Header list of 1ys5.pdb file
Complete list - r 2 2 Bytes
HEADER SIGNALING PROTEIN 07-FEB-05 1YS5
TITLE SOLUTION STRUCTURE OF THE ANTIGENIC DOMAIN OF GNA1870 OF NEISSERIA
TITLE 2 MENINGITIDIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPOPROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: IMMUNODOMINANT C-TERMINAL BC DOMAIN;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: NEISSERIA MENINGITIDIS;
SOURCE 3 ORGANISM_TAXID: 487;
SOURCE 4 GENE: GNA1870;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET20B+
KEYWDS VACCINE CANDIDATE, NEISSERIA MENINGITIDIS, BETA-BARREL STRUCTURE,
KEYWDS 2 SIGNALING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 30
AUTHOR F.CANTINI,S.SAVINO,V.MASIGNANI,M.PIZZA,M.SCARSELLI,E.SWENNEN,
AUTHOR 2 G.ROMAGNOLI,D.VEGGI,L.BANCI,R.RAPPUOLI
REVDAT 4 02-MAR-22 1YS5 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1YS5 1 VERSN
REVDAT 2 04-APR-06 1YS5 1 JRNL
REVDAT 1 07-FEB-06 1YS5 0
JRNL AUTH F.CANTINI,S.SAVINO,M.SCARSELLI,V.MASIGNANI,M.PIZZA,
JRNL AUTH 2 G.ROMAGNOLI,E.SWENNEN,D.VEGGI,L.BANCI,R.RAPPUOLI
JRNL TITL SOLUTION STRUCTURE OF THE IMMUNODOMINANT DOMAIN OF
JRNL TITL 2 PROTECTIVE ANTIGEN GNA1870 OF NEISSERIA MENINGITIDIS
JRNL REF J.BIOL.CHEM. V. 281 7220 2006
JRNL REFN ISSN 0021-9258
JRNL PMID 16407174
JRNL DOI 10.1074/JBC.M508595200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR, AMBER 5.0
REMARK 3 AUTHORS : PEARLMAN ET AL, 1987 (AMBER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES WERE BASED ON A TOTAL OF
REMARK 3 2242 MEANINGFUL DISTANCE CONSTRAINTS, 149 DIHEDRAL ANGLE
REMARK 3 RESTRAINTS.
REMARK 4
REMARK 4 1YS5 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 09-FEB-05.
REMARK 100 THE DEPOSITION ID IS D_1000031869.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7
REMARK 210 IONIC STRENGTH : 20MM PHOSPHATE BUFFER
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 4MM GNA1870; 20MM PHOSPHATE
REMARK 210 BUFFER; 1MM GNA1870 15N LABELLED;
REMARK 210 20MM PHOSPHATE BUFFER;; 2MM
REMARK 210 GNA1870 15N AND 13C LABELLED;
REMARK 210 20MM PHOSPHATE BUFFER;
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; HNHA; 3D_15N
REMARK 210 -SEPARATED_NOESY; CBCANH;
REMARK 210 CBCACONH; HNCO; HNCACO; CCH-
REMARK 210 TOCSY; 3D_13C-SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : CARA 1.2, DYANA 1.5, CANDID 2,
REMARK 210 PROCHECK-NMR AND AQUA
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS,
REMARK 210 SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 400
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 30
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 12
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-30
REMARK 465 RES C SSSEQI
REMARK 465 LEU A 157
REMARK 465 GLU A 158
REMARK 465 HIS A 159
REMARK 465 HIS A 160
REMARK 465 HIS A 161
REMARK 465 HIS A 162
