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HEADER STRUCTURAL PROTEIN 30-JUL-07 2QS9
TITLE CRYSTAL STRUCTURE OF THE HUMAN RETINOBLASTOMA-BINDING
TITLE 2 PROTEIN 9 (RBBP-9). NESG TARGET HR2978
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RETINOBLASTOMA-BINDING PROTEIN 9;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: RBBP-9, RETINOBLASTOMA-BINDING PROTEIN 10, RBBP-
COMPND 5 10, B5T OVEREXPRESSED GENE PROTEIN, BOG PROTEIN;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 GENE: RBBP9, BOG, RBBP10;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: BACTERIA;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)+MAGIC;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET21-23C
KEYWDS RETINOBLASTOMA-BINDING PROTEIN 9, RETINOBLASTOMA-BINDING
KEYWDS 2 PROTEIN 10, B5T OVEREXPRESSED GENE PROTEIN, BOG, RBBP9,
KEYWDS 3 RBBP10, HR2978, NESG, STRUCTURAL GENOMICS, PSI-2, PROTEIN
KEYWDS 4 STRUCTURE INITIATIVE, NORTHEAST STRUCTURAL GENOMICS
KEYWDS 5 CONSORTIUM, ALTERNATIVE SPLICING, CYTOPLASM, NUCLEUS,
KEYWDS 6 PHOSPHORYLATION, STRUCTURAL PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR S.M.VOROBIEV,M.SU,J.SEETHARAMAN,A.KUZIN,C.X.CHEN,
AUTHOR 2 K.CUNNINGHAM,L.OWENS,M.MAGLAQUI,R.XIAO,T.B.ACTON,
AUTHOR 3 G.T.MONTELIONE,J.F.HUNT,L.TONG,NORTHEAST STRUCTURAL
AUTHOR 4 GENOMICS CONSORTIUM (NESG)
REVDAT 1 14-AUG-07 2QS9 0
JRNL AUTH S.M.VOROBIEV,M.SU,J.SEETHARAMAN,A.KUZIN,C.X.CHEN,
JRNL AUTH 2 K.CUNNINGHAM,L.OWENS,R.XIAO,T.B.ACTON,
JRNL AUTH 3 G.T.MONTELIONE,J.F.HUNT,L.TONG
JRNL TITL CRYSTAL STRUCTURE OF THE HUMAN
JRNL TITL 2 RETINOBLASTOMA-BINDING PROTEIN 9 (RBBP-9).
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.72 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 : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.72
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.96
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 208046.590
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 96.5
REMARK 3 NUMBER OF REFLECTIONS : 67213
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) : 0.183
REMARK 3 FREE R VALUE : 0.203
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2691
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.004
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) : 1.72
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.83
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 89.30
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 9988
REMARK 3 BIN R VALUE (WORKING SET) : 0.2020
REMARK 3 BIN FREE R VALUE : 0.2330
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.10
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 422
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.011
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2963
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 414
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 11.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 12.90
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.40000
REMARK 3 B22 (A**2) : -0.34000
REMARK 3 B33 (A**2) : 0.74000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.88000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.17
REMARK 3 ESD FROM SIGMAA (A) : 0.05
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) : 0.20
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.08
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 1.30
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.60
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.85
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 : 0.36
REMARK 3 BSOL : 58.57
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_REP.PARAM
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : ION.TOP
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE FRIEDEL PAIRS WERE USED FOR
REMARK 3 PHASING
REMARK 4
REMARK 4 2QS9 COMPLIES WITH FORMAT V. 3.1, 1-AUG-2007
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB.
