HEADER UNKNOWN FUNCTION 12-MAR-07 2UVK
TITLE STRUCTURE OF YJHT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: YJHT;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 511693;
SOURCE 4 STRAIN: K12;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET22B
KEYWDS UNKNOWN FUNCTION, HYPOTHETICAL PROTEIN, SIALIC ACID
KEYWDS 2 METABOLISM, KELCH REPEAT, BETA-PROPELLER
EXPDTA X-RAY DIFFRACTION
AUTHOR A.MULLER,E.SEVERI,K.S.WILSON,G.H.THOMAS
REVDAT 3 13-OCT-09 2UVK 1 KEYWDS JRNL REMARK
REVDAT 2 24-FEB-09 2UVK 1 VERSN
REVDAT 1 04-DEC-07 2UVK 0
JRNL AUTH E.SEVERI,A.MULLER,J.R.POTTS,A.LEECH,D.WILLIAMSON,
JRNL AUTH 2 K.S.WILSON,G.H.THOMAS
JRNL TITL SIALIC ACID MUTAROTATION IS CATALYZED BY THE
JRNL TITL 2 ESCHERICHIA COLI BETA-PROPELLER PROTEIN YJHT.
JRNL REF J.BIOL.CHEM. V. 283 4841 2008
JRNL REFN ISSN 0021-9258
JRNL PMID 18063573
JRNL DOI 10.1074/JBC.M707822200
REMARK 2
REMARK 2 RESOLUTION. 1.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 73.13
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 102206
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 + TEST SET) : 0.182
REMARK 3 R VALUE (WORKING SET) : 0.180
REMARK 3 FREE R VALUE : 0.219
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 5376
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.54
REMARK 3 REFLECTION IN BIN (WORKING SET) : 7508
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.49
REMARK 3 BIN R VALUE (WORKING SET) : 0.2200
REMARK 3 BIN FREE R VALUE SET COUNT : 408
REMARK 3 BIN FREE R VALUE : 0.2970
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5245
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 56
REMARK 3 SOLVENT ATOMS : 729
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.98
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.49000
REMARK 3 B22 (A**2) : 0.52000
REMARK 3 B33 (A**2) : -1.04000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.09000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.098
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.082
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.058
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.403
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.964
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.948
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5462 ; 0.011 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 3500 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7455 ; 1.306 ; 1.918
REMARK 3 BOND ANGLES OTHERS (DEGREES): 8547 ; 0.808 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 722 ; 6.147 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 240 ;33.976 ;25.083
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 776 ;11.683 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 8 ;15.971 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 778 ; 0.085 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6407 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1161 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 962 ; 0.194 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 3533 ; 0.190 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2716 ; 0.185 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 2754 ; 0.084 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 515 ; 0.134 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 12 ; 0.241 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 33 ; 0.233 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 21 ; 0.158 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 2UVK COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-OCT-07.
