HEADER OXIDOREDUCTASE 19-AUG-08 3E82
TITLE CRYSTAL STRUCTURE OF A PUTATIVE OXIDOREDUCTASE FROM KLEBSIELLA
TITLE 2 PNEUMONIAE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE OXIDOREDUCTASE;
COMPND 3 CHAIN: A, B, D, E;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: KLEBSIELLA PNEUMONIAE SUBSP. PNEUMONIAE MGH
SOURCE 3 78578;
SOURCE 4 ORGANISM_TAXID: 272620;
SOURCE 5 GENE: KPN78578_13420, KPN_01371;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3)-CODON+RIL-STRATAGENE;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: BC-PSGX3(BC), TOP10-INVITROGEN
KEYWDS NAD, GFO/IDH/MOCA FAMILY, PSI-2, NYSGXRC, 11136F, STRUCTURAL
KEYWDS 2 GENOMICS, PROTEIN STRUCTURE INITIATIVE, NEW YORK SGX RESEARCH CENTER
KEYWDS 3 FOR STRUCTURAL GENOMICS, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.ESWARAMOORTHY,M.B.MOHAMMAD,C.A.THOMAS,A.C.BROWN,S.K.BURLEY,
AUTHOR 2 S.SWAMINATHAN,NEW YORK SGX RESEARCH CENTER FOR STRUCTURAL GENOMICS
AUTHOR 3 (NYSGXRC)
REVDAT 3 10-FEB-21 3E82 1 AUTHOR JRNL REMARK LINK
REVDAT 2 24-FEB-09 3E82 1 VERSN
REVDAT 1 26-AUG-08 3E82 0
JRNL AUTH S.ESWARAMOORTHY,M.B.MOHAMMAD,C.A.THOMAS,A.C.BROWN,
JRNL AUTH 2 S.K.BURLEY,S.SWAMINATHAN
JRNL TITL CRYSTAL STRUCTURE OF A PUTATIVE OXIDOREDUCTASE FROM
JRNL TITL 2 KLEBSIELLA PNEUMONIAE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.04 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) : 2.04
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.87
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 94.0
REMARK 3 NUMBER OF REFLECTIONS : 103973
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) : 0.209
REMARK 3 FREE R VALUE : 0.232
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 4166
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.04
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.17
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 88.00
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2470
REMARK 3 BIN FREE R VALUE : 0.2850
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 616
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.012
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 10670
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 4
REMARK 3 SOLVENT ATOMS : 684
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 16.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.90
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.30000
REMARK 3 B22 (A**2) : 4.66000
REMARK 3 B33 (A**2) : -5.96000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 1.39000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.24
REMARK 3 ESD FROM SIGMAA (A) : 0.19
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) : 0.28
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.24
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : ISOTROPIC
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 : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
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 3E82 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-AUG-08.
REMARK 100 THE DEPOSITION ID IS D_1000048992.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-JUN-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
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) : 0.979
