HEADER LIPOPROTEIN 07-SEP-07 2R76
TITLE CRYSTAL STRUCTURE OF THE RARE LIPOPROTEIN B (SO_1173) FROM SHEWANELLA
TITLE 2 ONEIDENSIS, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM TARGET SOR91A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RARE LIPOPROTEIN B;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RESIDUES 22-164;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SHEWANELLA ONEIDENSIS;
SOURCE 3 ORGANISM_TAXID: 211586;
SOURCE 4 STRAIN: MR-1;
SOURCE 5 GENE: SO_1173;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)+MAGIC;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR: BL21;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PET21
KEYWDS ALPHA-BETA PROTEIN, STRUCTURAL GENOMICS, PSI-2, PROTEIN STRUCTURE
KEYWDS 2 INITIATIVE, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM, NESG,
KEYWDS 3 LIPOPROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR F.FOROUHAR,Y.CHEN,J.SEETHARAMAN,L.MAO,M.MAGLAQUI,L.A.OWEN,
AUTHOR 2 K.CUNNINGHAM,Y.FANG,R.XIAO,M.C.BARAN,T.B.ACTON,G.T.MONTELIONE,
AUTHOR 3 J.F.HUNT,L.TONG,NORTHEAST STRUCTURAL GENOMICS CONSORTIUM (NESG)
REVDAT 4 25-OCT-17 2R76 1 REMARK
REVDAT 3 13-JUL-11 2R76 1 VERSN
REVDAT 2 24-FEB-09 2R76 1 VERSN
REVDAT 1 25-SEP-07 2R76 0
JRNL AUTH F.FOROUHAR,Y.CHEN,J.SEETHARAMAN,L.MAO,M.MAGLAQUI,L.A.OWEN,
JRNL AUTH 2 K.CUNNINGHAM,Y.FANG,R.XIAO,M.C.BARAN,T.B.ACTON,
JRNL AUTH 3 G.T.MONTELIONE,J.F.HUNT,L.TONG
JRNL TITL CRYSTAL STRUCTURE OF THE RARE LIPOPROTEIN B (SO_1173) FROM
JRNL TITL 2 SHEWANELLA ONEIDENSIS.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.2
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) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 423135.090
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 91.1
REMARK 3 NUMBER OF REFLECTIONS : 23459
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) : 0.247
REMARK 3 FREE R VALUE : 0.293
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.400
REMARK 3 FREE R VALUE TEST SET COUNT : 2196
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.006
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 10
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.69
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 66.80
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1574
REMARK 3 BIN R VALUE (WORKING SET) : 0.2810
REMARK 3 BIN FREE R VALUE : 0.3670
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 9.30
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 162
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.029
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2103
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 38
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 44.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 55.70
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 10.88000
REMARK 3 B22 (A**2) : 10.88000
REMARK 3 B33 (A**2) : -21.76000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.37
REMARK 3 ESD FROM SIGMAA (A) : 0.36
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) : 0.48
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.53
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 1.200
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.80
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.840
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : OVERALL
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 : 0.35
REMARK 3 BSOL : 42.05
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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2R76 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-SEP-07.
