HEADER ALLERGEN 12-AUG-02 1H2O
TITLE SOLUTION STRUCTURE OF THE MAJOR CHERRY ALLERGEN PRU AV 1
TITLE 2 MUTANT E45W
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MAJOR ALLERGEN PRU AV 1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PRU A 1;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES;
COMPND 7 OTHER_DETAILS: ENGINEERED MUTATION GLU 45 TRP
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PRUNUS AVIUM;
SOURCE 3 ORGANISM_COMMON: SWEET CHERRY;
SOURCE 4 ORGANISM_TAXID: 42229;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET11A
KEYWDS ALLERGEN, MAJOR CHERRY ALLERGEN, PATHOGENESIS-RELATED
KEYWDS 2 PROTEIN, HETERONUCLEAR NMR, STRUCTURE, PLANT DEFENSE
EXPDTA SOLUTION NMR
NUMMDL 24
AUTHOR P.NEUDECKER,K.LEHMANN,J.NERKAMP,K.SCHWEIMER,H.STICHT,
AUTHOR 2 M.BOEHM,S.SCHEURER,S.VIETHS,P.ROESCH
REVDAT 4 24-FEB-09 1H2O 1 VERSN
REVDAT 3 05-JAN-04 1H2O 1 JRNL
REVDAT 2 05-SEP-03 1H2O 1 SHEET
REVDAT 1 28-AUG-03 1H2O 0
JRNL AUTH P.NEUDECKER,K.LEHMANN,J.NERKAMP,T.HAASE,
JRNL AUTH 2 A.WANGORSCH,K.FOTISCH,S.HOFFMANN,P.ROESCH,S.VIETHS,
JRNL AUTH 3 S.SCHEURER
JRNL TITL MUTATIONAL EPITOPE ANALYSIS OF PRU AV 1 AND API G
JRNL TITL 2 1, THE MAJOR ALLERGENS OF CHERRY (PRUNUS AVIUM)
JRNL TITL 3 AND CELERY (APIUM GRAVEOLENS): CORRELATING IGE
JRNL TITL 4 REACTIVITY WITH THREE-DIMENSIONAL STRUCTURE
JRNL REF BIOCHEM.J. V. 376 97 2003
JRNL REFN ISSN 0264-6021
JRNL PMID 12943529
JRNL DOI 10.1042/BJ20031057
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH P.NEUDECKER,K.SCHWEIMER,J.NERKAMP,S.SCHEURER,
REMARK 1 AUTH 2 S.VIETHS,H.STICHT,P.ROESCH
REMARK 1 TITL ALLERGIC CROSS-REACTIVITY MADE VISIBLE: SOLUTION
REMARK 1 TITL 2 STRUCTURE OF THE MAJOR CHERRY ALLERGEN PRU AV 1
REMARK 1 REF J.BIOL.CHEM. V. 276 22756 2001
REMARK 1 REFN ISSN 0021-9258
REMARK 1 PMID 11287426
REMARK 1 DOI 10.1074/JBC.M101657200
REMARK 1 REFERENCE 2
REMARK 1 AUTH P.NEUDECKER,H.STICHT,P.ROESCH
REMARK 1 TITL IMPROVING THE EFFICIENCY OF THE GAUSSIAN
REMARK 1 TITL 2 CONFORMATIONAL DATABASE POTENTIAL FOR THE
REMARK 1 TITL 3 REFINEMENT OF PROTEIN AND NUCLEIC ACID STRUCTURES
REMARK 1 REF J.BIOMOL.NMR V. 21 373 2001
REMARK 1 REFN ISSN 0925-2738
REMARK 1 PMID 11824757
REMARK 1 DOI 10.1023/A:1013369107271
REMARK 1 REFERENCE 3
REMARK 1 AUTH P.NEUDECKER,K.SCHWEIMER,J.NERKAMP,M.BOEHM,
REMARK 1 AUTH 2 S.SCHEURER,S.VIETHS,H.STICHT,P.ROESCH
REMARK 1 TITL SEQUENCE-SPECIFIC 1H, 13C AND 15N RESONANCE
REMARK 1 TITL 2 ASSIGNMENTS OF THE MAJOR CHERRY ALLERGEN PRU A 1
REMARK 1 REF J.BIOMOL.NMR V. 18 71 2000
REMARK 1 REFN ISSN 0925-2738
REMARK 1 PMID 11061231
REMARK 1 DOI 10.1023/A:1008357100592
REMARK 1 REFERENCE 4
REMARK 1 AUTH K.SCHWEIMER,H.STICHT,J.NERKAMP,M.BOEHM,
REMARK 1 AUTH 2 M.BREITENBACH,S.VIETHS,P.ROESCH
REMARK 1 TITL NMR SPECTROSCOPY REVEALS COMMON STRUCTURAL
REMARK 1 TITL 2 FEATURES OF THE BIRCH POLLEN ALLERGEN BET V 1 AND
REMARK 1 TITL 3 THE CHERRY ALLERGEN PRU A 1
REMARK 1 REF APPL.MAGN.RESON. V. 17 449 1999
REMARK 1 REFN ISSN 0937-9347
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851 NIH 1.2.1
REMARK 3 AUTHORS : BRUNGER, CLORE, KUSZEWSKI, SCHWIETERS, TJ
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1H2O COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-AUG-02.