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 : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 109371
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.040
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 (%) : 98.8
REMARK 200 DATA REDUNDANCY : 7.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.09600
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.04
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.11
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.1
REMARK 200 DATA REDUNDANCY IN SHELL : 6.60
REMARK 200 R MERGE FOR SHELL (I) : 0.56000
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: SAD
REMARK 200 SOFTWARE USED: SHELX & SHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.85
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.72
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG3350, 0.1M BIS-TRIS, PH 5.5,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, 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,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 39.87500
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/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: 3250 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 27430 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -44.0 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 350
REMARK 350 BIOMOLECULE: 2
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: 3220 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 28470 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -41.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E
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 9
REMARK 465 SER A 10
REMARK 465 LEU A 11
REMARK 465 SER A 12
REMARK 465 ASN A 13
REMARK 465 ASN A 14
REMARK 465 ARG A 171
REMARK 465 VAL A 172
REMARK 465 ARG A 173
REMARK 465 TRP A 174
REMARK 465 ARG A 175
REMARK 465 GLU A 176
REMARK 465 GLN A 177
REMARK 465 ASN A 178
REMARK 465 VAL A 179
REMARK 465 PRO A 180
REMARK 465 GLY A 181
REMARK 465 HIS A 369
REMARK 465 HIS A 370
REMARK 465 HIS A 371
REMARK 465 HIS A 372
REMARK 465 MSE B 9
REMARK 465 SER B 10
REMARK 465 ARG B 171
REMARK 465 VAL B 172
REMARK 465 ARG B 173
REMARK 465 TRP B 174
REMARK 465 ARG B 175
REMARK 465 GLU B 176
REMARK 465 GLN B 177
REMARK 465 ASN B 178
REMARK 465 VAL B 179
REMARK 465 PRO B 180
REMARK 465 GLY B 181
REMARK 465 HIS B 369
REMARK 465 HIS B 370
REMARK 465 HIS B 371
REMARK 465 HIS B 372
REMARK 465 MSE D 9
REMARK 465 SER D 10
REMARK 465 LEU D 11
REMARK 465 SER D 12
REMARK 465 ASN D 13
REMARK 465 ASN D 14
REMARK 465 GLN D 177
REMARK 465 ASN D 178
REMARK 465 VAL D 179
REMARK 465 PRO D 180
REMARK 465 HIS D 369
REMARK 465 HIS D 370
REMARK 465 HIS D 371
REMARK 465 HIS D 372
REMARK 465 MSE E 9
REMARK 465 SER E 10
REMARK 465 LEU E 11
REMARK 465 SER E 12
REMARK 465 VAL E 170
REMARK 465 ARG E 171
REMARK 465 VAL E 172
REMARK 465 ARG E 173
REMARK 465 TRP E 174
REMARK 465 ARG E 175
REMARK 465 GLU E 176
REMARK 465 GLN E 177
REMARK 465 ASN E 178
REMARK 465 VAL E 179
REMARK 465 PRO E 180
REMARK 465 GLY E 181
REMARK 465 HIS E 369
REMARK 465 HIS E 370
REMARK 465 HIS E 371
REMARK 465 HIS E 372
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 ARG E 165 CG CD NE CZ NH1 NH2