REMARK 100 THE DEPOSITION ID IS D_1000044509.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-AUG-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X4C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97893
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25394
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 200 DATA REDUNDANCY : 14.60
REMARK 200 R MERGE (I) : 0.07600
REMARK 200 R SYM (I) : 0.06300
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 40.7200
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 (%) : 99.0
REMARK 200 DATA REDUNDANCY IN SHELL : 13.80
REMARK 200 R MERGE FOR SHELL (I) : 0.42400
REMARK 200 R SYM FOR SHELL (I) : 0.36400
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SNB, RESOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.58
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.04
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN SOLUTION: 10 MM TRIS-HCL PH
REMARK 280 7.5, 100 MM NACL, 5 MM DTT. RESERVOIR SOLUTION: 0.1 M SODIUM
REMARK 280 ACETATE PH 4.6, 15% PEG 20000, MICROBATCH UNDER OIL, TEMPERATURE
REMARK 280 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 56.11750
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 44.04550
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 44.04550
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 84.17625
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 44.04550
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 44.04550
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 28.05875
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 44.04550
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 44.04550
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 84.17625
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 44.04550
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 44.04550
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 28.05875
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 56.11750
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
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: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
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; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MSE A 21
REMARK 465 GLY A 22
REMARK 465 PHE A 23
REMARK 465 LYS A 24
REMARK 465 LEU A 25
REMARK 465 GLN A 26
REMARK 465 ARG A 27
REMARK 465 SER A 28
REMARK 465 TYR A 29
REMARK 465 GLN A 30
REMARK 465 ILE A 31
REMARK 465 PRO A 32
REMARK 465 GLU A 33
REMARK 465 GLN A 34
REMARK 465 LEU A 35
REMARK 465 HIS A 168
REMARK 465 HIS A 169
REMARK 465 HIS A 170
REMARK 465 HIS A 171
REMARK 465 HIS A 172
REMARK 465 MSE B 21
REMARK 465 GLY B 22
REMARK 465 PHE B 23
REMARK 465 LYS B 24
REMARK 465 LEU B 25
REMARK 465 GLN B 26
REMARK 465 ARG B 27
REMARK 465 SER B 28
REMARK 465 TYR B 29
REMARK 465 GLN B 30
REMARK 465 ILE B 31
REMARK 465 PRO B 32
REMARK 465 GLU B 33
REMARK 465 GLN B 34
REMARK 465 LEU B 35
REMARK 465 LEU B 165
REMARK 465 GLU B 166
REMARK 465 HIS B 167
REMARK 465 HIS B 168
REMARK 465 HIS B 169
REMARK 465 HIS B 170
REMARK 465 HIS B 171
REMARK 465 HIS B 172
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 ASP A 44 79.83 -158.90
REMARK 500 ALA A 67 50.89 34.68
REMARK 500 ARG A 130 -179.29 -52.91
REMARK 500 GLU A 166 2.95 -65.03
REMARK 500 LEU B 59 -7.84 -58.50
REMARK 500 TYR B 89 152.87 -49.30
REMARK 500 ALA B 95 -84.67 -68.20
REMARK 500 ARG B 130 -170.65 -58.73
REMARK 500 ALA B 132 20.35 -69.83
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: SOR91A RELATED DB: TARGETDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE N-TERMINAL 21 AMINO ACIDS HAVE BEEN DELETED.
REMARK 999 SERINE-47 HAS BEEN MODELED AS LYSINE-47 IN THE
REMARK 999 STURCTURE BASED ON UNAMBIGUOUS ELECTRON DENSITY.
REMARK 999 THIS MUTATION MIGHT OCCUR DURING CLONING.