REMARK 465 HIS A 163
REMARK 465 HIS A 164
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
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,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
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 ATM2 ATM3
REMARK 500 3 ARG A 148 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 6 ASP A 102 CB - CG - OD1 ANGL. DEV. = -6.2 DEGREES
REMARK 500 8 VAL A 135 CA - CB - CG2 ANGL. DEV. = 10.6 DEGREES
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 GLN A 2 95.56 -61.83
REMARK 500 1 ALA A 9 148.65 -174.41
REMARK 500 1 GLU A 13 73.97 -61.41
REMARK 500 1 GLN A 14 -43.91 -166.62
REMARK 500 1 ASP A 17 -53.92 69.32
REMARK 500 1 LYS A 23 -98.36 -72.11
REMARK 500 1 MET A 24 -87.89 -137.19
REMARK 500 1 VAL A 25 -79.94 69.27
REMARK 500 1 ALA A 26 108.50 179.21
REMARK 500 1 GLN A 29 -144.24 52.97
REMARK 500 1 PHE A 30 -70.31 -153.34
REMARK 500 1 ARG A 31 22.03 -170.61
REMARK 500 1 ALA A 36 -61.55 -135.57
REMARK 500 1 GLU A 38 -76.66 -45.60
REMARK 500 1 LYS A 44 57.07 136.33
REMARK 500 1 PRO A 46 -166.34 -79.49
REMARK 500 1 THR A 52 57.06 -105.28
REMARK 500 1 ASP A 62 67.04 17.85
REMARK 500 1 ALA A 63 57.01 -104.77
REMARK 500 1 THR A 70 87.32 -153.98
REMARK 500 1 ALA A 74 -41.46 -27.36
REMARK 500 1 ALA A 75 -22.16 -147.31
REMARK 500 1 LYS A 76 49.14 93.70
REMARK 500 1 GLU A 83 60.16 -155.56
REMARK 500 1 HIS A 84 45.72 -158.83
REMARK 500 1 ASP A 102 -122.57 -77.99
REMARK 500 1 LYS A 104 -116.03 56.72
REMARK 500 1 HIS A 106 76.72 59.22
REMARK 500 1 ALA A 107 37.86 -74.80
REMARK 500 1 ASN A 116 -67.57 54.18
REMARK 500 1 ALA A 132 106.39 99.52
REMARK 500 1 GLN A 133 -70.11 -124.68
REMARK 500 1 ARG A 148 -73.31 -19.35
REMARK 500 1 HIS A 149 78.72 -66.26
REMARK 500 2 GLN A 2 98.61 -65.20
REMARK 500 2 GLN A 11 176.66 66.30
REMARK 500 2 THR A 12 -167.71 56.59
REMARK 500 2 GLN A 16 100.08 75.00
REMARK 500 2 ASP A 17 -68.84 62.77
REMARK 500 2 MET A 24 33.29 169.97
REMARK 500 2 VAL A 25 -52.09 68.90
REMARK 500 2 ARG A 28 -60.92 75.38
REMARK 500 2 ILE A 32 155.32 -46.78
REMARK 500 2 ASP A 34 -175.05 -171.98
REMARK 500 2 ILE A 35 158.69 68.72
REMARK 500 2 ALA A 36 -84.03 -142.19
REMARK 500 2 GLU A 38 -75.43 -42.43
REMARK 500 2 THR A 40 -79.04 -65.65
REMARK 500 2 LYS A 44 53.46 169.56
REMARK 500 2 GLU A 47 48.42 -77.59
REMARK 500
REMARK 500 THIS ENTRY HAS 891 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ASP A 61 ASP A 62 1 -136.16
REMARK 500 ASP A 62 ALA A 63 1 148.17
REMARK 500 ASP A 61 ASP A 62 2 -128.01
REMARK 500 ASP A 62 ALA A 63 2 149.38
REMARK 500 GLU A 83 HIS A 84 2 31.14
REMARK 500 PRO A 101 ASP A 102 2 144.20
REMARK 500 GLU A 119 LYS A 120 2 140.89
REMARK 500 THR A 68 TYR A 69 3 -137.65
REMARK 500 THR A 70 ILE A 71 3 146.11
REMARK 500 HIS A 84 LEU A 85 3 -135.30
REMARK 500 THR A 68 TYR A 69 4 -148.36