REMARK 470 ARG E 167 CG CD NE CZ NH1 NH2
REMARK 470 GLU E 169 CG CD OE1 OE2
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 PHE A 30 -67.66 -105.34
REMARK 500 ASP A 306 96.72 -164.83
REMARK 500 HIS A 367 15.97 -59.60
REMARK 500 PHE B 30 -74.93 -104.55
REMARK 500 LEU B 58 74.38 -117.79
REMARK 500 ASP B 306 95.50 -161.91
REMARK 500 PHE D 30 -66.59 -102.38
REMARK 500 ASP D 75 41.94 -80.86
REMARK 500 ASN D 97 2.23 -68.95
REMARK 500 SER D 294 -3.94 170.20
REMARK 500 LEU D 295 -2.97 60.17
REMARK 500 ASP D 306 92.13 -170.52
REMARK 500 SER D 356 171.66 -52.65
REMARK 500 ASN E 14 52.78 94.86
REMARK 500 PHE E 30 -67.22 -105.86
REMARK 500 ASP E 75 49.88 -104.01
REMARK 500 ASP E 306 93.07 -170.59
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 CL A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 3
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL E 4
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: NYSGXRC-11136F RELATED DB: TARGETDB
DBREF 3E82 A 12 364 UNP A6T882 A6T882_KLEP7 12 364
DBREF 3E82 B 12 364 UNP A6T882 A6T882_KLEP7 12 364
DBREF 3E82 D 12 364 UNP A6T882 A6T882_KLEP7 12 364
DBREF 3E82 E 12 364 UNP A6T882 A6T882_KLEP7 12 364
SEQADV 3E82 MSE A 9 UNP A6T882 EXPRESSION TAG
SEQADV 3E82 SER A 10 UNP A6T882 EXPRESSION TAG
SEQADV 3E82 LEU A 11 UNP A6T882 EXPRESSION TAG
SEQADV 3E82 GLU A 365 UNP A6T882 EXPRESSION TAG
SEQADV 3E82 GLY A 366 UNP A6T882 EXPRESSION TAG
SEQADV 3E82 HIS A 367 UNP A6T882 EXPRESSION TAG
SEQADV 3E82 HIS A 368 UNP A6T882 EXPRESSION TAG
SEQADV 3E82 HIS A 369 UNP A6T882 EXPRESSION TAG
SEQADV 3E82 HIS A 370 UNP A6T882 EXPRESSION TAG
SEQADV 3E82 HIS A 371 UNP A6T882 EXPRESSION TAG
SEQADV 3E82 HIS A 372 UNP A6T882 EXPRESSION TAG
SEQADV 3E82 MSE B 9 UNP A6T882 EXPRESSION TAG
SEQADV 3E82 SER B 10 UNP A6T882 EXPRESSION TAG
SEQADV 3E82 LEU B 11 UNP A6T882 EXPRESSION TAG
SEQADV 3E82 GLU B 365 UNP A6T882 EXPRESSION TAG
SEQADV 3E82 GLY B 366 UNP A6T882 EXPRESSION TAG
SEQADV 3E82 HIS B 367 UNP A6T882 EXPRESSION TAG
SEQADV 3E82 HIS B 368 UNP A6T882 EXPRESSION TAG
SEQADV 3E82 HIS B 369 UNP A6T882 EXPRESSION TAG
SEQADV 3E82 HIS B 370 UNP A6T882 EXPRESSION TAG
SEQADV 3E82 HIS B 371 UNP A6T882 EXPRESSION TAG
SEQADV 3E82 HIS B 372 UNP A6T882 EXPRESSION TAG
SEQADV 3E82 MSE D 9 UNP A6T882 EXPRESSION TAG
SEQADV 3E82 SER D 10 UNP A6T882 EXPRESSION TAG
SEQADV 3E82 LEU D 11 UNP A6T882 EXPRESSION TAG
SEQADV 3E82 GLU D 365 UNP A6T882 EXPRESSION TAG
SEQADV 3E82 GLY D 366 UNP A6T882 EXPRESSION TAG
SEQADV 3E82 HIS D 367 UNP A6T882 EXPRESSION TAG
SEQADV 3E82 HIS D 368 UNP A6T882 EXPRESSION TAG
SEQADV 3E82 HIS D 369 UNP A6T882 EXPRESSION TAG
SEQADV 3E82 HIS D 370 UNP A6T882 EXPRESSION TAG
SEQADV 3E82 HIS D 371 UNP A6T882 EXPRESSION TAG
SEQADV 3E82 HIS D 372 UNP A6T882 EXPRESSION TAG
SEQADV 3E82 MSE E 9 UNP A6T882 EXPRESSION TAG
SEQADV 3E82 SER E 10 UNP A6T882 EXPRESSION TAG
SEQADV 3E82 LEU E 11 UNP A6T882 EXPRESSION TAG
SEQADV 3E82 GLU E 365 UNP A6T882 EXPRESSION TAG
SEQADV 3E82 GLY E 366 UNP A6T882 EXPRESSION TAG
SEQADV 3E82 HIS E 367 UNP A6T882 EXPRESSION TAG
SEQADV 3E82 HIS E 368 UNP A6T882 EXPRESSION TAG
SEQADV 3E82 HIS E 369 UNP A6T882 EXPRESSION TAG
SEQADV 3E82 HIS E 370 UNP A6T882 EXPRESSION TAG
SEQADV 3E82 HIS E 371 UNP A6T882 EXPRESSION TAG
SEQADV 3E82 HIS E 372 UNP A6T882 EXPRESSION TAG