REMARK 100 THE PDBE ID CODE IS EBI-11201.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7
REMARK 210 IONIC STRENGTH : 50 MM
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 90% H2O / 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D-NOESY, 1H,15N-HSQC,
REMARK 210 HNHA, 3D-1H,15N-TOCSY-HSQC,
REMARK 210 3D-1H,15N-NOESY-HSQC,
REMARK 210 3D-1H,15N/1H,15N-HMQC-NOESY-HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 600; 750
REMARK 210 SPECTROMETER MODEL : DRX600; DMX750
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NDEE, NMRVIEW 5.0.4,
REMARK 210 X-PLOR 3.851 NIH 1.2.1
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 60
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 24
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE CHANGES IN STRUCTURE COMPARED TO PRU AV 1 WT
REMARK 210 WERE DETERMINED USING DOUBLE-RESONANCE NMR SPECTROSCOPY
REMARK 210 ON 15N-LABELED PRU AV 1 E45W
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 400
REMARK 400 COMPOUND
REMARK 400 PLANT DEFENSE PROTEIN, MEMBER OF THE BETV1 FAMILY OF
REMARK 400 PATHOGENESIS-RELATED PROTEINS.
REMARK 400
REMARK 400 ENGINEERED MUTATION GLU 46 TRP
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 O PHE A 9 - H ILE A 114 1.60
REMARK 500 O SER A 11 - H SER A 112 1.58
REMARK 500 H LEU A 44 - O ILE A 53 1.51
REMARK 500 H LYS A 54 - O HIS A 69 1.56
REMARK 500 O LYS A 70 - H THR A 84 1.57
REMARK 500 H LYS A 70 - O THR A 84 1.56
REMARK 500 O TYR A 81 - H THR A 102 1.60
REMARK 500 H TYR A 81 - O THR A 102 1.55
REMARK 500 H LYS A 103 - O LYS A 115 1.58
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 ASP A 25 14.49 -146.52
REMARK 500 1 ASP A 93 34.68 -91.64
REMARK 500 1 THR A 94 -41.64 -131.31
REMARK 500 1 GLU A 96 -80.90 -141.08
REMARK 500 1 ALA A 157 108.74 -46.92
REMARK 500 1 TYR A 158 30.83 35.46
REMARK 500 2 VAL A 23 -60.30 -97.45
REMARK 500 2 ASP A 25 10.95 -146.16
REMARK 500 2 ALA A 37 -63.31 -101.93
REMARK 500 2 SER A 62 174.34 -46.67
REMARK 500 2 GLN A 63 -84.29 -43.48
REMARK 500 2 GLU A 96 -79.93 -139.35
REMARK 500 2 LYS A 134 -69.74 -104.95
REMARK 500 2 ALA A 157 108.32 -57.78
REMARK 500 2 TYR A 158 31.45 35.31
REMARK 500 3 ASP A 25 30.62 -153.36
REMARK 500 3 ALA A 34 97.40 -170.89
REMARK 500 3 HIS A 40 136.72 -170.97
REMARK 500 3 SER A 62 -169.06 -55.00
REMARK 500 3 GLU A 96 -79.94 -147.03
REMARK 500 3 ASN A 125 60.42 67.39
REMARK 500 3 LYS A 134 -70.05 -107.72
REMARK 500 3 ALA A 157 106.55 -53.34
REMARK 500 3 TYR A 158 30.27 36.23
REMARK 500 4 ASP A 25 16.52 -152.19
REMARK 500 4 ALA A 34 98.17 -160.44
REMARK 500 4 GLN A 63 -72.51 -51.54
REMARK 500 4 THR A 94 -33.73 -160.03
REMARK 500 4 GLU A 96 -77.72 -128.36
REMARK 500 4 TYR A 158 32.67 34.71
REMARK 500 5 ASP A 25 30.44 -155.66
