Header list of 2bl5.pdb file
Complete list - r 25 2 Bytes
HEADER RNA BINDING 01-MAR-05 2BL5
TITLE SOLUTION STRUCTURE OF THE KH-QUA2 REGION OF THE XENOPUS
TITLE 2 STAR-GSG QUAKING PROTEIN.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MGC83862 PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: KH-QUA2 REGION, RESIDUES 82-215;
COMPND 5 SYNONYM: QUAKING PROTEIN;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: XENOPUS LAEVIS;
SOURCE 3 ORGANISM_COMMON: AFRICAN CLAWED FROG;
SOURCE 4 ORGANISM_TAXID: 8355;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 OTHER_DETAILS: GENE EXPRESSION WAS INDUCED BY THE ADDITION
SOURCE 9 OF IPTG TO A FINAL CONCENTRATION OF 0.5 MM AND THE CELLS
SOURCE 10 WERE INCUBATED FOR 3 H AT 37 DEGREES C. THE CELLS WERE
SOURCE 11 HARVESTED BY CENTRIFUGATION AT 6000 RPM FOR 20 MIN AND
SOURCE 12 STORED AT -20 DEGREES C UNTIL REQUIRED. THE CELLS WERE
SOURCE 13 RESUSPENDED IN TE BUFFER (CONTAINING 1 MM EDTA, 25 MM
SOURCE 14 TRIS) AT PH 8.0 AND THEN BROKEN IN A FRENCH PRESS. THE
SOURCE 15 CELL DEBRIS WAS REMOVED BY CENTRIFUGATION AT 40000 G FOR
SOURCE 16 30 MIN, FOLLOWING WHICH THE PELLET WAS RESUSPENDED IN 50
SOURCE 17 ML OF 20 MM SODIUM PHOSPHATE CONTAINING 10 PER CENT
SOURCE 18 TRITON X-100 AND 100 MM SODIUM CHLORIDE. THE CRUDE
SOURCE 19 EXTRACT WAS ADDED TO 6 ML OF NI-NTA RESIN (QIAGEN), MIXED
SOURCE 20 FOR 2 H AT 4 DEGREES C, SPUN DOWN AT 5000 G FOR 10 MIN
SOURCE 21 AND THE SUPERNATANT DISCARDED. THE BEADS WERE LOADED ON
SOURCE 22 TO A COLUMN, WASHED WITH 2 VOLUMES OF RESUSPENSION BUFFER
SOURCE 23 AND THEN 2 VOLUMES OF ELUTION BUFFER (CONTAINING 500 MM
SOURCE 24 IMIDAZOLE, 50 MM SODIUM CHLORIDE AND 20 MM SODIUM
SOURCE 25 PHOSPHATE). THE ELUATE WAS DESALTED ON A SEPHADEX G-25
SOURCE 26 PD-10 COLUMN (PHARMACIA) AND THEN CONCENTRATED TO 1 MM
SOURCE 27 USING A BIOMAX 10K MEMBRANE TO A FINAL VOLUME OF 500
SOURCE 28 MICROLITRES. THE PROTEIN PRODUCT CORRESPONDS TO RESIDUES
SOURCE 29 81 TO 214 OF FULL LENGTH PXQUA, WITH A C-TERMINAL HIS6
SOURCE 30 EXTENSION
KEYWDS STAR PROTEINS, GSG PROTEINS, QUAKING, RNA BINDING
EXPDTA SOLUTION NMR
NUMMDL 17
AUTHOR M.L.MAGUIRE,G.GULER-GANE,D.NIETLISPACH,A.R.C.RAINE,A.M.ZORN,
AUTHOR 2 N.STANDART,R.W.BROADHURST
REVDAT 2 24-FEB-09 2BL5 1 VERSN
REVDAT 1 14-APR-05 2BL5 0
JRNL AUTH M.L.MAGUIRE,G.GULER-GANE,D.NIETLISPACH,A.R.C.RAINE,
JRNL AUTH 2 A.M.ZORN,N.STANDART,R.W.BROADHURST
JRNL TITL SOLUTION STRUCTURE AND BACKBONE DYNAMICS OF THE
JRNL TITL 2 KH-QUA2 REGION OF THE XENOPUS STAR/GSG QUAKING
JRNL TITL 3 PROTEIN
JRNL REF J.MOL.BIOL. V. 348 265 2005
JRNL REFN ISSN 0022-2836
JRNL PMID 15811367
JRNL DOI 10.1016/J.JMB.2005.02.058
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : ARIA 1.2
REMARK 3 AUTHORS : LINGE,HABECK,REIPING,NILGES
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN
REMARK 3 THE JRNL CITATION ABOVE.