REMARK 100 THE PDBE ID CODE IS EBI-31618.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-JUL-06
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 : ESRF
REMARK 200 BEAMLINE : ID14-4
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9793
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 107873
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.50
REMARK 200 RESOLUTION RANGE LOW (A) : 52.85
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 8.1
REMARK 200 R MERGE (I) : 0.04
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 30.10
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.58
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.3
REMARK 200 DATA REDUNDANCY IN SHELL : 8.2
REMARK 200 R MERGE FOR SHELL (I) : 0.38
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.90
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SHELXC,D,E
REMARK 200 STARTING MODEL: NONE
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.06
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 150 NL OF SEMET-SUBSTITUTED
REMARK 280 YJHT AND 150 NL OF 200 MM SODIUM MALONATE, 0.1M BIS TRIS
REMARK 280 PROPANE PH 7.5 AND 20% W/V PEG 3350
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 52.82950
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 GENERATING THE BIOMOLECULE
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2470 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 26780 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.48 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 GLY A 226
REMARK 465 ASN A 227
REMARK 465 ASN A 228
REMARK 465 ASN A 294
REMARK 465 GLY A 295
REMARK 465 LYS A 296
REMARK 465 LYS A 341
REMARK 465 LEU A 350
REMARK 465 GLU A 351
REMARK 465 HIS A 352
REMARK 465 HIS A 353
REMARK 465 HIS A 354
REMARK 465 HIS A 355
REMARK 465 HIS A 356
REMARK 465 HIS A 357
REMARK 465 LEU B 350
REMARK 465 GLU B 351
REMARK 465 HIS B 352
REMARK 465 HIS B 353
REMARK 465 HIS B 354
REMARK 465 HIS B 355
REMARK 465 HIS B 356
REMARK 465 HIS B 357
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 GLN A 39 CD OE1 NE2
REMARK 470 ASP A 42 CG OD1 OD2
REMARK 470 LYS A 44 CE NZ
REMARK 470 LYS A 90 NZ
REMARK 470 LYS A 94 CD CE NZ
REMARK 470 LYS A 120 CE NZ
REMARK 470 LYS A 144 CD CE NZ
REMARK 470 LYS A 160 CE NZ
REMARK 470 LYS A 199 CD CE NZ
REMARK 470 LYS A 230 CE NZ
REMARK 470 LYS A 233 NZ
REMARK 470 LYS A 274 CE NZ
REMARK 470 LYS A 282 CD CE NZ
REMARK 470 HIS A 293 CG ND1 CD2 CE1 NE2
REMARK 470 SER A 300 OG
REMARK 470 GLU A 302 CG CD OE1 OE2
