HEADER STRUCTURAL GENOMICS, OXIDOREDUCTASE 11-FEB-03 1NXU
TITLE CRYSTAL STRUCTURE OF E. COLI HYPOTHETICAL OXIDOREDUCTASE
TITLE 2 YIAK NORTHEAST STRUCTURAL GENOMICS CONSORTIUM TARGET ER82.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HYPOTHETICAL OXIDOREDUCTASE YIAK;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 1.1.1.-;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: YIAK OR B3575;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: BL21(DE3)
KEYWDS HYPOTHETICAL PROTEIN, OXIDOREDUCTASE, STRUCTURAL GENOMICS,
KEYWDS 2 PSI, PROTEIN STRUCTURE INITIATIVE, NORTHEAST STRUCTURAL
KEYWDS 3 GENOMICS CONSORTIUM, NESG
EXPDTA X-RAY DIFFRACTION
AUTHOR F.FOROUHAR,I.LEE,J.BENACH,K.KULKARNI,R.XIAO,T.B.ACTON,
AUTHOR 2 R.SHASTRY,B.ROST,G.T.MONTELIONE,L.TONG,NORTHEAST STRUCTURAL
AUTHOR 3 GENOMICS CONSORTIUM (NESG)
REVDAT 4 24-FEB-09 1NXU 1 VERSN
REVDAT 3 25-JAN-05 1NXU 1 AUTHOR KEYWDS REMARK
REVDAT 2 30-MAR-04 1NXU 1 JRNL
REVDAT 1 11-MAR-03 1NXU 0
JRNL AUTH F.FOROUHAR,I.LEE,J.BENACH,K.KULKARNI,R.XIAO,
JRNL AUTH 2 T.B.ACTON,G.T.MONTELIONE,L.TONG
JRNL TITL A NOVEL NAD-BINDING PROTEIN REVEALED BY THE
JRNL TITL 2 CRYSTAL STRUCTURE OF 2,3-DIKETO-L-GULONATE
JRNL TITL 3 REDUCTASE (YIAK).
JRNL REF J.BIOL.CHEM. V. 279 13148 2004
JRNL REFN ISSN 0021-9258
JRNL PMID 14718529
JRNL DOI 10.1074/JBC.M313580200
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.80 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) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.90
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 2419207.770
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 68.1
REMARK 3 NUMBER OF REFLECTIONS : 77015
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) : 0.192
REMARK 3 FREE R VALUE : 0.235
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.800
REMARK 3 FREE R VALUE TEST SET COUNT : 7529
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.003
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) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.91
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 22.30
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3773
REMARK 3 BIN R VALUE (WORKING SET) : 0.2970
REMARK 3 BIN FREE R VALUE : 0.2940
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 9.70
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 407
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.015
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5129
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 20
REMARK 3 SOLVENT ATOMS : 664
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 9.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.30
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -3.21000
REMARK 3 B22 (A**2) : -1.82000
REMARK 3 B33 (A**2) : 5.03000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -7.33000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.21
REMARK 3 ESD FROM SIGMAA (A) : 0.29
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) : 0.25
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.27
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 1.10
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.10
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.79
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) : 1.290 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.940 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.170 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.780 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.43
REMARK 3 BSOL : 87.68
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 : DNA-RNA_REP.PARAM
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : ION.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : DNA-RNA.TOP
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : ION.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1NXU COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-FEB-03.
