HEADER OXIDOREDUCTASE 03-OCT-05 2B6M
TITLE STRUCTURE OF THE DSBA MUTANT (P31A-C33A)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THIOL:DISULFIDE INTERCHANGE PROTEIN DSBA;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: DSBA;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: DSBA, DSF, PPFA;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS DISULFIDE; THIOREDOXIN; THIOL-OXIDASE, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.VIVES,A.ROYANT,L.SERRE
REVDAT 4 03-APR-24 2B6M 1 REMARK
REVDAT 3 20-OCT-21 2B6M 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2B6M 1 VERSN
REVDAT 1 17-OCT-06 2B6M 0
JRNL AUTH C.VIVES,A.ROYANT,L.SERRE
JRNL TITL STRUCTURE OF THE DSBA MUTANT
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.65 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) : 2.65
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.00
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) (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 11601
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) : 0.240
REMARK 3 FREE R VALUE : 0.258
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 582
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) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2877
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 14
REMARK 3 SOLVENT ATOMS : 10
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 78.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 8.13800
REMARK 3 B22 (A**2) : 8.13800
REMARK 3 B33 (A**2) : -16.27700
REMARK 3 B12 (A**2) : -2.60500
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) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.274
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
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: STRONG NCS RESTRAIN WAS APPLIED
REMARK 4
REMARK 4 2B6M COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-NOV-05.
REMARK 100 THE DEPOSITION ID IS D_1000034739.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-APR-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : BM30A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97951
REMARK 200 MONOCHROMATOR : MIRROR
REMARK 200 OPTICS : MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA, CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 11635
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.650
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 5.600
REMARK 200 R MERGE (I) : 0.07400
REMARK 200 R SYM (I) : 0.06700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.65
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.79
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.40
REMARK 200 R MERGE FOR SHELL (I) : 0.54900
REMARK 200 R SYM FOR SHELL (I) : 0.49600
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: REDUCED WILD TYPE DSBA
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.70
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, AMMONIUM PHOSPHATE, PH 8.2,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 76.02533
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 38.01267
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 300 REMARK: BIOLOGICAL ASSEMBLY CONSISTS IN ONE MONOMER