REMARK 500 5 LYS A 32 -32.90 -135.38
REMARK 500 5 ASP A 93 15.36 56.56
REMARK 500 5 GLU A 96 -78.35 -132.19
REMARK 500 5 THR A 117 117.98 -160.11
REMARK 500 5 ALA A 157 106.11 -53.91
REMARK 500 5 TYR A 158 30.38 36.23
REMARK 500 6 VAL A 23 -62.60 -107.60
REMARK 500 6 ASP A 25 28.40 -143.76
REMARK 500 6 ALA A 37 -69.04 -99.21
REMARK 500 6 HIS A 40 134.77 177.71
REMARK 500 6 SER A 73 163.08 179.92
REMARK 500 6 GLU A 96 -82.36 -149.90
REMARK 500 6 LYS A 134 -69.33 -98.11
REMARK 500 6 TYR A 158 31.80 35.15
REMARK 500 7 ASP A 25 17.82 -144.35
REMARK 500 7 GLN A 63 97.42 54.42
REMARK 500 7 TYR A 79 51.31 70.13
REMARK 500 7 GLU A 96 -80.33 -134.88
REMARK 500 7 ASN A 125 73.41 -112.72
REMARK 500 7 TYR A 158 32.54 35.06
REMARK 500 8 ASP A 25 23.95 -149.17
REMARK 500 8 ALA A 37 -86.05 -85.76
REMARK 500 8 HIS A 40 157.19 177.03
REMARK 500 8 GLU A 96 -80.31 -131.91
REMARK 500 8 TYR A 158 31.56 35.13
REMARK 500 9 ASP A 25 54.98 -157.20
REMARK 500 9 LYS A 32 -33.24 -131.99
REMARK 500 9 HIS A 40 179.38 173.53
REMARK 500 9 GLU A 96 -81.27 -142.46
REMARK 500 9 TYR A 158 32.63 35.05
REMARK 500 10 ASP A 25 21.79 -145.00
REMARK 500 10 GLU A 96 -82.02 -136.32
REMARK 500 10 ASN A 125 59.64 -113.87
REMARK 500 10 ILE A 128 173.25 -59.77
REMARK 500 10 ALA A 157 99.71 -69.20
REMARK 500 10 TYR A 158 32.33 34.77
REMARK 500 11 VAL A 23 -63.86 -91.26
REMARK 500 11 ALA A 37 -70.39 -85.54
REMARK 500 11 HIS A 40 148.41 -176.25
REMARK 500 11 SER A 62 -172.98 -56.34
REMARK 500 11 SER A 73 160.68 177.80
REMARK 500 11 GLU A 96 -78.73 -146.29
REMARK 500 11 ASN A 125 62.45 65.10
REMARK 500 11 TYR A 158 35.14 35.30
REMARK 500 12 ASP A 25 30.36 -151.20
REMARK 500 12 ALA A 34 77.32 -157.22
REMARK 500 12 ALA A 37 -69.27 -93.71
REMARK 500 12 HIS A 40 164.67 179.75
REMARK 500 12 SER A 62 -168.46 -56.15
REMARK 500 12 GLU A 96 -82.96 -142.28
REMARK 500 12 LYS A 134 -63.57 -102.87
REMARK 500 12 TYR A 158 37.28 34.65
REMARK 500 13 VAL A 23 -62.93 -106.32
REMARK 500 13 ASP A 25 15.70 -149.63
REMARK 500 13 ALA A 34 97.50 -161.90
REMARK 500 13 HIS A 40 175.16 173.03
REMARK 500 13 GLU A 96 -79.70 -137.74
REMARK 500 13 ASN A 125 64.17 -102.97
REMARK 500 13 TYR A 158 36.67 33.72
REMARK 500 14 VAL A 23 -66.39 -108.63
REMARK 500 14 ALA A 37 -67.66 -96.95
REMARK 500 14 GLU A 96 -79.85 -140.38
REMARK 500 14 TYR A 158 39.55 34.53
REMARK 500 15 ASP A 25 23.46 -147.78
REMARK 500 15 ALA A 37 -73.43 -86.08
REMARK 500 15 SER A 62 -140.92 -87.49
REMARK 500 15 GLU A 96 -80.81 -133.79
REMARK 500 15 LYS A 134 -72.51 -104.42
REMARK 500 15 ALA A 157 105.51 -59.76
REMARK 500 15 TYR A 158 30.53 35.64
REMARK 500 16 ASP A 25 38.82 -149.44
REMARK 500 16 ALA A 34 103.21 -160.43
REMARK 500 16 ALA A 37 -64.84 -92.13