REMARK 4
REMARK 4 2BL5 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 01-MAR-05.
REMARK 100 THE PDBE ID CODE IS EBI-22993.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298.0
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 50MM
REMARK 210 PRESSURE : 1.0
REMARK 210 SAMPLE CONTENTS : 90% WATER/10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 15N-TOCSY-HSQC; 15N-NOESY-
REMARK 210 HSQC; HNCACB; CBCACONH;
REMARK 210 HNCO; HCCH-TOCSY; 13C-
REMARK 210 NOESY-HSQCHCCH-TOCSY; 13C-
REMARK 210 NOESY-HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 600
REMARK 210 SPECTROMETER MODEL : DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : ANSIG
REMARK 210 METHOD USED : ARIA
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 17
REMARK 210 CONFORMERS, SELECTION CRITERIA : NO DISTANCE RESTRAINT
REMARK 210 VIOLATIONS GREATER THAN
REMARK 210 0.5 ANGSTROMS AND NO
REMARK 210 DIHEDRAL ANGLE RESTRAINT
REMARK 210 VIOLATIONS GREATER THAN 5
REMARK 210 DEGREES
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: STRUCTURE WAS DETERMINED USING A 13C,15N-LABELLED
REMARK 210 PROTEIN SAMPLE
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 HIS A 136
REMARK 465 HIS A 137
REMARK 465 HIS A 138
REMARK 465 HIS A 139
REMARK 465 HIS A 140
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 HIS A 135 CA C O CB CG ND1 CD2 CE1 NE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
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 HZ1 LYS A 11 - OD1 ASP A 70 1.57
REMARK 500 HD13 LEU A 23 - HG23 VAL A 43 1.45
REMARK 500 O LEU A 33 - HG1 THR A 37 1.58
REMARK 500 HB3 GLU A 34 - HA LYS A 40 1.45
REMARK 500 HA LYS A 46 - HD13 LEU A 67 1.58
REMARK 500 HB3 MET A 49 - HD3 LYS A 54 1.38
REMARK 500 HA PRO A 62 - HB3 GLU A 65 1.51
REMARK 500 HE3 TRP A 64 - HD21 LEU A 67 1.36
REMARK 500 HD11 ILE A 75 - HD13 LEU A 88 1.54
REMARK 500 HG2 GLU A 93 - HD3 LYS A 96 1.50
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 2 PHE A 18 CE2 PHE A 18 CZ 0.139
REMARK 500 7 PHE A 18 CE2 PHE A 18 CZ 0.116
REMARK 500 9 PHE A 18 CE1 PHE A 18 CZ -0.115
REMARK 500 9 PHE A 18 CE2 PHE A 18 CZ 0.145
REMARK 500 12 PHE A 18 CE1 PHE A 18 CZ -0.148
REMARK 500 12 PHE A 18 CE2 PHE A 18 CZ 0.170
REMARK 500 14 PHE A 18 CE2 PHE A 18 CZ 0.117
REMARK 500 15 PHE A 18 CE2 PHE A 18 CZ 0.132