REMARK 100 THE RCSB ID CODE IS RCSB018329.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X12C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97896, 0.9791, 0.9200
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 : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 106854
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 37.900
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.600
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : 0.07400
REMARK 200 R SYM (I) : 0.08600
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
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: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 35.83
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.93
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M LISO4, 19% PEG 3350, 1MM B-
REMARK 280 NADH, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 302K, PH 7.5
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 25.61450
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: 8150 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24160 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -145.0 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 ALA A 333
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 22 159.33 -47.38
REMARK 500 ASN A 157 68.89 21.09
REMARK 500 ASP A 201 92.84 -52.43
REMARK 500 GLU A 202 59.17 38.11
REMARK 500 TYR A 223 -115.69 54.84
REMARK 500 ASN B 157 72.67 15.62
REMARK 500 ASP B 201 129.40 -34.35
REMARK 500 GLU B 202 42.94 36.96
REMARK 500 ASN B 204 -161.94 -108.13
REMARK 500 LYS B 214 -76.81 -70.04
REMARK 500 ARG B 217 47.57 -83.10
REMARK 500 TYR B 223 -114.97 53.65
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 TYR A 123 0.07 SIDE_CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1001
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1002
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1003
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1004
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: ER82 RELATED DB: TARGETDB
DBREF 1NXU A 1 332 UNP P37672 YIAK_ECOLI 1 332
DBREF 1NXU B 1 332 UNP P37672 YIAK_ECOLI 1 332
SEQADV 1NXU MSE A 1 UNP P37672 MET 1 MODIFIED RESIDUE
SEQADV 1NXU MSE A 32 UNP P37672 MET 32 MODIFIED RESIDUE
SEQADV 1NXU MSE A 93 UNP P37672 MET 93 MODIFIED RESIDUE
SEQADV 1NXU MSE A 94 UNP P37672 MET 94 MODIFIED RESIDUE
SEQADV 1NXU MSE A 118 UNP P37672 MET 118 MODIFIED RESIDUE
SEQADV 1NXU MSE A 144 UNP P37672 MET 144 MODIFIED RESIDUE
SEQADV 1NXU MSE A 170 UNP P37672 MET 170 MODIFIED RESIDUE
