Header list of 1ees.pdb file
Complete list - b 16 2 Bytes
HEADER STRUCTURAL PROTEIN 02-FEB-00 1EES
TITLE SOLUTION STRUCTURE OF CDC42HS COMPLEXED WITH A PEPTIDE DERIVED FROM P-
TITLE 2 21 ACTIVATED KINASE, NMR, 20 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GTP-BINDING PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: AMINO ACIDS 1-178;
COMPND 5 SYNONYM: CDC42HS;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: P21-ACTIVATED KINASE;
COMPND 9 CHAIN: B;
COMPND 10 FRAGMENT: AMINO ACIDS 65-108;
COMPND 11 SYNONYM: MPAK-3;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 ORGAN: PLACENTA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET-15B;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 11 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 12 ORGANISM_TAXID: 10090;
SOURCE 13 CELL: FIBROBLAST;
SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 16 EXPRESSION_SYSTEM_PLASMID: PGEX-2T
KEYWDS PROTEIN-PROTEIN COMPLEX, STRUCTURAL PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR D.GIZACHEW,W.GUO,K.C.CHOHAN,M.J.SUTCLIFFE,R.E.OSWALD
REVDAT 5 16-FEB-22 1EES 1 REMARK
REVDAT 4 24-FEB-09 1EES 1 VERSN
REVDAT 3 01-APR-03 1EES 1 JRNL
REVDAT 2 12-APR-00 1EES 1 JRNL
REVDAT 1 29-MAR-00 1EES 0
JRNL AUTH D.GIZACHEW,W.GUO,K.K.CHOHAN,M.J.SUTCLIFFE,R.E.OSWALD
JRNL TITL STRUCTURE OF THE COMPLEX OF CDC42HS WITH A PEPTIDE DERIVED
JRNL TITL 2 FROM P-21 ACTIVATED KINASE.
JRNL REF BIOCHEMISTRY V. 39 3963 2000
JRNL REFN ISSN 0006-2960
JRNL PMID 10747784
JRNL DOI 10.1021/BI992646D
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH A.P.LOH,W.GUO,L.K.NICHOLSON,R.E.OSWALD
REMARK 1 TITL BACKBONE DYNAMICS OF INACTIVE, ACTIVE, AND EFFECTOR-BOUND
REMARK 1 TITL 2 CDC42HS FROM MEASUREMENTS OF (15)N RELAXATION PARAMETERS AT
REMARK 1 TITL 3 MULTIPLE FIELD STRENGTHS
REMARK 1 REF BIOCHEMISTRY V. 38 12547 1999
REMARK 1 REFN ISSN 0006-2960
REMARK 1 DOI 10.1021/BI9913707
REMARK 1 REFERENCE 2
REMARK 1 AUTH W.GUO,M.J.SUTCLIFFE,R.A.CERIONE,R.E.OSWALD
REMARK 1 TITL IDENTIFICATION OF THE BINDING SURFACE ON CDC42HS FOR
REMARK 1 TITL 2 P21-ACTIVATED KINASE
REMARK 1 REF BIOCHEMISTRY V. 37 14030 1998
REMARK 1 REFN ISSN 0006-2960
REMARK 1 DOI 10.1021/BI981352+
REMARK 1 REFERENCE 3
REMARK 1 AUTH J.L.FELTHAM,V.DOTSCH,S.RAZA,D.MANOR,R.A.CERIONE,
REMARK 1 AUTH 2 M.J.SUTCLIFFE,G.WAGNER,R.E.OSWALD
REMARK 1 TITL DEFINITION OF THE SWITCH SURFACE IN THE SOLUTION STRUCTURE
REMARK 1 TITL 2 OF CDC42HS
REMARK 1 REF BIOCHEMISTRY V. 36 8755 1997
REMARK 1 REFN ISSN 0006-2960
REMARK 1 DOI 10.1021/BI970694X
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 5.3,6.1, X-PLOR 3.851
REMARK 3 AUTHORS : VARIAN (VNMR), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: STRUCTURES ARE BASED ON 2412 DISTANCE
REMARK 3 AND DIHEDRAL RESTRAINTS
REMARK 4
REMARK 4 1EES COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-FEB-00.
