HEADER TRANSCRIPTION 11-JAN-06 2FNP
TITLE CRYSTAL STRUCTURE OF SARA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: STAPHYLOCOCCAL ACCESSORY REGULATOR A;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS;
SOURCE 3 ORGANISM_TAXID: 1280;
SOURCE 4 STRAIN: STRAIN MW2;
SOURCE 5 GENE: SARA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL-21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PET30-B
KEYWDS WING-HELIX, DNA BINDING, TRANSCRIPTION
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.LIU,A.C.MANNA,C.H.PAN,A.L.CHEUNG,G.ZHANG
REVDAT 4 14-FEB-24 2FNP 1 SEQADV
REVDAT 3 24-FEB-09 2FNP 1 VERSN
REVDAT 2 14-MAR-06 2FNP 1 JRNL
REVDAT 1 31-JAN-06 2FNP 0
JRNL AUTH Y.LIU,A.C.MANNA,C.H.PAN,I.A.KRIKSUNOV,D.J.THIEL,A.L.CHEUNG,
JRNL AUTH 2 G.ZHANG
JRNL TITL STRUCTURAL AND FUNCTION ANALYSES OF THE GLOBAL REGULATORY
JRNL TITL 2 PROTEIN SARA FROM STAPHYLOCOCCUS AUREUS.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 103 2392 2006
JRNL REFN ISSN 0027-8424
JRNL PMID 16455801
JRNL DOI 10.1073/PNAS.0510439103
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.17
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 732953.630
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 92.5
REMARK 3 NUMBER OF REFLECTIONS : 9426
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.285
REMARK 3 FREE R VALUE : 0.308
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.400
REMARK 3 FREE R VALUE TEST SET COUNT : 506
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.014
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.76
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 77.30
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1236
REMARK 3 BIN R VALUE (WORKING SET) : 0.5170
REMARK 3 BIN FREE R VALUE : 0.4460
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.50
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 72
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.053
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2052
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 11
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 36.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 70.50
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -10.18000
REMARK 3 B22 (A**2) : -30.62000
REMARK 3 B33 (A**2) : 40.81000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 23.24000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.52
REMARK 3 ESD FROM SIGMAA (A) : 0.93
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.59
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.86
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.900
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 21.40
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.910
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.33
REMARK 3 BSOL : 50.59
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER.PARAM
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2FNP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-JAN-06.
REMARK 100 THE DEPOSITION ID IS D_1000036093.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-MAR-05
REMARK 200 TEMPERATURE (KELVIN) : 52.074
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 4.2.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM, TRUNCATE
REMARK 200 DATA SCALING SOFTWARE : CCP4 (TRUNCATE)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 9772
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.06800
REMARK 200 R SYM (I) : 0.06800
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.69
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.90
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.80
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG 8000, 0.2M CALCIUM CHLORIDE,
REMARK 280 0.1M CACODYLATE, PH 6.5, VAPOR DIFFUSION, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 32.37900
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3130 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14020 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -32.0 KCAL/MOL
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 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 MET A 101