SEQADV 1NXU MSE A 173 UNP P37672 MET 173 MODIFIED RESIDUE
SEQADV 1NXU MSE A 175 UNP P37672 MET 175 MODIFIED RESIDUE
SEQADV 1NXU MSE A 177 UNP P37672 MET 177 MODIFIED RESIDUE
SEQADV 1NXU MSE A 182 UNP P37672 MET 182 MODIFIED RESIDUE
SEQADV 1NXU MSE A 221 UNP P37672 MET 221 MODIFIED RESIDUE
SEQADV 1NXU MSE A 229 UNP P37672 MET 229 MODIFIED RESIDUE
SEQADV 1NXU MSE A 235 UNP P37672 MET 235 MODIFIED RESIDUE
SEQADV 1NXU MSE A 285 UNP P37672 MET 285 MODIFIED RESIDUE
SEQADV 1NXU ALA A 333 UNP P37672 CLONING ARTIFACT
SEQADV 1NXU MSE B 1 UNP P37672 MET 1 MODIFIED RESIDUE
SEQADV 1NXU MSE B 32 UNP P37672 MET 32 MODIFIED RESIDUE
SEQADV 1NXU MSE B 93 UNP P37672 MET 93 MODIFIED RESIDUE
SEQADV 1NXU MSE B 94 UNP P37672 MET 94 MODIFIED RESIDUE
SEQADV 1NXU MSE B 118 UNP P37672 MET 118 MODIFIED RESIDUE
SEQADV 1NXU MSE B 144 UNP P37672 MET 144 MODIFIED RESIDUE
SEQADV 1NXU MSE B 170 UNP P37672 MET 170 MODIFIED RESIDUE
SEQADV 1NXU MSE B 173 UNP P37672 MET 173 MODIFIED RESIDUE
SEQADV 1NXU MSE B 175 UNP P37672 MET 175 MODIFIED RESIDUE
SEQADV 1NXU MSE B 177 UNP P37672 MET 177 MODIFIED RESIDUE
SEQADV 1NXU MSE B 182 UNP P37672 MET 182 MODIFIED RESIDUE
SEQADV 1NXU MSE B 221 UNP P37672 MET 221 MODIFIED RESIDUE
SEQADV 1NXU MSE B 229 UNP P37672 MET 229 MODIFIED RESIDUE
SEQADV 1NXU MSE B 235 UNP P37672 MET 235 MODIFIED RESIDUE
SEQADV 1NXU MSE B 285 UNP P37672 MET 285 MODIFIED RESIDUE
SEQADV 1NXU ALA B 333 UNP P37672 CLONING ARTIFACT
SEQRES 1 A 333 MSE LYS VAL THR PHE GLU GLN LEU LYS ALA ALA PHE ASN
SEQRES 2 A 333 ARG VAL LEU ILE SER ARG GLY VAL ASP SER GLU THR ALA
SEQRES 3 A 333 ASP ALA CYS ALA GLU MSE PHE ALA ARG THR THR GLU SER
SEQRES 4 A 333 GLY VAL TYR SER HIS GLY VAL ASN ARG PHE PRO ARG PHE
SEQRES 5 A 333 ILE GLN GLN LEU GLU ASN GLY ASP ILE ILE PRO ASP ALA
SEQRES 6 A 333 GLN PRO LYS ARG ILE THR SER LEU GLY ALA ILE GLU GLN
SEQRES 7 A 333 TRP ASP ALA GLN ARG SER ILE GLY ASN LEU THR ALA LYS
SEQRES 8 A 333 LYS MSE MSE ASP ARG ALA ILE GLU LEU ALA ALA ASP HIS
SEQRES 9 A 333 GLY ILE GLY LEU VAL ALA LEU ARG ASN ALA ASN HIS TRP
SEQRES 10 A 333 MSE ARG GLY GLY SER TYR GLY TRP GLN ALA ALA GLU LYS
SEQRES 11 A 333 GLY TYR ILE GLY ILE CYS TRP THR ASN SER ILE ALA VAL
SEQRES 12 A 333 MSE PRO PRO TRP GLY ALA LYS GLU CYS ARG ILE GLY THR
SEQRES 13 A 333 ASN PRO LEU ILE VAL ALA ILE PRO SER THR PRO ILE THR
SEQRES 14 A 333 MSE VAL ASP MSE SER MSE SER MSE PHE SER TYR GLY MSE
SEQRES 15 A 333 LEU GLU VAL ASN ARG LEU ALA GLY ARG GLN LEU PRO VAL
SEQRES 16 A 333 ASP GLY GLY PHE ASP ASP GLU GLY ASN LEU THR LYS GLU