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 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 PRO A 9 97.60 -66.15
REMARK 500 1 ARG A 50 24.69 -57.84
REMARK 500 1 PRO A 62 -32.50 -28.16
REMARK 500 1 ASP A 79 165.24 172.20
REMARK 500 1 PRO A 101 14.79 -67.61
REMARK 500 1 ASP A 107 -55.21 69.49
REMARK 500 1 ILE A 119 -72.50 -71.18
REMARK 500 1 ARG A 125 -66.91 66.99
REMARK 500 1 LYS A 130 86.35 -159.44
REMARK 500 1 ALA A 133 61.19 -102.55
REMARK 500 2 TYR A 13 78.30 -119.74
REMARK 500 2 ARG A 50 26.54 -65.36
REMARK 500 2 PRO A 62 -33.88 -22.34
REMARK 500 2 ASP A 79 142.52 -179.16
REMARK 500 2 ALA A 102 -78.11 77.69
REMARK 500 2 ALA A 118 10.31 179.91
REMARK 500 2 ILE A 119 -72.54 61.64
REMARK 500 2 ARG A 125 -53.61 71.26
REMARK 500 3 ARG A 50 28.09 -63.74
REMARK 500 3 PRO A 62 -32.94 -26.43
REMARK 500 3 ASP A 79 131.46 166.13
REMARK 500 3 LEU A 99 4.71 -67.35
REMARK 500 3 PRO A 101 7.24 -62.89
REMARK 500 3 ALA A 102 -37.16 81.53
REMARK 500 3 ALA A 118 39.81 -149.50
REMARK 500 3 ILE A 119 -99.60 33.22
REMARK 500 3 TYR A 124 -111.84 27.52
REMARK 500 3 ARG A 125 -57.97 64.68
REMARK 500 3 ALA A 133 -45.97 75.09
REMARK 500 4 ARG A 50 29.38 -67.03
REMARK 500 4 PRO A 62 -33.18 -27.44
REMARK 500 4 ASP A 79 161.03 172.95
REMARK 500 4 LEU A 99 5.77 -67.89
REMARK 500 4 ALA A 102 -162.86 64.50
REMARK 500 4 ASP A 107 -44.32 77.50
REMARK 500 4 LEU A 114 -64.89 -94.57
REMARK 500 4 ALA A 118 78.56 68.29
REMARK 500 4 TYR A 124 -82.92 -84.84
REMARK 500 4 ARG A 125 -30.59 67.74
REMARK 500 5 ARG A 50 27.56 -79.99
REMARK 500 5 PRO A 62 -34.51 -27.40
REMARK 500 5 ASP A 79 150.73 168.25
REMARK 500 5 ALA A 102 -58.07 77.17
REMARK 500 5 GLU A 106 -72.44 -141.51
REMARK 500 5 ILE A 119 -61.56 64.38
REMARK 500 5 PRO A 132 37.10 -74.18
REMARK 500 6 ARG A 50 25.50 -58.17
REMARK 500 6 PRO A 62 -35.73 -26.51
REMARK 500 6 ASP A 79 153.12 178.40
REMARK 500 6 PRO A 101 7.44 -68.94
REMARK 500 6 ASP A 107 -32.64 72.65
REMARK 500 6 LEU A 114 -64.36 -90.69
REMARK 500 6 ILE A 119 -149.22 38.72
REMARK 500 6 ASN A 128 -44.64 175.13
REMARK 500 7 ARG A 50 24.92 -60.63
REMARK 500 7 PRO A 62 -35.80 -27.04
REMARK 500 7 ASP A 79 131.97 169.40
REMARK 500 7 PRO A 101 3.33 -61.13
REMARK 500 7 ASP A 107 -93.37 69.34
REMARK 500 7 LEU A 114 -63.93 -94.30
REMARK 500 7 LYS A 130 112.07 69.72
REMARK 500 8 PRO A 9 90.00 -69.72
REMARK 500 8 PRO A 62 -39.36 -23.33
REMARK 500 8 ASP A 79 -176.29 -174.69
REMARK 500 8 GLN A 81 -53.53 90.51