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
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 ALA A 1
REMARK 465 LYS A 189
REMARK 465 LYS B 189
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 GLU A 4 CG CD OE1 OE2
REMARK 470 LYS A 7 CG CD CE NZ
REMARK 470 HIS A 32 CB CG ND1 CD2 CE1 NE2
REMARK 470 LYS A 47 CG CD CE NZ
REMARK 470 GLU A 52 CG CD OE1 OE2
REMARK 470 LYS A 55 CG CD CE NZ
REMARK 470 GLU A 120 CG CD OE1 OE2
REMARK 470 LYS A 132 CG CD CE NZ
REMARK 470 GLU B 4 CG CD OE1 OE2
REMARK 470 LYS B 7 CG CD CE NZ
REMARK 470 HIS B 32 CB CG ND1 CD2 CE1 NE2
REMARK 470 LYS B 47 CG CD CE NZ
REMARK 470 GLU B 52 CG CD OE1 OE2
REMARK 470 LYS B 55 CG CD CE NZ
REMARK 470 GLU B 120 CG CD OE1 OE2
REMARK 470 LYS B 132 CG CD CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O PHE A 63 O PHE B 63 2.18
REMARK 500
REMARK 500 REMARK: NULL
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 5 97.65 -57.14
REMARK 500 LYS A 7 -92.22 -99.93
REMARK 500 TYR A 9 -159.99 -152.93
REMARK 500 PHE A 36 -18.61 -39.78
REMARK 500 VAL A 39 -42.39 -139.64
REMARK 500 GLU A 52 96.43 -47.38
REMARK 500 PHE A 63 -101.76 -66.37
REMARK 500 LYS A 87 -37.76 -172.12
REMARK 500 LYS A 98 -74.27 -84.75
REMARK 500 ASN A 114 3.92 -65.17
REMARK 500 ASN A 156 21.32 45.85
REMARK 500 ASN A 170 128.18 171.49
REMARK 500 LEU A 185 -15.79 -45.66
REMARK 500 GLN B 2 -45.65 -164.83
REMARK 500 ASP B 5 106.10 -50.72
REMARK 500 LYS B 7 -95.40 -101.56
REMARK 500 PHE B 36 -18.56 -41.21
REMARK 500 HIS B 41 27.41 42.49
REMARK 500 LYS B 48 -71.36 -63.82
REMARK 500 PRO B 51 172.41 -51.73
REMARK 500 PHE B 63 -101.33 -66.51
REMARK 500 LYS B 87 -37.73 -172.20
REMARK 500 LYS B 98 -74.14 -84.90
REMARK 500 ASN B 114 4.28 -64.60
REMARK 500 ASN B 156 21.25 45.94
REMARK 500 ASN B 170 128.16 171.96
REMARK 500 LEU B 185 -15.53 -46.46
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 PEG A 190
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 191
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1DSB RELATED DB: PDB
REMARK 900 WILD TYPE DSBA
REMARK 900 RELATED ID: 1TI1 RELATED DB: PDB
REMARK 900 DSBA MUTANT C33A
REMARK 900 RELATED ID: 1U3A RELATED DB: PDB
REMARK 900 DSBA MUTANT C33A
REMARK 900 RELATED ID: 2B3S RELATED DB: PDB
REMARK 900 DSBA MUTANT P31G/C33A
DBREF 2B6M A 1 189 UNP P0AEG4 DSBA_ECOLI 20 208
DBREF 2B6M B 1 189 UNP P0AEG4 DSBA_ECOLI 20 208
SEQADV 2B6M ALA A 31 UNP P0AEG4 PRO 50 ENGINEERED MUTATION
SEQADV 2B6M ALA A 33 UNP P0AEG4 CYS 52 ENGINEERED MUTATION
SEQADV 2B6M ALA B 31 UNP P0AEG4 PRO 50 ENGINEERED MUTATION
SEQADV 2B6M ALA B 33 UNP P0AEG4 CYS 52 ENGINEERED MUTATION
SEQRES 1 A 189 ALA GLN TYR GLU ASP GLY LYS GLN TYR THR THR LEU GLU
SEQRES 2 A 189 LYS PRO VAL ALA GLY ALA PRO GLN VAL LEU GLU PHE PHE
SEQRES 3 A 189 SER PHE PHE CYS ALA HIS ALA TYR GLN PHE GLU GLU VAL
SEQRES 4 A 189 LEU HIS ILE SER ASP ASN VAL LYS LYS LYS LEU PRO GLU
SEQRES 5 A 189 GLY VAL LYS MET THR LYS TYR HIS VAL ASN PHE MET GLY
SEQRES 6 A 189 GLY ASP LEU GLY LYS ASP LEU THR GLN ALA TRP ALA VAL
SEQRES 7 A 189 ALA MET ALA LEU GLY VAL GLU ASP LYS VAL THR VAL PRO