SEQRES 17 A 333 PRO GLY VAL ILE GLU LYS ASN ARG ARG ILE LEU PRO MSE
SEQRES 18 A 333 GLY TYR TRP LYS GLY SER GLY MSE SER ILE VAL LEU ASP
SEQRES 19 A 333 MSE ILE ALA THR LEU LEU SER ASP GLY ALA SER VAL ALA
SEQRES 20 A 333 GLU VAL THR GLN ASP ASN SER ASP GLU TYR GLY ILE SER
SEQRES 21 A 333 GLN ILE PHE ILE ALA ILE GLU VAL ASP LYS LEU ILE ASP
SEQRES 22 A 333 GLY PRO THR ARG ASP ALA LYS LEU GLN ARG ILE MSE ASP
SEQRES 23 A 333 TYR VAL THR SER ALA GLU ARG ALA ASP GLU ASN GLN ALA
SEQRES 24 A 333 ILE ARG LEU PRO GLY HIS GLU PHE THR THR LEU LEU ALA
SEQRES 25 A 333 GLU ASN ARG ARG ASN GLY ILE THR VAL ASP ASP SER VAL
SEQRES 26 A 333 TRP ALA LYS ILE GLN ALA LEU ALA
SEQRES 1 B 333 MSE LYS VAL THR PHE GLU GLN LEU LYS ALA ALA PHE ASN
SEQRES 2 B 333 ARG VAL LEU ILE SER ARG GLY VAL ASP SER GLU THR ALA
SEQRES 3 B 333 ASP ALA CYS ALA GLU MSE PHE ALA ARG THR THR GLU SER
SEQRES 4 B 333 GLY VAL TYR SER HIS GLY VAL ASN ARG PHE PRO ARG PHE
SEQRES 5 B 333 ILE GLN GLN LEU GLU ASN GLY ASP ILE ILE PRO ASP ALA
SEQRES 6 B 333 GLN PRO LYS ARG ILE THR SER LEU GLY ALA ILE GLU GLN
SEQRES 7 B 333 TRP ASP ALA GLN ARG SER ILE GLY ASN LEU THR ALA LYS
SEQRES 8 B 333 LYS MSE MSE ASP ARG ALA ILE GLU LEU ALA ALA ASP HIS
SEQRES 9 B 333 GLY ILE GLY LEU VAL ALA LEU ARG ASN ALA ASN HIS TRP
SEQRES 10 B 333 MSE ARG GLY GLY SER TYR GLY TRP GLN ALA ALA GLU LYS
SEQRES 11 B 333 GLY TYR ILE GLY ILE CYS TRP THR ASN SER ILE ALA VAL
SEQRES 12 B 333 MSE PRO PRO TRP GLY ALA LYS GLU CYS ARG ILE GLY THR
SEQRES 13 B 333 ASN PRO LEU ILE VAL ALA ILE PRO SER THR PRO ILE THR
SEQRES 14 B 333 MSE VAL ASP MSE SER MSE SER MSE PHE SER TYR GLY MSE
SEQRES 15 B 333 LEU GLU VAL ASN ARG LEU ALA GLY ARG GLN LEU PRO VAL
SEQRES 16 B 333 ASP GLY GLY PHE ASP ASP GLU GLY ASN LEU THR LYS GLU
SEQRES 17 B 333 PRO GLY VAL ILE GLU LYS ASN ARG ARG ILE LEU PRO MSE
SEQRES 18 B 333 GLY TYR TRP LYS GLY SER GLY MSE SER ILE VAL LEU ASP
SEQRES 19 B 333 MSE ILE ALA THR LEU LEU SER ASP GLY ALA SER VAL ALA
SEQRES 20 B 333 GLU VAL THR GLN ASP ASN SER ASP GLU TYR GLY ILE SER
SEQRES 21 B 333 GLN ILE PHE ILE ALA ILE GLU VAL ASP LYS LEU ILE ASP
SEQRES 22 B 333 GLY PRO THR ARG ASP ALA LYS LEU GLN ARG ILE MSE ASP
SEQRES 23 B 333 TYR VAL THR SER ALA GLU ARG ALA ASP GLU ASN GLN ALA
SEQRES 24 B 333 ILE ARG LEU PRO GLY HIS GLU PHE THR THR LEU LEU ALA
SEQRES 25 B 333 GLU ASN ARG ARG ASN GLY ILE THR VAL ASP ASP SER VAL
SEQRES 26 B 333 TRP ALA LYS ILE GLN ALA LEU ALA
MODRES 1NXU MSE A 1 MET SELENOMETHIONINE
MODRES 1NXU MSE A 32 MET SELENOMETHIONINE
MODRES 1NXU MSE A 93 MET SELENOMETHIONINE