REMARK 500 8 LEU A 99 16.03 -67.17
REMARK 500 8 PRO A 101 1.75 -67.95
REMARK 500 8 ALA A 102 -1.36 74.90
REMARK 500 8 GLU A 106 164.83 55.45
REMARK 500 8 ALA A 133 17.11 -154.32
REMARK 500 9 ARG A 50 25.12 -57.92
REMARK 500 9 PRO A 62 -34.40 -24.95
REMARK 500 9 ASP A 79 -172.91 -170.11
REMARK 500 9 ALA A 80 -72.27 -66.33
REMARK 500 9 GLN A 81 -79.27 -178.96
REMARK 500 9 LEU A 99 14.09 -67.52
REMARK 500 9 ALA A 102 -174.19 65.68
REMARK 500 9 ALA A 103 102.19 63.57
REMARK 500 9 ASP A 107 -57.58 -143.60
REMARK 500 9 LEU A 114 -65.27 -95.71
REMARK 500 9 ILE A 119 -71.60 -46.06
REMARK 500 9 LYS A 130 -105.08 56.58
REMARK 500 9 SER A 131 93.27 -164.65
REMARK 500 9 ALA A 133 -31.84 -173.25
REMARK 500 10 ARG A 50 29.71 -75.09
REMARK 500 10 PRO A 62 -32.44 -27.48
REMARK 500 10 GLN A 81 -74.13 179.27
REMARK 500 10 LEU A 99 28.07 -75.38
REMARK 500 10 ALA A 102 -165.32 70.13
REMARK 500 10 ASP A 107 -131.40 -129.65
REMARK 500 10 LEU A 114 -65.85 -95.19
REMARK 500 10 THR A 123 -55.31 -133.58
REMARK 500 11 ARG A 50 25.26 -62.88
REMARK 500 11 PRO A 62 -32.75 -27.66
REMARK 500 11 GLN A 81 -77.93 172.06
REMARK 500 11 LEU A 99 3.20 -66.84
REMARK 500 11 PRO A 101 2.08 -66.23
REMARK 500 11 LEU A 114 -65.92 -95.32
REMARK 500 11 ALA A 118 105.45 -179.22
REMARK 500 12 PRO A 9 95.17 -68.50
REMARK 500 12 ARG A 50 26.31 -63.79
REMARK 500 12 PRO A 62 -35.70 -27.12
REMARK 500 12 ASP A 79 -172.98 -174.48
REMARK 500 12 ALA A 80 -75.95 -58.96
REMARK 500 12 GLN A 81 -49.42 171.14
REMARK 500 12 ALA A 102 -33.90 75.38
REMARK 500 12 GLU A 106 105.98 -48.37
REMARK 500 12 ASP A 107 -27.73 68.40
REMARK 500 13 ARG A 50 26.01 -64.72
REMARK 500 13 PRO A 62 -34.87 -26.61
REMARK 500 13 ASP A 79 137.25 169.49
REMARK 500 13 LEU A 99 2.79 -66.57
REMARK 500 13 ALA A 102 -144.34 58.44
REMARK 500 13 ALA A 103 -111.42 62.53
REMARK 500 13 ASP A 107 -75.65 -58.23
REMARK 500 13 ILE A 119 -52.55 69.95
REMARK 500 13 LYS A 130 -170.69 65.21
REMARK 500 14 PRO A 9 94.82 -69.40
REMARK 500 14 ARG A 50 27.70 -56.87
REMARK 500 14 PRO A 62 -36.12 -28.45
REMARK 500 14 GLN A 81 -74.24 169.78
REMARK 500 14 LEU A 99 26.34 -73.71
REMARK 500 14 LEU A 114 -65.11 -92.52
REMARK 500 14 ALA A 118 18.79 -175.93
REMARK 500 14 ILE A 119 -160.94 55.53
REMARK 500 14 ARG A 125 -39.76 75.54
REMARK 500 14 PRO A 132 40.58 -82.85
REMARK 500 15 PRO A 62 -38.47 -23.55
REMARK 500 15 ASP A 79 164.58 172.37