SEQRES 1 A 364 MSE SER LEU SER ASN ASN THR ILE ASN ILE ALA LEU ILE
SEQRES 2 A 364 GLY TYR GLY PHE VAL GLY LYS THR PHE HIS ALA PRO LEU
SEQRES 3 A 364 ILE ARG SER VAL PRO GLY LEU ASN LEU ALA PHE VAL ALA
SEQRES 4 A 364 SER ARG ASP GLU GLU LYS VAL LYS ARG ASP LEU PRO ASP
SEQRES 5 A 364 VAL THR VAL ILE ALA SER PRO GLU ALA ALA VAL GLN HIS
SEQRES 6 A 364 PRO ASP VAL ASP LEU VAL VAL ILE ALA SER PRO ASN ALA
SEQRES 7 A 364 THR HIS ALA PRO LEU ALA ARG LEU ALA LEU ASN ALA GLY
SEQRES 8 A 364 LYS HIS VAL VAL VAL ASP LYS PRO PHE THR LEU ASP MSE
SEQRES 9 A 364 GLN GLU ALA ARG GLU LEU ILE ALA LEU ALA GLU GLU LYS
SEQRES 10 A 364 GLN ARG LEU LEU SER VAL PHE HIS ASN ARG ARG TRP ASP
SEQRES 11 A 364 SER ASP TYR LEU GLY ILE ARG GLN VAL ILE GLU GLN GLY
SEQRES 12 A 364 THR LEU GLY ALA VAL LYS HIS PHE GLU SER HIS PHE ASP
SEQRES 13 A 364 ARG PHE ARG PRO GLU VAL ARG VAL ARG TRP ARG GLU GLN
SEQRES 14 A 364 ASN VAL PRO GLY SER GLY LEU TRP PHE ASP LEU GLY PRO
SEQRES 15 A 364 HIS LEU ILE ASP GLN ALA LEU GLN LEU PHE GLY LEU PRO
SEQRES 16 A 364 GLN SER VAL GLN GLY ASN ILE ALA THR LEU ARG ASP GLY
SEQRES 17 A 364 ALA GLU ILE ASN ASP TRP ALA HIS VAL VAL LEU ASN TYR
SEQRES 18 A 364 PRO ALA HIS LYS VAL ILE LEU HIS CYS SER MSE LEU VAL
SEQRES 19 A 364 ALA GLY GLY SER SER ARG PHE THR VAL HIS GLY ASP LYS
SEQRES 20 A 364 GLY SER VAL ILE LYS ALA ARG ALA ASP GLN GLN GLU SER
SEQRES 21 A 364 GLN LEU LEU ALA GLY VAL VAL PRO GLY SER ALA ASP TRP
SEQRES 22 A 364 GLY GLN ASP ASP ASP PRO LEU VAL ILE TYR ASP ALA SER
SEQRES 23 A 364 LEU GLN ALA HIS ALA GLN ALA THR PRO GLN GLY ASP GLN
SEQRES 24 A 364 ARG GLN TYR TYR MSE LEU ILE ARG ASP ALA LEU LYS GLY
SEQRES 25 A 364 GLN ILE ALA ASN PRO VAL PRO PRO VAL GLU ALA LEU ALA
SEQRES 26 A 364 VAL MSE ALA VAL LEU GLU ALA ALA VAL ARG SER ALA GLU
SEQRES 27 A 364 SER GLY MSE VAL GLN THR LEU ASP LEU SER ASP ASP GLU
SEQRES 28 A 364 ARG ASN THR LEU ARG GLU GLY HIS HIS HIS HIS HIS HIS
SEQRES 1 B 364 MSE SER LEU SER ASN ASN THR ILE ASN ILE ALA LEU ILE
SEQRES 2 B 364 GLY TYR GLY PHE VAL GLY LYS THR PHE HIS ALA PRO LEU
SEQRES 3 B 364 ILE ARG SER VAL PRO GLY LEU ASN LEU ALA PHE VAL ALA
SEQRES 4 B 364 SER ARG ASP GLU GLU LYS VAL LYS ARG ASP LEU PRO ASP
SEQRES 5 B 364 VAL THR VAL ILE ALA SER PRO GLU ALA ALA VAL GLN HIS
SEQRES 6 B 364 PRO ASP VAL ASP LEU VAL VAL ILE ALA SER PRO ASN ALA
SEQRES 7 B 364 THR HIS ALA PRO LEU ALA ARG LEU ALA LEU ASN ALA GLY
SEQRES 8 B 364 LYS HIS VAL VAL VAL ASP LYS PRO PHE THR LEU ASP MSE
SEQRES 9 B 364 GLN GLU ALA ARG GLU LEU ILE ALA LEU ALA GLU GLU LYS
SEQRES 10 B 364 GLN ARG LEU LEU SER VAL PHE HIS ASN ARG ARG TRP ASP
SEQRES 11 B 364 SER ASP TYR LEU GLY ILE ARG GLN VAL ILE GLU GLN GLY
SEQRES 12 B 364 THR LEU GLY ALA VAL LYS HIS PHE GLU SER HIS PHE ASP
SEQRES 13 B 364 ARG PHE ARG PRO GLU VAL ARG VAL ARG TRP ARG GLU GLN
SEQRES 14 B 364 ASN VAL PRO GLY SER GLY LEU TRP PHE ASP LEU GLY PRO
SEQRES 15 B 364 HIS LEU ILE ASP GLN ALA LEU GLN LEU PHE GLY LEU PRO
SEQRES 16 B 364 GLN SER VAL GLN GLY ASN ILE ALA THR LEU ARG ASP GLY
SEQRES 17 B 364 ALA GLU ILE ASN ASP TRP ALA HIS VAL VAL LEU ASN TYR
SEQRES 18 B 364 PRO ALA HIS LYS VAL ILE LEU HIS CYS SER MSE LEU VAL
SEQRES 19 B 364 ALA GLY GLY SER SER ARG PHE THR VAL HIS GLY ASP LYS
SEQRES 20 B 364 GLY SER VAL ILE LYS ALA ARG ALA ASP GLN GLN GLU SER