MODRES 1NXU MSE A 94 MET SELENOMETHIONINE
MODRES 1NXU MSE A 118 MET SELENOMETHIONINE
MODRES 1NXU MSE A 144 MET SELENOMETHIONINE
MODRES 1NXU MSE A 170 MET SELENOMETHIONINE
MODRES 1NXU MSE A 173 MET SELENOMETHIONINE
MODRES 1NXU MSE A 175 MET SELENOMETHIONINE
MODRES 1NXU MSE A 177 MET SELENOMETHIONINE
MODRES 1NXU MSE A 182 MET SELENOMETHIONINE
MODRES 1NXU MSE A 221 MET SELENOMETHIONINE
MODRES 1NXU MSE A 229 MET SELENOMETHIONINE
MODRES 1NXU MSE A 235 MET SELENOMETHIONINE
MODRES 1NXU MSE A 285 MET SELENOMETHIONINE
MODRES 1NXU MSE B 1 MET SELENOMETHIONINE
MODRES 1NXU MSE B 32 MET SELENOMETHIONINE
MODRES 1NXU MSE B 93 MET SELENOMETHIONINE
MODRES 1NXU MSE B 94 MET SELENOMETHIONINE
MODRES 1NXU MSE B 118 MET SELENOMETHIONINE
MODRES 1NXU MSE B 144 MET SELENOMETHIONINE
MODRES 1NXU MSE B 170 MET SELENOMETHIONINE
MODRES 1NXU MSE B 173 MET SELENOMETHIONINE
MODRES 1NXU MSE B 175 MET SELENOMETHIONINE
MODRES 1NXU MSE B 177 MET SELENOMETHIONINE
MODRES 1NXU MSE B 182 MET SELENOMETHIONINE
MODRES 1NXU MSE B 221 MET SELENOMETHIONINE
MODRES 1NXU MSE B 229 MET SELENOMETHIONINE
MODRES 1NXU MSE B 235 MET SELENOMETHIONINE
MODRES 1NXU MSE B 285 MET SELENOMETHIONINE
HET MSE A 1 8
HET MSE A 32 8
HET MSE A 93 8
HET MSE A 94 8
HET MSE A 118 8
HET MSE A 144 8
HET MSE A 170 8
HET MSE A 173 8
HET MSE A 175 8
HET MSE A 177 8
HET MSE A 182 8
HET MSE A 221 8
HET MSE A 229 8
HET MSE A 235 8
HET MSE A 285 8
HET MSE B 1 8
HET MSE B 32 8
HET MSE B 93 8
HET MSE B 94 8
HET MSE B 118 8
HET MSE B 144 8
HET MSE B 170 8
HET MSE B 173 8
HET MSE B 175 8
HET MSE B 177 8
HET MSE B 182 8
HET MSE B 221 8
HET MSE B 229 8
HET MSE B 235 8
HET MSE B 285 8
HET SO4 A1001 5
HET SO4 A1002 5
HET SO4 B1003 5
HET SO4 B1004 5
HETNAM MSE SELENOMETHIONINE
HETNAM SO4 SULFATE ION
FORMUL 1 MSE 30(C5 H11 N O2 SE)
FORMUL 3 SO4 4(O4 S 2-)
FORMUL 7 HOH *664(H2 O)
HELIX 1 1 THR A 4 ARG A 19 1 16
HELIX 2 2 ASP A 22 SER A 39 1 18
HELIX 3 3 GLY A 45 ASN A 47 5 3
HELIX 4 4 ARG A 48 ASN A 58 1 11
HELIX 5 5 ILE A 85 GLY A 105 1 21
HELIX 6 6 GLY A 120 LYS A 130 1 11
HELIX 7 7 SER A 179 ALA A 189 1 11
HELIX 8 8 GLU A 208 ARG A 216 1 9
HELIX 9 9 TYR A 223 ASP A 242 1 20
HELIX 10 10 SER A 245 ASN A 253 1 9
HELIX 11 11 ASP A 273 SER A 290 1 18
HELIX 12 12 HIS A 305 GLY A 318 1 14
HELIX 13 13 ASP A 322 LEU A 332 1 11
HELIX 14 14 THR B 4 ARG B 19 1 16
HELIX 15 15 ASP B 22 SER B 39 1 18
HELIX 16 16 GLY B 45 ASN B 47 5 3
HELIX 17 17 ARG B 48 ASN B 58 1 11
HELIX 18 18 ILE B 85 GLY B 105 1 21
HELIX 19 19 ARG B 119 LYS B 130 1 12
HELIX 20 20 SER B 179 ALA B 189 1 11