REMARK 500 HIS A 84 LEU A 85 4 -133.41
REMARK 500 GLU A 119 LYS A 120 4 133.10
REMARK 500 ASP A 61 ASP A 62 5 -144.88
REMARK 500 ASP A 61 ASP A 62 7 -146.76
REMARK 500 ASP A 62 ALA A 63 7 149.23
REMARK 500 GLU A 83 HIS A 84 8 41.48
REMARK 500 ASP A 61 ASP A 62 9 -136.76
REMARK 500 ASP A 62 ALA A 63 9 147.48
REMARK 500 VAL A 108 ILE A 109 9 144.09
REMARK 500 GLU A 119 LYS A 120 9 135.14
REMARK 500 ILE A 71 ASP A 72 10 148.39
REMARK 500 HIS A 84 LEU A 85 10 -140.74
REMARK 500 LYS A 104 ARG A 105 10 -146.34
REMARK 500 GLU A 119 LYS A 120 10 141.63
REMARK 500 GLU A 83 HIS A 84 12 58.12
REMARK 500 HIS A 84 LEU A 85 12 -145.76
REMARK 500 GLY A 33 ASP A 34 13 146.50
REMARK 500 ASP A 61 ASP A 62 13 -143.83
REMARK 500 ASP A 62 ALA A 63 13 148.09
REMARK 500 GLN A 77 GLY A 78 13 -137.20
REMARK 500 GLU A 119 LYS A 120 13 131.64
REMARK 500 LYS A 155 GLN A 156 14 142.23
REMARK 500 ASP A 62 ALA A 63 15 143.10
REMARK 500 HIS A 84 LEU A 85 15 -123.59
REMARK 500 TYR A 53 ARG A 54 16 141.94
REMARK 500 ASP A 62 ALA A 63 16 146.09
REMARK 500 GLU A 119 LYS A 120 16 135.28
REMARK 500 ASP A 61 ASP A 62 17 -137.21
REMARK 500 ILE A 82 GLU A 83 17 -147.96
REMARK 500 ASP A 61 ASP A 62 18 -143.39
REMARK 500 THR A 68 TYR A 69 18 -139.81
REMARK 500 THR A 70 ILE A 71 18 147.14
REMARK 500 LYS A 120 GLY A 121 19 144.17
REMARK 500 ASP A 62 ALA A 63 20 146.39
REMARK 500 ASP A 61 ASP A 62 21 -146.46
REMARK 500 ASP A 62 ALA A 63 21 149.26
REMARK 500 HIS A 84 LEU A 85 21 -147.12
REMARK 500 GLY A 33 ASP A 34 22 -148.18
REMARK 500 ASP A 61 ASP A 62 23 -137.67
REMARK 500
REMARK 500 THIS ENTRY HAS 64 NON CIS, NON-TRANS OMEGA 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 HIS A 84 0.10 SIDE CHAIN
REMARK 500 1 ARG A 105 0.24 SIDE CHAIN
REMARK 500 1 TYR A 123 0.14 SIDE CHAIN
REMARK 500 2 ARG A 54 0.08 SIDE CHAIN
REMARK 500 2 PHE A 73 0.11 SIDE CHAIN
REMARK 500 2 ARG A 105 0.10 SIDE CHAIN
REMARK 500 2 TYR A 123 0.10 SIDE CHAIN
REMARK 500 3 ARG A 50 0.18 SIDE CHAIN
REMARK 500 3 TYR A 53 0.06 SIDE CHAIN
REMARK 500 3 TYR A 115 0.16 SIDE CHAIN
REMARK 500 4 TYR A 53 0.14 SIDE CHAIN
REMARK 500 4 TYR A 115 0.08 SIDE CHAIN
REMARK 500 5 TYR A 53 0.06 SIDE CHAIN
REMARK 500 5 PHE A 73 0.14 SIDE CHAIN
REMARK 500 5 TYR A 123 0.15 SIDE CHAIN
REMARK 500 5 ARG A 148 0.08 SIDE CHAIN
REMARK 500 6 TYR A 53 0.09 SIDE CHAIN
REMARK 500 6 ARG A 54 0.08 SIDE CHAIN
REMARK 500 6 PHE A 73 0.12 SIDE CHAIN
REMARK 500 6 TYR A 123 0.10 SIDE CHAIN
REMARK 500 7 ARG A 31 0.11 SIDE CHAIN
REMARK 500 7 PHE A 73 0.20 SIDE CHAIN
REMARK 500 7 TYR A 115 0.14 SIDE CHAIN
REMARK 500 7 ARG A 148 0.09 SIDE CHAIN
REMARK 500 8 TYR A 69 0.08 SIDE CHAIN
REMARK 500 8 TYR A 123 0.15 SIDE CHAIN
REMARK 500 8 ARG A 148 0.11 SIDE CHAIN
REMARK 500 9 TYR A 53 0.07 SIDE CHAIN
REMARK 500 9 ARG A 148 0.11 SIDE CHAIN