SEQRES 21 B 364 GLN LEU LEU ALA GLY VAL VAL PRO GLY SER ALA ASP TRP
SEQRES 22 B 364 GLY GLN ASP ASP ASP PRO LEU VAL ILE TYR ASP ALA SER
SEQRES 23 B 364 LEU GLN ALA HIS ALA GLN ALA THR PRO GLN GLY ASP GLN
SEQRES 24 B 364 ARG GLN TYR TYR MSE LEU ILE ARG ASP ALA LEU LYS GLY
SEQRES 25 B 364 GLN ILE ALA ASN PRO VAL PRO PRO VAL GLU ALA LEU ALA
SEQRES 26 B 364 VAL MSE ALA VAL LEU GLU ALA ALA VAL ARG SER ALA GLU
SEQRES 27 B 364 SER GLY MSE VAL GLN THR LEU ASP LEU SER ASP ASP GLU
SEQRES 28 B 364 ARG ASN THR LEU ARG GLU GLY HIS HIS HIS HIS HIS HIS
SEQRES 1 D 364 MSE SER LEU SER ASN ASN THR ILE ASN ILE ALA LEU ILE
SEQRES 2 D 364 GLY TYR GLY PHE VAL GLY LYS THR PHE HIS ALA PRO LEU
SEQRES 3 D 364 ILE ARG SER VAL PRO GLY LEU ASN LEU ALA PHE VAL ALA
SEQRES 4 D 364 SER ARG ASP GLU GLU LYS VAL LYS ARG ASP LEU PRO ASP
SEQRES 5 D 364 VAL THR VAL ILE ALA SER PRO GLU ALA ALA VAL GLN HIS
SEQRES 6 D 364 PRO ASP VAL ASP LEU VAL VAL ILE ALA SER PRO ASN ALA
SEQRES 7 D 364 THR HIS ALA PRO LEU ALA ARG LEU ALA LEU ASN ALA GLY
SEQRES 8 D 364 LYS HIS VAL VAL VAL ASP LYS PRO PHE THR LEU ASP MSE
SEQRES 9 D 364 GLN GLU ALA ARG GLU LEU ILE ALA LEU ALA GLU GLU LYS
SEQRES 10 D 364 GLN ARG LEU LEU SER VAL PHE HIS ASN ARG ARG TRP ASP
SEQRES 11 D 364 SER ASP TYR LEU GLY ILE ARG GLN VAL ILE GLU GLN GLY
SEQRES 12 D 364 THR LEU GLY ALA VAL LYS HIS PHE GLU SER HIS PHE ASP
SEQRES 13 D 364 ARG PHE ARG PRO GLU VAL ARG VAL ARG TRP ARG GLU GLN
SEQRES 14 D 364 ASN VAL PRO GLY SER GLY LEU TRP PHE ASP LEU GLY PRO
SEQRES 15 D 364 HIS LEU ILE ASP GLN ALA LEU GLN LEU PHE GLY LEU PRO
SEQRES 16 D 364 GLN SER VAL GLN GLY ASN ILE ALA THR LEU ARG ASP GLY
SEQRES 17 D 364 ALA GLU ILE ASN ASP TRP ALA HIS VAL VAL LEU ASN TYR
SEQRES 18 D 364 PRO ALA HIS LYS VAL ILE LEU HIS CYS SER MSE LEU VAL
SEQRES 19 D 364 ALA GLY GLY SER SER ARG PHE THR VAL HIS GLY ASP LYS
SEQRES 20 D 364 GLY SER VAL ILE LYS ALA ARG ALA ASP GLN GLN GLU SER
SEQRES 21 D 364 GLN LEU LEU ALA GLY VAL VAL PRO GLY SER ALA ASP TRP
SEQRES 22 D 364 GLY GLN ASP ASP ASP PRO LEU VAL ILE TYR ASP ALA SER
SEQRES 23 D 364 LEU GLN ALA HIS ALA GLN ALA THR PRO GLN GLY ASP GLN
SEQRES 24 D 364 ARG GLN TYR TYR MSE LEU ILE ARG ASP ALA LEU LYS GLY
SEQRES 25 D 364 GLN ILE ALA ASN PRO VAL PRO PRO VAL GLU ALA LEU ALA
SEQRES 26 D 364 VAL MSE ALA VAL LEU GLU ALA ALA VAL ARG SER ALA GLU
SEQRES 27 D 364 SER GLY MSE VAL GLN THR LEU ASP LEU SER ASP ASP GLU
SEQRES 28 D 364 ARG ASN THR LEU ARG GLU GLY HIS HIS HIS HIS HIS HIS
SEQRES 1 E 364 MSE SER LEU SER ASN ASN THR ILE ASN ILE ALA LEU ILE
SEQRES 2 E 364 GLY TYR GLY PHE VAL GLY LYS THR PHE HIS ALA PRO LEU
SEQRES 3 E 364 ILE ARG SER VAL PRO GLY LEU ASN LEU ALA PHE VAL ALA
SEQRES 4 E 364 SER ARG ASP GLU GLU LYS VAL LYS ARG ASP LEU PRO ASP
SEQRES 5 E 364 VAL THR VAL ILE ALA SER PRO GLU ALA ALA VAL GLN HIS
SEQRES 6 E 364 PRO ASP VAL ASP LEU VAL VAL ILE ALA SER PRO ASN ALA
SEQRES 7 E 364 THR HIS ALA PRO LEU ALA ARG LEU ALA LEU ASN ALA GLY
SEQRES 8 E 364 LYS HIS VAL VAL VAL ASP LYS PRO PHE THR LEU ASP MSE
SEQRES 9 E 364 GLN GLU ALA ARG GLU LEU ILE ALA LEU ALA GLU GLU LYS
SEQRES 10 E 364 GLN ARG LEU LEU SER VAL PHE HIS ASN ARG ARG TRP ASP
SEQRES 11 E 364 SER ASP TYR LEU GLY ILE ARG GLN VAL ILE GLU GLN GLY