REMARK 470 LYS A 330 CD CE NZ
REMARK 470 ASP A 342 CB CG OD1 OD2
REMARK 470 ASN A 343 CB CG OD1 ND2
REMARK 470 LYS A 344 CG CD CE NZ
REMARK 470 GLN B 39 CD OE1 NE2
REMARK 470 LYS B 41 CB CG CD CE NZ
REMARK 470 ASP B 42 CG OD1 OD2
REMARK 470 LYS B 44 CE NZ
REMARK 470 LYS B 144 CB CG CD CE NZ
REMARK 470 LYS B 199 CE NZ
REMARK 470 ASN B 252 CG OD1 ND2
REMARK 470 ASP B 253 CB CG OD1 OD2
REMARK 470 LYS B 264 CD CE NZ
REMARK 470 LYS B 274 CD CE NZ
REMARK 470 LYS B 282 CD CE NZ
REMARK 470 HIS B 293 ND1 CD2 CE1 NE2
REMARK 470 LYS B 299 CD CE NZ
REMARK 470 LYS B 341 CB CG CD CE NZ
REMARK 470 ASP B 342 CB CG OD1 OD2
REMARK 470 ASN B 343 CB CG OD1 ND2
REMARK 470 LYS B 344 CG CD CE NZ
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 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 ASN A 19 -104.71 49.11
REMARK 500 TRP A 188 -98.41 -108.47
REMARK 500 ASP A 253 -7.17 73.39
REMARK 500 ASN A 343 -2.05 78.67
REMARK 500 ASN B 19 -99.92 56.86
REMARK 500 ASP B 42 77.31 -106.80
REMARK 500 TRP B 188 -98.93 -113.39
REMARK 500 ASN B 343 48.58 -94.55
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
DBREF 2UVK A 1 349 UNP P39371 YJHT_ECOLI 20 368
DBREF 2UVK A 350 357 PDB 2UVK 2UVK 350 357
DBREF 2UVK B 1 349 UNP P39371 YJHT_ECOLI 20 368
DBREF 2UVK B 350 357 PDB 2UVK 2UVK 350 357
SEQRES 1 A 357 SER VAL LEU PRO GLU THR PRO VAL PRO PHE LYS SER GLY
SEQRES 2 A 357 THR GLY ALA ILE ASP ASN ASP THR VAL TYR ILE GLY LEU
SEQRES 3 A 357 GLY SER ALA GLY THR ALA TRP TYR LYS LEU ASP THR GLN
SEQRES 4 A 357 ALA LYS ASP LYS LYS TRP THR ALA LEU ALA ALA PHE PRO
SEQRES 5 A 357 GLY GLY PRO ARG ASP GLN ALA THR SER ALA PHE ILE ASP
SEQRES 6 A 357 GLY ASN LEU TYR VAL PHE GLY GLY ILE GLY LYS ASN SER
SEQRES 7 A 357 GLU GLY LEU THR GLN VAL PHE ASN ASP VAL HIS LYS TYR
SEQRES 8 A 357 ASN PRO LYS THR ASN SER TRP VAL LYS LEU MSE SER HIS
SEQRES 9 A 357 ALA PRO MSE GLY MSE ALA GLY HIS VAL THR PHE VAL HIS
SEQRES 10 A 357 ASN GLY LYS ALA TYR VAL THR GLY GLY VAL ASN GLN ASN
SEQRES 11 A 357 ILE PHE ASN GLY TYR PHE GLU ASP LEU ASN GLU ALA GLY
SEQRES 12 A 357 LYS ASP SER THR ALA ILE ASP LYS ILE ASN ALA HIS TYR
SEQRES 13 A 357 PHE ASP LYS LYS ALA GLU ASP TYR PHE PHE ASN LYS PHE
SEQRES 14 A 357 LEU LEU SER PHE ASP PRO SER THR GLN GLN TRP SER TYR
SEQRES 15 A 357 ALA GLY GLU SER PRO TRP TYR GLY THR ALA GLY ALA ALA
SEQRES 16 A 357 VAL VAL ASN LYS GLY ASP LYS THR TRP LEU ILE ASN GLY
SEQRES 17 A 357 GLU ALA LYS PRO GLY LEU ARG THR ASP ALA VAL PHE GLU
SEQRES 18 A 357 LEU ASP PHE THR GLY ASN ASN LEU LYS TRP ASN LYS LEU