HELIX 21 21 GLU B 208 ARG B 216 1 9
HELIX 22 22 TYR B 223 ASP B 242 1 20
HELIX 23 23 SER B 245 ASP B 252 1 8
HELIX 24 24 ASP B 273 SER B 290 1 18
HELIX 25 25 GLU B 306 GLY B 318 1 13
HELIX 26 26 ASP B 322 LEU B 332 1 11
SHEET 1 A 2 LYS A 2 VAL A 3 0
SHEET 2 A 2 ILE A 319 THR A 320 -1 O ILE A 319 N VAL A 3
SHEET 1 B 7 LYS A 68 LEU A 73 0
SHEET 2 B 7 ILE A 76 ASP A 80 -1 O ASP A 80 N LYS A 68
SHEET 3 B 7 ILE A 106 ALA A 114 1 O ALA A 110 N TRP A 79
SHEET 4 B 7 ILE A 259 ILE A 266 -1 O ILE A 259 N ALA A 114
SHEET 5 B 7 ILE A 133 THR A 138 -1 N ILE A 135 O ILE A 264
SHEET 6 B 7 LEU A 159 ILE A 163 -1 O ILE A 160 N CYS A 136
SHEET 7 B 7 THR A 169 MSE A 173 -1 O THR A 169 N ILE A 163
SHEET 1 C 2 GLY A 198 PHE A 199 0
SHEET 2 C 2 LEU A 205 THR A 206 -1 O THR A 206 N GLY A 198
SHEET 1 D 2 LYS B 2 VAL B 3 0
SHEET 2 D 2 ILE B 319 THR B 320 -1 O ILE B 319 N VAL B 3
SHEET 1 E 7 LYS B 68 LEU B 73 0
SHEET 2 E 7 ILE B 76 ASP B 80 -1 O ILE B 76 N LEU B 73
SHEET 3 E 7 ILE B 106 ALA B 114 1 O ALA B 110 N TRP B 79
SHEET 4 E 7 ILE B 259 GLU B 267 -1 O ILE B 259 N ALA B 114
SHEET 5 E 7 TYR B 132 THR B 138 -1 N ILE B 135 O ILE B 264
SHEET 6 E 7 LEU B 159 ILE B 163 -1 O ALA B 162 N GLY B 134
SHEET 7 E 7 THR B 169 MSE B 173 -1 O THR B 169 N ILE B 163
SHEET 1 F 2 GLY B 198 PHE B 199 0
SHEET 2 F 2 LEU B 205 THR B 206 -1 O THR B 206 N GLY B 198
LINK C MSE A 1 N LYS A 2 1555 1555 1.33
LINK C GLU A 31 N MSE A 32 1555 1555 1.33
LINK C MSE A 32 N PHE A 33 1555 1555 1.33
LINK C LYS A 92 N MSE A 93 1555 1555 1.33
LINK C MSE A 93 N MSE A 94 1555 1555 1.33
LINK C MSE A 94 N ASP A 95 1555 1555 1.33
LINK C TRP A 117 N MSE A 118 1555 1555 1.33
LINK C MSE A 118 N ARG A 119 1555 1555 1.33
LINK C VAL A 143 N MSE A 144 1555 1555 1.34
LINK C MSE A 144 N PRO A 145 1555 1555 1.34
LINK C THR A 169 N MSE A 170 1555 1555 1.33
LINK C MSE A 170 N VAL A 171 1555 1555 1.33
LINK C ASP A 172 N MSE A 173 1555 1555 1.33
LINK C MSE A 173 N SER A 174 1555 1555 1.33
LINK C SER A 174 N MSE A 175 1555 1555 1.33
LINK C MSE A 175 N SER A 176 1555 1555 1.33
LINK C SER A 176 N MSE A 177 1555 1555 1.33
LINK C MSE A 177 N PHE A 178 1555 1555 1.33
LINK C GLY A 181 N MSE A 182 1555 1555 1.33
LINK C MSE A 182 N LEU A 183 1555 1555 1.33
LINK C PRO A 220 N MSE A 221 1555 1555 1.33
LINK C MSE A 221 N GLY A 222 1555 1555 1.33
LINK C GLY A 228 N MSE A 229 1555 1555 1.33
LINK C MSE A 229 N SER A 230 1555 1555 1.33
LINK C ASP A 234 N MSE A 235 1555 1555 1.33
LINK C MSE A 235 N ILE A 236 1555 1555 1.33
LINK C ILE A 284 N MSE A 285 1555 1555 1.33