SEQRES 12 E 364 THR LEU GLY ALA VAL LYS HIS PHE GLU SER HIS PHE ASP
SEQRES 13 E 364 ARG PHE ARG PRO GLU VAL ARG VAL ARG TRP ARG GLU GLN
SEQRES 14 E 364 ASN VAL PRO GLY SER GLY LEU TRP PHE ASP LEU GLY PRO
SEQRES 15 E 364 HIS LEU ILE ASP GLN ALA LEU GLN LEU PHE GLY LEU PRO
SEQRES 16 E 364 GLN SER VAL GLN GLY ASN ILE ALA THR LEU ARG ASP GLY
SEQRES 17 E 364 ALA GLU ILE ASN ASP TRP ALA HIS VAL VAL LEU ASN TYR
SEQRES 18 E 364 PRO ALA HIS LYS VAL ILE LEU HIS CYS SER MSE LEU VAL
SEQRES 19 E 364 ALA GLY GLY SER SER ARG PHE THR VAL HIS GLY ASP LYS
SEQRES 20 E 364 GLY SER VAL ILE LYS ALA ARG ALA ASP GLN GLN GLU SER
SEQRES 21 E 364 GLN LEU LEU ALA GLY VAL VAL PRO GLY SER ALA ASP TRP
SEQRES 22 E 364 GLY GLN ASP ASP ASP PRO LEU VAL ILE TYR ASP ALA SER
SEQRES 23 E 364 LEU GLN ALA HIS ALA GLN ALA THR PRO GLN GLY ASP GLN
SEQRES 24 E 364 ARG GLN TYR TYR MSE LEU ILE ARG ASP ALA LEU LYS GLY
SEQRES 25 E 364 GLN ILE ALA ASN PRO VAL PRO PRO VAL GLU ALA LEU ALA
SEQRES 26 E 364 VAL MSE ALA VAL LEU GLU ALA ALA VAL ARG SER ALA GLU
SEQRES 27 E 364 SER GLY MSE VAL GLN THR LEU ASP LEU SER ASP ASP GLU
SEQRES 28 E 364 ARG ASN THR LEU ARG GLU GLY HIS HIS HIS HIS HIS HIS
MODRES 3E82 MSE A 112 MET SELENOMETHIONINE
MODRES 3E82 MSE A 240 MET SELENOMETHIONINE
MODRES 3E82 MSE A 312 MET SELENOMETHIONINE
MODRES 3E82 MSE A 335 MET SELENOMETHIONINE
MODRES 3E82 MSE A 349 MET SELENOMETHIONINE
MODRES 3E82 MSE B 112 MET SELENOMETHIONINE
MODRES 3E82 MSE B 240 MET SELENOMETHIONINE
MODRES 3E82 MSE B 312 MET SELENOMETHIONINE
MODRES 3E82 MSE B 335 MET SELENOMETHIONINE
MODRES 3E82 MSE B 349 MET SELENOMETHIONINE
MODRES 3E82 MSE D 112 MET SELENOMETHIONINE
MODRES 3E82 MSE D 240 MET SELENOMETHIONINE
MODRES 3E82 MSE D 312 MET SELENOMETHIONINE
MODRES 3E82 MSE D 335 MET SELENOMETHIONINE
MODRES 3E82 MSE D 349 MET SELENOMETHIONINE
MODRES 3E82 MSE E 112 MET SELENOMETHIONINE
MODRES 3E82 MSE E 240 MET SELENOMETHIONINE
MODRES 3E82 MSE E 312 MET SELENOMETHIONINE
MODRES 3E82 MSE E 335 MET SELENOMETHIONINE
MODRES 3E82 MSE E 349 MET SELENOMETHIONINE
HET MSE A 112 8
HET MSE A 240 8
HET MSE A 312 8
HET MSE A 335 8
HET MSE A 349 8
HET MSE B 112 8
HET MSE B 240 8
HET MSE B 312 8
HET MSE B 335 8
HET MSE B 349 8
HET MSE D 112 8
HET MSE D 240 8
HET MSE D 312 8
HET MSE D 335 8
HET MSE D 349 8
HET MSE E 112 8
HET MSE E 240 8
HET MSE E 312 8
HET MSE E 335 8
HET MSE E 349 8
HET CL A 1 1
HET CL B 2 1
HET CL D 3 1
HET CL E 4 1
HETNAM MSE SELENOMETHIONINE
HETNAM CL CHLORIDE ION
FORMUL 1 MSE 20(C5 H11 N O2 SE)
FORMUL 5 CL 4(CL 1-)
FORMUL 9 HOH *684(H2 O)
HELIX 1 1 GLY A 24 PHE A 30 1 7
HELIX 2 2 PHE A 30 SER A 37 1 8
HELIX 3 3 ASP A 50 LEU A 58 1 9
HELIX 4 4 SER A 66 GLN A 72 1 7
HELIX 5 5 PRO A 84 ALA A 86 5 3
HELIX 6 6 THR A 87 ALA A 98 1 12
HELIX 7 7 ASP A 111 LYS A 125 1 15
HELIX 8 8 ASP A 138 GLY A 151 1 14
HELIX 9 9 GLY A 183 GLY A 201 1 19
HELIX 10 10 GLN A 265 GLY A 273 1 9
HELIX 11 11 GLN A 307 LYS A 319 1 13
HELIX 12 12 PRO A 327 GLY A 348 1 22
HELIX 13 13 SER A 356 HIS A 367 1 12
HELIX 14 14 GLY B 24 PHE B 30 1 7
HELIX 15 15 PHE B 30 SER B 37 1 8
HELIX 16 16 ASP B 50 LEU B 58 1 9
HELIX 17 17 SER B 66 HIS B 73 1 8
HELIX 18 18 PRO B 84 ALA B 86 5 3
HELIX 19 19 THR B 87 ALA B 98 1 12
HELIX 20 20 ASP B 111 LYS B 125 1 15
HELIX 21 21 ASP B 138 GLY B 151 1 14
HELIX 22 22 GLY B 183 GLY B 201 1 19