REMARK 100 THE DEPOSITION ID IS D_1000010504.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 5.5
REMARK 210 IONIC STRENGTH : 64 MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.8 MM U-15N,13C CDC42HS, 0.8 MM
REMARK 210 PBD46; 25 MM NACL, 5 MM NA2PO4,
REMARK 210 5 MM MGCL2, 1 MM NAN3, PH 5.5;
REMARK 210 0.8 MM U-15N CDC42HS, 0.8 MM
REMARK 210 PBD46; 25 MM NACL, 5 MM NA2PO4,
REMARK 210 5 MM MGCL2, 1 MM NAN3, PH 5.5;
REMARK 210 0.8 MM CDC42HS, 0.8 MM U-15N,13C
REMARK 210 PBD46; 25 MM NACL, 5 MM NA2PO4,
REMARK 210 5 MM MGCL2, 1 MM NAN3, PH 5.5;
REMARK 210 0.8 MM CDC42HS, 0.8 MM U-15N
REMARK 210 PBD46; 25 MM NACL, 5 MM NA2PO4,
REMARK 210 5 MM MGCL2, 1 MM NAN3, PH 5.5;
REMARK 210 0.8 MM 70%-2H,U-15N,13C CDC42HS,
REMARK 210 0.8 MM PBD46; 25 MM NACL, 5 MM
REMARK 210 NA2PO4, 5 MM MGCL2, 1 MM NAN3,
REMARK 210 PH 5.5; 0.8 MM U-2H,15N CDC42HS,
REMARK 210 0.8 MM PBD46; 25 MM NACL, 5 MM
REMARK 210 NA2PO4, 5 MM MGCL2, 1 MM NAN3,
REMARK 210 PH 5.5; 0.8 MM U-15N,13C CDC42HS,
REMARK 210 0.8 MM PBD46; 25 MM NACL, 5 MM
REMARK 210 NA2PO4, 5 MM MGCL2, 1 MM NAN3,
REMARK 210 PH 5.5; 0.8 MM CDC42HS, 0.8 MM U-
REMARK 210 15N,13C PBD46; 25 MM NACL, 5 MM
REMARK 210 NA2PO4, 5 MM MGCL2, 1 MM NAN3,
REMARK 210 PH 5.5
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : FELIX 2.3, NMRPIPE 1.7, XEASY
REMARK 210 1.3.13, X-PLOR 3.851
REMARK 210 METHOD USED : DISTANCE GEOMETRY SIMULATED
REMARK 210 ANNEALING RAMACHANDRAN REFINEMENT
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH ACCEPTABLE
REMARK 210 COVALENT GEOMETRY,STRUCTURES
REMARK 210 WITH FAVORABLE NON-BOND ENERGY,
REMARK 210 STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS,STRUCTURES
REMARK 210 WITH THE LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 9
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE AND
REMARK 210 DOUBLE-RESONANCE NMR 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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 H GLY A 47 O SER B 9 1.38
REMARK 500 O ILE A 117 H LEU A 119 1.44
REMARK 500 O SER A 89 HD21 ASN A 92 1.47
REMARK 500 O LEU A 119 H ASP A 122 1.51
REMARK 500 O LYS A 27 O GLY B 27 2.19
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 THR A 25 -34.97 -178.99
REMARK 500 1 LYS A 27 -131.60 33.59
REMARK 500 1 PHE A 28 50.65 -145.33
REMARK 500 1 PRO A 29 -86.64 -103.53
REMARK 500 1 SER A 30 36.63 -166.98
REMARK 500 1 GLU A 31 -169.65 -78.61
REMARK 500 1 VAL A 36 -77.42 -45.99
REMARK 500 1 PHE A 37 154.52 -32.29
REMARK 500 1 ASP A 38 83.00 -168.03
REMARK 500 1 THR A 58 -168.80 -56.31
REMARK 500 1 ALA A 59 70.55 53.50
REMARK 500 1 GLN A 61 24.51 -156.45
REMARK 500 1 GLU A 62 -7.63 79.30
REMARK 500 1 SER A 71 27.08 41.98
REMARK 500 1 TYR A 72 120.60 -179.84
REMARK 500 1 ASP A 76 -53.51 -24.63