DBREF 2R76 A 22 164 UNP Q8EHP5 Q8EHP5_SHEON 22 164
DBREF 2R76 B 22 164 UNP Q8EHP5 Q8EHP5_SHEON 22 164
SEQADV 2R76 MSE A 21 UNP Q8EHP5 EXPRESSION TAG
SEQADV 2R76 LYS A 47 UNP Q8EHP5 SER 47 SEE REMARK 999
SEQADV 2R76 LEU A 165 UNP Q8EHP5 EXPRESSION TAG
SEQADV 2R76 GLU A 166 UNP Q8EHP5 EXPRESSION TAG
SEQADV 2R76 HIS A 167 UNP Q8EHP5 EXPRESSION TAG
SEQADV 2R76 HIS A 168 UNP Q8EHP5 EXPRESSION TAG
SEQADV 2R76 HIS A 169 UNP Q8EHP5 EXPRESSION TAG
SEQADV 2R76 HIS A 170 UNP Q8EHP5 EXPRESSION TAG
SEQADV 2R76 HIS A 171 UNP Q8EHP5 EXPRESSION TAG
SEQADV 2R76 HIS A 172 UNP Q8EHP5 EXPRESSION TAG
SEQADV 2R76 MSE B 21 UNP Q8EHP5 EXPRESSION TAG
SEQADV 2R76 LYS B 47 UNP Q8EHP5 SER 47 SEE REMARK 999
SEQADV 2R76 LEU B 165 UNP Q8EHP5 EXPRESSION TAG
SEQADV 2R76 GLU B 166 UNP Q8EHP5 EXPRESSION TAG
SEQADV 2R76 HIS B 167 UNP Q8EHP5 EXPRESSION TAG
SEQADV 2R76 HIS B 168 UNP Q8EHP5 EXPRESSION TAG
SEQADV 2R76 HIS B 169 UNP Q8EHP5 EXPRESSION TAG
SEQADV 2R76 HIS B 170 UNP Q8EHP5 EXPRESSION TAG
SEQADV 2R76 HIS B 171 UNP Q8EHP5 EXPRESSION TAG
SEQADV 2R76 HIS B 172 UNP Q8EHP5 EXPRESSION TAG
SEQRES 1 A 152 MSE GLY PHE LYS LEU GLN ARG SER TYR GLN ILE PRO GLU
SEQRES 2 A 152 GLN LEU ASN GLN LEU SER LEU SER SER SER ASP GLU TYR
SEQRES 3 A 152 LYS GLU LEU THR ARG LEU VAL ARG GLU ARG LEU ARG LEU
SEQRES 4 A 152 ASN ASN VAL LYS ILE VAL ASP ALA ALA ASN ASP VAL PRO
SEQRES 5 A 152 VAL LEU ARG LEU ILE THR ASP SER LEU GLU ARG SER THR
SEQRES 6 A 152 LEU SER LEU TYR PRO THR GLY ASN VAL ALA GLU TYR GLU
SEQRES 7 A 152 LEU ILE TYR PHE VAL GLU PHE ALA VAL ALA LEU PRO GLY
SEQRES 8 A 152 LYS GLU ALA GLN PRO PHE LYS ILE GLU ILE ARG ARG ASP
SEQRES 9 A 152 TYR LEU ASP ASP PRO ARG THR ALA LEU ALA LYS SER ARG
SEQRES 10 A 152 GLU MSE GLU LEU LEU VAL LYS GLU MSE ARG ILE GLN ALA
SEQRES 11 A 152 ALA ASP ARG ILE LEU GLN SER MSE ALA SER THR GLU VAL
SEQRES 12 A 152 ASN LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 152 MSE GLY PHE LYS LEU GLN ARG SER TYR GLN ILE PRO GLU
SEQRES 2 B 152 GLN LEU ASN GLN LEU SER LEU SER SER SER ASP GLU TYR
SEQRES 3 B 152 LYS GLU LEU THR ARG LEU VAL ARG GLU ARG LEU ARG LEU
SEQRES 4 B 152 ASN ASN VAL LYS ILE VAL ASP ALA ALA ASN ASP VAL PRO
SEQRES 5 B 152 VAL LEU ARG LEU ILE THR ASP SER LEU GLU ARG SER THR
SEQRES 6 B 152 LEU SER LEU TYR PRO THR GLY ASN VAL ALA GLU TYR GLU
SEQRES 7 B 152 LEU ILE TYR PHE VAL GLU PHE ALA VAL ALA LEU PRO GLY
SEQRES 8 B 152 LYS GLU ALA GLN PRO PHE LYS ILE GLU ILE ARG ARG ASP
SEQRES 9 B 152 TYR LEU ASP ASP PRO ARG THR ALA LEU ALA LYS SER ARG