REMARK 100 THE RCSB ID CODE IS RCSB043990.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-JUN-2007
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 5.00
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X4A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97913
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 67796
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.720
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 (%) : 96.7
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : 0.04600
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 25.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.72
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.78
REMARK 200 COMPLETENESS FOR SHELL (%) : 85.5
REMARK 200 DATA REDUNDANCY IN SHELL : 2.80
REMARK 200 R MERGE FOR SHELL (I) : 0.08200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 14.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SHELX D/E, SOLVE, RESOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: THE STRUCTURE FACTOR FILE CONTAINS FRIEDEL PAIRS
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 35.43
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.90
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 40% PEG 4000, 0.1M MAGNESIUM
REMARK 280 NITRATE, 0.1M SODIUM ACETATE PH 5.0, MICROBATCH UNDER OIL,
REMARK 280 TEMPERATURE 291K
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,1/2+Y,-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 65.17000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND 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: MONOMER
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMER
REMARK 350 SOFTWARE USED: PISA
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMER
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMER
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSEQI
REMARK 465 MSE A 1
REMARK 465 ALA A 2
REMARK 465 MSE B 1
REMARK 465 ALA B 2
REMARK 465 LYS B 183
REMARK 465 VAL B 184
REMARK 465 PRO B 185
REMARK 465 ALA B 186
REMARK 465 LEU B 187
REMARK 465 GLU B 188
REMARK 465 HIS B 189
REMARK 465 HIS B 190
REMARK 465 HIS B 191
REMARK 465 HIS B 192
REMARK 465 HIS B 193
REMARK 465 HIS B 194
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 SER A 3 OG
REMARK 470 LYS A 183 CG CD CE NZ
REMARK 470 GLU A 188 CG CD OE1 OE2
REMARK 470 HIS A 194 CG ND1 CD2 CE1 NE2
REMARK 470 SER B 3 OG
REMARK 470 ARG B 109 CG CD NE CZ NH1 NH2
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 SER A 75 -111.44 56.08
REMARK 500 SER A 97 61.85 60.85
REMARK 500 PHE A 171 69.32 -158.67
REMARK 500 VAL A 184 73.11 55.28
REMARK 500 SER B 75 -111.98 57.22
REMARK 500 SER B 97 61.46 62.47
REMARK 500 LEU B 103 18.02 58.01
REMARK 500 PHE B 171 69.33 -155.89
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HR2978 RELATED DB: TARGETDB
DBREF 2QS9 A 1 186 UNP O75884 RBBP9_HUMAN 1 186
DBREF 2QS9 B 1 186 UNP O75884 RBBP9_HUMAN 1 186
SEQADV 2QS9 LEU A 187 UNP O75884 EXPRESSION TAG
SEQADV 2QS9 GLU A 188 UNP O75884 EXPRESSION TAG
SEQADV 2QS9 HIS A 189 UNP O75884 EXPRESSION TAG
SEQADV 2QS9 HIS A 190 UNP O75884 EXPRESSION TAG
SEQADV 2QS9 HIS A 191 UNP O75884 EXPRESSION TAG
SEQADV 2QS9 HIS A 192 UNP O75884 EXPRESSION TAG
SEQADV 2QS9 HIS A 193 UNP O75884 EXPRESSION TAG
SEQADV 2QS9 HIS A 194 UNP O75884 EXPRESSION TAG
SEQADV 2QS9 LEU B 187 UNP O75884 EXPRESSION TAG
SEQADV 2QS9 GLU B 188 UNP O75884 EXPRESSION TAG
SEQADV 2QS9 HIS B 189 UNP O75884 EXPRESSION TAG
SEQADV 2QS9 HIS B 190 UNP O75884 EXPRESSION TAG
SEQADV 2QS9 HIS B 191 UNP O75884 EXPRESSION TAG
SEQADV 2QS9 HIS B 192 UNP O75884 EXPRESSION TAG
SEQADV 2QS9 HIS B 193 UNP O75884 EXPRESSION TAG
SEQADV 2QS9 HIS B 194 UNP O75884 EXPRESSION TAG
SEQRES 1 A 194 MSE ALA SER PRO SER LYS ALA VAL ILE VAL PRO GLY ASN
SEQRES 2 A 194 GLY GLY GLY ASP VAL THR THR HIS GLY TRP TYR GLY TRP