REMARK 500 16 GLU A 96 -82.18 -140.05
REMARK 500 16 ASN A 125 76.39 -113.20
REMARK 500 16 ALA A 157 107.38 -57.76
REMARK 500 16 TYR A 158 29.61 36.56
REMARK 500 17 ASP A 25 32.49 -150.70
REMARK 500 17 ALA A 34 102.95 -175.33
REMARK 500 17 HIS A 40 162.08 173.24
REMARK 500 17 GLN A 63 150.72 -45.68
REMARK 500 17 THR A 94 -35.07 -160.05
REMARK 500 17 GLU A 96 -78.98 -148.64
REMARK 500 17 ALA A 157 104.92 -59.81
REMARK 500 17 TYR A 158 31.12 35.77
REMARK 500 18 VAL A 23 -61.46 -104.39
REMARK 500 18 ALA A 34 102.63 -161.37
REMARK 500 18 ALA A 37 -70.45 -89.41
REMARK 500 18 HIS A 40 155.45 178.00
REMARK 500 18 GLU A 96 -80.99 -146.16
REMARK 500 18 ASN A 125 74.00 -118.65
REMARK 500 18 TYR A 158 33.08 33.76
REMARK 500 19 ASP A 25 39.29 -157.55
REMARK 500 19 ALA A 37 -65.08 -99.89
REMARK 500 19 SER A 62 -89.78 58.96
REMARK 500 19 GLU A 96 -80.30 -142.68
REMARK 500 19 ALA A 157 107.76 -48.48
REMARK 500 19 TYR A 158 30.85 35.61
REMARK 500 20 ASP A 25 49.49 -154.91
REMARK 500 20 GLU A 96 -81.36 -146.64
REMARK 500 20 ASN A 125 54.37 -119.94
REMARK 500 20 LYS A 134 -71.85 -108.91
REMARK 500 20 ALA A 157 108.26 -51.35
REMARK 500 20 TYR A 158 30.70 35.73
REMARK 500 21 ASP A 25 36.57 -148.48
REMARK 500 21 ALA A 34 91.97 -169.89
REMARK 500 21 SER A 62 177.80 -56.73
REMARK 500 21 GLU A 96 -80.01 -142.63
REMARK 500 21 LYS A 134 -73.74 -112.00
REMARK 500 21 ALA A 157 104.47 -53.65
REMARK 500 21 TYR A 158 30.96 35.33
REMARK 500 22 VAL A 23 -60.89 -104.20
REMARK 500 22 ASP A 25 44.18 -148.17
REMARK 500 22 ALA A 34 99.82 -160.66
REMARK 500 22 HIS A 40 159.32 179.03
REMARK 500 22 GLN A 63 -83.60 -137.07
REMARK 500 22 GLU A 96 -84.21 -142.44
REMARK 500 22 PRO A 108 85.09 -66.54
REMARK 500 22 TYR A 158 32.18 34.86
REMARK 500 23 VAL A 23 -60.60 -100.88
REMARK 500 23 ASP A 25 30.14 -149.04
REMARK 500 23 ALA A 34 102.27 -170.24
REMARK 500 23 GLU A 96 -82.85 -144.77
REMARK 500 23 ASN A 125 77.19 -115.72
REMARK 500 23 TYR A 158 31.27 35.67
REMARK 500 24 ASP A 25 30.92 -154.15
REMARK 500 24 ALA A 37 -63.40 -98.24
REMARK 500 24 HIS A 40 159.85 178.69
REMARK 500 24 SER A 62 -168.95 -54.03
REMARK 500 24 GLU A 96 -81.38 -151.20
REMARK 500 24 LYS A 134 -71.17 -104.04
REMARK 500 24 ALA A 157 102.31 -46.84
REMARK 500 24 TYR A 158 -59.12 58.71
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 4 ARG A 17 0.15 SIDE CHAIN
REMARK 500 6 ARG A 17 0.22 SIDE CHAIN
REMARK 500 9 ARG A 17 0.18 SIDE CHAIN
REMARK 500 10 ARG A 17 0.18 SIDE CHAIN
REMARK 500 12 ARG A 17 0.12 SIDE CHAIN
REMARK 500 14 ARG A 17 0.11 SIDE CHAIN
REMARK 500 17 ARG A 17 0.08 SIDE CHAIN
REMARK 500 21 ARG A 17 0.08 SIDE CHAIN
REMARK 500 22 ARG A 17 0.19 SIDE CHAIN
REMARK 500 23 ARG A 17 0.19 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: AUTHOR PROVIDED.