LINK C MSE A 285 N ASP A 286 1555 1555 1.33
LINK C MSE B 1 N LYS B 2 1555 1555 1.33
LINK C GLU B 31 N MSE B 32 1555 1555 1.33
LINK C MSE B 32 N PHE B 33 1555 1555 1.33
LINK C LYS B 92 N MSE B 93 1555 1555 1.33
LINK C MSE B 93 N MSE B 94 1555 1555 1.33
LINK C MSE B 94 N ASP B 95 1555 1555 1.33
LINK C TRP B 117 N MSE B 118 1555 1555 1.33
LINK C MSE B 118 N ARG B 119 1555 1555 1.33
LINK C VAL B 143 N MSE B 144 1555 1555 1.33
LINK C MSE B 144 N PRO B 145 1555 1555 1.34
LINK C THR B 169 N MSE B 170 1555 1555 1.33
LINK C MSE B 170 N VAL B 171 1555 1555 1.33
LINK C ASP B 172 N MSE B 173 1555 1555 1.33
LINK C MSE B 173 N SER B 174 1555 1555 1.33
LINK C SER B 174 N MSE B 175 1555 1555 1.33
LINK C MSE B 175 N SER B 176 1555 1555 1.33
LINK C SER B 176 N MSE B 177 1555 1555 1.33
LINK C MSE B 177 N PHE B 178 1555 1555 1.33
LINK C GLY B 181 N MSE B 182 1555 1555 1.33
LINK C MSE B 182 N LEU B 183 1555 1555 1.33
LINK C PRO B 220 N MSE B 221 1555 1555 1.32
LINK C MSE B 221 N GLY B 222 1555 1555 1.33
LINK C GLY B 228 N MSE B 229 1555 1555 1.33
LINK C MSE B 229 N SER B 230 1555 1555 1.33
LINK C ASP B 234 N MSE B 235 1555 1555 1.33
LINK C MSE B 235 N ILE B 236 1555 1555 1.33
LINK C ILE B 284 N MSE B 285 1555 1555 1.33
LINK C MSE B 285 N ASP B 286 1555 1555 1.33
CISPEP 1 THR A 166 PRO A 167 0 0.01
CISPEP 2 THR B 166 PRO B 167 0 -0.36
SITE 1 AC1 7 HIS A 44 ARG A 48 TYR A 180 GLY A 181
SITE 2 AC1 7 HOH A1021 HOH A1148 HOH A1164
SITE 1 AC2 10 MSE A 173 SER A 174 PHE A 178 SER A 179
SITE 2 AC2 10 MSE A 182 HOH A1007 HOH A1066 HOH A1067
SITE 3 AC2 10 HOH A1217 LYS B 225
SITE 1 AC3 8 LYS A 225 MSE B 173 SER B 174 PHE B 178
SITE 2 AC3 8 SER B 179 HOH B1092 HOH B1127 HOH B1166
SITE 1 AC4 9 HIS B 44 ARG B 48 TYR B 180 GLY B 181
SITE 2 AC4 9 HOH B1078 HOH B1081 HOH B1083 HOH B1131
SITE 3 AC4 9 HOH B1143
CRYST1 58.012 51.229 108.930 90.00 103.78 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 0.017238 0.000000 0.004228 0.00000
SCALE2 0.000000 0.019520 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009452 0.00000
HETATM 1 N MSE A 1 -24.980 -9.043 -37.499 1.00 47.24 N
HETATM 2 CA MSE A 1 -24.868 -9.648 -38.861 1.00 47.11 C
HETATM 3 C MSE A 1 -23.712 -10.639 -38.888 1.00 45.44 C
HETATM 4 O MSE A 1 -22.552 -10.249 -38.755 1.00 43.81 O
HETATM 5 CB MSE A 1 -24.620 -8.554 -39.904 1.00 49.37 C
HETATM 6 CG MSE A 1 -25.658 -8.480 -41.010 1.00 53.94 C
HETATM 7 SE MSE A 1 -25.725 -10.062 -42.126 1.00 60.44 SE
HETATM 8 CE MSE A 1 -27.140 -11.010 -41.210 1.00 57.91 C
(ATOM LINES ARE NOT SHOWN.)
END