SEQRES 3 A 194 VAL LYS LYS GLU LEU GLU LYS ILE PRO GLY PHE GLN CYS
SEQRES 4 A 194 LEU ALA LYS ASN MSE PRO ASP PRO ILE THR ALA ARG GLU
SEQRES 5 A 194 SER ILE TRP LEU PRO PHE MSE GLU THR GLU LEU HIS CYS
SEQRES 6 A 194 ASP GLU LYS THR ILE ILE ILE GLY HIS SER SER GLY ALA
SEQRES 7 A 194 ILE ALA ALA MSE ARG TYR ALA GLU THR HIS ARG VAL TYR
SEQRES 8 A 194 ALA ILE VAL LEU VAL SER ALA TYR THR SER ASP LEU GLY
SEQRES 9 A 194 ASP GLU ASN GLU ARG ALA SER GLY TYR PHE THR ARG PRO
SEQRES 10 A 194 TRP GLN TRP GLU LYS ILE LYS ALA ASN CYS PRO TYR ILE
SEQRES 11 A 194 VAL GLN PHE GLY SER THR ASP ASP PRO PHE LEU PRO TRP
SEQRES 12 A 194 LYS GLU GLN GLN GLU VAL ALA ASP ARG LEU GLU THR LYS
SEQRES 13 A 194 LEU HIS LYS PHE THR ASP CYS GLY HIS PHE GLN ASN THR
SEQRES 14 A 194 GLU PHE HIS GLU LEU ILE THR VAL VAL LYS SER LEU LEU
SEQRES 15 A 194 LYS VAL PRO ALA LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 194 MSE ALA SER PRO SER LYS ALA VAL ILE VAL PRO GLY ASN
SEQRES 2 B 194 GLY GLY GLY ASP VAL THR THR HIS GLY TRP TYR GLY TRP
SEQRES 3 B 194 VAL LYS LYS GLU LEU GLU LYS ILE PRO GLY PHE GLN CYS
SEQRES 4 B 194 LEU ALA LYS ASN MSE PRO ASP PRO ILE THR ALA ARG GLU
SEQRES 5 B 194 SER ILE TRP LEU PRO PHE MSE GLU THR GLU LEU HIS CYS
SEQRES 6 B 194 ASP GLU LYS THR ILE ILE ILE GLY HIS SER SER GLY ALA
SEQRES 7 B 194 ILE ALA ALA MSE ARG TYR ALA GLU THR HIS ARG VAL TYR
SEQRES 8 B 194 ALA ILE VAL LEU VAL SER ALA TYR THR SER ASP LEU GLY
SEQRES 9 B 194 ASP GLU ASN GLU ARG ALA SER GLY TYR PHE THR ARG PRO
SEQRES 10 B 194 TRP GLN TRP GLU LYS ILE LYS ALA ASN CYS PRO TYR ILE
SEQRES 11 B 194 VAL GLN PHE GLY SER THR ASP ASP PRO PHE LEU PRO TRP
SEQRES 12 B 194 LYS GLU GLN GLN GLU VAL ALA ASP ARG LEU GLU THR LYS
SEQRES 13 B 194 LEU HIS LYS PHE THR ASP CYS GLY HIS PHE GLN ASN THR
SEQRES 14 B 194 GLU PHE HIS GLU LEU ILE THR VAL VAL LYS SER LEU LEU
SEQRES 15 B 194 LYS VAL PRO ALA LEU GLU HIS HIS HIS HIS HIS HIS
MODRES 2QS9 MSE A 44 MET SELENOMETHIONINE
MODRES 2QS9 MSE A 59 MET SELENOMETHIONINE
MODRES 2QS9 MSE A 82 MET SELENOMETHIONINE
MODRES 2QS9 MSE B 44 MET SELENOMETHIONINE
MODRES 2QS9 MSE B 59 MET SELENOMETHIONINE
MODRES 2QS9 MSE B 82 MET SELENOMETHIONINE
HET MSE A 44 8
HET MSE A 59 8
HET MSE A 82 8
HET MSE B 44 8
HET MSE B 59 8
HET MSE B 82 8
HETNAM MSE SELENOMETHIONINE
FORMUL 1 MSE 6(C5 H11 N O2 SE)
FORMUL 3 HOH *414(H2 O)
HELIX 1 1 TRP A 23 GLU A 32 1 10
HELIX 2 2 ARG A 51 GLU A 62 1 12
HELIX 3 3 SER A 75 HIS A 88 1 14
HELIX 4 4 ASP A 105 SER A 111 1 7
HELIX 5 5 GLN A 119 CYS A 127 1 9
HELIX 6 6 PRO A 142 GLU A 154 1 13
HELIX 7 7 PHE A 171 LYS A 183 1 13
HELIX 8 8 TRP B 23 GLU B 32 1 10
HELIX 9 9 ARG B 51 GLU B 62 1 12
HELIX 10 10 SER B 75 ALA B 85 1 11
HELIX 11 11 ASP B 105 SER B 111 1 7
HELIX 12 12 GLN B 119 CYS B 127 1 9
HELIX 13 13 PRO B 142 GLU B 154 1 13
HELIX 14 14 PHE B 171 LEU B 182 1 12
SHEET 1 A 6 CYS A 39 ALA A 41 0
SHEET 2 A 6 LYS A 6 VAL A 10 1 N ILE A 9 O LEU A 40
SHEET 3 A 6 THR A 69 HIS A 74 1 O ILE A 72 N VAL A 8
SHEET 4 A 6 ALA A 92 VAL A 96 1 O VAL A 94 N ILE A 71
SHEET 5 A 6 TYR A 129 SER A 135 1 O PHE A 133 N LEU A 95
SHEET 6 A 6 LYS A 156 PHE A 160 1 O HIS A 158 N GLN A 132
SHEET 1 B 6 GLN B 38 LEU B 40 0
SHEET 2 B 6 LYS B 6 VAL B 10 1 N ILE B 9 O LEU B 40
SHEET 3 B 6 THR B 69 HIS B 74 1 O ILE B 72 N VAL B 8
SHEET 4 B 6 ALA B 92 VAL B 96 1 O VAL B 94 N ILE B 71
SHEET 5 B 6 TYR B 129 SER B 135 1 O PHE B 133 N LEU B 95
SHEET 6 B 6 LYS B 156 PHE B 160 1 O HIS B 158 N GLN B 132
CRYST1 37.081 130.340 39.047 90.00 115.87 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 0.026968 0.000000 0.013075 0.00000
SCALE2 0.000000 0.007672 0.000000 0.00000
SCALE3 0.000000 0.000000 0.028462 0.00000
TER 1532 HIS A 194
TER 2965 LEU B 182
MASTER 283 0 6 14 12 0 0 6 3377 2 48 30
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