SEQRES 19 A 357 ALA PRO VAL SER SER PRO ASP GLY VAL ALA GLY GLY PHE
SEQRES 20 A 357 ALA GLY ILE SER ASN ASP SER LEU ILE PHE ALA GLY GLY
SEQRES 21 A 357 ALA GLY PHE LYS GLY SER ARG GLU ASN TYR GLN ASN GLY
SEQRES 22 A 357 LYS ASN TYR ALA HIS GLU GLY LEU LYS LYS SER TYR SER
SEQRES 23 A 357 THR ASP ILE HIS LEU TRP HIS ASN GLY LYS TRP ASP LYS
SEQRES 24 A 357 SER GLY GLU LEU SER GLN GLY ARG ALA TYR GLY VAL SER
SEQRES 25 A 357 LEU PRO TRP ASN ASN SER LEU LEU ILE ILE GLY GLY GLU
SEQRES 26 A 357 THR ALA GLY GLY LYS ALA VAL THR ASP SER VAL LEU ILE
SEQRES 27 A 357 THR VAL LYS ASP ASN LYS VAL THR VAL GLN ASN LEU GLU
SEQRES 28 A 357 HIS HIS HIS HIS HIS HIS
SEQRES 1 B 357 SER VAL LEU PRO GLU THR PRO VAL PRO PHE LYS SER GLY
SEQRES 2 B 357 THR GLY ALA ILE ASP ASN ASP THR VAL TYR ILE GLY LEU
SEQRES 3 B 357 GLY SER ALA GLY THR ALA TRP TYR LYS LEU ASP THR GLN
SEQRES 4 B 357 ALA LYS ASP LYS LYS TRP THR ALA LEU ALA ALA PHE PRO
SEQRES 5 B 357 GLY GLY PRO ARG ASP GLN ALA THR SER ALA PHE ILE ASP
SEQRES 6 B 357 GLY ASN LEU TYR VAL PHE GLY GLY ILE GLY LYS ASN SER
SEQRES 7 B 357 GLU GLY LEU THR GLN VAL PHE ASN ASP VAL HIS LYS TYR
SEQRES 8 B 357 ASN PRO LYS THR ASN SER TRP VAL LYS LEU MSE SER HIS
SEQRES 9 B 357 ALA PRO MSE GLY MSE ALA GLY HIS VAL THR PHE VAL HIS
SEQRES 10 B 357 ASN GLY LYS ALA TYR VAL THR GLY GLY VAL ASN GLN ASN
SEQRES 11 B 357 ILE PHE ASN GLY TYR PHE GLU ASP LEU ASN GLU ALA GLY
SEQRES 12 B 357 LYS ASP SER THR ALA ILE ASP LYS ILE ASN ALA HIS TYR
SEQRES 13 B 357 PHE ASP LYS LYS ALA GLU ASP TYR PHE PHE ASN LYS PHE
SEQRES 14 B 357 LEU LEU SER PHE ASP PRO SER THR GLN GLN TRP SER TYR
SEQRES 15 B 357 ALA GLY GLU SER PRO TRP TYR GLY THR ALA GLY ALA ALA
SEQRES 16 B 357 VAL VAL ASN LYS GLY ASP LYS THR TRP LEU ILE ASN GLY
SEQRES 17 B 357 GLU ALA LYS PRO GLY LEU ARG THR ASP ALA VAL PHE GLU
SEQRES 18 B 357 LEU ASP PHE THR GLY ASN ASN LEU LYS TRP ASN LYS LEU
SEQRES 19 B 357 ALA PRO VAL SER SER PRO ASP GLY VAL ALA GLY GLY PHE
SEQRES 20 B 357 ALA GLY ILE SER ASN ASP SER LEU ILE PHE ALA GLY GLY
SEQRES 21 B 357 ALA GLY PHE LYS GLY SER ARG GLU ASN TYR GLN ASN GLY
SEQRES 22 B 357 LYS ASN TYR ALA HIS GLU GLY LEU LYS LYS SER TYR SER
SEQRES 23 B 357 THR ASP ILE HIS LEU TRP HIS ASN GLY LYS TRP ASP LYS
SEQRES 24 B 357 SER GLY GLU LEU SER GLN GLY ARG ALA TYR GLY VAL SER
SEQRES 25 B 357 LEU PRO TRP ASN ASN SER LEU LEU ILE ILE GLY GLY GLU
SEQRES 26 B 357 THR ALA GLY GLY LYS ALA VAL THR ASP SER VAL LEU ILE
SEQRES 27 B 357 THR VAL LYS ASP ASN LYS VAL THR VAL GLN ASN LEU GLU
SEQRES 28 B 357 HIS HIS HIS HIS HIS HIS