REMARK 500 10 TYR A 53 0.10 SIDE CHAIN
REMARK 500 10 TYR A 69 0.17 SIDE CHAIN
REMARK 500 10 PHE A 73 0.11 SIDE CHAIN
REMARK 500 10 HIS A 84 0.14 SIDE CHAIN
REMARK 500 10 TYR A 115 0.10 SIDE CHAIN
REMARK 500 11 TYR A 115 0.17 SIDE CHAIN
REMARK 500 11 TYR A 123 0.13 SIDE CHAIN
REMARK 500 12 PHE A 42 0.08 SIDE CHAIN
REMARK 500 12 PHE A 73 0.11 SIDE CHAIN
REMARK 500 12 TYR A 115 0.08 SIDE CHAIN
REMARK 500 12 TYR A 123 0.12 SIDE CHAIN
REMARK 500 13 ARG A 28 0.10 SIDE CHAIN
REMARK 500 13 TYR A 53 0.12 SIDE CHAIN
REMARK 500 13 PHE A 73 0.10 SIDE CHAIN
REMARK 500 14 TYR A 53 0.11 SIDE CHAIN
REMARK 500 14 TYR A 123 0.14 SIDE CHAIN
REMARK 500 15 TYR A 53 0.12 SIDE CHAIN
REMARK 500 16 ARG A 105 0.15 SIDE CHAIN
REMARK 500 16 TYR A 115 0.14 SIDE CHAIN
REMARK 500 16 TYR A 123 0.10 SIDE CHAIN
REMARK 500 17 TYR A 69 0.15 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 93 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1YS5 A 2 156 GB 46562309 AAT01290 120 274
SEQADV 1YS5 MET A 1 GB 46562309 INITIATING METHIONINE
SEQADV 1YS5 LEU A 157 GB 46562309 EXPRESSION TAG
SEQADV 1YS5 GLU A 158 GB 46562309 EXPRESSION TAG
SEQADV 1YS5 HIS A 159 GB 46562309 EXPRESSION TAG
SEQADV 1YS5 HIS A 160 GB 46562309 EXPRESSION TAG
SEQADV 1YS5 HIS A 161 GB 46562309 EXPRESSION TAG
SEQADV 1YS5 HIS A 162 GB 46562309 EXPRESSION TAG
SEQADV 1YS5 HIS A 163 GB 46562309 EXPRESSION TAG
SEQADV 1YS5 HIS A 164 GB 46562309 EXPRESSION TAG
SEQRES 1 A 164 MET GLN SER HIS SER ALA LEU THR ALA PHE GLN THR GLU
SEQRES 2 A 164 GLN ILE GLN ASP SER GLU HIS SER GLY LYS MET VAL ALA
SEQRES 3 A 164 LYS ARG GLN PHE ARG ILE GLY ASP ILE ALA GLY GLU HIS
SEQRES 4 A 164 THR SER PHE ASP LYS LEU PRO GLU GLY GLY ARG ALA THR
SEQRES 5 A 164 TYR ARG GLY THR ALA PHE GLY SER ASP ASP ALA GLY GLY
SEQRES 6 A 164 LYS LEU THR TYR THR ILE ASP PHE ALA ALA LYS GLN GLY
SEQRES 7 A 164 ASN GLY LYS ILE GLU HIS LEU LYS SER PRO GLU LEU ASN
SEQRES 8 A 164 VAL ASP LEU ALA ALA ALA ASP ILE LYS PRO ASP GLY LYS
SEQRES 9 A 164 ARG HIS ALA VAL ILE SER GLY SER VAL LEU TYR ASN GLN
SEQRES 10 A 164 ALA GLU LYS GLY SER TYR SER LEU GLY ILE PHE GLY GLY
SEQRES 11 A 164 LYS ALA GLN GLU VAL ALA GLY SER ALA GLU VAL LYS THR
SEQRES 12 A 164 VAL ASN GLY ILE ARG HIS ILE GLY LEU ALA ALA LYS GLN
SEQRES 13 A 164 LEU GLU HIS HIS HIS HIS HIS HIS
HELIX 1 1 ASP A 17 LYS A 23 1 7
HELIX 2 2 GLY A 37 ASP A 43 1 7
HELIX 3 3 SER A 87 LEU A 90 5 4
SHEET 1 A 7 GLY A 65 LEU A 67 0
SHEET 2 A 7 GLY A 55 PHE A 58 -1 N ALA A 57 O GLY A 65
SHEET 3 A 7 ARG A 148 ALA A 154 -1 O ALA A 153 N THR A 56
SHEET 4 A 7 GLY A 137 VAL A 141 -1 N ALA A 139 O ILE A 150
SHEET 5 A 7 ALA A 118 LEU A 125 -1 N SER A 124 O SER A 138
SHEET 6 A 7 SER A 112 TYR A 115 -1 N VAL A 113 O GLY A 121
SHEET 7 A 7 VAL A 92 LEU A 94 -1 N ASP A 93 O LEU A 114
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 2 2 Bytes