HEADER OXIDOREDUCTASE 17-SEP-01 1JZO
TITLE DSBC C101S
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THIOL:DISULFIDE INTERCHANGE PROTEIN DSBC;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: DSBC;
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: DSBC;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21 DE3;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PPROEX HT
KEYWDS DISULFIDE BOND ISOMERASE, THIOL OXIDOREDUCTASE, DSBC, THIOREDOXIN
KEYWDS 2 FOLD, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.W.HAEBEL,D.GOLDSTONE,F.KATZEN,J.BECKWITH,P.METCALF
REVDAT 4 16-AUG-23 1JZO 1 REMARK
REVDAT 3 27-OCT-21 1JZO 1 SEQADV
REVDAT 2 24-FEB-09 1JZO 1 VERSN
REVDAT 1 08-MAR-03 1JZO 0
JRNL AUTH P.W.HAEBEL,D.GOLDSTONE,F.KATZEN,J.BECKWITH,P.METCALF
JRNL TITL THE DISULFIDE BOND ISOMERASE DSBC IS ACTIVATED BY AN
JRNL TITL 2 IMMUNOGLOBULIN-FOLD THIOL OXIDOREDUCTASE: CRYSTAL STRUCTURE
JRNL TITL 3 OF THE DSBC-DSBDALPHA COMPLEX.
JRNL REF EMBO J. V. 21 4774 2002
JRNL REFN ISSN 0261-4189
JRNL PMID 12234918
JRNL DOI 10.1093/EMBOJ/CDF489
REMARK 2
REMARK 2 RESOLUTION. 1.92 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
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) : 1.92
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 32.69
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 382422.570
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 95.5
REMARK 3 NUMBER OF REFLECTIONS : 33417
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) : 0.220
REMARK 3 FREE R VALUE : 0.246
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1660
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.006
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.02
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 71.60
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 4005
REMARK 3 BIN R VALUE (WORKING SET) : 0.2530
REMARK 3 BIN FREE R VALUE : 0.2540
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.90
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 205
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.018
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3270
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 247
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 25.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 33.60
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -5.86000
REMARK 3 B22 (A**2) : 7.27000
REMARK 3 B33 (A**2) : -1.41000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.23
REMARK 3 ESD FROM SIGMAA (A) : 0.16
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) : 0.26
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.14
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 1.200
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.10
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.780
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) : 1.460 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.270 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.190 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.260 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.41
REMARK 3 BSOL : 88.94
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 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 PARAMETER FILE 4 : NULL
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 1JZO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-SEP-01.
