REMARK 500 1 ASN A 24 76.45 -157.49
REMARK 500 1 LYS A 29 71.30 40.29
REMARK 500 1 CYS A 37 -79.79 -113.87
REMARK 500 1 THR A 38 -68.39 68.25
REMARK 500 1 ASP A 43 98.46 177.21
REMARK 500 1 THR A 48 -164.88 -115.89
REMARK 500 1 THR A 49 94.04 -49.63
REMARK 500 1 THR A 51 40.13 -87.86
REMARK 500 1 SER A 55 -162.62 -105.73
REMARK 500 1 THR A 66 -93.80 54.64
REMARK 500 1 CYS A 67 -167.50 70.30
REMARK 500 1 ILE A 69 167.99 -42.47
REMARK 500 1 THR A 70 -139.67 -137.61
REMARK 500 1 ALA A 75 173.94 60.78
REMARK 500 1 SER A 88 94.62 -176.02
REMARK 500 1 ALA A 89 172.57 50.89
REMARK 500 2 SER A 3 -69.11 64.45
REMARK 500 2 CYS A 4 -75.42 -133.76
REMARK 500 2 ASN A 8 -17.52 168.49
REMARK 500 2 SER A 9 -160.44 -108.02
REMARK 500 2 SER A 12 104.82 53.34
REMARK 500 2 SER A 15 -162.98 -101.12
REMARK 500 2 GLU A 18 53.99 -105.32
REMARK 500 2 THR A 21 139.04 60.21
REMARK 500 2 LEU A 22 -83.61 -95.52
REMARK 500 2 THR A 23 38.19 -171.39
REMARK 500 2 ASN A 24 67.92 -157.32
REMARK 500 2 TYR A 33 -152.60 -114.25
REMARK 500 2 CYS A 37 102.65 -174.33
REMARK 500 2 ASP A 43 116.13 -171.74
REMARK 500 2 THR A 48 -162.31 -106.01
REMARK 500 2 THR A 49 91.48 -64.16
REMARK 500 2 THR A 51 72.17 -108.68
REMARK 500 2 THR A 66 109.81 46.08
REMARK 500 2 ILE A 68 -179.28 -55.36
REMARK 500 2 THR A 70 -122.16 -98.33
REMARK 500
REMARK 500 THIS ENTRY HAS 456 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 1 ARG A 41 0.26 SIDE CHAIN
REMARK 500 1 ARG A 56 0.31 SIDE CHAIN
REMARK 500 2 ARG A 41 0.20 SIDE CHAIN
REMARK 500 2 ARG A 56 0.21 SIDE CHAIN
REMARK 500 3 ARG A 41 0.21 SIDE CHAIN
REMARK 500 3 ARG A 56 0.22 SIDE CHAIN
REMARK 500 4 ARG A 56 0.28 SIDE CHAIN
REMARK 500 5 ARG A 41 0.12 SIDE CHAIN
REMARK 500 5 ARG A 56 0.23 SIDE CHAIN
REMARK 500 6 ARG A 41 0.28 SIDE CHAIN
REMARK 500 7 ARG A 41 0.31 SIDE CHAIN
REMARK 500 7 ARG A 56 0.31 SIDE CHAIN
REMARK 500 8 ARG A 41 0.31 SIDE CHAIN
REMARK 500 8 ARG A 56 0.21 SIDE CHAIN
REMARK 500 9 ARG A 41 0.32 SIDE CHAIN
REMARK 500 9 ARG A 56 0.25 SIDE CHAIN
REMARK 500 10 ARG A 41 0.19 SIDE CHAIN
REMARK 500 10 ARG A 56 0.32 SIDE CHAIN
REMARK 500 11 ARG A 41 0.11 SIDE CHAIN
REMARK 500 11 ARG A 56 0.23 SIDE CHAIN
REMARK 500 12 ARG A 41 0.17 SIDE CHAIN
REMARK 500 12 ARG A 56 0.31 SIDE CHAIN
REMARK 500 13 ARG A 41 0.32 SIDE CHAIN
REMARK 500 13 ARG A 56 0.25 SIDE CHAIN
REMARK 500 14 ARG A 41 0.30 SIDE CHAIN
REMARK 500 14 ARG A 56 0.24 SIDE CHAIN
REMARK 500 15 ARG A 41 0.26 SIDE CHAIN
REMARK 500 15 ARG A 56 0.30 SIDE CHAIN
REMARK 500 16 ARG A 41 0.23 SIDE CHAIN
REMARK 500 16 ARG A 56 0.31 SIDE CHAIN
REMARK 500 17 ARG A 41 0.29 SIDE CHAIN
REMARK 500 17 ARG A 56 0.30 SIDE CHAIN
REMARK 500 18 ARG A 41 0.31 SIDE CHAIN
REMARK 500 18 ARG A 56 0.30 SIDE CHAIN
REMARK 500 19 ARG A 41 0.25 SIDE CHAIN
REMARK 500 19 ARG A 56 0.32 SIDE CHAIN
REMARK 500 20 ARG A 41 0.32 SIDE CHAIN
REMARK 500 20 ARG A 56 0.27 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1EWW A 1 90 UNP Q9GTP0 Q9GTP0_CHOFU 19 108
SEQRES 1 A 90 ASP GLY SER CYS THR ASN THR ASN SER GLN LEU SER ALA
SEQRES 2 A 90 ASN SER LYS CYS GLU LYS SER THR LEU THR ASN CYS TYR
SEQRES 3 A 90 VAL ASP LYS SER GLU VAL TYR GLY THR THR CYS THR GLY
SEQRES 4 A 90 SER ARG PHE ASP GLY VAL THR ILE THR THR SER THR SER
SEQRES 5 A 90 THR GLY SER ARG ILE SER GLY PRO GLY CYS LYS ILE SER
SEQRES 6 A 90 THR CYS ILE ILE THR GLY GLY VAL PRO ALA PRO SER ALA
SEQRES 7 A 90 ALA CYS LYS ILE SER GLY CYS THR PHE SER ALA ASN
SHEET 1 A 3 ARG A 41 ASP A 43 0
SHEET 2 A 3 ARG A 56 SER A 58 1 N ILE A 57 O ARG A 41
SHEET 3 A 3 THR A 86 PHE A 87 -1 N THR A 86 O SER A 58
SSBOND 1 CYS A 4 CYS A 17 1555 1555 2.02
SSBOND 2 CYS A 25 CYS A 37 1555 1555 2.02
SSBOND 3 CYS A 62 CYS A 85 1555 1555 2.02
SSBOND 4 CYS A 67 CYS A 80 1555 1555 2.02
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 - b 16 2 Bytes