HELIX 23 23 GLN B 265 ALA B 272 1 8
HELIX 24 24 GLN B 307 LYS B 319 1 13
HELIX 25 25 PRO B 327 GLY B 348 1 22
HELIX 26 26 SER B 356 GLU B 365 1 10
HELIX 27 27 GLY D 24 PHE D 30 1 7
HELIX 28 28 PHE D 30 SER D 37 1 8
HELIX 29 29 ASP D 50 LEU D 58 1 9
HELIX 30 30 SER D 66 GLN D 72 1 7
HELIX 31 31 PRO D 84 ALA D 86 5 3
HELIX 32 32 THR D 87 ASN D 97 1 11
HELIX 33 33 ASP D 111 LYS D 125 1 15
HELIX 34 34 ASP D 138 GLN D 150 1 13
HELIX 35 35 GLY D 183 GLY D 201 1 19
HELIX 36 36 GLN D 265 ALA D 272 1 8
HELIX 37 37 GLN D 307 LYS D 319 1 13
HELIX 38 38 PRO D 327 GLY D 348 1 22
HELIX 39 39 SER D 356 HIS D 367 1 12
HELIX 40 40 GLY E 24 PHE E 30 1 7
HELIX 41 41 PHE E 30 SER E 37 1 8
HELIX 42 42 ASP E 50 ARG E 56 1 7
HELIX 43 43 SER E 66 GLN E 72 1 7
HELIX 44 44 PRO E 84 ALA E 86 5 3
HELIX 45 45 THR E 87 ALA E 98 1 12
HELIX 46 46 ASP E 111 LYS E 125 1 15
HELIX 47 47 HIS E 133 TRP E 137 5 5
HELIX 48 48 ASP E 138 GLN E 150 1 13
HELIX 49 49 GLY E 183 GLY E 201 1 19
HELIX 50 50 GLN E 265 GLY E 273 1 9
HELIX 51 51 GLN E 307 LYS E 319 1 13
HELIX 52 52 PRO E 327 GLY E 348 1 22
HELIX 53 53 SER E 356 HIS E 368 1 13
SHEET 1 A 6 THR A 62 ILE A 64 0
SHEET 2 A 6 LEU A 41 ALA A 47 1 N ALA A 44 O THR A 62
SHEET 3 A 6 ILE A 16 ILE A 21 1 N ILE A 16 O ASN A 42
SHEET 4 A 6 LEU A 78 ILE A 81 1 O VAL A 80 N ILE A 21
SHEET 5 A 6 HIS A 101 VAL A 104 1 O HIS A 101 N VAL A 79
SHEET 6 A 6 LEU A 129 VAL A 131 1 O SER A 130 N VAL A 104
SHEET 1 B 8 SER A 205 ALA A 211 0
SHEET 2 B 8 TRP A 222 ASN A 228 -1 O TRP A 222 N ALA A 211
SHEET 3 B 8 LYS A 233 SER A 239 -1 O LEU A 236 N VAL A 225
SHEET 4 B 8 VAL A 156 ASP A 164 1 N PHE A 159 O ILE A 235
SHEET 5 B 8 PHE A 249 GLY A 253 -1 O HIS A 252 N HIS A 158
SHEET 6 B 8 GLY A 256 LYS A 260 -1 O VAL A 258 N VAL A 251
SHEET 7 B 8 LEU A 288 ASP A 292 -1 O TYR A 291 N SER A 257
SHEET 8 B 8 ALA A 297 GLN A 300 -1 O HIS A 298 N ILE A 290
SHEET 1 C 6 THR B 62 ILE B 64 0
SHEET 2 C 6 LEU B 41 ALA B 47 1 N ALA B 44 O THR B 62
SHEET 3 C 6 ILE B 16 ILE B 21 1 N ILE B 18 O ASN B 42
SHEET 4 C 6 LEU B 78 ILE B 81 1 O VAL B 80 N ILE B 21
SHEET 5 C 6 HIS B 101 VAL B 104 1 O HIS B 101 N VAL B 79
SHEET 6 C 6 LEU B 129 VAL B 131 1 O SER B 130 N VAL B 104
SHEET 1 D 8 SER B 205 ALA B 211 0
SHEET 2 D 8 TRP B 222 ASN B 228 -1 O TRP B 222 N ALA B 211
SHEET 3 D 8 LYS B 233 SER B 239 -1 O LEU B 236 N VAL B 225
SHEET 4 D 8 VAL B 156 ASP B 164 1 N PHE B 159 O ILE B 235
SHEET 5 D 8 PHE B 249 GLY B 253 -1 O HIS B 252 N HIS B 158
SHEET 6 D 8 GLY B 256 LYS B 260 -1 O GLY B 256 N GLY B 253
SHEET 7 D 8 LEU B 288 ASP B 292 -1 O TYR B 291 N SER B 257
SHEET 8 D 8 ALA B 297 GLN B 300 -1 O HIS B 298 N ILE B 290
SHEET 1 E 5 LEU D 41 ALA D 47 0
SHEET 2 E 5 ILE D 16 ILE D 21 1 N LEU D 20 O ALA D 47
SHEET 3 E 5 LEU D 78 ILE D 81 1 O VAL D 80 N ILE D 21
SHEET 4 E 5 HIS D 101 VAL D 104 1 O VAL D 103 N ILE D 81
SHEET 5 E 5 LEU D 129 VAL D 131 1 O SER D 130 N VAL D 104
SHEET 1 F 8 SER D 205 ALA D 211 0
SHEET 2 F 8 TRP D 222 TYR D 229 -1 O TRP D 222 N ALA D 211
SHEET 3 F 8 HIS D 232 SER D 239 -1 O LEU D 236 N VAL D 225
SHEET 4 F 8 VAL D 156 ASP D 164 1 N PHE D 159 O ILE D 235
SHEET 5 F 8 PHE D 249 GLY D 253 -1 O THR D 250 N GLU D 160
SHEET 6 F 8 SER D 257 LYS D 260 -1 O LYS D 260 N PHE D 249