REMARK 100 THE DEPOSITION ID IS D_1000014376.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-JAN-01
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 9.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL9-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.98
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 : 34245
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.04000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 28.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.02
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.2
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.42000
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB CODE: 1EEJ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.02
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.37
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG550 MME, TRIS, PH 9.0, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-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 29.70000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 47.79350
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 39.14700
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 47.79350
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 29.70000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 39.14700
REMARK 290 SMTRY3 4 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: 1780 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20710 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 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 LYS A 216
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 18 140.02 167.14
REMARK 500 GLN A 85 74.57 -107.91
REMARK 500 GLU A 86 108.11 -58.57
REMARK 500 ASP A 129 66.15 -107.74
REMARK 500 CYS A 163 -172.06 -174.34
REMARK 500 SER A 180 -62.81 -108.04
REMARK 500 MET A 212 44.78 -99.95
REMARK 500 THR A 213 -34.80 -146.89
REMARK 500 ASP B 129 -10.39 77.18
REMARK 500 ALA B 159 96.65 -60.08
REMARK 500 PRO B 160 168.44 -47.42
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1EEJ RELATED DB: PDB
REMARK 900 RELATED ID: 1JZD RELATED DB: PDB
DBREF 1JZO A 1 216 UNP P21892 DSBC_ECOLI 21 236
DBREF 1JZO B 1 216 UNP P21892 DSBC_ECOLI 21 236
SEQADV 1JZO SER A 101 UNP P21892 CYS 121 ENGINEERED MUTATION
SEQADV 1JZO SER B 101 UNP P21892 CYS 121 ENGINEERED MUTATION
SEQRES 1 A 216 ASP ASP ALA ALA ILE GLN GLN THR LEU ALA LYS MET GLY
SEQRES 2 A 216 ILE LYS SER SER ASP ILE GLN PRO ALA PRO VAL ALA GLY
SEQRES 3 A 216 MET LYS THR VAL LEU THR ASN SER GLY VAL LEU TYR ILE
SEQRES 4 A 216 THR ASP ASP GLY LYS HIS ILE ILE GLN GLY PRO MET TYR
SEQRES 5 A 216 ASP VAL SER GLY THR ALA PRO VAL ASN VAL THR ASN LYS
SEQRES 6 A 216 MET LEU LEU LYS GLN LEU ASN ALA LEU GLU LYS GLU MET
SEQRES 7 A 216 ILE VAL TYR LYS ALA PRO GLN GLU LYS HIS VAL ILE THR
SEQRES 8 A 216 VAL PHE THR ASP ILE THR CYS GLY TYR SER HIS LYS LEU
SEQRES 9 A 216 HIS GLU GLN MET ALA ASP TYR ASN ALA LEU GLY ILE THR
SEQRES 10 A 216 VAL ARG TYR LEU ALA PHE PRO ARG GLN GLY LEU ASP SER
SEQRES 11 A 216 ASP ALA GLU LYS GLU MET LYS ALA ILE TRP CYS ALA LYS
SEQRES 12 A 216 ASP LYS ASN LYS ALA PHE ASP ASP VAL MET ALA GLY LYS
SEQRES 13 A 216 SER VAL ALA PRO ALA SER CYS ASP VAL ASP ILE ALA ASP
SEQRES 14 A 216 HIS TYR ALA LEU GLY VAL GLN LEU GLY VAL SER GLY THR
SEQRES 15 A 216 PRO ALA VAL VAL LEU SER ASN GLY THR LEU VAL PRO GLY
SEQRES 16 A 216 TYR GLN PRO PRO LYS GLU MET LYS GLU PHE LEU ASP GLU
SEQRES 17 A 216 HIS GLN LYS MET THR SER GLY LYS