REMARK 465 ALA A 102
REMARK 465 MET B 101
REMARK 465 ALA B 102
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 OD1 ASN A 197 OE1 GLN A 200 2.11
REMARK 500 O ASN B 146 OH TYR B 151 2.14
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O GLU B 129 ND2 ASN B 185 2455 2.17
REMARK 500
REMARK 500 REMARK: NULL
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 ASN A 185 N - CA - C ANGL. DEV. = 19.1 DEGREES
REMARK 500 ASP A 188 N - CA - C ANGL. DEV. = -16.8 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 THR A 104 84.78 82.62
REMARK 500 ASP A 120 -34.08 -39.55
REMARK 500 LYS A 127 7.23 -68.28
REMARK 500 HIS A 159 -28.40 -27.76
REMARK 500 LEU A 160 -84.06 -85.56
REMARK 500 ASN A 161 8.06 146.31
REMARK 500 LYS A 163 58.07 -106.94
REMARK 500 GLN A 164 -83.82 40.72
REMARK 500 VAL A 167 -82.22 -59.60
REMARK 500 VAL A 168 -56.18 -18.68
REMARK 500 ASP A 178 87.49 72.74
REMARK 500 GLU A 186 -71.34 -103.71
REMARK 500 ASP A 188 12.15 84.17
REMARK 500 ARG A 190 72.87 -7.48
REMARK 500 THR A 191 50.59 -175.27
REMARK 500 ALA A 198 -31.31 -33.20
REMARK 500 ASP B 108 -160.77 -170.32
REMARK 500 ASN B 146 72.20 -119.39
REMARK 500 LYS B 147 106.50 -55.63
REMARK 500 ASN B 161 45.59 99.71
REMARK 500 TYR B 162 -155.08 -112.50
REMARK 500 GLN B 164 -67.93 -4.05
REMARK 500 VAL B 167 -86.13 -74.94
REMARK 500 VAL B 168 -61.05 -11.20
REMARK 500 GLU B 186 -101.72 95.36
REMARK 500 HIS B 187 77.68 -44.06
REMARK 500 GLU B 189 -13.18 64.84
REMARK 500 ARG B 190 -82.76 -71.45
REMARK 500 THR B 191 133.55 -29.57
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2FNP A 102 224 UNP Q7A1N5 SARA_STAAW 1 123
DBREF 2FNP B 102 224 UNP Q7A1N5 SARA_STAAW 1 123
SEQADV 2FNP MET A 101 UNP Q7A1N5 INITIATING METHIONINE
SEQADV 2FNP MET B 101 UNP Q7A1N5 INITIATING METHIONINE
SEQRES 1 A 124 MET ALA ILE THR LYS ILE ASN ASP CYS PHE GLU LEU LEU
SEQRES 2 A 124 SER MET VAL THR TYR ALA ASP LYS LEU LYS SER LEU ILE
SEQRES 3 A 124 LYS LYS GLU PHE SER ILE SER PHE GLU GLU PHE ALA VAL
SEQRES 4 A 124 LEU THR TYR ILE SER GLU ASN LYS GLU LYS GLU TYR TYR
SEQRES 5 A 124 PHE LYS ASP ILE ILE ASN HIS LEU ASN TYR LYS GLN PRO
SEQRES 6 A 124 GLN VAL VAL LYS ALA VAL LYS ILE LEU SER GLN GLU ASP
SEQRES 7 A 124 TYR PHE ASP LYS LYS ARG ASN GLU HIS ASP GLU ARG THR
SEQRES 8 A 124 VAL LEU ILE LEU VAL ASN ALA GLN GLN ARG LYS LYS ILE
SEQRES 9 A 124 GLU SER LEU LEU SER ARG VAL ASN LYS ARG ILE THR GLU
SEQRES 10 A 124 ALA ASN ASN GLU ILE GLU LEU
SEQRES 1 B 124 MET ALA ILE THR LYS ILE ASN ASP CYS PHE GLU LEU LEU
SEQRES 2 B 124 SER MET VAL THR TYR ALA ASP LYS LEU LYS SER LEU ILE
SEQRES 3 B 124 LYS LYS GLU PHE SER ILE SER PHE GLU GLU PHE ALA VAL
SEQRES 4 B 124 LEU THR TYR ILE SER GLU ASN LYS GLU LYS GLU TYR TYR
SEQRES 5 B 124 PHE LYS ASP ILE ILE ASN HIS LEU ASN TYR LYS GLN PRO
SEQRES 6 B 124 GLN VAL VAL LYS ALA VAL LYS ILE LEU SER GLN GLU ASP
SEQRES 7 B 124 TYR PHE ASP LYS LYS ARG ASN GLU HIS ASP GLU ARG THR
SEQRES 8 B 124 VAL LEU ILE LEU VAL ASN ALA GLN GLN ARG LYS LYS ILE
SEQRES 9 B 124 GLU SER LEU LEU SER ARG VAL ASN LYS ARG ILE THR GLU
SEQRES 10 B 124 ALA ASN ASN GLU ILE GLU LEU
FORMUL 3 HOH *11(H2 O)
HELIX 1 1 ASP A 108 PHE A 130 1 23
HELIX 2 2 SER A 133 ASN A 146 1 14
HELIX 3 3 PHE A 153 ASN A 161 1 9
HELIX 4 4 GLN A 164 ASP A 178 1 15
HELIX 5 5 GLN A 199 ASN A 219 1 21
HELIX 6 6 ASP B 108 SER B 131 1 24
HELIX 7 7 SER B 133 ASN B 146 1 14
HELIX 8 8 PHE B 153 ASN B 161 1 9
HELIX 9 9 LYS B 163 GLN B 176 1 14
HELIX 10 10 GLU B 186 ARG B 190 5 5
HELIX 11 11 GLN B 199 ASN B 219 1 21
SHEET 1 A 3 GLU A 150 TYR A 152 0
SHEET 2 A 3 VAL A 192 LEU A 195 -1 O ILE A 194 N TYR A 151
SHEET 3 A 3 ASP A 181 ARG A 184 -1 N LYS A 183 O LEU A 193
SHEET 1 B 3 GLU B 150 TYR B 152 0
SHEET 2 B 3 LEU B 193 LEU B 195 -1 O ILE B 194 N TYR B 151
SHEET 3 B 3 ASP B 181 LYS B 183 -1 N LYS B 183 O LEU B 193
CRYST1 52.074 64.758 55.564 90.00 117.73 90.00 P 1 21 1 4
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 0.019203 0.000000 0.010095 0.00000
SCALE2 0.000000 0.015442 0.000000 0.00000
SCALE3 0.000000 0.000000 0.020332 0.00000
(ATOM LINES ARE NOT SHOWN.)
END