MODRES 2UVK MSE A 102 MET SELENOMETHIONINE
MODRES 2UVK MSE A 107 MET SELENOMETHIONINE
MODRES 2UVK MSE A 109 MET SELENOMETHIONINE
MODRES 2UVK MSE B 102 MET SELENOMETHIONINE
MODRES 2UVK MSE B 107 MET SELENOMETHIONINE
MODRES 2UVK MSE B 109 MET SELENOMETHIONINE
HET MSE A 102 8
HET MSE A 107 8
HET MSE A 109 8
HET MSE B 102 8
HET MSE B 107 16
HET MSE B 109 8
HETNAM MSE SELENOMETHIONINE
FORMUL 3 MSE 6(C5 H11 N O2 SE)
FORMUL 4 HOH *729(H2 O1)
HELIX 1 1 GLY A 27 GLY A 30 5 4
HELIX 2 2 ASN A 128 GLY A 143 1 16
HELIX 3 3 ASP A 145 ASP A 158 1 14
HELIX 4 4 LYS A 160 PHE A 165 5 6
HELIX 5 5 GLY A 265 ASN A 272 1 8
HELIX 6 6 ALA A 327 GLY A 329 5 3
HELIX 7 7 GLY B 27 GLY B 30 5 4
HELIX 8 8 ASN B 128 GLY B 143 1 16
HELIX 9 9 ASP B 145 ASP B 158 1 14
HELIX 10 10 LYS B 160 PHE B 165 5 6
HELIX 11 11 GLY B 265 ASN B 272 1 8
HELIX 12 12 ALA B 327 GLY B 329 5 3
SHEET 1 AA 4 THR A 14 ASP A 18 0
SHEET 2 AA 4 THR A 21 GLY A 25 -1 O THR A 21 N ASP A 18
SHEET 3 AA 4 TRP A 33 ASP A 37 -1 O TYR A 34 N ILE A 24
SHEET 4 AA 4 TRP A 45 ALA A 47 -1 O THR A 46 N LYS A 35
SHEET 1 AB 4 THR A 60 ILE A 64 0
SHEET 2 AB 4 ASN A 67 PHE A 71 -1 O ASN A 67 N ILE A 64
SHEET 3 AB 4 VAL A 88 ASN A 92 -1 O HIS A 89 N VAL A 70
SHEET 4 AB 4 SER A 97 LYS A 100 -1 O SER A 97 N ASN A 92
SHEET 1 AC 2 ILE A 74 LYS A 76 0
SHEET 2 AC 2 THR A 82 VAL A 84 -1 O GLN A 83 N GLY A 75
SHEET 1 AD 4 VAL A 113 HIS A 117 0
SHEET 2 AD 4 LYS A 120 THR A 124 -1 O LYS A 120 N HIS A 117
SHEET 3 AD 4 PHE A 169 PHE A 173 -1 O LEU A 171 N VAL A 123
SHEET 4 AD 4 TRP A 180 GLU A 185 -1 O SER A 181 N SER A 172
SHEET 1 AE 4 ALA A 195 LYS A 199 0
SHEET 2 AE 4 LYS A 202 ILE A 206 -1 O LYS A 202 N LYS A 199
SHEET 3 AE 4 VAL A 219 ASP A 223 -1 O PHE A 220 N LEU A 205
SHEET 4 AE 4 LYS A 230 LYS A 233 -1 O LYS A 230 N ASP A 223
SHEET 1 AF 2 GLU A 209 LYS A 211 0
SHEET 2 AF 2 LEU A 214 ARG A 215 -1 O LEU A 214 N ALA A 210
SHEET 1 AG 4 PHE A 247 SER A 251 0
SHEET 2 AG 4 SER A 254 ALA A 258 -1 O SER A 254 N SER A 251
SHEET 3 AG 4 ASP A 288 LEU A 291 -1 O HIS A 290 N PHE A 257
SHEET 4 AG 4 ASP A 298 GLU A 302 -1 O ASP A 298 N LEU A 291
SHEET 1 AH 2 ALA A 261 GLY A 262 0
SHEET 2 AH 2 SER A 284 TYR A 285 -1 O SER A 284 N GLY A 262
SHEET 1 AI 4 VAL A 311 TRP A 315 0
SHEET 2 AI 4 SER A 318 GLU A 325 -1 O SER A 318 N TRP A 315
SHEET 3 AI 4 ALA A 331 THR A 339 -1 N VAL A 332 O GLY A 324
SHEET 4 AI 4 THR A 346 GLN A 348 -1 O THR A 346 N THR A 339
SHEET 1 BA 4 THR B 14 ASP B 18 0
SHEET 2 BA 4 THR B 21 GLY B 25 -1 O THR B 21 N ASP B 18