REMARK 500 1 SER A 88 42.90 39.46
REMARK 500 1 ILE A 101 125.16 60.55
REMARK 500 1 THR A 102 -78.22 -40.84
REMARK 500 1 HIS A 104 14.08 82.52
REMARK 500 1 CYS A 105 -60.81 -170.65
REMARK 500 1 THR A 108 150.48 -45.65
REMARK 500 1 GLN A 116 57.38 34.41
REMARK 500 1 ASP A 118 61.60 -51.88
REMARK 500 1 LEU A 119 -39.95 152.79
REMARK 500 1 ASN A 132 -53.61 -126.90
REMARK 500 1 ALA A 151 -150.36 -86.24
REMARK 500 1 LYS A 153 142.31 -172.42
REMARK 500 1 VAL A 155 -168.40 -116.19
REMARK 500 1 ALA A 159 -49.67 -24.37
REMARK 500 1 GLN A 162 77.05 79.26
REMARK 500 1 LYS A 163 47.99 -78.35
REMARK 500 1 ARG B 5 -149.76 -69.62
REMARK 500 1 GLU B 7 -169.70 -49.56
REMARK 500 1 LEU B 10 98.02 -167.25
REMARK 500 1 SER B 12 -169.46 -53.13
REMARK 500 1 PHE B 14 -165.04 -54.92
REMARK 500 1 GLU B 15 -175.81 -43.59
REMARK 500 1 PHE B 22 134.02 175.86
REMARK 500 1 ASP B 23 131.37 -39.00
REMARK 500 1 ILE B 32 70.45 -150.81
REMARK 500 1 TRP B 36 36.53 70.18
REMARK 500 1 ALA B 37 -27.27 -168.57
REMARK 500 1 GLN B 41 47.53 -169.68
REMARK 500 1 THR B 42 -168.72 -104.91
REMARK 500 2 THR A 3 99.77 -43.20
REMARK 500 2 ALA A 13 -77.98 -160.32
REMARK 500 2 THR A 25 -76.25 -88.07
REMARK 500 2 ASN A 26 -33.66 -156.17
REMARK 500 2 LYS A 27 -130.34 175.03
REMARK 500
REMARK 500 THIS ENTRY HAS 898 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 66 0.20 SIDE CHAIN
REMARK 500 1 ARG A 68 0.14 SIDE CHAIN
REMARK 500 1 ARG A 120 0.20 SIDE CHAIN
REMARK 500 1 ARG A 147 0.24 SIDE CHAIN
REMARK 500 1 ARG B 5 0.21 SIDE CHAIN
REMARK 500 1 ARG B 38 0.20 SIDE CHAIN
REMARK 500 2 ARG A 66 0.21 SIDE CHAIN
REMARK 500 2 ARG A 68 0.32 SIDE CHAIN
REMARK 500 2 ARG A 120 0.28 SIDE CHAIN
REMARK 500 2 ARG A 147 0.23 SIDE CHAIN
REMARK 500 2 ARG B 5 0.27 SIDE CHAIN
REMARK 500 2 ARG B 38 0.32 SIDE CHAIN
REMARK 500 3 ARG A 66 0.20 SIDE CHAIN
REMARK 500 3 ARG A 68 0.21 SIDE CHAIN
REMARK 500 3 ARG A 120 0.16 SIDE CHAIN
REMARK 500 3 ARG A 147 0.31 SIDE CHAIN
REMARK 500 3 ARG B 5 0.31 SIDE CHAIN
REMARK 500 3 ARG B 38 0.17 SIDE CHAIN
REMARK 500 4 ARG A 66 0.28 SIDE CHAIN
REMARK 500 4 ARG A 68 0.32 SIDE CHAIN
REMARK 500 4 ARG A 120 0.28 SIDE CHAIN
REMARK 500 4 ARG A 147 0.18 SIDE CHAIN
REMARK 500 4 ARG B 5 0.28 SIDE CHAIN
REMARK 500 4 ARG B 38 0.31 SIDE CHAIN
REMARK 500 5 ARG A 66 0.25 SIDE CHAIN
REMARK 500 5 ARG A 68 0.18 SIDE CHAIN
REMARK 500 5 ARG A 120 0.30 SIDE CHAIN
REMARK 500 5 ARG A 147 0.32 SIDE CHAIN
REMARK 500 5 ARG B 5 0.29 SIDE CHAIN
REMARK 500 5 ARG B 38 0.29 SIDE CHAIN
REMARK 500 6 ARG A 66 0.32 SIDE CHAIN
REMARK 500 6 ARG A 68 0.27 SIDE CHAIN
REMARK 500 6 ARG A 120 0.30 SIDE CHAIN
REMARK 500 6 ARG A 147 0.25 SIDE CHAIN
REMARK 500 6 ARG B 5 0.14 SIDE CHAIN
REMARK 500 6 ARG B 38 0.32 SIDE CHAIN
REMARK 500 7 ARG A 66 0.28 SIDE CHAIN
REMARK 500 7 ARG A 68 0.29 SIDE CHAIN