REMARK 500 15 LEU A 99 30.99 -72.90
REMARK 500 15 ALA A 102 -167.86 66.98
REMARK 500 15 ALA A 103 -106.46 54.11
REMARK 500 15 ALA A 118 -60.54 -137.21
REMARK 500 15 ILE A 119 -59.69 69.41
REMARK 500 15 ASP A 126 132.72 178.79
REMARK 500 15 ALA A 127 -20.45 69.63
REMARK 500 15 LEU A 129 28.00 -71.58
REMARK 500 15 PRO A 132 34.44 -72.80
REMARK 500 16 PRO A 62 -34.46 -24.17
REMARK 500 16 PRO A 101 23.90 -71.00
REMARK 500 16 ALA A 102 102.45 -52.93
REMARK 500 16 ALA A 118 -25.51 176.05
REMARK 500 16 ILE A 119 -50.68 72.18
REMARK 500 16 LEU A 120 111.30 55.14
REMARK 500 16 PRO A 132 22.35 -69.92
REMARK 500 16 ALA A 133 26.06 -144.42
REMARK 500 17 ARG A 50 26.21 -60.61
REMARK 500 17 PRO A 62 -31.93 -27.47
REMARK 500 17 ASP A 79 155.60 165.43
REMARK 500 17 ALA A 102 -162.27 62.81
REMARK 500 17 LEU A 114 -64.55 -94.62
REMARK 500 17 ALA A 118 83.61 73.29
REMARK 500 17 ILE A 119 -167.50 -77.91
REMARK 500 17 ALA A 133 -71.87 -124.05
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 14 PHE A 16 0.09 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2BL5 A 1 134 UNP Q6IRN2 Q6IRN2_XENLA 82 215
DBREF 2BL5 A 135 140 PDB 2BL5 2BL5 135 140
SEQRES 1 A 140 GLN LEU GLN GLU LYS LEU TYR VAL PRO VAL LYS GLU TYR
SEQRES 2 A 140 PRO ASP PHE ASN PHE VAL GLY ARG ILE LEU GLY PRO ARG
SEQRES 3 A 140 GLY LEU THR ALA LYS GLN LEU GLU ALA GLU THR GLY CYS
SEQRES 4 A 140 LYS ILE MET VAL ARG GLY LYS GLY SER MET ARG ASP LYS
SEQRES 5 A 140 LYS LYS GLU GLU GLN ASN ARG GLY LYS PRO ASN TRP GLU
SEQRES 6 A 140 HIS LEU ASN GLU ASP LEU HIS VAL LEU ILE THR VAL GLU
SEQRES 7 A 140 ASP ALA GLN ASN ARG ALA GLU LEU LYS LEU LYS ARG ALA
SEQRES 8 A 140 VAL GLU GLU VAL LYS LYS LEU LEU VAL PRO ALA ALA GLU
SEQRES 9 A 140 GLY GLU ASP SER LEU LYS LYS MET LYS LEU MET GLU LEU
SEQRES 10 A 140 ALA ILE LEU ASN GLY THR TYR ARG ASP ALA ASN LEU LYS
SEQRES 11 A 140 SER PRO ALA LEU HIS HIS HIS HIS HIS HIS
HELIX 1 1 ASN A 17 LEU A 23 1 7
HELIX 2 2 ARG A 26 GLY A 38 1 13
HELIX 3 3 ASP A 51 GLN A 57 1 7
HELIX 4 4 LYS A 61 HIS A 66 1 6
HELIX 5 5 GLN A 81 LEU A 99 1 19
HELIX 6 6 ASP A 107 MET A 115 1 9
HELIX 7 7 GLU A 116 ILE A 119 5 4
HELIX 8 8 ARG A 125 LYS A 130 5 6
SHEET 1 AA 3 LEU A 2 TYR A 7 0
SHEET 2 AA 3 HIS A 72 VAL A 77 -1 O VAL A 73 N LEU A 6
SHEET 3 AA 3 CYS A 39 ARG A 44 -1 O LYS A 40 N THR A 76
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 25 2 Bytes