SEQRES 10 B 152 GLU MSE GLU LEU LEU VAL LYS GLU MSE ARG ILE GLN ALA
SEQRES 11 B 152 ALA ASP ARG ILE LEU GLN SER MSE ALA SER THR GLU VAL
SEQRES 12 B 152 ASN LEU GLU HIS HIS HIS HIS HIS HIS
MODRES 2R76 MSE A 139 MET SELENOMETHIONINE
MODRES 2R76 MSE A 146 MET SELENOMETHIONINE
MODRES 2R76 MSE A 158 MET SELENOMETHIONINE
MODRES 2R76 MSE B 139 MET SELENOMETHIONINE
MODRES 2R76 MSE B 146 MET SELENOMETHIONINE
MODRES 2R76 MSE B 158 MET SELENOMETHIONINE
HET MSE A 139 8
HET MSE A 146 8
HET MSE A 158 8
HET MSE B 139 8
HET MSE B 146 8
HET MSE B 158 8
HETNAM MSE SELENOMETHIONINE
FORMUL 1 MSE 6(C5 H11 N O2 SE)
FORMUL 3 HOH *38(H2 O)
HELIX 1 1 LYS A 47 ASN A 60 1 14
HELIX 2 2 THR A 131 GLU A 166 1 36
HELIX 3 3 LYS B 47 LEU B 59 1 13
HELIX 4 4 LEU B 133 ASN B 164 1 32
SHEET 1 A 8 LYS A 63 ILE A 64 0
SHEET 2 A 8 GLN A 37 SER A 42 1 N LEU A 38 O LYS A 63
SHEET 3 A 8 VAL A 73 LEU A 88 1 O LEU A 76 N SER A 41
SHEET 4 A 8 VAL A 94 ALA A 108 -1 O GLU A 96 N LEU A 86
SHEET 5 A 8 GLN A 115 LEU A 126 -1 O ARG A 123 N LEU A 99
SHEET 6 A 8 VAL B 73 LEU B 88 -1 O ARG B 83 N GLU A 120
SHEET 7 A 8 GLN B 37 SER B 42 1 N SER B 41 O LEU B 76
SHEET 8 A 8 LYS B 63 ILE B 64 1 O LYS B 63 N LEU B 38
SHEET 1 B 8 LYS A 63 ILE A 64 0
SHEET 2 B 8 GLN A 37 SER A 42 1 N LEU A 38 O LYS A 63
SHEET 3 B 8 VAL A 73 LEU A 88 1 O LEU A 76 N SER A 41
SHEET 4 B 8 VAL A 94 ALA A 108 -1 O GLU A 96 N LEU A 86
SHEET 5 B 8 GLN A 115 LEU A 126 -1 O ARG A 123 N LEU A 99
SHEET 6 B 8 VAL B 73 LEU B 88 -1 O ARG B 83 N GLU A 120
SHEET 7 B 8 VAL B 94 ALA B 108 -1 O PHE B 102 N SER B 80
SHEET 8 B 8 GLN B 115 LEU B 126 -1 O ARG B 123 N LEU B 99
LINK C GLU A 138 N MSE A 139 1555 1555 1.32
LINK C MSE A 139 N GLU A 140 1555 1555 1.33
LINK C GLU A 145 N MSE A 146 1555 1555 1.33
LINK C MSE A 146 N ARG A 147 1555 1555 1.33
LINK C SER A 157 N MSE A 158 1555 1555 1.33
LINK C MSE A 158 N ALA A 159 1555 1555 1.33
LINK C GLU B 138 N MSE B 139 1555 1555 1.33
LINK C MSE B 139 N GLU B 140 1555 1555 1.32
LINK C GLU B 145 N MSE B 146 1555 1555 1.33
LINK C MSE B 146 N ARG B 147 1555 1555 1.33
LINK C SER B 157 N MSE B 158 1555 1555 1.33
LINK C MSE B 158 N ALA B 159 1555 1555 1.33
CRYST1 88.091 88.091 112.235 90.00 90.00 90.00 P 43 21 2 16
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 0.011352 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011352 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008910 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