SHEET 3 BA 4 TRP B 33 ASP B 37 -1 O TYR B 34 N ILE B 24
SHEET 4 BA 4 THR B 46 ALA B 47 -1 O THR B 46 N LYS B 35
SHEET 1 BB 4 THR B 60 ILE B 64 0
SHEET 2 BB 4 ASN B 67 PHE B 71 -1 O ASN B 67 N ILE B 64
SHEET 3 BB 4 VAL B 88 ASN B 92 -1 O HIS B 89 N VAL B 70
SHEET 4 BB 4 SER B 97 LYS B 100 -1 O SER B 97 N ASN B 92
SHEET 1 BC 2 ILE B 74 LYS B 76 0
SHEET 2 BC 2 THR B 82 VAL B 84 -1 O GLN B 83 N GLY B 75
SHEET 1 BD 4 VAL B 113 HIS B 117 0
SHEET 2 BD 4 LYS B 120 THR B 124 -1 O LYS B 120 N HIS B 117
SHEET 3 BD 4 PHE B 169 PHE B 173 -1 O LEU B 171 N VAL B 123
SHEET 4 BD 4 TRP B 180 GLU B 185 -1 O SER B 181 N SER B 172
SHEET 1 BE 4 ALA B 195 LYS B 199 0
SHEET 2 BE 4 LYS B 202 ILE B 206 -1 O LYS B 202 N LYS B 199
SHEET 3 BE 4 VAL B 219 ASP B 223 -1 O PHE B 220 N LEU B 205
SHEET 4 BE 4 LYS B 230 LYS B 233 -1 O LYS B 230 N ASP B 223
SHEET 1 BF 2 GLU B 209 LYS B 211 0
SHEET 2 BF 2 LEU B 214 ARG B 215 -1 O LEU B 214 N ALA B 210
SHEET 1 BG 4 PHE B 247 SER B 251 0
SHEET 2 BG 4 SER B 254 ALA B 258 -1 O SER B 254 N SER B 251
SHEET 3 BG 4 ASP B 288 HIS B 293 -1 O HIS B 290 N PHE B 257
SHEET 4 BG 4 LYS B 296 GLU B 302 -1 O LYS B 296 N HIS B 293
SHEET 1 BH 2 ALA B 261 GLY B 262 0
SHEET 2 BH 2 SER B 284 TYR B 285 -1 O SER B 284 N GLY B 262
SHEET 1 BI 4 VAL B 311 TRP B 315 0
SHEET 2 BI 4 SER B 318 ILE B 322 -1 O SER B 318 N TRP B 315
SHEET 3 BI 4 SER B 335 LYS B 341 -1 O VAL B 336 N ILE B 321
SHEET 4 BI 4 LYS B 344 GLN B 348 -1 O LYS B 344 N LYS B 341
SHEET 1 BJ 2 GLU B 325 THR B 326 0
SHEET 2 BJ 2 LYS B 330 ALA B 331 -1 O LYS B 330 N THR B 326
LINK C LEU A 101 N MSE A 102 1555 1555 1.33
LINK C MSE A 102 N SER A 103 1555 1555 1.33
LINK C PRO A 106 N MSE A 107 1555 1555 1.32
LINK C MSE A 107 N GLY A 108 1555 1555 1.33
LINK C GLY A 108 N MSE A 109 1555 1555 1.33
LINK C MSE A 109 N ALA A 110 1555 1555 1.34
LINK C LEU B 101 N MSE B 102 1555 1555 1.33
LINK C MSE B 102 N SER B 103 1555 1555 1.33
LINK C PRO B 106 N BMSE B 107 1555 1555 1.33
LINK C PRO B 106 N AMSE B 107 1555 1555 1.33
LINK C AMSE B 107 N GLY B 108 1555 1555 1.33
LINK C BMSE B 107 N GLY B 108 1555 1555 1.33
LINK C GLY B 108 N MSE B 109 1555 1555 1.33
LINK C MSE B 109 N ALA B 110 1555 1555 1.33
CISPEP 1 SER A 239 PRO A 240 0 -1.78
CISPEP 2 SER B 239 PRO B 240 0 3.00
CISPEP 3 ASP B 342 ASN B 343 0 -14.70
CRYST1 44.758 105.659 74.222 90.00 99.95 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 0.022342 0.000000 0.003919 0.00000
SCALE2 0.000000 0.009464 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013679 0.00000
(ATOM LINES ARE NOT SHOWN.)
END