SEQRES 1 B 216 ASP ASP ALA ALA ILE GLN GLN THR LEU ALA LYS MET GLY
SEQRES 2 B 216 ILE LYS SER SER ASP ILE GLN PRO ALA PRO VAL ALA GLY
SEQRES 3 B 216 MET LYS THR VAL LEU THR ASN SER GLY VAL LEU TYR ILE
SEQRES 4 B 216 THR ASP ASP GLY LYS HIS ILE ILE GLN GLY PRO MET TYR
SEQRES 5 B 216 ASP VAL SER GLY THR ALA PRO VAL ASN VAL THR ASN LYS
SEQRES 6 B 216 MET LEU LEU LYS GLN LEU ASN ALA LEU GLU LYS GLU MET
SEQRES 7 B 216 ILE VAL TYR LYS ALA PRO GLN GLU LYS HIS VAL ILE THR
SEQRES 8 B 216 VAL PHE THR ASP ILE THR CYS GLY TYR SER HIS LYS LEU
SEQRES 9 B 216 HIS GLU GLN MET ALA ASP TYR ASN ALA LEU GLY ILE THR
SEQRES 10 B 216 VAL ARG TYR LEU ALA PHE PRO ARG GLN GLY LEU ASP SER
SEQRES 11 B 216 ASP ALA GLU LYS GLU MET LYS ALA ILE TRP CYS ALA LYS
SEQRES 12 B 216 ASP LYS ASN LYS ALA PHE ASP ASP VAL MET ALA GLY LYS
SEQRES 13 B 216 SER VAL ALA PRO ALA SER CYS ASP VAL ASP ILE ALA ASP
SEQRES 14 B 216 HIS TYR ALA LEU GLY VAL GLN LEU GLY VAL SER GLY THR
SEQRES 15 B 216 PRO ALA VAL VAL LEU SER ASN GLY THR LEU VAL PRO GLY
SEQRES 16 B 216 TYR GLN PRO PRO LYS GLU MET LYS GLU PHE LEU ASP GLU
SEQRES 17 B 216 HIS GLN LYS MET THR SER GLY LYS
FORMUL 3 HOH *247(H2 O)
HELIX 1 1 ASP A 1 MET A 12 1 12
HELIX 2 2 VAL A 62 ALA A 73 1 12
HELIX 3 3 LEU A 74 MET A 78 5 5
HELIX 4 4 CYS A 98 GLN A 107 1 10
HELIX 5 5 GLN A 107 LEU A 114 1 8
HELIX 6 6 SER A 130 CYS A 141 1 12
HELIX 7 7 ASP A 144 ALA A 154 1 11
HELIX 8 8 ASP A 166 GLY A 178 1 13
HELIX 9 9 PRO A 198 GLY A 215 1 18
HELIX 10 10 ASP B 1 LYS B 11 1 11
HELIX 11 11 VAL B 62 LEU B 74 1 13
HELIX 12 12 GLU B 75 MET B 78 5 4
HELIX 13 13 CYS B 98 GLN B 107 1 10
HELIX 14 14 GLN B 107 LEU B 114 1 8
HELIX 15 15 SER B 130 CYS B 141 1 12
HELIX 16 16 ASP B 144 ALA B 154 1 11
HELIX 17 17 ASP B 166 GLY B 178 1 13
HELIX 18 18 PRO B 198 GLY B 215 1 18
SHEET 1 A 6 SER A 16 PRO A 21 0
SHEET 2 A 6 MET A 27 THR A 32 -1 O THR A 29 N GLN A 20
SHEET 3 A 6 GLY A 35 THR A 40 -1 O LEU A 37 N VAL A 30
SHEET 4 A 6 HIS A 45 GLN A 48 -1 O ILE A 47 N TYR A 38
SHEET 5 A 6 MET B 51 ASP B 53 -1 O TYR B 52 N ILE A 46
SHEET 6 A 6 VAL B 60 ASN B 61 -1 O VAL B 60 N ASP B 53
SHEET 1 B 6 VAL A 60 ASN A 61 0
SHEET 2 B 6 MET A 51 ASP A 53 -1 N ASP A 53 O VAL A 60
SHEET 3 B 6 HIS B 45 ILE B 47 -1 O ILE B 46 N TYR A 52
SHEET 4 B 6 GLY B 35 THR B 40 -1 N TYR B 38 O ILE B 47
SHEET 5 B 6 MET B 27 THR B 32 -1 N VAL B 30 O LEU B 37
SHEET 6 B 6 SER B 16 PRO B 21 -1 N GLN B 20 O THR B 29
SHEET 1 C 5 ILE A 79 TYR A 81 0
SHEET 2 C 5 ILE A 116 ALA A 122 -1 O TYR A 120 N ILE A 79
SHEET 3 C 5 HIS A 88 THR A 94 1 N HIS A 88 O THR A 117
SHEET 4 C 5 ALA A 184 VAL A 186 -1 O VAL A 186 N THR A 91
SHEET 5 C 5 LEU A 192 PRO A 194 -1 O VAL A 193 N VAL A 185
SHEET 1 D 5 ILE B 79 TYR B 81 0
SHEET 2 D 5 ILE B 116 ALA B 122 -1 O VAL B 118 N TYR B 81
SHEET 3 D 5 HIS B 88 THR B 94 1 N VAL B 92 O ARG B 119
SHEET 4 D 5 ALA B 184 VAL B 186 -1 O VAL B 186 N THR B 91
SHEET 5 D 5 LEU B 192 PRO B 194 -1 O VAL B 193 N VAL B 185
SSBOND 1 CYS A 141 CYS A 163 1555 1555 2.04
SSBOND 2 CYS B 141 CYS B 163 1555 1555 2.03
CISPEP 1 GLY A 49 PRO A 50 0 -0.07
CISPEP 2 THR A 182 PRO A 183 0 -0.13
CISPEP 3 GLY B 49 PRO B 50 0 0.39
CISPEP 4 THR B 182 PRO B 183 0 -0.33
CRYST1 59.400 78.294 95.587 90.00 90.00 90.00 P 21 21 21 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 0.016835 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012772 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010462 0.00000
(ATOM LINES ARE NOT SHOWN.)
END