SHEET 7 F 8 LEU D 288 TYR D 291 -1 O TYR D 291 N SER D 257
SHEET 8 F 8 ALA D 297 GLN D 300 -1 O GLN D 300 N LEU D 288
SHEET 1 G 6 THR E 62 ILE E 64 0
SHEET 2 G 6 LEU E 41 ALA E 47 1 N VAL E 46 O THR E 62
SHEET 3 G 6 ILE E 16 ILE E 21 1 N ILE E 18 O ASN E 42
SHEET 4 G 6 LEU E 78 ILE E 81 1 O VAL E 80 N ILE E 21
SHEET 5 G 6 HIS E 101 VAL E 104 1 O VAL E 103 N VAL E 79
SHEET 6 G 6 LEU E 129 VAL E 131 1 O SER E 130 N VAL E 104
SHEET 1 H 8 SER E 205 ALA E 211 0
SHEET 2 H 8 TRP E 222 ASN E 228 -1 O VAL E 226 N GLN E 207
SHEET 3 H 8 LYS E 233 SER E 239 -1 O LEU E 236 N VAL E 225
SHEET 4 H 8 VAL E 156 ASP E 164 1 N PHE E 159 O ILE E 235
SHEET 5 H 8 PHE E 249 GLY E 253 -1 O HIS E 252 N HIS E 158
SHEET 6 H 8 SER E 257 LYS E 260 -1 O VAL E 258 N VAL E 251
SHEET 7 H 8 LEU E 288 TYR E 291 -1 O VAL E 289 N ILE E 259
SHEET 8 H 8 ALA E 297 GLN E 300 -1 O GLN E 300 N LEU E 288
LINK C ASP A 111 N MSE A 112 1555 1555 1.33
LINK C MSE A 112 N GLN A 113 1555 1555 1.33
LINK C SER A 239 N MSE A 240 1555 1555 1.33
LINK C MSE A 240 N LEU A 241 1555 1555 1.33
LINK C TYR A 311 N MSE A 312 1555 1555 1.33
LINK C MSE A 312 N LEU A 313 1555 1555 1.33
LINK C VAL A 334 N MSE A 335 1555 1555 1.33
LINK C MSE A 335 N ALA A 336 1555 1555 1.33
LINK C GLY A 348 N MSE A 349 1555 1555 1.33
LINK C MSE A 349 N VAL A 350 1555 1555 1.33
LINK C ASP B 111 N MSE B 112 1555 1555 1.33
LINK C MSE B 112 N GLN B 113 1555 1555 1.33
LINK C SER B 239 N MSE B 240 1555 1555 1.33
LINK C MSE B 240 N LEU B 241 1555 1555 1.33
LINK C TYR B 311 N MSE B 312 1555 1555 1.33
LINK C MSE B 312 N LEU B 313 1555 1555 1.33
LINK C VAL B 334 N MSE B 335 1555 1555 1.33
LINK C MSE B 335 N ALA B 336 1555 1555 1.33
LINK C GLY B 348 N MSE B 349 1555 1555 1.33
LINK C MSE B 349 N VAL B 350 1555 1555 1.34
LINK C ASP D 111 N MSE D 112 1555 1555 1.33
LINK C MSE D 112 N GLN D 113 1555 1555 1.33
LINK C SER D 239 N MSE D 240 1555 1555 1.33
LINK C MSE D 240 N LEU D 241 1555 1555 1.33
LINK C TYR D 311 N MSE D 312 1555 1555 1.33
LINK C MSE D 312 N LEU D 313 1555 1555 1.33
LINK C VAL D 334 N MSE D 335 1555 1555 1.33
LINK C MSE D 335 N ALA D 336 1555 1555 1.33
LINK C GLY D 348 N MSE D 349 1555 1555 1.33
LINK C MSE D 349 N VAL D 350 1555 1555 1.33
LINK C ASP E 111 N MSE E 112 1555 1555 1.33
LINK C MSE E 112 N GLN E 113 1555 1555 1.33
LINK C SER E 239 N MSE E 240 1555 1555 1.33
LINK C MSE E 240 N LEU E 241 1555 1555 1.33
LINK C TYR E 311 N MSE E 312 1555 1555 1.33
LINK C MSE E 312 N LEU E 313 1555 1555 1.33
LINK C VAL E 334 N MSE E 335 1555 1555 1.33
LINK C MSE E 335 N ALA E 336 1555 1555 1.33
LINK C GLY E 348 N MSE E 349 1555 1555 1.33
LINK C MSE E 349 N VAL E 350 1555 1555 1.33
CISPEP 1 LYS A 106 PRO A 107 0 -0.40
CISPEP 2 LYS B 106 PRO B 107 0 -0.93
CISPEP 3 LYS D 106 PRO D 107 0 -0.30
CISPEP 4 LYS E 106 PRO E 107 0 -0.09
SITE 1 AC1 3 LYS A 106 HIS A 133 HIS A 191
SITE 1 AC2 4 LYS B 106 HIS B 133 HIS B 191 HOH B 425
SITE 1 AC3 4 LYS D 106 HIS D 133 HIS D 191 HOH D 392
SITE 1 AC4 4 LYS E 106 HIS E 133 HIS E 191 HOH E 427
CRYST1 52.910 79.750 209.144 90.00 94.00 90.00 P 1 21 1 8
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 0.018900 0.000000 0.001322 0.00000
SCALE2 0.000000 0.012539 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004793 0.00000
(ATOM LINES ARE NOT SHOWN.)
END