SEQRES 8 A 189 LEU PHE GLU GLY VAL GLN LYS THR GLN THR ILE ARG SER
SEQRES 9 A 189 ALA SER ASP ILE ARG ASP VAL PHE ILE ASN ALA GLY ILE
SEQRES 10 A 189 LYS GLY GLU GLU TYR ASP ALA ALA TRP ASN SER PHE VAL
SEQRES 11 A 189 VAL LYS SER LEU VAL ALA GLN GLN GLU LYS ALA ALA ALA
SEQRES 12 A 189 ASP VAL GLN LEU ARG GLY VAL PRO ALA MET PHE VAL ASN
SEQRES 13 A 189 GLY LYS TYR GLN LEU ASN PRO GLN GLY MET ASP THR SER
SEQRES 14 A 189 ASN MET ASP VAL PHE VAL GLN GLN TYR ALA ASP THR VAL
SEQRES 15 A 189 LYS TYR LEU SER GLU LYS LYS
SEQRES 1 B 189 ALA GLN TYR GLU ASP GLY LYS GLN TYR THR THR LEU GLU
SEQRES 2 B 189 LYS PRO VAL ALA GLY ALA PRO GLN VAL LEU GLU PHE PHE
SEQRES 3 B 189 SER PHE PHE CYS ALA HIS ALA TYR GLN PHE GLU GLU VAL
SEQRES 4 B 189 LEU HIS ILE SER ASP ASN VAL LYS LYS LYS LEU PRO GLU
SEQRES 5 B 189 GLY VAL LYS MET THR LYS TYR HIS VAL ASN PHE MET GLY
SEQRES 6 B 189 GLY ASP LEU GLY LYS ASP LEU THR GLN ALA TRP ALA VAL
SEQRES 7 B 189 ALA MET ALA LEU GLY VAL GLU ASP LYS VAL THR VAL PRO
SEQRES 8 B 189 LEU PHE GLU GLY VAL GLN LYS THR GLN THR ILE ARG SER
SEQRES 9 B 189 ALA SER ASP ILE ARG ASP VAL PHE ILE ASN ALA GLY ILE
SEQRES 10 B 189 LYS GLY GLU GLU TYR ASP ALA ALA TRP ASN SER PHE VAL
SEQRES 11 B 189 VAL LYS SER LEU VAL ALA GLN GLN GLU LYS ALA ALA ALA
SEQRES 12 B 189 ASP VAL GLN LEU ARG GLY VAL PRO ALA MET PHE VAL ASN
SEQRES 13 B 189 GLY LYS TYR GLN LEU ASN PRO GLN GLY MET ASP THR SER
SEQRES 14 B 189 ASN MET ASP VAL PHE VAL GLN GLN TYR ALA ASP THR VAL
SEQRES 15 B 189 LYS TYR LEU SER GLU LYS LYS
HET PEG A 190 7
HET PEG A 191 7
HETNAM PEG DI(HYDROXYETHYL)ETHER
FORMUL 3 PEG 2(C4 H10 O3)
FORMUL 5 HOH *10(H2 O)
HELIX 1 1 ALA A 31 VAL A 39 1 9
HELIX 2 2 HIS A 41 LYS A 49 1 9
HELIX 3 3 GLY A 66 GLY A 83 1 18
HELIX 4 4 VAL A 84 GLN A 97 1 14
HELIX 5 5 SER A 104 ASN A 114 1 11
HELIX 6 6 LYS A 118 ASN A 127 1 10
HELIX 7 7 SER A 128 VAL A 145 1 18
HELIX 8 8 ASN A 162 MET A 166 5 5
HELIX 9 9 ASN A 170 LEU A 185 1 16
HELIX 10 10 TYR B 34 VAL B 39 1 6
HELIX 11 11 HIS B 41 LEU B 50 1 10
HELIX 12 12 GLY B 66 GLY B 83 1 18
HELIX 13 13 VAL B 84 GLN B 97 1 14
HELIX 14 14 SER B 104 ASN B 114 1 11
HELIX 15 15 LYS B 118 ASN B 127 1 10
HELIX 16 16 SER B 128 VAL B 145 1 18
HELIX 17 17 ASN B 162 MET B 166 5 5
HELIX 18 18 ASN B 170 LEU B 185 1 16
SHEET 1 A 4 MET A 56 HIS A 60 0
SHEET 2 A 4 VAL A 22 PHE A 26 1 N GLU A 24 O THR A 57
SHEET 3 A 4 ALA A 152 VAL A 155 -1 O ALA A 152 N PHE A 25
SHEET 4 A 4 TYR A 159 GLN A 160 -1 O TYR A 159 N VAL A 155
SHEET 1 B 4 MET B 56 HIS B 60 0
SHEET 2 B 4 VAL B 22 PHE B 26 1 N GLU B 24 O THR B 57
SHEET 3 B 4 ALA B 152 VAL B 155 -1 O ALA B 152 N PHE B 25
SHEET 4 B 4 TYR B 159 GLN B 160 -1 O TYR B 159 N VAL B 155
SSBOND 1 CYS A 30 CYS B 30 1555 1555 2.06
CISPEP 1 VAL A 150 PRO A 151 0 -0.43
CISPEP 2 VAL B 150 PRO B 151 0 -0.50
SITE 1 AC1 4 ALA A 31 GLN A 35 THR B 168 MET B 171
SITE 1 AC2 4 THR A 168 MET A 171 ALA B 31 GLN B 35
CRYST1 56.047 56.047 114.038 90.00 90.00 120.00 P 32 6
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 0.017842 0.010301 0.000000 0.00000
SCALE2 0.000000 0.020602 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008769 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