REMARK 500 7 ARG A 120 0.12 SIDE CHAIN
REMARK 500 7 ARG A 147 0.26 SIDE CHAIN
REMARK 500 7 ARG B 5 0.30 SIDE CHAIN
REMARK 500 7 ARG B 38 0.12 SIDE CHAIN
REMARK 500 8 ARG A 66 0.13 SIDE CHAIN
REMARK 500 8 ARG A 68 0.31 SIDE CHAIN
REMARK 500 8 ARG A 120 0.27 SIDE CHAIN
REMARK 500 8 ARG A 147 0.23 SIDE CHAIN
REMARK 500 8 ARG B 5 0.27 SIDE CHAIN
REMARK 500 8 ARG B 38 0.32 SIDE CHAIN
REMARK 500 9 ARG A 66 0.25 SIDE CHAIN
REMARK 500 9 ARG A 68 0.25 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 118 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1AJE RELATED DB: PDB
REMARK 900 CDC42 FROM HUMAN, NMR, 20 STRUCTURES
REMARK 900 RELATED ID: 1CF4 RELATED DB: PDB
REMARK 900 CDC42 FROM HUMAN COMPLEXED WITH ACK, NMR, 20 STRUCTURES
REMARK 900 RELATED ID: 1CEE RELATED DB: PDB
REMARK 900 CDC42 FROM HUMAN COMPLEXED WITH WASP, NMR, 20 STRUCTURES
DBREF 1EES A 1 178 UNP P60953 CDC42_HUMAN 1 178
DBREF 1EES B 1 46 UNP Q61036 PAK3_MOUSE 63 108
SEQADV 1EES GLY B 1 UNP Q61036 LYS 63 SEE REMARK 999
SEQADV 1EES SER B 2 UNP Q61036 GLU 64 SEE REMARK 999
SEQRES 1 A 178 MET GLN THR ILE LYS CYS VAL VAL VAL GLY ASP GLY ALA
SEQRES 2 A 178 VAL GLY LYS THR CYS LEU LEU ILE SER TYR THR THR ASN
SEQRES 3 A 178 LYS PHE PRO SER GLU TYR VAL PRO THR VAL PHE ASP ASN
SEQRES 4 A 178 TYR ALA VAL THR VAL MET ILE GLY GLY GLU PRO TYR THR
SEQRES 5 A 178 LEU GLY LEU PHE ASP THR ALA GLY GLN GLU ASP TYR ASP
SEQRES 6 A 178 ARG LEU ARG PRO LEU SER TYR PRO GLN THR ASP VAL PHE
SEQRES 7 A 178 LEU VAL CYS PHE SER VAL VAL SER PRO SER SER PHE GLU
SEQRES 8 A 178 ASN VAL LYS GLU LYS TRP VAL PRO GLU ILE THR HIS HIS
SEQRES 9 A 178 CYS PRO LYS THR PRO PHE LEU LEU VAL GLY THR GLN ILE
SEQRES 10 A 178 ASP LEU ARG ASP ASP PRO SER THR ILE GLU LYS LEU ALA
SEQRES 11 A 178 LYS ASN LYS GLN LYS PRO ILE THR PRO GLU THR ALA GLU
SEQRES 12 A 178 LYS LEU ALA ARG ASP LEU LYS ALA VAL LYS TYR VAL GLU
SEQRES 13 A 178 CYS SER ALA LEU THR GLN LYS GLY LEU LYS ASN VAL PHE
SEQRES 14 A 178 ASP GLU ALA ILE LEU ALA ALA LEU GLU
SEQRES 1 B 46 GLY SER LYS GLU ARG PRO GLU ILE SER LEU PRO SER ASP
SEQRES 2 B 46 PHE GLU HIS THR ILE HIS VAL GLY PHE ASP ALA VAL THR
SEQRES 3 B 46 GLY GLU PHE THR GLY ILE PRO GLU GLN TRP ALA ARG LEU
SEQRES 4 B 46 LEU GLN THR SER ASN ILE THR
HELIX 1 1 LYS A 16 TYR A 23 1 8
HELIX 2 2 SER A 89 GLU A 95 1 7
HELIX 3 3 GLN A 116 ASP A 121 1 6
HELIX 4 4 THR A 125 LYS A 131 1 7
HELIX 5 5 THR A 138 LYS A 150 1 13
HELIX 6 6 LEU A 165 GLU A 178 1 14
HELIX 7 7 ALA B 37 THR B 42 5 6
SHEET 1 A 3 CYS A 6 VAL A 8 0
SHEET 2 A 3 VAL A 77 LEU A 79 1 O VAL A 77 N VAL A 7
SHEET 3 A 3 PHE A 110 LEU A 111 1 N LEU A 111 O PHE A 78
SHEET 1 B 2 THR A 43 ILE A 46 0
SHEET 2 B 2 GLU A 49 THR A 52 -1 N GLU A 49 O ILE A 46
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