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: AUTHOR PROVIDED.
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1BTV RELATED DB: PDB
REMARK 900 STRUCTURE OF BET V 1, NMR, 20 STRUCTURES
REMARK 900 RELATED ID: 1B6F RELATED DB: PDB
REMARK 900 BIRCH POLLEN ALLERGEN BET V 1
REMARK 900 RELATED ID: 1BV1 RELATED DB: PDB
REMARK 900 BIRCH POLLEN ALLERGEN BET V 1
REMARK 900 RELATED ID: 1E09 RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF THE MAJOR CHERRY
REMARK 900 ALLERGEN PRU AV 1
REMARK 900 RELATED ID: 1FSK RELATED DB: PDB
REMARK 900 COMPLEX FORMATION BETWEEN A FAB FRAGMENT
REMARK 900 OF A MONOCLONAL IGG ANTIBODY AND THE MAJOR
REMARK 900 ALLERGEN FROM BIRCH POLLEN BET V
REMARK 900 RELATED ID: 1QMR RELATED DB: PDB
REMARK 900 BIRCH POLLEN ALLERGEN BET V 1 MUTANT N28T,
REMARK 900 K32Q, E45S, P108G
DBREF 1H2O A 1 159 UNP O24248 PRU1_PRUAV 2 160
SEQADV 1H2O TRP A 45 UNP O24248 GLU 46 ENGINEERED MUTATION
SEQRES 1 A 159 GLY VAL PHE THR TYR GLU SER GLU PHE THR SER GLU ILE
SEQRES 2 A 159 PRO PRO PRO ARG LEU PHE LYS ALA PHE VAL LEU ASP ALA
SEQRES 3 A 159 ASP ASN LEU VAL PRO LYS ILE ALA PRO GLN ALA ILE LYS
SEQRES 4 A 159 HIS SER GLU ILE LEU TRP GLY ASP GLY GLY PRO GLY THR
SEQRES 5 A 159 ILE LYS LYS ILE THR PHE GLY GLU GLY SER GLN TYR GLY
SEQRES 6 A 159 TYR VAL LYS HIS LYS ILE ASP SER ILE ASP LYS GLU ASN
SEQRES 7 A 159 TYR SER TYR SER TYR THR LEU ILE GLU GLY ASP ALA LEU
SEQRES 8 A 159 GLY ASP THR LEU GLU LYS ILE SER TYR GLU THR LYS LEU
SEQRES 9 A 159 VAL ALA SER PRO SER GLY GLY SER ILE ILE LYS SER THR
SEQRES 10 A 159 SER HIS TYR HIS THR LYS GLY ASN VAL GLU ILE LYS GLU
SEQRES 11 A 159 GLU HIS VAL LYS ALA GLY LYS GLU LYS ALA SER ASN LEU
SEQRES 12 A 159 PHE LYS LEU ILE GLU THR TYR LEU LYS GLY HIS PRO ASP
SEQRES 13 A 159 ALA TYR ASN
HELIX 1 1 PRO A 15 PHE A 22 1 8
HELIX 2 2 ALA A 26 ILE A 33 1 8
HELIX 4 4 GLU A 130 GLY A 153 1 24
SHEET 1 A 5 VAL A 2 SER A 11 0
SHEET 2 A 5 SER A 112 THR A 122 -1 N SER A 118 O TYR A 5
SHEET 3 A 5 LYS A 97 LEU A 104 -1 N GLU A 101 O THR A 117
SHEET 4 A 5 SER A 80 LEU A 85 -1 N TYR A 83 O TYR A 100
SHEET 5 A 5 SER A 73 ASP A 75 -1 N ASP A 75 O SER A 80
SHEET 1 B 3 SER A 41 ILE A 43 0
SHEET 2 B 3 ILE A 53 PHE A 58 -1 N LYS A 55 O GLU A 42
SHEET 3 B 3 GLY A 65 ILE A 71 -1 N VAL A 67 O ILE A 56
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
(ATOM LINES ARE NOT SHOWN.)
END
